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Database: PDB
Entry: 6ALJ
LinkDB: 6ALJ
Original site: 6ALJ 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 08-AUG-17   6ALJ              
TITLE     ALDH1A2 LIGANDED WITH NAD AND COMPOUND WIN18,446                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDEHYDE DEHYDROGENASE 1A2;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 26-518;                                       
COMPND   5 SYNONYM: RETINAL DEHYDROGENASE 2, RALDH2, ALDEHYDE DEHYDROGENASE     
COMPND   6 FAMILY 1 MEMBER A2, RETINALDEHYDE-SPECIFIC DEHYDROGENASE TYPE 2,     
COMPND   7 RALDH(II);                                                           
COMPND   8 EC: 1.2.1.36;                                                        
COMPND   9 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: ALDH1A2, RALDH2;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21STAR (DE3)                             
KEYWDS    RETINOIC ACID SIGNALING, MALE CONTRACEPTION, DRUG DISCOVERY, DRUG     
KEYWDS   2 DEVELOPMENT, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.CHEN,J.-Y.ZHU,E.SCHONBRUNN                                          
REVDAT   4   11-DEC-19 6ALJ    1       REMARK                                   
REVDAT   3   28-MAR-18 6ALJ    1       JRNL                                     
REVDAT   2   17-JAN-18 6ALJ    1       JRNL                                     
REVDAT   1   10-JAN-18 6ALJ    0                                                
JRNL        AUTH   Y.CHEN,J.Y.ZHU,K.H.HONG,D.C.MIKLES,G.I.GEORG,A.S.GOLDSTEIN,  
JRNL        AUTH 2 J.K.AMORY,E.SCHONBRUNN                                       
JRNL        TITL   STRUCTURAL BASIS OF ALDH1A2 INHIBITION BY IRREVERSIBLE AND   
JRNL        TITL 2 REVERSIBLE SMALL MOLECULE INHIBITORS.                        
JRNL        REF    ACS CHEM. BIOL.               V.  13   582 2018              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   29240402                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.7B00685                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.89 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1-2575_2575                              
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) : 1.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 150490                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.137                           
REMARK   3   R VALUE            (WORKING SET) : 0.137                           
REMARK   3   FREE R VALUE                     : 0.177                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1505                            
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 40.8410 -  4.2019    0.96    13328   134  0.1274 0.1513        
REMARK   3     2  4.2019 -  3.3356    0.98    13384   136  0.1181 0.1575        
REMARK   3     3  3.3356 -  2.9141    0.98    13449   135  0.1391 0.1653        
REMARK   3     4  2.9141 -  2.6477    0.99    13560   137  0.1480 0.2129        
REMARK   3     5  2.6477 -  2.4580    0.99    13650   138  0.1438 0.1854        
REMARK   3     6  2.4580 -  2.3131    1.00    13596   138  0.1405 0.1873        
REMARK   3     7  2.3131 -  2.1973    1.00    13620   137  0.1388 0.1883        
REMARK   3     8  2.1973 -  2.1016    1.00    13573   137  0.1385 0.1766        
REMARK   3     9  2.1016 -  2.0207    1.00    13615   138  0.1397 0.1878        
REMARK   3    10  2.0207 -  1.9510    1.00    13611   137  0.1482 0.1909        
REMARK   3    11  1.9510 -  1.8900    1.00    13599   138  0.1747 0.2216        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.700           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.11                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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          15898                                  
REMARK   3   ANGLE     :  1.028          21549                                  
REMARK   3   CHIRALITY :  0.064           2353                                  
REMARK   3   PLANARITY :  0.006           2810                                  
REMARK   3   DIHEDRAL  :  6.668          13065                                  
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 : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ALJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229408.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE-CRYSTAL      
REMARK 200                                   SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 150515                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.831                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.703                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.32                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.040                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1BI9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40 MG/ML ALDH1A2, 0.2 M SODIUM CITRATE   
REMARK 280  TRIBASIC DEHYDRATE, 20% W/V POLYETHYLENE GLYCOL 3,350, 1.3 MM       
REMARK 280  WIN18,446 AND 10%DMSO, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 291.1K                                                  
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       69.91000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 24610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 58260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     LEU A    26                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     LEU C    26                                                      
REMARK 465     LEU D    26                                                      
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   NZ   LYS B   370     O3D  NAD B   601              1.31            
REMARK 500   NH1  ARG A   173     O    HOH A   701              1.81            
REMARK 500   O    HOH A  1052     O    HOH A  1162              1.85            
REMARK 500   O    HOH A   905     O    HOH C  1113              1.92            
REMARK 500   O    HOH A   969     O    HOH C  1099              1.92            
REMARK 500   O    HOH C  1073     O    HOH C  1093              2.04            
REMARK 500   O    HOH B   722     O    HOH B   959              2.06            
REMARK 500   O    HOH D   999     O    HOH D  1173              2.06            
REMARK 500   O    HOH C  1113     O    HOH C  1200              2.07            
REMARK 500   O    HOH D   735     O    HOH D  1133              2.08            
REMARK 500   O    HOH B  1008     O    HOH B  1099              2.09            
REMARK 500   O    HOH A   718     O    HOH B   848              2.09            
REMARK 500   O    HOH B  1125     O    HOH B  1136              2.10            
REMARK 500   O    HOH C  1173     O    HOH C  1193              2.12            
REMARK 500   OE1  GLU B   286     O    HOH B   701              2.12            
REMARK 500   NZ   LYS A   108     O    HOH A   702              2.12            
REMARK 500   O    HOH A   989     O    HOH C  1037              2.14            
REMARK 500   O    HOH A  1105     O    HOH A  1175              2.14            
REMARK 500   O    HOH B  1000     O    HOH B  1150              2.14            
REMARK 500   O    HOH D   704     O    HOH D  1130              2.15            
REMARK 500   O    HOH B  1101     O    HOH B  1118              2.15            
REMARK 500   O    HOH C   707     O    HOH C  1099              2.15            
REMARK 500   O    HOH C   721     O    HOH C  1105              2.15            
REMARK 500   O    HOH A   712     O    HOH A   732              2.15            
REMARK 500   O    HOH B  1062     O    HOH B  1095              2.16            
REMARK 500   OE1  GLU D   273     O    HOH D   701              2.16            
REMARK 500   O    HOH B   986     O    HOH B  1141              2.16            
REMARK 500   O    HOH C  1002     O    HOH C  1212              2.16            
REMARK 500   O    HOH C   876     O    HOH C  1184              2.17            
REMARK 500   O    THR C    30     O    HOH C   701              2.17            
REMARK 500   O    HOH C  1043     O    HOH C  1212              2.17            
REMARK 500   O    HOH D  1209     O    HOH D  1210              2.18            
REMARK 500   O    HOH B  1056     O    HOH B  1070              2.19            
REMARK 500   O    HOH C   948     O    HOH C  1070              2.19            
REMARK 500   O    HOH B   705     O    HOH B   886              2.19            
REMARK 500   O    HOH B   986     O    HOH B  1025              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1162     O    HOH D  1077     1556     2.10            
REMARK 500   NH2  ARG A    53     O    GLY D   396     1556     2.14            
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    CYS A  67     -179.59   -172.28                                   
REMARK 500    VAL A 138      -68.88   -104.63                                   
REMARK 500    THR A 245      -79.89    -97.53                                   
REMARK 500    SER A 278      -87.83    -88.90                                   
REMARK 500    LEU A 287     -149.51   -123.24                                   
REMARK 500    THR A 451      148.79   -170.29                                   
REMARK 500    LYS A 487     -134.82     53.49                                   
REMARK 500    MET A 495      165.56     66.74                                   
REMARK 500    VAL B 138      -74.38   -104.54                                   
REMARK 500    THR B 245      -75.50   -104.76                                   
REMARK 500    SER B 278      -97.38    -94.69                                   
REMARK 500    LEU B 287     -150.40   -126.81                                   
REMARK 500    LYS B 487     -136.68     53.22                                   
REMARK 500    MET B 495      162.79     67.68                                   
REMARK 500    CYS C  67     -178.05   -173.03                                   
REMARK 500    VAL C 138      -72.48   -105.86                                   
REMARK 500    THR C 245      -79.63   -104.80                                   
REMARK 500    SER C 278      -95.75    -96.88                                   
REMARK 500    LEU C 287     -148.11   -125.08                                   
REMARK 500    PHE C 397       64.41   -109.90                                   
REMARK 500    LYS C 487     -137.18     59.46                                   
REMARK 500    MET C 495      169.85     71.23                                   
REMARK 500    CYS D  67     -177.50   -171.78                                   
REMARK 500    VAL D 138      -68.67   -103.95                                   
REMARK 500    THR D 245      -76.21   -100.28                                   
REMARK 500    SER D 278      -86.58    -91.77                                   
REMARK 500    LEU D 287     -148.88   -126.55                                   
REMARK 500    LYS D 487     -133.01     52.74                                   
REMARK 500    MET D 495      165.92     72.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1220        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A1221        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH A1222        DISTANCE =  7.30 ANGSTROMS                       
REMARK 525    HOH B1183        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH B1184        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH C1241        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH C1242        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH C1243        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH C1244        DISTANCE =  8.18 ANGSTROMS                       
REMARK 525    HOH D1224        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH D1225        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH D1226        DISTANCE =  6.89 ANGSTROMS                       
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 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CW2 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CW2 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CW2 C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CW2 D 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6B5G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6B5H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6B5I   RELATED DB: PDB                                   
DBREF  6ALJ A   26   518  UNP    O94788   AL1A2_HUMAN     26    518             
DBREF  6ALJ B   26   518  UNP    O94788   AL1A2_HUMAN     26    518             
DBREF  6ALJ C   26   518  UNP    O94788   AL1A2_HUMAN     26    518             
DBREF  6ALJ D   26   518  UNP    O94788   AL1A2_HUMAN     26    518             
SEQRES   1 A  493  LEU PRO SER PRO THR PRO ASN LEU GLU ILE LYS TYR THR          
SEQRES   2 A  493  LYS ILE PHE ILE ASN ASN GLU TRP GLN ASN SER GLU SER          
SEQRES   3 A  493  GLY ARG VAL PHE PRO VAL TYR ASN PRO ALA THR GLY GLU          
SEQRES   4 A  493  GLN VAL CYS GLU VAL GLN GLU ALA ASP LYS ALA ASP ILE          
SEQRES   5 A  493  ASP LYS ALA VAL GLN ALA ALA ARG LEU ALA PHE SER LEU          
SEQRES   6 A  493  GLY SER VAL TRP ARG ARG MET ASP ALA SER GLU ARG GLY          
SEQRES   7 A  493  ARG LEU LEU ASP LYS LEU ALA ASP LEU VAL GLU ARG ASP          
SEQRES   8 A  493  ARG ALA VAL LEU ALA THR MET GLU SER LEU ASN GLY GLY          
SEQRES   9 A  493  LYS PRO PHE LEU GLN ALA PHE TYR VAL ASP LEU GLN GLY          
SEQRES  10 A  493  VAL ILE LYS THR PHE ARG TYR TYR ALA GLY TRP ALA ASP          
SEQRES  11 A  493  LYS ILE HIS GLY MET THR ILE PRO VAL ASP GLY ASP TYR          
SEQRES  12 A  493  PHE THR PHE THR ARG HIS GLU PRO ILE GLY VAL CYS GLY          
SEQRES  13 A  493  GLN ILE ILE PRO TRP ASN PHE PRO LEU LEU MET PHE ALA          
SEQRES  14 A  493  TRP LYS ILE ALA PRO ALA LEU CYS CYS GLY ASN THR VAL          
SEQRES  15 A  493  VAL ILE LYS PRO ALA GLU GLN THR PRO LEU SER ALA LEU          
SEQRES  16 A  493  TYR MET GLY ALA LEU ILE LYS GLU ALA GLY PHE PRO PRO          
SEQRES  17 A  493  GLY VAL ILE ASN ILE LEU PRO GLY TYR GLY PRO THR ALA          
SEQRES  18 A  493  GLY ALA ALA ILE ALA SER HIS ILE GLY ILE ASP LYS ILE          
SEQRES  19 A  493  ALA PHE THR GLY SER THR GLU VAL GLY LYS LEU ILE GLN          
SEQRES  20 A  493  GLU ALA ALA GLY ARG SER ASN LEU LYS ARG VAL THR LEU          
SEQRES  21 A  493  GLU LEU GLY GLY LYS SER PRO ASN ILE ILE PHE ALA ASP          
SEQRES  22 A  493  ALA ASP LEU ASP TYR ALA VAL GLU GLN ALA HIS GLN GLY          
SEQRES  23 A  493  VAL PHE PHE ASN GLN GLY GLN CYS CYS THR ALA GLY SER          
SEQRES  24 A  493  ARG ILE PHE VAL GLU GLU SER ILE TYR GLU GLU PHE VAL          
SEQRES  25 A  493  ARG ARG SER VAL GLU ARG ALA LYS ARG ARG VAL VAL GLY          
SEQRES  26 A  493  SER PRO PHE ASP PRO THR THR GLU GLN GLY PRO GLN ILE          
SEQRES  27 A  493  ASP LYS LYS GLN TYR ASN LYS ILE LEU GLU LEU ILE GLN          
SEQRES  28 A  493  SER GLY VAL ALA GLU GLY ALA LYS LEU GLU CYS GLY GLY          
SEQRES  29 A  493  LYS GLY LEU GLY ARG LYS GLY PHE PHE ILE GLU PRO THR          
SEQRES  30 A  493  VAL PHE SER ASN VAL THR ASP ASP MET ARG ILE ALA LYS          
SEQRES  31 A  493  GLU GLU ILE PHE GLY PRO VAL GLN GLU ILE LEU ARG PHE          
SEQRES  32 A  493  LYS THR MET ASP GLU VAL ILE GLU ARG ALA ASN ASN SER          
SEQRES  33 A  493  ASP PHE GLY LEU VAL ALA ALA VAL PHE THR ASN ASP ILE          
SEQRES  34 A  493  ASN LYS ALA LEU THR VAL SER SER ALA MET GLN ALA GLY          
SEQRES  35 A  493  THR VAL TRP ILE ASN CYS TYR ASN ALA LEU ASN ALA GLN          
SEQRES  36 A  493  SER PRO PHE GLY GLY PHE LYS MET SER GLY ASN GLY ARG          
SEQRES  37 A  493  GLU MET GLY GLU PHE GLY LEU ARG GLU TYR SER GLU VAL          
SEQRES  38 A  493  LYS THR VAL THR VAL LYS ILE PRO GLN LYS ASN SER              
SEQRES   1 B  493  LEU PRO SER PRO THR PRO ASN LEU GLU ILE LYS TYR THR          
SEQRES   2 B  493  LYS ILE PHE ILE ASN ASN GLU TRP GLN ASN SER GLU SER          
SEQRES   3 B  493  GLY ARG VAL PHE PRO VAL TYR ASN PRO ALA THR GLY GLU          
SEQRES   4 B  493  GLN VAL CYS GLU VAL GLN GLU ALA ASP LYS ALA ASP ILE          
SEQRES   5 B  493  ASP LYS ALA VAL GLN ALA ALA ARG LEU ALA PHE SER LEU          
SEQRES   6 B  493  GLY SER VAL TRP ARG ARG MET ASP ALA SER GLU ARG GLY          
SEQRES   7 B  493  ARG LEU LEU ASP LYS LEU ALA ASP LEU VAL GLU ARG ASP          
SEQRES   8 B  493  ARG ALA VAL LEU ALA THR MET GLU SER LEU ASN GLY GLY          
SEQRES   9 B  493  LYS PRO PHE LEU GLN ALA PHE TYR VAL ASP LEU GLN GLY          
SEQRES  10 B  493  VAL ILE LYS THR PHE ARG TYR TYR ALA GLY TRP ALA ASP          
SEQRES  11 B  493  LYS ILE HIS GLY MET THR ILE PRO VAL ASP GLY ASP TYR          
SEQRES  12 B  493  PHE THR PHE THR ARG HIS GLU PRO ILE GLY VAL CYS GLY          
SEQRES  13 B  493  GLN ILE ILE PRO TRP ASN PHE PRO LEU LEU MET PHE ALA          
SEQRES  14 B  493  TRP LYS ILE ALA PRO ALA LEU CYS CYS GLY ASN THR VAL          
SEQRES  15 B  493  VAL ILE LYS PRO ALA GLU GLN THR PRO LEU SER ALA LEU          
SEQRES  16 B  493  TYR MET GLY ALA LEU ILE LYS GLU ALA GLY PHE PRO PRO          
SEQRES  17 B  493  GLY VAL ILE ASN ILE LEU PRO GLY TYR GLY PRO THR ALA          
SEQRES  18 B  493  GLY ALA ALA ILE ALA SER HIS ILE GLY ILE ASP LYS ILE          
SEQRES  19 B  493  ALA PHE THR GLY SER THR GLU VAL GLY LYS LEU ILE GLN          
SEQRES  20 B  493  GLU ALA ALA GLY ARG SER ASN LEU LYS ARG VAL THR LEU          
SEQRES  21 B  493  GLU LEU GLY GLY LYS SER PRO ASN ILE ILE PHE ALA ASP          
SEQRES  22 B  493  ALA ASP LEU ASP TYR ALA VAL GLU GLN ALA HIS GLN GLY          
SEQRES  23 B  493  VAL PHE PHE ASN GLN GLY GLN CYS CYS THR ALA GLY SER          
SEQRES  24 B  493  ARG ILE PHE VAL GLU GLU SER ILE TYR GLU GLU PHE VAL          
SEQRES  25 B  493  ARG ARG SER VAL GLU ARG ALA LYS ARG ARG VAL VAL GLY          
SEQRES  26 B  493  SER PRO PHE ASP PRO THR THR GLU GLN GLY PRO GLN ILE          
SEQRES  27 B  493  ASP LYS LYS GLN TYR ASN LYS ILE LEU GLU LEU ILE GLN          
SEQRES  28 B  493  SER GLY VAL ALA GLU GLY ALA LYS LEU GLU CYS GLY GLY          
SEQRES  29 B  493  LYS GLY LEU GLY ARG LYS GLY PHE PHE ILE GLU PRO THR          
SEQRES  30 B  493  VAL PHE SER ASN VAL THR ASP ASP MET ARG ILE ALA LYS          
SEQRES  31 B  493  GLU GLU ILE PHE GLY PRO VAL GLN GLU ILE LEU ARG PHE          
SEQRES  32 B  493  LYS THR MET ASP GLU VAL ILE GLU ARG ALA ASN ASN SER          
SEQRES  33 B  493  ASP PHE GLY LEU VAL ALA ALA VAL PHE THR ASN ASP ILE          
SEQRES  34 B  493  ASN LYS ALA LEU THR VAL SER SER ALA MET GLN ALA GLY          
SEQRES  35 B  493  THR VAL TRP ILE ASN CYS TYR ASN ALA LEU ASN ALA GLN          
SEQRES  36 B  493  SER PRO PHE GLY GLY PHE LYS MET SER GLY ASN GLY ARG          
SEQRES  37 B  493  GLU MET GLY GLU PHE GLY LEU ARG GLU TYR SER GLU VAL          
SEQRES  38 B  493  LYS THR VAL THR VAL LYS ILE PRO GLN LYS ASN SER              
SEQRES   1 C  493  LEU PRO SER PRO THR PRO ASN LEU GLU ILE LYS TYR THR          
SEQRES   2 C  493  LYS ILE PHE ILE ASN ASN GLU TRP GLN ASN SER GLU SER          
SEQRES   3 C  493  GLY ARG VAL PHE PRO VAL TYR ASN PRO ALA THR GLY GLU          
SEQRES   4 C  493  GLN VAL CYS GLU VAL GLN GLU ALA ASP LYS ALA ASP ILE          
SEQRES   5 C  493  ASP LYS ALA VAL GLN ALA ALA ARG LEU ALA PHE SER LEU          
SEQRES   6 C  493  GLY SER VAL TRP ARG ARG MET ASP ALA SER GLU ARG GLY          
SEQRES   7 C  493  ARG LEU LEU ASP LYS LEU ALA ASP LEU VAL GLU ARG ASP          
SEQRES   8 C  493  ARG ALA VAL LEU ALA THR MET GLU SER LEU ASN GLY GLY          
SEQRES   9 C  493  LYS PRO PHE LEU GLN ALA PHE TYR VAL ASP LEU GLN GLY          
SEQRES  10 C  493  VAL ILE LYS THR PHE ARG TYR TYR ALA GLY TRP ALA ASP          
SEQRES  11 C  493  LYS ILE HIS GLY MET THR ILE PRO VAL ASP GLY ASP TYR          
SEQRES  12 C  493  PHE THR PHE THR ARG HIS GLU PRO ILE GLY VAL CYS GLY          
SEQRES  13 C  493  GLN ILE ILE PRO TRP ASN PHE PRO LEU LEU MET PHE ALA          
SEQRES  14 C  493  TRP LYS ILE ALA PRO ALA LEU CYS CYS GLY ASN THR VAL          
SEQRES  15 C  493  VAL ILE LYS PRO ALA GLU GLN THR PRO LEU SER ALA LEU          
SEQRES  16 C  493  TYR MET GLY ALA LEU ILE LYS GLU ALA GLY PHE PRO PRO          
SEQRES  17 C  493  GLY VAL ILE ASN ILE LEU PRO GLY TYR GLY PRO THR ALA          
SEQRES  18 C  493  GLY ALA ALA ILE ALA SER HIS ILE GLY ILE ASP LYS ILE          
SEQRES  19 C  493  ALA PHE THR GLY SER THR GLU VAL GLY LYS LEU ILE GLN          
SEQRES  20 C  493  GLU ALA ALA GLY ARG SER ASN LEU LYS ARG VAL THR LEU          
SEQRES  21 C  493  GLU LEU GLY GLY LYS SER PRO ASN ILE ILE PHE ALA ASP          
SEQRES  22 C  493  ALA ASP LEU ASP TYR ALA VAL GLU GLN ALA HIS GLN GLY          
SEQRES  23 C  493  VAL PHE PHE ASN GLN GLY GLN CYS CYS THR ALA GLY SER          
SEQRES  24 C  493  ARG ILE PHE VAL GLU GLU SER ILE TYR GLU GLU PHE VAL          
SEQRES  25 C  493  ARG ARG SER VAL GLU ARG ALA LYS ARG ARG VAL VAL GLY          
SEQRES  26 C  493  SER PRO PHE ASP PRO THR THR GLU GLN GLY PRO GLN ILE          
SEQRES  27 C  493  ASP LYS LYS GLN TYR ASN LYS ILE LEU GLU LEU ILE GLN          
SEQRES  28 C  493  SER GLY VAL ALA GLU GLY ALA LYS LEU GLU CYS GLY GLY          
SEQRES  29 C  493  LYS GLY LEU GLY ARG LYS GLY PHE PHE ILE GLU PRO THR          
SEQRES  30 C  493  VAL PHE SER ASN VAL THR ASP ASP MET ARG ILE ALA LYS          
SEQRES  31 C  493  GLU GLU ILE PHE GLY PRO VAL GLN GLU ILE LEU ARG PHE          
SEQRES  32 C  493  LYS THR MET ASP GLU VAL ILE GLU ARG ALA ASN ASN SER          
SEQRES  33 C  493  ASP PHE GLY LEU VAL ALA ALA VAL PHE THR ASN ASP ILE          
SEQRES  34 C  493  ASN LYS ALA LEU THR VAL SER SER ALA MET GLN ALA GLY          
SEQRES  35 C  493  THR VAL TRP ILE ASN CYS TYR ASN ALA LEU ASN ALA GLN          
SEQRES  36 C  493  SER PRO PHE GLY GLY PHE LYS MET SER GLY ASN GLY ARG          
SEQRES  37 C  493  GLU MET GLY GLU PHE GLY LEU ARG GLU TYR SER GLU VAL          
SEQRES  38 C  493  LYS THR VAL THR VAL LYS ILE PRO GLN LYS ASN SER              
SEQRES   1 D  493  LEU PRO SER PRO THR PRO ASN LEU GLU ILE LYS TYR THR          
SEQRES   2 D  493  LYS ILE PHE ILE ASN ASN GLU TRP GLN ASN SER GLU SER          
SEQRES   3 D  493  GLY ARG VAL PHE PRO VAL TYR ASN PRO ALA THR GLY GLU          
SEQRES   4 D  493  GLN VAL CYS GLU VAL GLN GLU ALA ASP LYS ALA ASP ILE          
SEQRES   5 D  493  ASP LYS ALA VAL GLN ALA ALA ARG LEU ALA PHE SER LEU          
SEQRES   6 D  493  GLY SER VAL TRP ARG ARG MET ASP ALA SER GLU ARG GLY          
SEQRES   7 D  493  ARG LEU LEU ASP LYS LEU ALA ASP LEU VAL GLU ARG ASP          
SEQRES   8 D  493  ARG ALA VAL LEU ALA THR MET GLU SER LEU ASN GLY GLY          
SEQRES   9 D  493  LYS PRO PHE LEU GLN ALA PHE TYR VAL ASP LEU GLN GLY          
SEQRES  10 D  493  VAL ILE LYS THR PHE ARG TYR TYR ALA GLY TRP ALA ASP          
SEQRES  11 D  493  LYS ILE HIS GLY MET THR ILE PRO VAL ASP GLY ASP TYR          
SEQRES  12 D  493  PHE THR PHE THR ARG HIS GLU PRO ILE GLY VAL CYS GLY          
SEQRES  13 D  493  GLN ILE ILE PRO TRP ASN PHE PRO LEU LEU MET PHE ALA          
SEQRES  14 D  493  TRP LYS ILE ALA PRO ALA LEU CYS CYS GLY ASN THR VAL          
SEQRES  15 D  493  VAL ILE LYS PRO ALA GLU GLN THR PRO LEU SER ALA LEU          
SEQRES  16 D  493  TYR MET GLY ALA LEU ILE LYS GLU ALA GLY PHE PRO PRO          
SEQRES  17 D  493  GLY VAL ILE ASN ILE LEU PRO GLY TYR GLY PRO THR ALA          
SEQRES  18 D  493  GLY ALA ALA ILE ALA SER HIS ILE GLY ILE ASP LYS ILE          
SEQRES  19 D  493  ALA PHE THR GLY SER THR GLU VAL GLY LYS LEU ILE GLN          
SEQRES  20 D  493  GLU ALA ALA GLY ARG SER ASN LEU LYS ARG VAL THR LEU          
SEQRES  21 D  493  GLU LEU GLY GLY LYS SER PRO ASN ILE ILE PHE ALA ASP          
SEQRES  22 D  493  ALA ASP LEU ASP TYR ALA VAL GLU GLN ALA HIS GLN GLY          
SEQRES  23 D  493  VAL PHE PHE ASN GLN GLY GLN CYS CYS THR ALA GLY SER          
SEQRES  24 D  493  ARG ILE PHE VAL GLU GLU SER ILE TYR GLU GLU PHE VAL          
SEQRES  25 D  493  ARG ARG SER VAL GLU ARG ALA LYS ARG ARG VAL VAL GLY          
SEQRES  26 D  493  SER PRO PHE ASP PRO THR THR GLU GLN GLY PRO GLN ILE          
SEQRES  27 D  493  ASP LYS LYS GLN TYR ASN LYS ILE LEU GLU LEU ILE GLN          
SEQRES  28 D  493  SER GLY VAL ALA GLU GLY ALA LYS LEU GLU CYS GLY GLY          
SEQRES  29 D  493  LYS GLY LEU GLY ARG LYS GLY PHE PHE ILE GLU PRO THR          
SEQRES  30 D  493  VAL PHE SER ASN VAL THR ASP ASP MET ARG ILE ALA LYS          
SEQRES  31 D  493  GLU GLU ILE PHE GLY PRO VAL GLN GLU ILE LEU ARG PHE          
SEQRES  32 D  493  LYS THR MET ASP GLU VAL ILE GLU ARG ALA ASN ASN SER          
SEQRES  33 D  493  ASP PHE GLY LEU VAL ALA ALA VAL PHE THR ASN ASP ILE          
SEQRES  34 D  493  ASN LYS ALA LEU THR VAL SER SER ALA MET GLN ALA GLY          
SEQRES  35 D  493  THR VAL TRP ILE ASN CYS TYR ASN ALA LEU ASN ALA GLN          
SEQRES  36 D  493  SER PRO PHE GLY GLY PHE LYS MET SER GLY ASN GLY ARG          
SEQRES  37 D  493  GLU MET GLY GLU PHE GLY LEU ARG GLU TYR SER GLU VAL          
SEQRES  38 D  493  LYS THR VAL THR VAL LYS ILE PRO GLN LYS ASN SER              
HET    NAD  A 601      44                                                       
HET    CW2  A 602      19                                                       
HET    NAD  B 601      44                                                       
HET    CW2  B 602      19                                                       
HET    NAD  C 601      44                                                       
HET    CW2  C 602      19                                                       
HET    CW2  D 601      19                                                       
HET    NAD  D 602      44                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     CW2 N,N'-(OCTANE-1,8-DIYL)BIS(2,2-DICHLOROACETAMIDE)                 
FORMUL   5  NAD    4(C21 H27 N7 O14 P2)                                         
FORMUL   6  CW2    4(C12 H20 CL4 N2 O2)                                         
FORMUL  13  HOH   *2076(H2 O)                                                   
HELIX    1 AA1 ASP A   73  PHE A   88  1                                  16    
HELIX    2 AA2 SER A   92  MET A   97  1                                   6    
HELIX    3 AA3 ASP A   98  ASP A  116  1                                  19    
HELIX    4 AA4 ASP A  116  GLY A  129  1                                  14    
HELIX    5 AA5 PRO A  131  VAL A  138  1                                   8    
HELIX    6 AA6 VAL A  138  GLY A  152  1                                  15    
HELIX    7 AA7 TRP A  153  ILE A  157  5                                   5    
HELIX    8 AA8 PHE A  188  CYS A  203  1                                  16    
HELIX    9 AA9 PRO A  216  GLY A  230  1                                  15    
HELIX   10 AB1 THR A  245  SER A  252  1                                   8    
HELIX   11 AB2 SER A  264  SER A  278  1                                  15    
HELIX   12 AB3 ASP A  300  PHE A  314  1                                  15    
HELIX   13 AB4 ASN A  315  GLN A  318  5                                   4    
HELIX   14 AB5 GLU A  330  ARG A  347  1                                  18    
HELIX   15 AB6 ASP A  364  GLU A  381  1                                  18    
HELIX   16 AB7 MET A  411  GLU A  416  1                                   6    
HELIX   17 AB8 THR A  430  ASN A  440  1                                  11    
HELIX   18 AB9 ASP A  453  MET A  464  1                                  12    
HELIX   19 AC1 GLU A  497  GLU A  502  5                                   6    
HELIX   20 AC2 ASP B   73  PHE B   88  1                                  16    
HELIX   21 AC3 SER B   92  MET B   97  1                                   6    
HELIX   22 AC4 ASP B   98  ASP B  116  1                                  19    
HELIX   23 AC5 ASP B  116  GLY B  129  1                                  14    
HELIX   24 AC6 PRO B  131  VAL B  138  1                                   8    
HELIX   25 AC7 VAL B  138  ALA B  154  1                                  17    
HELIX   26 AC8 ASP B  155  ILE B  157  5                                   3    
HELIX   27 AC9 PHE B  188  CYS B  203  1                                  16    
HELIX   28 AD1 PRO B  216  GLY B  230  1                                  15    
HELIX   29 AD2 THR B  245  SER B  252  1                                   8    
HELIX   30 AD3 SER B  264  SER B  278  1                                  15    
HELIX   31 AD4 ASP B  300  PHE B  314  1                                  15    
HELIX   32 AD5 ASN B  315  GLN B  318  5                                   4    
HELIX   33 AD6 GLU B  330  ARG B  347  1                                  18    
HELIX   34 AD7 ASP B  364  GLU B  381  1                                  18    
HELIX   35 AD8 MET B  411  GLU B  416  1                                   6    
HELIX   36 AD9 THR B  430  ASN B  440  1                                  11    
HELIX   37 AE1 ASP B  453  MET B  464  1                                  12    
HELIX   38 AE2 PHE B  486  MET B  488  5                                   3    
HELIX   39 AE3 GLU B  497  GLU B  502  5                                   6    
HELIX   40 AE4 ASP C   73  PHE C   88  1                                  16    
HELIX   41 AE5 SER C   92  MET C   97  1                                   6    
HELIX   42 AE6 ASP C   98  ASP C  116  1                                  19    
HELIX   43 AE7 ASP C  116  GLY C  129  1                                  14    
HELIX   44 AE8 PRO C  131  VAL C  138  1                                   8    
HELIX   45 AE9 VAL C  138  ALA C  154  1                                  17    
HELIX   46 AF1 ASP C  155  ILE C  157  5                                   3    
HELIX   47 AF2 PHE C  188  CYS C  203  1                                  16    
HELIX   48 AF3 PRO C  216  GLY C  230  1                                  15    
HELIX   49 AF4 THR C  245  SER C  252  1                                   8    
HELIX   50 AF5 SER C  264  SER C  278  1                                  15    
HELIX   51 AF6 ASP C  300  PHE C  314  1                                  15    
HELIX   52 AF7 ASN C  315  GLN C  318  5                                   4    
HELIX   53 AF8 GLU C  330  ARG C  347  1                                  18    
HELIX   54 AF9 ASP C  364  GLU C  381  1                                  18    
HELIX   55 AG1 MET C  411  GLU C  416  1                                   6    
HELIX   56 AG2 THR C  430  ASN C  440  1                                  11    
HELIX   57 AG3 ASP C  453  MET C  464  1                                  12    
HELIX   58 AG4 PHE C  486  MET C  488  5                                   3    
HELIX   59 AG5 GLU C  497  GLU C  502  5                                   6    
HELIX   60 AG6 ASP D   73  PHE D   88  1                                  16    
HELIX   61 AG7 SER D   92  MET D   97  1                                   6    
HELIX   62 AG8 ASP D   98  ASP D  116  1                                  19    
HELIX   63 AG9 ASP D  116  GLY D  129  1                                  14    
HELIX   64 AH1 PRO D  131  VAL D  138  1                                   8    
HELIX   65 AH2 VAL D  138  GLY D  152  1                                  15    
HELIX   66 AH3 TRP D  153  ILE D  157  5                                   5    
HELIX   67 AH4 PHE D  188  CYS D  203  1                                  16    
HELIX   68 AH5 PRO D  216  GLY D  230  1                                  15    
HELIX   69 AH6 THR D  245  SER D  252  1                                   8    
HELIX   70 AH7 SER D  264  SER D  278  1                                  15    
HELIX   71 AH8 ASP D  300  PHE D  314  1                                  15    
HELIX   72 AH9 ASN D  315  GLN D  318  5                                   4    
HELIX   73 AI1 GLU D  330  ARG D  347  1                                  18    
HELIX   74 AI2 ASP D  364  GLU D  381  1                                  18    
HELIX   75 AI3 MET D  411  LYS D  415  5                                   5    
HELIX   76 AI4 THR D  430  ASN D  440  1                                  11    
HELIX   77 AI5 ASP D  453  MET D  464  1                                  12    
HELIX   78 AI6 PHE D  486  MET D  488  5                                   3    
HELIX   79 AI7 GLU D  497  GLU D  502  5                                   6    
SHEET    1 AA1 2 ILE A  40  ILE A  42  0                                        
SHEET    2 AA1 2 GLU A  45  GLN A  47 -1  O  GLN A  47   N  ILE A  40           
SHEET    1 AA2 2 VAL A  54  TYR A  58  0                                        
SHEET    2 AA2 2 GLN A  65  GLN A  70 -1  O  VAL A  66   N  VAL A  57           
SHEET    1 AA320 LYS C 384  CYS C 387  0                                        
SHEET    2 AA320 THR C 402  SER C 405 -1  O  VAL C 403   N  GLU C 386           
SHEET    3 AA320 VAL C 422  PHE C 428  1  O  GLN C 423   N  PHE C 404           
SHEET    4 AA320 ARG C 325  GLU C 329  1  N  ILE C 326   O  LEU C 426           
SHEET    5 AA320 PRO C 292  ILE C 295  1  N  ILE C 295   O  PHE C 327           
SHEET    6 AA320 VAL C 446  PHE C 450  1  O  PHE C 450   N  ILE C 294           
SHEET    7 AA320 THR C 468  ILE C 471  1  O  TRP C 470   N  ALA C 447           
SHEET    8 AA320 SER A 504  LYS A 512  1  N  THR A 508   O  VAL C 469           
SHEET    9 AA320 TYR A 168  PRO A 176 -1  N  PHE A 171   O  VAL A 509           
SHEET   10 AA320 GLY A 159  ILE A 162 -1  N  ILE A 162   O  THR A 170           
SHEET   11 AA320 GLY B 159  ILE B 162 -1  O  THR B 161   N  GLY A 159           
SHEET   12 AA320 TYR B 168  PRO B 176 -1  O  THR B 170   N  ILE B 162           
SHEET   13 AA320 SER B 504  LYS B 512 -1  O  VAL B 509   N  PHE B 171           
SHEET   14 AA320 THR D 468  ILE D 471  1  O  VAL D 469   N  THR B 508           
SHEET   15 AA320 VAL D 446  PHE D 450  1  N  ALA D 447   O  TRP D 470           
SHEET   16 AA320 PRO D 292  ILE D 295  1  N  ILE D 294   O  ALA D 448           
SHEET   17 AA320 ARG D 325  GLU D 329  1  O  PHE D 327   N  ILE D 295           
SHEET   18 AA320 VAL D 422  PHE D 428  1  O  LEU D 426   N  ILE D 326           
SHEET   19 AA320 THR D 402  SER D 405  1  N  PHE D 404   O  GLN D 423           
SHEET   20 AA320 LYS D 384  CYS D 387 -1  N  GLU D 386   O  VAL D 403           
SHEET    1 AA4 6 ILE A 236  ILE A 238  0                                        
SHEET    2 AA4 6 THR A 206  LYS A 210  1  N  ILE A 209   O  ASN A 237           
SHEET    3 AA4 6 VAL A 179  ILE A 183  1  N  GLN A 182   O  LYS A 210           
SHEET    4 AA4 6 LYS A 258  THR A 262  1  O  LYS A 258   N  GLY A 181           
SHEET    5 AA4 6 ARG A 282  GLU A 286  1  O  ARG A 282   N  ILE A 259           
SHEET    6 AA4 6 GLY A 490  ASN A 491 -1  O  ASN A 491   N  LEU A 285           
SHEET    1 AA520 LYS A 384  CYS A 387  0                                        
SHEET    2 AA520 THR A 402  SER A 405 -1  O  VAL A 403   N  GLU A 386           
SHEET    3 AA520 VAL A 422  PHE A 428  1  O  GLN A 423   N  THR A 402           
SHEET    4 AA520 ARG A 325  GLU A 329  1  N  ILE A 326   O  LEU A 426           
SHEET    5 AA520 PRO A 292  ILE A 295  1  N  ILE A 295   O  PHE A 327           
SHEET    6 AA520 VAL A 446  PHE A 450  1  O  ALA A 448   N  ILE A 294           
SHEET    7 AA520 THR A 468  ILE A 471  1  O  TRP A 470   N  ALA A 447           
SHEET    8 AA520 SER C 504  LYS C 512  1  O  THR C 508   N  VAL A 469           
SHEET    9 AA520 TYR C 168  PRO C 176 -1  N  PHE C 169   O  VAL C 511           
SHEET   10 AA520 GLY C 159  ILE C 162 -1  N  ILE C 162   O  THR C 170           
SHEET   11 AA520 GLY D 159  ILE D 162 -1  O  THR D 161   N  GLY C 159           
SHEET   12 AA520 TYR D 168  PRO D 176 -1  O  THR D 170   N  ILE D 162           
SHEET   13 AA520 SER D 504  LYS D 512 -1  O  VAL D 509   N  PHE D 171           
SHEET   14 AA520 THR B 468  ILE B 471  1  N  VAL B 469   O  THR D 508           
SHEET   15 AA520 VAL B 446  PHE B 450  1  N  ALA B 447   O  TRP B 470           
SHEET   16 AA520 PRO B 292  ILE B 295  1  N  ILE B 294   O  ALA B 448           
SHEET   17 AA520 ARG B 325  GLU B 329  1  O  PHE B 327   N  ILE B 295           
SHEET   18 AA520 VAL B 422  PHE B 428  1  O  LEU B 426   N  ILE B 326           
SHEET   19 AA520 THR B 402  SER B 405  1  N  PHE B 404   O  GLN B 423           
SHEET   20 AA520 LYS B 384  CYS B 387 -1  N  GLU B 386   O  VAL B 403           
SHEET    1 AA6 2 PHE A 443  GLY A 444  0                                        
SHEET    2 AA6 2 PHE A 486  LYS A 487 -1  O  PHE A 486   N  GLY A 444           
SHEET    1 AA7 2 ILE B  40  ILE B  42  0                                        
SHEET    2 AA7 2 GLU B  45  GLN B  47 -1  O  GLN B  47   N  ILE B  40           
SHEET    1 AA8 2 VAL B  54  TYR B  58  0                                        
SHEET    2 AA8 2 GLN B  65  GLN B  70 -1  O  VAL B  66   N  VAL B  57           
SHEET    1 AA9 6 ILE B 236  ILE B 238  0                                        
SHEET    2 AA9 6 THR B 206  LYS B 210  1  N  ILE B 209   O  ASN B 237           
SHEET    3 AA9 6 VAL B 179  ILE B 183  1  N  CYS B 180   O  THR B 206           
SHEET    4 AA9 6 LYS B 258  THR B 262  1  O  LYS B 258   N  GLY B 181           
SHEET    5 AA9 6 ARG B 282  GLU B 286  1  O  ARG B 282   N  ILE B 259           
SHEET    6 AA9 6 GLY B 490  ASN B 491 -1  O  ASN B 491   N  LEU B 285           
SHEET    1 AB1 2 ILE C  40  ILE C  42  0                                        
SHEET    2 AB1 2 GLU C  45  GLN C  47 -1  O  GLN C  47   N  ILE C  40           
SHEET    1 AB2 2 VAL C  54  TYR C  58  0                                        
SHEET    2 AB2 2 GLN C  65  GLN C  70 -1  O  VAL C  66   N  VAL C  57           
SHEET    1 AB3 6 ILE C 236  ILE C 238  0                                        
SHEET    2 AB3 6 THR C 206  LYS C 210  1  N  ILE C 209   O  ASN C 237           
SHEET    3 AB3 6 VAL C 179  ILE C 183  1  N  CYS C 180   O  THR C 206           
SHEET    4 AB3 6 LYS C 258  THR C 262  1  O  LYS C 258   N  GLY C 181           
SHEET    5 AB3 6 ARG C 282  GLU C 286  1  O  ARG C 282   N  ILE C 259           
SHEET    6 AB3 6 GLY C 490  ASN C 491 -1  O  ASN C 491   N  LEU C 285           
SHEET    1 AB4 2 ILE D  40  ILE D  42  0                                        
SHEET    2 AB4 2 GLU D  45  GLN D  47 -1  O  GLN D  47   N  ILE D  40           
SHEET    1 AB5 2 VAL D  54  TYR D  58  0                                        
SHEET    2 AB5 2 GLN D  65  GLN D  70 -1  O  VAL D  66   N  VAL D  57           
SHEET    1 AB6 6 ILE D 236  ILE D 238  0                                        
SHEET    2 AB6 6 THR D 206  LYS D 210  1  N  ILE D 209   O  ASN D 237           
SHEET    3 AB6 6 VAL D 179  ILE D 183  1  N  GLN D 182   O  LYS D 210           
SHEET    4 AB6 6 LYS D 258  THR D 262  1  O  LYS D 258   N  GLY D 181           
SHEET    5 AB6 6 ARG D 282  GLU D 286  1  O  ARG D 282   N  ILE D 259           
SHEET    6 AB6 6 GLY D 490  ASN D 491 -1  O  ASN D 491   N  LEU D 285           
LINK         SG  CYS A 320                 C05 CW2 A 602     1555   1555  1.78  
LINK         SG  CYS B 320                 C05 CW2 B 602     1555   1555  1.76  
LINK         SG  CYS C 320                 C05 CW2 C 602     1555   1555  1.77  
LINK         SG  CYS D 320                 C05 CW2 D 601     1555   1555  1.77  
SITE     1 AC1 26 ILE A 183  ILE A 184  PRO A 185  TRP A 186                    
SITE     2 AC1 26 ASN A 187  LYS A 210  ALA A 212  GLU A 213                    
SITE     3 AC1 26 GLY A 243  GLY A 247  ALA A 248  PHE A 261                    
SITE     4 AC1 26 GLY A 263  SER A 264  VAL A 267  GLU A 286                    
SITE     5 AC1 26 LEU A 287  LYS A 366  GLN A 367  LYS A 370                    
SITE     6 AC1 26 GLU A 417  PHE A 419  CW2 A 602  HOH A 729                    
SITE     7 AC1 26 HOH A 745  HOH A 880                                          
SITE     1 AC2 13 THR A 146  ASN A 187  PHE A 188  LEU A 191                    
SITE     2 AC2 13 MET A 192  TRP A 195  GLU A 286  CYS A 319                    
SITE     3 AC2 13 CYS A 320  LEU A 477  ASN A 478  ALA A 479                    
SITE     4 AC2 13 NAD A 601                                                     
SITE     1 AC3 31 ILE C 183  ILE C 184  PRO C 185  TRP C 186                    
SITE     2 AC3 31 ASN C 187  MET C 192  LYS C 210  ALA C 212                    
SITE     3 AC3 31 GLU C 213  GLY C 243  GLY C 247  ALA C 248                    
SITE     4 AC3 31 PHE C 261  GLY C 263  SER C 264  VAL C 267                    
SITE     5 AC3 31 GLU C 286  LEU C 287  CYS C 320  LYS C 366                    
SITE     6 AC3 31 GLN C 367  LYS C 370  GLU C 417  PHE C 419                    
SITE     7 AC3 31 CW2 C 602  HOH C 719  HOH C 772  HOH C 924                    
SITE     8 AC3 31 HOH C1002  HOH C1003  HOH C1043                               
SITE     1 AC4 25 ILE D 183  ILE D 184  PRO D 185  TRP D 186                    
SITE     2 AC4 25 ASN D 187  LYS D 210  ALA D 212  GLU D 213                    
SITE     3 AC4 25 GLY D 243  GLY D 247  ALA D 248  PHE D 261                    
SITE     4 AC4 25 GLY D 263  SER D 264  VAL D 267  GLU D 286                    
SITE     5 AC4 25 LEU D 287  LYS D 366  GLN D 367  LYS D 370                    
SITE     6 AC4 25 GLU D 417  PHE D 419  CW2 D 601  HOH D 736                    
SITE     7 AC4 25 HOH D 841                                                     
SITE     1 AC5 38 ILE B 183  ILE B 184  PRO B 185  TRP B 186                    
SITE     2 AC5 38 ASN B 187  MET B 192  LYS B 210  ALA B 212                    
SITE     3 AC5 38 GLU B 213  GLY B 243  GLY B 247  ALA B 248                    
SITE     4 AC5 38 PHE B 261  GLY B 263  SER B 264  VAL B 267                    
SITE     5 AC5 38 GLU B 286  LEU B 287  LYS B 366  GLN B 367                    
SITE     6 AC5 38 TYR B 368  ASN B 369  ILE B 371  LEU B 372                    
SITE     7 AC5 38 GLU B 373  LEU B 374  GLU B 417  ILE B 418                    
SITE     8 AC5 38 PHE B 419  CW2 B 602  HOH B 742  HOH B 838                    
SITE     9 AC5 38 HOH B 940  HOH B 985  HOH B1000  HOH B1014                    
SITE    10 AC5 38 HOH B1015  HOH B1020                                          
SITE     1 AC6 19 VAL B 138  THR B 146  ASN B 187  PHE B 188                    
SITE     2 AC6 19 LEU B 191  MET B 192  TRP B 195  CYS B 319                    
SITE     3 AC6 19 THR B 321  ALA B 322  PHE B 419  LEU B 445                    
SITE     4 AC6 19 LEU B 477  ASN B 478  ALA B 479  NAD B 601                    
SITE     5 AC6 19 HOH B 741  HOH B 749  HOH B1017                               
SITE     1 AC7 20 GLY C 142  THR C 146  ASN C 187  PHE C 188                    
SITE     2 AC7 20 LEU C 191  MET C 192  TRP C 195  GLU C 286                    
SITE     3 AC7 20 PHE C 314  CYS C 319  THR C 321  ALA C 322                    
SITE     4 AC7 20 PHE C 419  LEU C 445  LEU C 477  ASN C 478                    
SITE     5 AC7 20 ALA C 479  NAD C 601  HOH C 759  HOH C 924                    
SITE     1 AC8 17 GLY D 142  THR D 146  ASN D 187  PHE D 188                    
SITE     2 AC8 17 LEU D 191  MET D 192  TRP D 195  GLU D 286                    
SITE     3 AC8 17 CYS D 319  THR D 321  ALA D 322  PHE D 419                    
SITE     4 AC8 17 LEU D 445  ASN D 478  ALA D 479  NAD D 602                    
SITE     5 AC8 17 HOH D 823                                                     
CRYST1   81.960  139.820   84.900  90.00  94.07  90.00 P 1 21 1      8          
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      0.012201  0.000000  0.000869        0.00000                         
SCALE2      0.000000  0.007152  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011808        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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