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Database: PDB
Entry: 3NT5
LinkDB: 3NT5
Original site: 3NT5 
HEADER    OXIDOREDUCTASE                          02-JUL-10   3NT5              
TITLE     CRYSTAL STRUCTURE OF MYO-INOSITOL DEHYDROGENASE FROM BACILLUS SUBTILIS
TITLE    2 WITH BOUND COFACTOR AND PRODUCT INOSOSE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INOSITOL 2-DEHYDROGENASE/D-CHIRO-INOSITOL 3-DEHYDROGENASE; 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MYO-INOSITOL 2-DEHYDROGENASE/D-CHIRO-INOSITOL 3-            
COMPND   5 DEHYDROGENASE, MI 2-DEHYDROGENASE/DCI 3-DEHYDROGENASE;               
COMPND   6 EC: 1.1.1.18;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: BSU39700, E83G, IDH, IOLG, NP_391849.2;                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHISTEV                                   
KEYWDS    BSIDH, OXIDOREDUCTASE, N-TERMINAL ROSSMANN FOLD DOMAIN,               
KEYWDS   2 GLYCERALDEHYDE-3-PHOSPHATE LIKE C-TERMINAL DOMAIN, NAD(H), INOSITOL, 
KEYWDS   3 INOSOSE                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.E.VAN STRAATEN,D.R.J.PALMER,D.A.R.SANDERS                           
REVDAT   4   06-SEP-23 3NT5    1       REMARK HETSYN                            
REVDAT   3   08-NOV-17 3NT5    1       REMARK                                   
REVDAT   2   01-DEC-10 3NT5    1       JRNL                                     
REVDAT   1   15-SEP-10 3NT5    0                                                
JRNL        AUTH   K.E.VAN STRAATEN,H.ZHENG,D.R.PALMER,D.A.SANDERS              
JRNL        TITL   STRUCTURAL INVESTIGATION OF MYO-INOSITOL DEHYDROGENASE FROM  
JRNL        TITL 2 BACILLUS SUBTILIS: IMPLICATIONS FOR CATALYTIC MECHANISM AND  
JRNL        TITL 3 INOSITOL DEHYDROGENASE SUBFAMILY CLASSIFICATION.             
JRNL        REF    BIOCHEM.J.                    V. 432   237 2010              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   20809899                                                     
JRNL        DOI    10.1042/BJ20101079                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.5_2                                         
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22866                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.243                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1170                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.1254 -  5.7958    1.00     2802   156  0.2008 0.2698        
REMARK   3     2  5.7958 -  4.6026    1.00     2725   140  0.2048 0.2371        
REMARK   3     3  4.6026 -  4.0215    1.00     2711   162  0.2257 0.2599        
REMARK   3     4  4.0215 -  3.6541    1.00     2706   133  0.2788 0.3449        
REMARK   3     5  3.6541 -  3.3923    1.00     2690   142  0.3073 0.3609        
REMARK   3     6  3.3923 -  3.1924    1.00     2698   150  0.3078 0.3590        
REMARK   3     7  3.1924 -  3.0326    1.00     2690   140  0.3279 0.3335        
REMARK   3     8  3.0326 -  2.9006    1.00     2674   147  0.3185 0.3418        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 79.12                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.980           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 80.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 111.7                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           5494                                  
REMARK   3   ANGLE     :  1.335           7470                                  
REMARK   3   CHIRALITY :  0.080            844                                  
REMARK   3   PLANARITY :  0.005            950                                  
REMARK   3   DIHEDRAL  : 20.076           2128                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 4                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:40 ) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN 'B' AND (RESSEQ 1:40 ) AND (NOT       
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 291                                         
REMARK   3     RMSD               : 0.038                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 48:74 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN 'B' AND (RESSEQ 48:74 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 206                                         
REMARK   3     RMSD               : 0.033                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 76:117 ) AND (NOT     
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN 'B' AND (RESSEQ 76:117 ) AND (NOT     
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 317                                         
REMARK   3     RMSD               : 0.037                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 120:337 ) AND (NOT    
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN 'B' AND (RESSEQ 120:337 ) AND (NOT    
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 1737                                        
REMARK   3     RMSD               : 0.039                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3NT5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000060247.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED                  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK 9.9.8.0L                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25421                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.122                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 22.38                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 22.80                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.90500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3MZ0 (APO-IDH)                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE PH 5.4, 2.6M     
REMARK 280  AMMONIUM SULFATE, MICROBATCH, TEMPERATURE 298K                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X,-Y+1/2,Z                                             
REMARK 290      15555   -X+1/2,Y,-Z                                             
REMARK 290      16555   X,-Y,-Z+1/2                                             
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z,-X,-Y+1/2                                             
REMARK 290      19555   -Z,-X+1/2,Y                                             
REMARK 290      20555   -Z+1/2,X,-Y                                             
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z,-X                                             
REMARK 290      23555   Y,-Z,-X+1/2                                             
REMARK 290      24555   -Y,-Z+1/2,X                                             
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       91.74900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       91.74900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       91.74900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       91.74900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       91.74900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       91.74900            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       91.74900            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       91.74900            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       91.74900            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       91.74900            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       91.74900            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       91.74900            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       91.74900            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       91.74900            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       91.74900            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       91.74900            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       91.74900            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       91.74900            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       91.74900            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       91.74900            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       91.74900            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       91.74900            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       91.74900            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       91.74900            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       91.74900            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       91.74900            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 50260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -91.74900            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17230 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 83220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       91.74900            
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000       91.74900            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000      -91.74900            
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000       91.74900            
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000        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     SER A   338                                                      
REMARK 465     PHE A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     THR A   341                                                      
REMARK 465     VAL A   342                                                      
REMARK 465     GLN A   343                                                      
REMARK 465     ASN A   344                                                      
REMARK 465     SER B   338                                                      
REMARK 465     PHE B   339                                                      
REMARK 465     THR B   340                                                      
REMARK 465     THR B   341                                                      
REMARK 465     VAL B   342                                                      
REMARK 465     GLN B   343                                                      
REMARK 465     ASN B   344                                                      
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   NE2  HIS B   176     O2   ISE B   345              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  10       43.01    -88.01                                   
REMARK 500    ALA A  32      126.18    177.83                                   
REMARK 500    VAL A  45      -37.96    -39.63                                   
REMARK 500    GLN A  47      -51.99    -27.46                                   
REMARK 500    GLN A  49       58.44     34.34                                   
REMARK 500    ASN A  51       70.14   -116.30                                   
REMARK 500    ALA A  63      -70.46    -48.20                                   
REMARK 500    ASP A  64      138.19    -28.79                                   
REMARK 500    THR A  73       53.05   -141.87                                   
REMARK 500    VAL A 116       20.95    -62.60                                   
REMARK 500    VAL A 144      -54.84    -25.11                                   
REMARK 500    THR A 166       -9.81    -46.77                                   
REMARK 500    GLU A 190      -71.75    -79.85                                   
REMARK 500    GLN A 193      146.50   -170.54                                   
REMARK 500    LYS A 198      105.03    -42.05                                   
REMARK 500    LYS A 232      -37.03     72.68                                   
REMARK 500    ILE A 288      -75.93    -53.87                                   
REMARK 500    LYS A 294      -13.02   -162.70                                   
REMARK 500    GLU A 331      135.00    -38.91                                   
REMARK 500    THR B  10       44.07    -84.29                                   
REMARK 500    ALA B  32      124.40    175.10                                   
REMARK 500    GLN B  49       58.98     31.38                                   
REMARK 500    ASN B  51       68.55   -114.58                                   
REMARK 500    ALA B  63      -70.78    -47.54                                   
REMARK 500    ASP B  64      136.43    -27.69                                   
REMARK 500    THR B  73       51.62   -143.53                                   
REMARK 500    TRP B  75      134.39    -38.49                                   
REMARK 500    VAL B 116       21.05    -62.67                                   
REMARK 500    HIS B 143       -0.26     72.73                                   
REMARK 500    VAL B 144      -54.56    -25.10                                   
REMARK 500    LEU B 149      -50.32   -123.10                                   
REMARK 500    THR B 166       -6.57    -47.77                                   
REMARK 500    THR B 173      -60.49   -100.11                                   
REMARK 500    GLU B 190      -72.69    -77.88                                   
REMARK 500    LYS B 198      107.89    -42.18                                   
REMARK 500    LYS B 232      -34.79     72.60                                   
REMARK 500    ILE B 288      -75.67    -55.86                                   
REMARK 500    LYS B 294      -14.96   -160.14                                   
REMARK 500    GLU B 331      135.55    -36.78                                   
REMARK 500    PHE B 335      -51.85    -28.55                                   
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 NAD A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ISE A 345                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ISE B 345                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3MZ0   RELATED DB: PDB                                   
REMARK 900 APO-IDH                                                              
REMARK 900 RELATED ID: 3NT2   RELATED DB: PDB                                   
REMARK 900 HOLO-IDH IDH WITH BOUND COFACTOR NAD(H)                              
REMARK 900 RELATED ID: 3NT4   RELATED DB: PDB                                   
REMARK 900 IDH WITH BOUND COFACTOR AND INOSITOL                                 
REMARK 900 RELATED ID: 3NTQ   RELATED DB: PDB                                   
REMARK 900 K97V MUTANT IDH WITH BOUND COFACTOR                                  
REMARK 900 RELATED ID: 3NTR   RELATED DB: PDB                                   
REMARK 900 K97V MUTANT IDH WITH BOUND COFACTOR AND INOSITOL                     
DBREF  3NT5 A    1   344  UNP    P26935   IOLG_BACSU       1    344             
DBREF  3NT5 B    1   344  UNP    P26935   IOLG_BACSU       1    344             
SEQRES   1 A  344  MET SER LEU ARG ILE GLY VAL ILE GLY THR GLY ALA ILE          
SEQRES   2 A  344  GLY LYS GLU HIS ILE ASN ARG ILE THR ASN LYS LEU SER          
SEQRES   3 A  344  GLY ALA GLU ILE VAL ALA VAL THR ASP VAL ASN GLN GLU          
SEQRES   4 A  344  ALA ALA GLN LYS VAL VAL GLU GLN TYR GLN LEU ASN ALA          
SEQRES   5 A  344  THR VAL TYR PRO ASN ASP ASP SER LEU LEU ALA ASP GLU          
SEQRES   6 A  344  ASN VAL ASP ALA VAL LEU VAL THR SER TRP GLY PRO ALA          
SEQRES   7 A  344  HIS GLU SER SER VAL LEU LYS ALA ILE LYS ALA GLN LYS          
SEQRES   8 A  344  TYR VAL PHE CYS GLU LYS PRO LEU ALA THR THR ALA GLU          
SEQRES   9 A  344  GLY CYS MET ARG ILE VAL GLU GLU GLU ILE LYS VAL GLY          
SEQRES  10 A  344  LYS ARG LEU VAL GLN VAL GLY PHE MET ARG ARG TYR ASP          
SEQRES  11 A  344  SER GLY TYR VAL GLN LEU LYS GLU ALA LEU ASP ASN HIS          
SEQRES  12 A  344  VAL ILE GLY GLU PRO LEU MET ILE HIS CYS ALA HIS ARG          
SEQRES  13 A  344  ASN PRO THR VAL GLY ASP ASN TYR THR THR ASP MET ALA          
SEQRES  14 A  344  VAL VAL ASP THR LEU VAL HIS GLU ILE ASP VAL LEU HIS          
SEQRES  15 A  344  TRP LEU VAL ASN ASP ASP TYR GLU SER VAL GLN VAL ILE          
SEQRES  16 A  344  TYR PRO LYS LYS SER LYS ASN ALA LEU PRO HIS LEU LYS          
SEQRES  17 A  344  ASP PRO GLN ILE VAL VAL ILE GLU THR LYS GLY GLY ILE          
SEQRES  18 A  344  VAL ILE ASN ALA GLU ILE TYR VAL ASN CYS LYS TYR GLY          
SEQRES  19 A  344  TYR ASP ILE GLN CYS GLU ILE VAL GLY GLU ASP GLY ILE          
SEQRES  20 A  344  ILE LYS LEU PRO GLU PRO SER SER ILE SER LEU ARG LYS          
SEQRES  21 A  344  GLU GLY ARG PHE SER THR ASP ILE LEU MET ASP TRP GLN          
SEQRES  22 A  344  ARG ARG PHE VAL ALA ALA TYR ASP VAL GLU ILE GLN ASP          
SEQRES  23 A  344  PHE ILE ASP SER ILE GLN LYS LYS GLY GLU VAL SER GLY          
SEQRES  24 A  344  PRO THR ALA TRP ASP GLY TYR ILE ALA ALA VAL THR THR          
SEQRES  25 A  344  ASP ALA CYS VAL LYS ALA GLN GLU SER GLY GLN LYS GLU          
SEQRES  26 A  344  LYS VAL GLU LEU LYS GLU LYS PRO GLU PHE TYR GLN SER          
SEQRES  27 A  344  PHE THR THR VAL GLN ASN                                      
SEQRES   1 B  344  MET SER LEU ARG ILE GLY VAL ILE GLY THR GLY ALA ILE          
SEQRES   2 B  344  GLY LYS GLU HIS ILE ASN ARG ILE THR ASN LYS LEU SER          
SEQRES   3 B  344  GLY ALA GLU ILE VAL ALA VAL THR ASP VAL ASN GLN GLU          
SEQRES   4 B  344  ALA ALA GLN LYS VAL VAL GLU GLN TYR GLN LEU ASN ALA          
SEQRES   5 B  344  THR VAL TYR PRO ASN ASP ASP SER LEU LEU ALA ASP GLU          
SEQRES   6 B  344  ASN VAL ASP ALA VAL LEU VAL THR SER TRP GLY PRO ALA          
SEQRES   7 B  344  HIS GLU SER SER VAL LEU LYS ALA ILE LYS ALA GLN LYS          
SEQRES   8 B  344  TYR VAL PHE CYS GLU LYS PRO LEU ALA THR THR ALA GLU          
SEQRES   9 B  344  GLY CYS MET ARG ILE VAL GLU GLU GLU ILE LYS VAL GLY          
SEQRES  10 B  344  LYS ARG LEU VAL GLN VAL GLY PHE MET ARG ARG TYR ASP          
SEQRES  11 B  344  SER GLY TYR VAL GLN LEU LYS GLU ALA LEU ASP ASN HIS          
SEQRES  12 B  344  VAL ILE GLY GLU PRO LEU MET ILE HIS CYS ALA HIS ARG          
SEQRES  13 B  344  ASN PRO THR VAL GLY ASP ASN TYR THR THR ASP MET ALA          
SEQRES  14 B  344  VAL VAL ASP THR LEU VAL HIS GLU ILE ASP VAL LEU HIS          
SEQRES  15 B  344  TRP LEU VAL ASN ASP ASP TYR GLU SER VAL GLN VAL ILE          
SEQRES  16 B  344  TYR PRO LYS LYS SER LYS ASN ALA LEU PRO HIS LEU LYS          
SEQRES  17 B  344  ASP PRO GLN ILE VAL VAL ILE GLU THR LYS GLY GLY ILE          
SEQRES  18 B  344  VAL ILE ASN ALA GLU ILE TYR VAL ASN CYS LYS TYR GLY          
SEQRES  19 B  344  TYR ASP ILE GLN CYS GLU ILE VAL GLY GLU ASP GLY ILE          
SEQRES  20 B  344  ILE LYS LEU PRO GLU PRO SER SER ILE SER LEU ARG LYS          
SEQRES  21 B  344  GLU GLY ARG PHE SER THR ASP ILE LEU MET ASP TRP GLN          
SEQRES  22 B  344  ARG ARG PHE VAL ALA ALA TYR ASP VAL GLU ILE GLN ASP          
SEQRES  23 B  344  PHE ILE ASP SER ILE GLN LYS LYS GLY GLU VAL SER GLY          
SEQRES  24 B  344  PRO THR ALA TRP ASP GLY TYR ILE ALA ALA VAL THR THR          
SEQRES  25 B  344  ASP ALA CYS VAL LYS ALA GLN GLU SER GLY GLN LYS GLU          
SEQRES  26 B  344  LYS VAL GLU LEU LYS GLU LYS PRO GLU PHE TYR GLN SER          
SEQRES  27 B  344  PHE THR THR VAL GLN ASN                                      
HET    NAD  A 400      44                                                       
HET    ISE  A 345      12                                                       
HET    NAI  B 400      44                                                       
HET    ISE  B 345      12                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     ISE (2R,3S,4S,5R,6S)-2,3,4,5,6-PENTAHYDROXYCYCLOHEXANONE             
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETSYN     ISE INOSOSE; MYO-INOSOSE                                             
HETSYN     NAI NADH                                                             
FORMUL   3  NAD    C21 H27 N7 O14 P2                                            
FORMUL   4  ISE    2(C6 H10 O6)                                                 
FORMUL   5  NAI    C21 H29 N7 O14 P2                                            
HELIX    1   1 GLY A   11  LYS A   24  1                                  14    
HELIX    2   2 ASN A   37  TYR A   48  1                                  12    
HELIX    3   3 ASN A   57  ASP A   64  1                                   8    
HELIX    4   4 TRP A   75  PRO A   77  5                                   3    
HELIX    5   5 ALA A   78  ALA A   89  1                                  12    
HELIX    6   6 THR A  102  VAL A  116  1                                  15    
HELIX    7   7 PHE A  125  TYR A  129  5                                   5    
HELIX    8   8 ASP A  130  ASN A  142  1                                  13    
HELIX    9   9 ASP A  167  ASP A  172  1                                   6    
HELIX   10  10 LEU A  174  ASN A  186  1                                  13    
HELIX   11  11 ASP A  271  PHE A  276  1                                   6    
HELIX   12  12 PHE A  276  LYS A  293  1                                  18    
HELIX   13  13 THR A  301  GLY A  322  1                                  22    
HELIX   14  14 GLY B   11  LYS B   24  1                                  14    
HELIX   15  15 ASN B   37  TYR B   48  1                                  12    
HELIX   16  16 ASN B   57  ASP B   64  1                                   8    
HELIX   17  17 TRP B   75  PRO B   77  5                                   3    
HELIX   18  18 ALA B   78  ALA B   89  1                                  12    
HELIX   19  19 THR B  102  VAL B  116  1                                  15    
HELIX   20  20 PHE B  125  TYR B  129  5                                   5    
HELIX   21  21 ASP B  130  ASN B  142  1                                  13    
HELIX   22  22 ASP B  167  ASP B  172  1                                   6    
HELIX   23  23 LEU B  174  ASN B  186  1                                  13    
HELIX   24  24 ASP B  271  LYS B  293  1                                  23    
HELIX   25  25 THR B  301  GLY B  322  1                                  22    
SHEET    1   A 6 THR A  53  VAL A  54  0                                        
SHEET    2   A 6 ALA A  28  THR A  34  1  N  VAL A  33   O  THR A  53           
SHEET    3   A 6 LEU A   3  ILE A   8  1  N  VAL A   7   O  ALA A  32           
SHEET    4   A 6 ALA A  69  VAL A  72  1  O  ALA A  69   N  GLY A   6           
SHEET    5   A 6 TYR A  92  CYS A  95  1  O  TYR A  92   N  VAL A  70           
SHEET    6   A 6 VAL A 121  VAL A 123  1  O  GLN A 122   N  CYS A  95           
SHEET    1   B 6 TYR A 189  ILE A 195  0                                        
SHEET    2   B 6 GLN A 211  THR A 217 -1  O  ILE A 212   N  ILE A 195           
SHEET    3   B 6 VAL A 222  TYR A 228 -1  O  ILE A 223   N  ILE A 215           
SHEET    4   B 6 PRO A 148  ARG A 156  1  N  ILE A 151   O  ASN A 224           
SHEET    5   B 6 ASP A 236  GLY A 243 -1  O  GLU A 240   N  HIS A 152           
SHEET    6   B 6 ILE A 247  LYS A 249 -1  O  ILE A 248   N  ILE A 241           
SHEET    1   C 2 LEU A 258  LYS A 260  0                                        
SHEET    2   C 2 ARG A 263  SER A 265 -1  O  SER A 265   N  LEU A 258           
SHEET    1   D 6 THR B  53  VAL B  54  0                                        
SHEET    2   D 6 ALA B  28  THR B  34  1  N  VAL B  33   O  THR B  53           
SHEET    3   D 6 LEU B   3  ILE B   8  1  N  VAL B   7   O  ALA B  32           
SHEET    4   D 6 ALA B  69  VAL B  72  1  O  ALA B  69   N  GLY B   6           
SHEET    5   D 6 TYR B  92  CYS B  95  1  O  TYR B  92   N  VAL B  70           
SHEET    6   D 6 VAL B 121  VAL B 123  1  O  GLN B 122   N  CYS B  95           
SHEET    1   E 6 TYR B 189  ILE B 195  0                                        
SHEET    2   E 6 GLN B 211  THR B 217 -1  O  GLU B 216   N  SER B 191           
SHEET    3   E 6 VAL B 222  TYR B 228 -1  O  ILE B 223   N  ILE B 215           
SHEET    4   E 6 PRO B 148  ARG B 156  1  N  ILE B 151   O  ASN B 224           
SHEET    5   E 6 ASP B 236  GLY B 243 -1  O  GLU B 240   N  HIS B 152           
SHEET    6   E 6 ILE B 247  LYS B 249 -1  O  ILE B 248   N  ILE B 241           
SHEET    1   F 2 LEU B 258  LYS B 260  0                                        
SHEET    2   F 2 ARG B 263  SER B 265 -1  O  SER B 265   N  LEU B 258           
CISPEP   1 LYS A   97    PRO A   98          0         2.17                     
CISPEP   2 ASP A  209    PRO A  210          0         0.41                     
CISPEP   3 LYS B   97    PRO B   98          0         3.32                     
CISPEP   4 ASP B  209    PRO B  210          0         3.33                     
SITE     1 AC1 17 GLY A   9  GLY A  11  ALA A  12  ILE A  13                    
SITE     2 AC1 17 THR A  34  ASP A  35  VAL A  36  GLN A  42                    
SITE     3 AC1 17 SER A  74  TRP A  75  GLY A  76  ALA A  78                    
SITE     4 AC1 17 GLU A  96  LYS A  97  GLY A 124  MET A 126                    
SITE     5 AC1 17 TYR A 280                                                     
SITE     1 AC2 12 ALA B  12  ILE B  13  THR B  34  ASP B  35                    
SITE     2 AC2 12 VAL B  36  SER B  74  TRP B  75  ALA B  78                    
SITE     3 AC2 12 HIS B  79  LYS B  97  TRP B 272  ISE B 345                    
SITE     1 AC3  6 LYS A  97  HIS A 155  ASN A 157  ASP A 172                    
SITE     2 AC3  6 HIS A 176  TYR A 235                                          
SITE     1 AC4  8 LYS B  97  ARG B 127  HIS B 155  ASN B 157                    
SITE     2 AC4  8 ASP B 172  HIS B 176  TYR B 235  NAI B 400                    
CRYST1  183.498  183.498  183.498  90.00  90.00  90.00 I 21 3       48          
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      0.005450  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005450  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005450        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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