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Database: PDB
Entry: 5N6C
LinkDB: 5N6C
Original site: 5N6C 
HEADER    OXIDOREDUCTASE                          14-FEB-17   5N6C              
TITLE     CRYSTAL STRUCTURE OF HUMAN 3-PHOSPHOGLYCERATE DEHYDROGENASE IN COMPLEX
TITLE    2 WITH NAD AND L-TARTRATE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-3-PHOSPHOGLYCERATE DEHYDROGENASE;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 3-PGDH;                                                     
COMPND   5 EC: 1.1.1.95;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PHGDH, PGDH3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DEHYDROGENASE, SERINE METABOLISM, ENZYMOLOGY, OXIDOREDUCTASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.UNTERLASS,A.BASLE,J.TUCKER,C.CANO,M.E.M.NOBLE,N.J.CURTIN          
REVDAT   3   20-FEB-19 5N6C    1       REMARK LINK                              
REVDAT   2   03-JAN-18 5N6C    1       JRNL                                     
REVDAT   1   22-NOV-17 5N6C    0                                                
JRNL        AUTH   J.E.UNTERLASS,R.J.WOOD,A.BASLE,J.TUCKER,C.CANO,M.M.E.NOBLE,  
JRNL        AUTH 2 N.J.CURTIN                                                   
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE ENZYMATIC ACTIVITY AND          
JRNL        TITL 2 POTENTIAL SUBSTRATE PROMISCUITY OF HUMAN 3-PHOSPHOGLYCERATE  
JRNL        TITL 3 DEHYDROGENASE (PHGDH).                                       
JRNL        REF    ONCOTARGET                    V.   8 04478 2017              
JRNL        REFN                   ESSN 1949-2553                               
JRNL        PMID   29262655                                                     
JRNL        DOI    10.18632/ONCOTARGET.22327                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 66.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 26108                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1319                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1911                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 89                           
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4392                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 98                                      
REMARK   3   SOLVENT ATOMS            : 74                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.38000                                              
REMARK   3    B22 (A**2) : 0.15000                                              
REMARK   3    B33 (A**2) : -3.50000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.08000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.387         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.251         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.239         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.384        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4597 ; 0.024 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4311 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6255 ; 2.217 ; 2.002       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10019 ; 1.176 ; 2.999       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   613 ; 6.236 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   173 ;40.980 ;25.491       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   787 ;15.806 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;16.540 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   750 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5132 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   828 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     8    305       B     8    305   17298 0.120 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     7        A    95                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.2580  54.5910  29.0390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3560 T22:   0.8037                                     
REMARK   3      T33:   1.0856 T12:  -0.1552                                     
REMARK   3      T13:   0.2750 T23:   0.1915                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0010 L22:   4.4569                                     
REMARK   3      L33:   5.5624 L12:   0.8139                                     
REMARK   3      L13:  -0.8869 L23:  -0.2768                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4767 S12:   0.9632 S13:   0.2513                       
REMARK   3      S21:  -0.9727 S22:   0.3081 S23:  -0.5416                       
REMARK   3      S31:  -0.3558 S32:   0.6028 S33:   0.1686                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    96        A   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.2980  50.8650  54.5540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0065 T22:   0.2887                                     
REMARK   3      T33:   0.8108 T12:  -0.0174                                     
REMARK   3      T13:   0.0482 T23:  -0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9755 L22:   2.2773                                     
REMARK   3      L33:   0.8531 L12:   0.3592                                     
REMARK   3      L13:   0.0086 L23:   0.0803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0010 S12:  -0.1063 S13:   0.2927                       
REMARK   3      S21:   0.0123 S22:   0.0183 S23:   0.0250                       
REMARK   3      S31:  -0.0426 S32:   0.0097 S33:  -0.0192                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     8        B    95                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9410  26.8520  90.1970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0783 T22:   0.3466                                     
REMARK   3      T33:   0.7574 T12:   0.0209                                     
REMARK   3      T13:   0.0517 T23:  -0.1097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8532 L22:   9.5068                                     
REMARK   3      L33:   9.9070 L12:  -2.6553                                     
REMARK   3      L13:   2.5235 L23:  -5.2964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4916 S12:  -0.2328 S13:   0.2135                       
REMARK   3      S21:   2.2738 S22:   0.3071 S23:  -0.0329                       
REMARK   3      S31:  -2.6979 S32:  -0.3620 S33:   0.1846                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    96        B   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0540  27.1380  59.1010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0350 T22:   0.3552                                     
REMARK   3      T33:   0.9397 T12:  -0.0180                                     
REMARK   3      T13:   0.0584 T23:   0.0407                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5193 L22:   2.5274                                     
REMARK   3      L33:   0.4375 L12:   0.2851                                     
REMARK   3      L13:  -0.0110 L23:  -0.3021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0302 S12:  -0.2695 S13:  -0.4471                       
REMARK   3      S21:   0.1783 S22:   0.0323 S23:  -0.0274                       
REMARK   3      S31:   0.0491 S32:   0.0023 S33:  -0.0022                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5N6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003529.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27448                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 66.730                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.880                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.85                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2G76                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.5 0.2 M MGCL2           
REMARK 280  HEXAHYDRATE 20 % (W/V) PEG 3350, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 277K                                                    
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       54.85950            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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     ALA B     7                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   8    CG   CD   CE   NZ                                   
REMARK 470     LYS A  33    CD   CE   NZ                                        
REMARK 470     LYS A  38    CD   CE   NZ                                        
REMARK 470     GLN A  46    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 136    CD   CE   NZ                                        
REMARK 470     LYS A 137    CE   NZ                                             
REMARK 470     LYS A 227    NZ                                                  
REMARK 470     ARG A 268    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B  20    CZ   NH1  NH2                                       
REMARK 470     LYS B  21    CG   CD   CE   NZ                                   
REMARK 470     GLN B  29    CD   OE1  NE2                                       
REMARK 470     LYS B  33    CD   CE   NZ                                        
REMARK 470     LYS B  38    CD   CE   NZ                                        
REMARK 470     GLU B  39    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  46    CG   CD   OE1  NE2                                  
REMARK 470     ASP B  47    CG   OD1  OD2                                       
REMARK 470     ARG B  54    NE   CZ   NH1  NH2                                  
REMARK 470     ASP B  62    OD1  OD2                                            
REMARK 470     LYS B  69    CE   NZ                                             
REMARK 470     GLU B  86    CD   OE1  OE2                                       
REMARK 470     LYS B 136    CD   CE   NZ                                        
REMARK 470     LYS B 227    CD   CE   NZ                                        
REMARK 470     ARG B 268    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 289    CD   CE   NZ                                        
REMARK 470     MET B 306    CB   CG   SD   CE                                   
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   OD1  ASP B   260     SG   CYS B   281              2.18            
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    SER A 166   CB    SER A 166   OG      0.101                       
REMARK 500    GLU A 297   CD    GLU A 297   OE1     0.072                       
REMARK 500    GLY B 131   C     GLY B 131   O      -0.101                       
REMARK 500    ARG B 135   CD    ARG B 135   NE     -0.109                       
REMARK 500    GLU B 181   CD    GLU B 181   OE1     0.068                       
REMARK 500    GLU B 195   CD    GLU B 195   OE1     0.074                       
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    ASP A  62   CB  -  CG  -  OD1 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    MET A 115   CG  -  SD  -  CE  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ASP A 130   CB  -  CG  -  OD1 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP A 130   CB  -  CG  -  OD2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ASP A 201   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A 236   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 236   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASP A 241   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ASP A 274   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    LYS A 289   CB  -  CG  -  CD  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    ASP B  81   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP B 130   CB  -  CG  -  OD1 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ASP B 130   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG B 135   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ASP B 201   CB  -  CG  -  OD2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ARG B 236   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    GLU B 290   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.8 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    ASN A  35       97.38     56.42                                   
REMARK 500    ARG A  54     -108.44   -117.15                                   
REMARK 500    ASP A  62      -78.24    -49.34                                   
REMARK 500    VAL A  80       36.41   -143.30                                   
REMARK 500    GLU A 134       74.51   -115.38                                   
REMARK 500    HIS A 206       46.70   -151.68                                   
REMARK 500    ALA A 235      -86.01   -106.06                                   
REMARK 500    LYS B  33      119.20    178.62                                   
REMARK 500    GLN B  34     -164.39   -106.89                                   
REMARK 500    ASN B  35       27.80     43.28                                   
REMARK 500    ARG B  54     -102.91   -121.05                                   
REMARK 500    VAL B  80       33.08   -141.23                                   
REMARK 500    GLU B 134       77.66   -117.55                                   
REMARK 500    HIS B 206       50.69   -148.78                                   
REMARK 500    ALA B 235      -86.30   -109.10                                   
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 TLA A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD B 401                 
DBREF  5N6C A    8   306  UNP    O43175   SERA_HUMAN       8    306             
DBREF  5N6C B    8   306  UNP    O43175   SERA_HUMAN       8    306             
SEQADV 5N6C ALA A    7  UNP  O43175              EXPRESSION TAG                 
SEQADV 5N6C ALA B    7  UNP  O43175              EXPRESSION TAG                 
SEQRES   1 A  300  ALA LYS VAL LEU ILE SER ASP SER LEU ASP PRO CYS CYS          
SEQRES   2 A  300  ARG LYS ILE LEU GLN ASP GLY GLY LEU GLN VAL VAL GLU          
SEQRES   3 A  300  LYS GLN ASN LEU SER LYS GLU GLU LEU ILE ALA GLU LEU          
SEQRES   4 A  300  GLN ASP CYS GLU GLY LEU ILE VAL ARG SER ALA THR LYS          
SEQRES   5 A  300  VAL THR ALA ASP VAL ILE ASN ALA ALA GLU LYS LEU GLN          
SEQRES   6 A  300  VAL VAL GLY ARG ALA GLY THR GLY VAL ASP ASN VAL ASP          
SEQRES   7 A  300  LEU GLU ALA ALA THR ARG LYS GLY ILE LEU VAL MET ASN          
SEQRES   8 A  300  THR PRO ASN GLY ASN SER LEU SER ALA ALA GLU LEU THR          
SEQRES   9 A  300  CYS GLY MET ILE MET CYS LEU ALA ARG GLN ILE PRO GLN          
SEQRES  10 A  300  ALA THR ALA SER MET LYS ASP GLY LYS TRP GLU ARG LYS          
SEQRES  11 A  300  LYS PHE MET GLY THR GLU LEU ASN GLY LYS THR LEU GLY          
SEQRES  12 A  300  ILE LEU GLY LEU GLY ARG ILE GLY ARG GLU VAL ALA THR          
SEQRES  13 A  300  ARG MET GLN SER PHE GLY MET LYS THR ILE GLY TYR ASP          
SEQRES  14 A  300  PRO ILE ILE SER PRO GLU VAL SER ALA SER PHE GLY VAL          
SEQRES  15 A  300  GLN GLN LEU PRO LEU GLU GLU ILE TRP PRO LEU CYS ASP          
SEQRES  16 A  300  PHE ILE THR VAL HIS THR PRO LEU LEU PRO SER THR THR          
SEQRES  17 A  300  GLY LEU LEU ASN ASP ASN THR PHE ALA GLN CYS LYS LYS          
SEQRES  18 A  300  GLY VAL ARG VAL VAL ASN CYS ALA ARG GLY GLY ILE VAL          
SEQRES  19 A  300  ASP GLU GLY ALA LEU LEU ARG ALA LEU GLN SER GLY GLN          
SEQRES  20 A  300  CYS ALA GLY ALA ALA LEU ASP VAL PHE THR GLU GLU PRO          
SEQRES  21 A  300  PRO ARG ASP ARG ALA LEU VAL ASP HIS GLU ASN VAL ILE          
SEQRES  22 A  300  SER CYS PRO HIS LEU GLY ALA SER THR LYS GLU ALA GLN          
SEQRES  23 A  300  SER ARG CYS GLY GLU GLU ILE ALA VAL GLN PHE VAL ASP          
SEQRES  24 A  300  MET                                                          
SEQRES   1 B  300  ALA LYS VAL LEU ILE SER ASP SER LEU ASP PRO CYS CYS          
SEQRES   2 B  300  ARG LYS ILE LEU GLN ASP GLY GLY LEU GLN VAL VAL GLU          
SEQRES   3 B  300  LYS GLN ASN LEU SER LYS GLU GLU LEU ILE ALA GLU LEU          
SEQRES   4 B  300  GLN ASP CYS GLU GLY LEU ILE VAL ARG SER ALA THR LYS          
SEQRES   5 B  300  VAL THR ALA ASP VAL ILE ASN ALA ALA GLU LYS LEU GLN          
SEQRES   6 B  300  VAL VAL GLY ARG ALA GLY THR GLY VAL ASP ASN VAL ASP          
SEQRES   7 B  300  LEU GLU ALA ALA THR ARG LYS GLY ILE LEU VAL MET ASN          
SEQRES   8 B  300  THR PRO ASN GLY ASN SER LEU SER ALA ALA GLU LEU THR          
SEQRES   9 B  300  CYS GLY MET ILE MET CYS LEU ALA ARG GLN ILE PRO GLN          
SEQRES  10 B  300  ALA THR ALA SER MET LYS ASP GLY LYS TRP GLU ARG LYS          
SEQRES  11 B  300  LYS PHE MET GLY THR GLU LEU ASN GLY LYS THR LEU GLY          
SEQRES  12 B  300  ILE LEU GLY LEU GLY ARG ILE GLY ARG GLU VAL ALA THR          
SEQRES  13 B  300  ARG MET GLN SER PHE GLY MET LYS THR ILE GLY TYR ASP          
SEQRES  14 B  300  PRO ILE ILE SER PRO GLU VAL SER ALA SER PHE GLY VAL          
SEQRES  15 B  300  GLN GLN LEU PRO LEU GLU GLU ILE TRP PRO LEU CYS ASP          
SEQRES  16 B  300  PHE ILE THR VAL HIS THR PRO LEU LEU PRO SER THR THR          
SEQRES  17 B  300  GLY LEU LEU ASN ASP ASN THR PHE ALA GLN CYS LYS LYS          
SEQRES  18 B  300  GLY VAL ARG VAL VAL ASN CYS ALA ARG GLY GLY ILE VAL          
SEQRES  19 B  300  ASP GLU GLY ALA LEU LEU ARG ALA LEU GLN SER GLY GLN          
SEQRES  20 B  300  CYS ALA GLY ALA ALA LEU ASP VAL PHE THR GLU GLU PRO          
SEQRES  21 B  300  PRO ARG ASP ARG ALA LEU VAL ASP HIS GLU ASN VAL ILE          
SEQRES  22 B  300  SER CYS PRO HIS LEU GLY ALA SER THR LYS GLU ALA GLN          
SEQRES  23 B  300  SER ARG CYS GLY GLU GLU ILE ALA VAL GLN PHE VAL ASP          
SEQRES  24 B  300  MET                                                          
HET    TLA  A 401      10                                                       
HET    NAD  A 402      44                                                       
HET    NAD  B 401      44                                                       
HETNAM     TLA L(+)-TARTARIC ACID                                               
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   3  TLA    C4 H6 O6                                                     
FORMUL   4  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   6  HOH   *74(H2 O)                                                     
HELIX    1 AA1 PRO A   17  GLY A   27  1                                  11    
HELIX    2 AA2 SER A   37  GLN A   46  1                                  10    
HELIX    3 AA3 THR A   60  ALA A   67  1                                   8    
HELIX    4 AA4 ASP A   84  LYS A   91  1                                   8    
HELIX    5 AA5 ASN A  102  GLN A  120  1                                  19    
HELIX    6 AA6 GLN A  120  ASP A  130  1                                  11    
HELIX    7 AA7 ARG A  135  MET A  139  5                                   5    
HELIX    8 AA8 GLY A  154  SER A  166  1                                  13    
HELIX    9 AA9 SER A  179  PHE A  186  1                                   8    
HELIX   10 AB1 PRO A  192  TRP A  197  1                                   6    
HELIX   11 AB2 PRO A  198  CYS A  200  5                                   3    
HELIX   12 AB3 ASN A  218  CYS A  225  1                                   8    
HELIX   13 AB4 ASP A  241  GLY A  252  1                                  12    
HELIX   14 AB5 ARG A  270  HIS A  275  1                                   6    
HELIX   15 AB6 THR A  288  MET A  306  1                                  19    
HELIX   16 AB7 PRO B   17  GLY B   27  1                                  11    
HELIX   17 AB8 SER B   37  GLN B   46  1                                  10    
HELIX   18 AB9 THR B   60  ALA B   67  1                                   8    
HELIX   19 AC1 ASP B   84  LYS B   91  1                                   8    
HELIX   20 AC2 ASN B  102  GLN B  120  1                                  19    
HELIX   21 AC3 GLN B  120  ASP B  130  1                                  11    
HELIX   22 AC4 ARG B  135  MET B  139  5                                   5    
HELIX   23 AC5 GLY B  154  SER B  166  1                                  13    
HELIX   24 AC6 SER B  179  PHE B  186  1                                   8    
HELIX   25 AC7 PRO B  192  TRP B  197  1                                   6    
HELIX   26 AC8 PRO B  198  CYS B  200  5                                   3    
HELIX   27 AC9 ASN B  218  CYS B  225  1                                   8    
HELIX   28 AD1 ASP B  241  GLY B  252  1                                  12    
HELIX   29 AD2 ARG B  270  HIS B  275  1                                   6    
HELIX   30 AD3 THR B  288  MET B  306  1                                  19    
SHEET    1 AA1 5 GLN A  29  GLU A  32  0                                        
SHEET    2 AA1 5 LYS A   8  ILE A  11  1  N  ILE A  11   O  VAL A  31           
SHEET    3 AA1 5 GLY A  50  VAL A  53  1  O  GLY A  50   N  LEU A  10           
SHEET    4 AA1 5 VAL A  72  ARG A  75  1  O  GLY A  74   N  VAL A  53           
SHEET    5 AA1 5 LEU A  94  MET A  96  1  O  MET A  96   N  VAL A  73           
SHEET    1 AA2 7 GLN A 189  GLN A 190  0                                        
SHEET    2 AA2 7 LYS A 170  TYR A 174  1  N  THR A 171   O  GLN A 189           
SHEET    3 AA2 7 THR A 147  LEU A 151  1  N  LEU A 148   O  LYS A 170           
SHEET    4 AA2 7 PHE A 202  VAL A 205  1  O  PHE A 202   N  GLY A 149           
SHEET    5 AA2 7 ARG A 230  ASN A 233  1  O  VAL A 232   N  ILE A 203           
SHEET    6 AA2 7 GLY A 256  LEU A 259  1  O  ALA A 258   N  ASN A 233           
SHEET    7 AA2 7 VAL A 278  SER A 280  1  O  ILE A 279   N  ALA A 257           
SHEET    1 AA3 5 VAL B  30  GLU B  32  0                                        
SHEET    2 AA3 5 VAL B   9  ILE B  11  1  N  ILE B  11   O  VAL B  31           
SHEET    3 AA3 5 GLY B  50  VAL B  53  1  O  GLY B  50   N  LEU B  10           
SHEET    4 AA3 5 VAL B  72  ARG B  75  1  O  GLY B  74   N  LEU B  51           
SHEET    5 AA3 5 LEU B  94  MET B  96  1  O  MET B  96   N  VAL B  73           
SHEET    1 AA4 7 GLN B 189  GLN B 190  0                                        
SHEET    2 AA4 7 LYS B 170  TYR B 174  1  N  GLY B 173   O  GLN B 189           
SHEET    3 AA4 7 THR B 147  LEU B 151  1  N  LEU B 148   O  LYS B 170           
SHEET    4 AA4 7 PHE B 202  VAL B 205  1  O  PHE B 202   N  GLY B 149           
SHEET    5 AA4 7 ARG B 230  ASN B 233  1  O  VAL B 232   N  ILE B 203           
SHEET    6 AA4 7 GLY B 256  LEU B 259  1  O  ALA B 258   N  ASN B 233           
SHEET    7 AA4 7 VAL B 278  SER B 280  1  O  ILE B 279   N  ALA B 257           
CISPEP   1 GLU A  265    PRO A  266          0         5.33                     
CISPEP   2 GLU B  265    PRO B  266          0        -1.07                     
SITE     1 AC1 11 ARG A  54  SER A  55  ARG A  75  THR A  78                    
SITE     2 AC1 11 ARG A 236  HIS A 283  ALA A 286  GLN A 292                    
SITE     3 AC1 11 NAD A 402  HOH A 514  ARG B 135                               
SITE     1 AC2 26 THR A  78  ASN A 102  GLY A 152  GLY A 154                    
SITE     2 AC2 26 ARG A 155  ILE A 156  TYR A 174  ASP A 175                    
SITE     3 AC2 26 PRO A 176  ILE A 177  HIS A 206  THR A 207                    
SITE     4 AC2 26 PRO A 208  THR A 213  CYS A 234  ALA A 235                    
SITE     5 AC2 26 ARG A 236  ASP A 260  HIS A 283  GLY A 285                    
SITE     6 AC2 26 ALA A 286  TLA A 401  HOH A 505  HOH A 509                    
SITE     7 AC2 26 HOH A 520  HOH A 524                                          
SITE     1 AC3 21 GLY B 152  GLY B 154  ARG B 155  ILE B 156                    
SITE     2 AC3 21 TYR B 174  ASP B 175  PRO B 176  ILE B 177                    
SITE     3 AC3 21 HIS B 206  THR B 207  PRO B 208  THR B 213                    
SITE     4 AC3 21 CYS B 234  ALA B 235  ARG B 236  ASP B 260                    
SITE     5 AC3 21 HIS B 283  GLY B 285  ALA B 286  HOH B 503                    
SITE     6 AC3 21 HOH B 514                                                     
CRYST1   43.523  109.719   66.923  90.00  94.40  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      0.022976  0.000000  0.001769        0.00000                         
SCALE2      0.000000  0.009114  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014987        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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