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Database: PDB
Entry: 4LCJ
LinkDB: 4LCJ
Original site: 4LCJ 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE SUBSTRATE 21-JUN-13   4LCJ              
TITLE     CTBP2 IN COMPLEX WITH SUBSTRATE MTOB                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-TERMINAL-BINDING PROTEIN 2;                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: UNP RESIDUES 31-362;                                       
COMPND   5 SYNONYM: CTBP2;                                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CTBP2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIL;                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ROSSMANN FOLD, TRANSCRIPTIONAL COREPRESSOR, D-ISOMER 2-HYDROXYACID    
KEYWDS   2 DEHYDROGENASE, OXIDOREDUCTASE-OXIDOREDUCTASE SUBSTRATE COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.HILBERT,C.A.SCHIFFER,W.E.ROYER JR.                                
REVDAT   5   15-NOV-17 4LCJ    1       REMARK                                   
REVDAT   4   12-NOV-14 4LCJ    1       KEYWDS                                   
REVDAT   3   14-MAY-14 4LCJ    1       JRNL                                     
REVDAT   2   09-APR-14 4LCJ    1       JRNL                                     
REVDAT   1   19-MAR-14 4LCJ    0                                                
JRNL        AUTH   B.J.HILBERT,S.R.GROSSMANN,C.A.SCHIFFER,W.E.ROYER             
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN CTBP IN COMPLEX WITH SUBSTRATE   
JRNL        TITL 2 MTOB REVEAL ACTIVE SITE FEATURES USEFUL FOR INHIBITOR        
JRNL        TITL 3 DESIGN.                                                      
JRNL        REF    FEBS LETT.                    V. 588  1743 2014              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   24657618                                                     
JRNL        DOI    10.1016/J.FEBSLET.2014.03.026                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.1_1168                                    
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) : 2.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 73303                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3692                            
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 32.3046 -  8.4143    0.98     2713   146  0.1846 0.2058        
REMARK   3     2  8.4143 -  6.6982    1.00     2726   136  0.1817 0.2061        
REMARK   3     3  6.6982 -  5.8572    1.00     2722   146  0.2171 0.2296        
REMARK   3     4  5.8572 -  5.3243    1.00     2732   138  0.2034 0.2394        
REMARK   3     5  5.3243 -  4.9441    1.00     2688   164  0.1791 0.2219        
REMARK   3     6  4.9441 -  4.6535    1.00     2698   129  0.1761 0.2118        
REMARK   3     7  4.6535 -  4.4211    1.00     2689   157  0.1753 0.2073        
REMARK   3     8  4.4211 -  4.2291    1.00     2680   133  0.1871 0.2358        
REMARK   3     9  4.2291 -  4.0666    1.00     2699   145  0.1950 0.2283        
REMARK   3    10  4.0666 -  3.9265    1.00     2655   163  0.1966 0.2105        
REMARK   3    11  3.9265 -  3.8039    1.00     2689   160  0.2138 0.2538        
REMARK   3    12  3.8039 -  3.6953    1.00     2709   126  0.2153 0.3004        
REMARK   3    13  3.6953 -  3.5982    1.00     2666   146  0.2206 0.2402        
REMARK   3    14  3.5982 -  3.5105    1.00     2708   146  0.2363 0.2853        
REMARK   3    15  3.5105 -  3.4308    1.00     2635   151  0.2321 0.2790        
REMARK   3    16  3.4308 -  3.3579    1.00     2723   143  0.2422 0.3184        
REMARK   3    17  3.3579 -  3.2908    1.00     2671   134  0.2431 0.2894        
REMARK   3    18  3.2908 -  3.2287    0.99     2673   149  0.2679 0.3503        
REMARK   3    19  3.2287 -  3.1711    0.99     2681   117  0.2698 0.2898        
REMARK   3    20  3.1711 -  3.1174    0.99     2681   124  0.2678 0.3814        
REMARK   3    21  3.1174 -  3.0671    0.99     2608   153  0.2648 0.2959        
REMARK   3    22  3.0671 -  3.0200    0.99     2655   152  0.2813 0.2800        
REMARK   3    23  3.0200 -  2.9756    0.99     2651   148  0.2845 0.3290        
REMARK   3    24  2.9756 -  2.9337    0.99     2666   137  0.2819 0.3426        
REMARK   3    25  2.9337 -  2.8941    0.99     2648   128  0.2900 0.3245        
REMARK   3    26  2.8941 -  2.8600    0.93     2545   121  0.3121 0.3319        
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)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.700           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.69                          
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      :  0.009          20200                                  
REMARK   3   ANGLE     :  1.219          27553                                  
REMARK   3   CHIRALITY :  0.057           3243                                  
REMARK   3   PLANARITY :  0.007           3581                                  
REMARK   3   DIHEDRAL  : 17.341           7111                                  
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 4LCJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080458.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99                               
REMARK 200  MONOCHROMATOR                  : BENT GE(111) MONOCHROMATOR         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73374                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.1                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM POTASSIUM NITRATE, 15-20% PEG     
REMARK 280  3350, 100 MM BIS TRIS PROPANE, PH 7.0, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 298K                                              
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       70.30250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     MET A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     MET A    20                                                      
REMARK 465     THR A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     MET A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     PRO A    32                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     HIS B    16                                                      
REMARK 465     MET B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     MET B    20                                                      
REMARK 465     THR B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     GLN B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     MET B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     ARG B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     SER B    30                                                      
REMARK 465     HIS B    31                                                      
REMARK 465     PRO B    32                                                      
REMARK 465     GLY C    14                                                      
REMARK 465     SER C    15                                                      
REMARK 465     HIS C    16                                                      
REMARK 465     MET C    17                                                      
REMARK 465     ALA C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     MET C    20                                                      
REMARK 465     THR C    21                                                      
REMARK 465     GLY C    22                                                      
REMARK 465     GLY C    23                                                      
REMARK 465     GLN C    24                                                      
REMARK 465     GLN C    25                                                      
REMARK 465     MET C    26                                                      
REMARK 465     GLY C    27                                                      
REMARK 465     ARG C    28                                                      
REMARK 465     GLY C    29                                                      
REMARK 465     SER C    30                                                      
REMARK 465     HIS C    31                                                      
REMARK 465     PRO C    32                                                      
REMARK 465     GLY D    14                                                      
REMARK 465     SER D    15                                                      
REMARK 465     HIS D    16                                                      
REMARK 465     MET D    17                                                      
REMARK 465     ALA D    18                                                      
REMARK 465     SER D    19                                                      
REMARK 465     MET D    20                                                      
REMARK 465     THR D    21                                                      
REMARK 465     GLY D    22                                                      
REMARK 465     GLY D    23                                                      
REMARK 465     GLN D    24                                                      
REMARK 465     GLN D    25                                                      
REMARK 465     MET D    26                                                      
REMARK 465     GLY D    27                                                      
REMARK 465     ARG D    28                                                      
REMARK 465     GLY D    29                                                      
REMARK 465     SER D    30                                                      
REMARK 465     HIS D    31                                                      
REMARK 465     PRO D    32                                                      
REMARK 465     PHE D   362                                                      
REMARK 465     GLY E    14                                                      
REMARK 465     SER E    15                                                      
REMARK 465     HIS E    16                                                      
REMARK 465     MET E    17                                                      
REMARK 465     ALA E    18                                                      
REMARK 465     SER E    19                                                      
REMARK 465     MET E    20                                                      
REMARK 465     THR E    21                                                      
REMARK 465     GLY E    22                                                      
REMARK 465     GLY E    23                                                      
REMARK 465     GLN E    24                                                      
REMARK 465     GLN E    25                                                      
REMARK 465     MET E    26                                                      
REMARK 465     GLY E    27                                                      
REMARK 465     ARG E    28                                                      
REMARK 465     GLY E    29                                                      
REMARK 465     SER E    30                                                      
REMARK 465     HIS E    31                                                      
REMARK 465     PRO E    32                                                      
REMARK 465     ARG E    33                                                      
REMARK 465     PHE E   361                                                      
REMARK 465     PHE E   362                                                      
REMARK 465     GLY F    14                                                      
REMARK 465     SER F    15                                                      
REMARK 465     HIS F    16                                                      
REMARK 465     MET F    17                                                      
REMARK 465     ALA F    18                                                      
REMARK 465     SER F    19                                                      
REMARK 465     MET F    20                                                      
REMARK 465     THR F    21                                                      
REMARK 465     GLY F    22                                                      
REMARK 465     GLY F    23                                                      
REMARK 465     GLN F    24                                                      
REMARK 465     GLN F    25                                                      
REMARK 465     MET F    26                                                      
REMARK 465     GLY F    27                                                      
REMARK 465     ARG F    28                                                      
REMARK 465     GLY F    29                                                      
REMARK 465     SER F    30                                                      
REMARK 465     HIS F    31                                                      
REMARK 465     PRO F    32                                                      
REMARK 465     PHE F   362                                                      
REMARK 465     GLY G    14                                                      
REMARK 465     SER G    15                                                      
REMARK 465     HIS G    16                                                      
REMARK 465     MET G    17                                                      
REMARK 465     ALA G    18                                                      
REMARK 465     SER G    19                                                      
REMARK 465     MET G    20                                                      
REMARK 465     THR G    21                                                      
REMARK 465     GLY G    22                                                      
REMARK 465     GLY G    23                                                      
REMARK 465     GLN G    24                                                      
REMARK 465     GLN G    25                                                      
REMARK 465     MET G    26                                                      
REMARK 465     GLY G    27                                                      
REMARK 465     ARG G    28                                                      
REMARK 465     GLY G    29                                                      
REMARK 465     SER G    30                                                      
REMARK 465     HIS G    31                                                      
REMARK 465     PRO G    32                                                      
REMARK 465     ARG G    33                                                      
REMARK 465     PRO G    34                                                      
REMARK 465     ARG G    99                                                      
REMARK 465     PHE G   361                                                      
REMARK 465     PHE G   362                                                      
REMARK 465     GLY H    14                                                      
REMARK 465     SER H    15                                                      
REMARK 465     HIS H    16                                                      
REMARK 465     MET H    17                                                      
REMARK 465     ALA H    18                                                      
REMARK 465     SER H    19                                                      
REMARK 465     MET H    20                                                      
REMARK 465     THR H    21                                                      
REMARK 465     GLY H    22                                                      
REMARK 465     GLY H    23                                                      
REMARK 465     GLN H    24                                                      
REMARK 465     GLN H    25                                                      
REMARK 465     MET H    26                                                      
REMARK 465     GLY H    27                                                      
REMARK 465     ARG H    28                                                      
REMARK 465     GLY H    29                                                      
REMARK 465     SER H    30                                                      
REMARK 465     HIS H    31                                                      
REMARK 465     PRO H    32                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A  48    SD   CE                                             
REMARK 470     LYS A  52    CD   CE   NZ                                        
REMARK 470     GLN A  66    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  71    CG   CD   CE   NZ                                   
REMARK 470     GLU A  90    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     LYS A  96    CG   CD   CE   NZ                                   
REMARK 470     LYS A 114    CG   CD   CE   NZ                                   
REMARK 470     ARG A 157    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 161    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 170    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 207    CD1                                                 
REMARK 470     GLN A 214    CD   OE1  NE2                                       
REMARK 470     ILE A 217    CD1                                                 
REMARK 470     GLN A 224    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 230    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 279    CG   CD   CE   NZ                                   
REMARK 470     ARG A 289    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A 307    CD   OE1  NE2                                       
REMARK 470     LYS A 311    CD   CE   NZ                                        
REMARK 470     GLU A 327    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 349    CD1                                                 
REMARK 470     ARG B  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  52    CD   CE   NZ                                        
REMARK 470     GLN B  63    CG   CD   OE1  NE2                                  
REMARK 470     SER B  64    OG                                                  
REMARK 470     GLU B  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  71    CG   CD   CE   NZ                                   
REMARK 470     GLU B  75    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  90    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  93    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  94    CE   NZ                                             
REMARK 470     LYS B  96    CG   CD   CE   NZ                                   
REMARK 470     ARG B  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 114    CG   CD   CE   NZ                                   
REMARK 470     GLN B 214    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 234    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     LYS B 259    CG   CD   CE   NZ                                   
REMARK 470     LYS B 279    CD   CE   NZ                                        
REMARK 470     ARG B 289    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 307    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 311    NZ                                                  
REMARK 470     ASP B 312    CG   OD1  OD2                                       
REMARK 470     GLU B 327    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 348    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 349    CD1                                                 
REMARK 470     LYS B 359    CD   CE   NZ                                        
REMARK 470     GLU C  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  71    CG   CD   CE   NZ                                   
REMARK 470     LYS C  94    NZ                                                  
REMARK 470     LYS C  96    CG   CD   CE   NZ                                   
REMARK 470     ARG C 161    CD   NE   CZ   NH1  NH2                             
REMARK 470     SER C 164    OG                                                  
REMARK 470     GLU C 170    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 224    CD   OE1  NE2                                       
REMARK 470     TYR C 234    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     LYS C 259    CE   NZ                                             
REMARK 470     LYS C 279    CG   CD   CE   NZ                                   
REMARK 470     LYS C 286    CD   CE   NZ                                        
REMARK 470     ARG C 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 307    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 311    CG   CD   CE   NZ                                   
REMARK 470     ASP C 312    CG   OD1  OD2                                       
REMARK 470     GLU C 327    CD   OE1  OE2                                       
REMARK 470     ARG C 348    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE C 349    CD1                                                 
REMARK 470     ARG C 354    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     CYS D  44    SG                                                  
REMARK 470     MET D  48    CG   SD   CE                                        
REMARK 470     LYS D  52    CD   CE   NZ                                        
REMARK 470     LEU D  54    CG   CD1  CD2                                       
REMARK 470     THR D  56    OG1  CG2                                            
REMARK 470     GLN D  63    CG   CD   OE1  NE2                                  
REMARK 470     GLN D  66    CG   CD   OE1  NE2                                  
REMARK 470     HIS D  69    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU D  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  71    CG   CD   CE   NZ                                   
REMARK 470     VAL D  72    CG1  CG2                                            
REMARK 470     ASN D  74    OD1  ND2                                            
REMARK 470     GLU D  75    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  90    CG   CD   OE1  OE2                                  
REMARK 470     LEU D  92    CG   CD1  CD2                                       
REMARK 470     GLU D  93    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  94    CD   CE   NZ                                        
REMARK 470     PHE D  95    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS D  96    CG   CD   CE   NZ                                   
REMARK 470     ARG D  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 114    CG   CD   CE   NZ                                   
REMARK 470     ARG D 157    NE   CZ   NH1  NH2                                  
REMARK 470     GLU D 170    CG   CD   OE1  OE2                                  
REMARK 470     ILE D 207    CD1                                                 
REMARK 470     GLN D 214    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 224    CD   OE1  NE2                                       
REMARK 470     GLU D 247    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 255    CG   OD1  OD2                                       
REMARK 470     LYS D 279    CG   CD   CE   NZ                                   
REMARK 470     LYS D 286    CG   CD   CE   NZ                                   
REMARK 470     LYS D 311    CG   CD   CE   NZ                                   
REMARK 470     ASP D 312    CG   OD1  OD2                                       
REMARK 470     GLU D 327    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 335    CD   OE1  OE2                                       
REMARK 470     ARG D 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE D 345    CG1  CG2  CD1                                       
REMARK 470     THR D 346    OG1  CG2                                            
REMARK 470     ARG D 348    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE D 349    CD1                                                 
REMARK 470     GLU D 351    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 354    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS D 359    CD   CE   NZ                                        
REMARK 470     PHE D 361    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG E  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E  50    CG1  CG2  CD1                                       
REMARK 470     LYS E  52    CG   CD   CE   NZ                                   
REMARK 470     ASP E  53    CG   OD1  OD2                                       
REMARK 470     LEU E  54    CG   CD1  CD2                                       
REMARK 470     THR E  56    OG1  CG2                                            
REMARK 470     GLN E  63    CG   CD   OE1  NE2                                  
REMARK 470     GLN E  66    CG   CD   OE1  NE2                                  
REMARK 470     ILE E  68    CG1  CG2  CD1                                       
REMARK 470     HIS E  69    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU E  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  71    CG   CD   CE   NZ                                   
REMARK 470     VAL E  72    CG1  CG2                                            
REMARK 470     GLU E  75    CG   CD   OE1  OE2                                  
REMARK 470     ILE E  85    CG1  CG2  CD1                                       
REMARK 470     ARG E  89    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E  90    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  93    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  94    CE   NZ                                             
REMARK 470     PHE E  95    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     LYS E  96    CG   CD   CE   NZ                                   
REMARK 470     ARG E  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 114    CG   CD   CE   NZ                                   
REMARK 470     ARG E 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E 166    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 170    CG   CD   OE1  OE2                                  
REMARK 470     GLN E 214    CG   CD   OE1  NE2                                  
REMARK 470     GLN E 224    CD   OE1  NE2                                       
REMARK 470     GLU E 247    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 259    CG   CD   CE   NZ                                   
REMARK 470     LYS E 279    CG   CD   CE   NZ                                   
REMARK 470     GLN E 283    CG   CD   OE1  NE2                                  
REMARK 470     LEU E 285    CG   CD1  CD2                                       
REMARK 470     LYS E 286    CE   NZ                                             
REMARK 470     GLN E 307    CG   CD   OE1  NE2                                  
REMARK 470     LYS E 311    CG   CD   CE   NZ                                   
REMARK 470     ASP E 312    CG   OD1  OD2                                       
REMARK 470     GLU E 327    CG   CD   OE1  OE2                                  
REMARK 470     ILE E 345    CG1  CG2  CD1                                       
REMARK 470     ARG E 348    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E 349    CG1  CG2  CD1                                       
REMARK 470     GLU E 351    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 359    CD   CE   NZ                                        
REMARK 470     ARG F  42    NE   CZ   NH1  NH2                                  
REMARK 470     LYS F  52    CG   CD   CE   NZ                                   
REMARK 470     LEU F  54    CG   CD1  CD2                                       
REMARK 470     GLN F  63    CG   CD   OE1  NE2                                  
REMARK 470     GLN F  66    CG   CD   OE1  NE2                                  
REMARK 470     GLU F  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  71    CG   CD   CE   NZ                                   
REMARK 470     LYS F  96    CE   NZ                                             
REMARK 470     ARG F  99    NE   CZ   NH1  NH2                                  
REMARK 470     ARG F 157    CZ   NH1  NH2                                       
REMARK 470     ARG F 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN F 163    CG   CD   OE1  NE2                                  
REMARK 470     GLU F 170    CD   OE1  OE2                                       
REMARK 470     LYS F 200    CG   CD   CE   NZ                                   
REMARK 470     ASP F 215    CG   OD1  OD2                                       
REMARK 470     ILE F 217    CG1  CG2  CD1                                       
REMARK 470     GLN F 224    CD   OE1  NE2                                       
REMARK 470     GLU F 247    OE1  OE2                                            
REMARK 470     ASP F 255    CG   OD1  OD2                                       
REMARK 470     LYS F 259    CG   CD   CE   NZ                                   
REMARK 470     LYS F 279    CG   CD   CE   NZ                                   
REMARK 470     GLN F 283    CG   CD   OE1  NE2                                  
REMARK 470     LYS F 286    CG   CD   CE   NZ                                   
REMARK 470     ARG F 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN F 307    CD   OE1  NE2                                       
REMARK 470     LYS F 311    CG   CD   CE   NZ                                   
REMARK 470     ASP F 312    CG   OD1  OD2                                       
REMARK 470     GLU F 327    CG   CD   OE1  OE2                                  
REMARK 470     GLN F 328    CD   OE1  NE2                                       
REMARK 470     ARG F 348    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 359    CD   CE   NZ                                        
REMARK 470     VAL G  36    CG1  CG2                                            
REMARK 470     LEU G  38    CD1  CD2                                            
REMARK 470     LEU G  39    CD1  CD2                                            
REMARK 470     ARG G  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL G  46    CG1  CG2                                            
REMARK 470     ILE G  50    CG1  CG2  CD1                                       
REMARK 470     LYS G  52    CG   CD   CE   NZ                                   
REMARK 470     ASP G  53    CG   OD1  OD2                                       
REMARK 470     LEU G  54    CG   CD1  CD2                                       
REMARK 470     THR G  56    OG1  CG2                                            
REMARK 470     PHE G  59    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     GLN G  63    CG   CD   OE1  NE2                                  
REMARK 470     SER G  64    OG                                                  
REMARK 470     THR G  65    OG1  CG2                                            
REMARK 470     GLN G  66    CG   CD   OE1  NE2                                  
REMARK 470     GLU G  67    CG   CD   OE1  OE2                                  
REMARK 470     HIS G  69    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU G  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS G  71    CG   CD   CE   NZ                                   
REMARK 470     VAL G  72    CG1  CG2                                            
REMARK 470     LEU G  73    CG   CD1  CD2                                       
REMARK 470     ASN G  74    CG   OD1  ND2                                       
REMARK 470     GLU G  75    CG   CD   OE1  OE2                                  
REMARK 470     VAL G  77    CG1  CG2                                            
REMARK 470     THR G  84    OG1  CG2                                            
REMARK 470     ARG G  89    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU G  93    CG   CD   OE1  OE2                                  
REMARK 470     LYS G  94    CG   CD   CE   NZ                                   
REMARK 470     PHE G  95    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS G  96    CG   CD   CE   NZ                                   
REMARK 470     LEU G  98    CG   CD1  CD2                                       
REMARK 470     VAL G 102    CG1  CG2                                            
REMARK 470     VAL G 111    CG1  CG2                                            
REMARK 470     ILE G 113    CG1  CG2  CD1                                       
REMARK 470     LYS G 114    CG   CD   CE   NZ                                   
REMARK 470     LEU G 119    CG   CD1  CD2                                       
REMARK 470     ARG G 157    NE   CZ   NH1  NH2                                  
REMARK 470     GLN G 163    CG   CD   OE1  NE2                                  
REMARK 470     LYS G 200    CG   CD   CE   NZ                                   
REMARK 470     GLN G 214    CG   CD   OE1  NE2                                  
REMARK 470     ILE G 217    CG1  CG2  CD1                                       
REMARK 470     GLN G 224    CD   OE1  NE2                                       
REMARK 470     ASP G 255    CG   OD1  OD2                                       
REMARK 470     PHE G 256    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS G 259    CD   CE   NZ                                        
REMARK 470     LYS G 279    CG   CD   CE   NZ                                   
REMARK 470     GLN G 283    CG   CD   OE1  NE2                                  
REMARK 470     GLU G 287    CG   CD   OE1  OE2                                  
REMARK 470     ARG G 289    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN G 307    CG   CD   OE1  NE2                                  
REMARK 470     LYS G 311    CG   CD   CE   NZ                                   
REMARK 470     GLU G 327    CG   CD   OE1  OE2                                  
REMARK 470     LEU G 331    CG   CD1  CD2                                       
REMARK 470     ARG G 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE G 345    CG1  CG2  CD1                                       
REMARK 470     THR G 346    OG1  CG2                                            
REMARK 470     ARG G 348    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE G 349    CG1  CG2  CD1                                       
REMARK 470     GLU G 351    CG   CD   OE1  OE2                                  
REMARK 470     SER G 352    OG                                                  
REMARK 470     ARG G 354    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G 359    CG   CD   CE   NZ                                   
REMARK 470     LYS H  52    CD   CE   NZ                                        
REMARK 470     GLN H  63    CG   CD   OE1  NE2                                  
REMARK 470     SER H  64    OG                                                  
REMARK 470     GLN H  66    CG   CD   OE1  NE2                                  
REMARK 470     HIS H  69    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU H  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  71    CG   CD   CE   NZ                                   
REMARK 470     ASN H  74    CG   OD1  ND2                                       
REMARK 470     GLU H  90    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  94    NZ                                                  
REMARK 470     LYS H  96    CG   CD   CE   NZ                                   
REMARK 470     LYS H 114    CE   NZ                                             
REMARK 470     ARG H 157    NE   CZ   NH1  NH2                                  
REMARK 470     ARG H 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN H 163    CD   OE1  NE2                                       
REMARK 470     GLU H 166    CD   OE1  OE2                                       
REMARK 470     GLU H 170    CG   CD   OE1  OE2                                  
REMARK 470     ILE H 207    CD1                                                 
REMARK 470     GLN H 214    CG   CD   OE1  NE2                                  
REMARK 470     GLN H 224    CG   CD   OE1  NE2                                  
REMARK 470     GLU H 247    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 279    CG   CD   CE   NZ                                   
REMARK 470     GLN H 283    CG   CD   OE1  NE2                                  
REMARK 470     LYS H 286    CD   CE   NZ                                        
REMARK 470     ARG H 289    NE   CZ   NH1  NH2                                  
REMARK 470     ARG H 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN H 307    CD   OE1  NE2                                       
REMARK 470     ILE H 349    CD1                                                 
REMARK 470     ARG H 354    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS H 359    CD   CE   NZ                                        
REMARK 470     PHE H 362    CG   CD1  CD2  CE1  CE2  CZ                         
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  44       17.24   -143.60                                   
REMARK 500    TYR A  82     -150.24    -94.58                                   
REMARK 500    ARG A 148       30.17     70.74                                   
REMARK 500    HIS A 242       33.10   -143.46                                   
REMARK 500    ALA A 271      -87.24    -98.15                                   
REMARK 500    ASN A 358       58.37   -140.54                                   
REMARK 500    CYS B  44       22.22   -142.42                                   
REMARK 500    TYR B  82     -154.27    -96.58                                   
REMARK 500    HIS B 242       31.94   -145.37                                   
REMARK 500    ALA B 271      -88.09   -100.07                                   
REMARK 500    ASP C  40       50.06   -112.69                                   
REMARK 500    CYS C  44       29.38   -145.89                                   
REMARK 500    TYR C  82     -150.21    -95.34                                   
REMARK 500    ASP C 112       84.96    -69.89                                   
REMARK 500    HIS C 242       31.78   -144.31                                   
REMARK 500    ALA C 271      -87.26    -99.03                                   
REMARK 500    CYS D  44       21.61   -142.75                                   
REMARK 500    TYR D  82     -151.61    -94.93                                   
REMARK 500    HIS D 242       32.70   -145.28                                   
REMARK 500    ALA D 271      -91.15    -98.54                                   
REMARK 500    ASN D 358       58.54   -141.25                                   
REMARK 500    CYS E  44       26.10   -142.91                                   
REMARK 500    TYR E  82     -152.22    -94.70                                   
REMARK 500    HIS E 242       32.47   -145.53                                   
REMARK 500    ALA E 271      -87.00    -98.85                                   
REMARK 500    ASN E 358       58.61   -141.17                                   
REMARK 500    CYS F  44       19.38   -143.84                                   
REMARK 500    TYR F  82     -152.41    -95.01                                   
REMARK 500    HIS F 242       32.88   -145.12                                   
REMARK 500    ALA F 271      -89.35    -98.25                                   
REMARK 500    CYS G  44       22.26   -143.97                                   
REMARK 500    TYR G  82     -149.96    -98.12                                   
REMARK 500    ASP G 112       87.54    -68.79                                   
REMARK 500    HIS G 242       33.58   -145.10                                   
REMARK 500    ALA G 271      -90.18    -99.75                                   
REMARK 500    THR G 346       27.08    -78.30                                   
REMARK 500    CYS H  44       18.39   -143.75                                   
REMARK 500    TYR H  82     -149.64    -94.65                                   
REMARK 500    HIS H 242       31.94   -145.36                                   
REMARK 500    ALA H 271      -88.74    -98.17                                   
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 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KMT A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KMT B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KMT C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KMT D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KMT E 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KMT F 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KMT G 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD H 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KMT H 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LCE   RELATED DB: PDB                                   
DBREF  4LCJ A   31   362  UNP    P56545   CTBP2_HUMAN     31    362             
DBREF  4LCJ B   31   362  UNP    P56545   CTBP2_HUMAN     31    362             
DBREF  4LCJ C   31   362  UNP    P56545   CTBP2_HUMAN     31    362             
DBREF  4LCJ D   31   362  UNP    P56545   CTBP2_HUMAN     31    362             
DBREF  4LCJ E   31   362  UNP    P56545   CTBP2_HUMAN     31    362             
DBREF  4LCJ F   31   362  UNP    P56545   CTBP2_HUMAN     31    362             
DBREF  4LCJ G   31   362  UNP    P56545   CTBP2_HUMAN     31    362             
DBREF  4LCJ H   31   362  UNP    P56545   CTBP2_HUMAN     31    362             
SEQADV 4LCJ GLY A   14  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER A   15  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ HIS A   16  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET A   17  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ALA A   18  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER A   19  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET A   20  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ THR A   21  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY A   22  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY A   23  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN A   24  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN A   25  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET A   26  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY A   27  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ARG A   28  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY A   29  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER A   30  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY B   14  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER B   15  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ HIS B   16  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET B   17  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ALA B   18  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER B   19  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET B   20  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ THR B   21  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY B   22  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY B   23  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN B   24  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN B   25  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET B   26  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY B   27  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ARG B   28  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY B   29  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER B   30  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY C   14  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER C   15  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ HIS C   16  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET C   17  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ALA C   18  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER C   19  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET C   20  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ THR C   21  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY C   22  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY C   23  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN C   24  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN C   25  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET C   26  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY C   27  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ARG C   28  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY C   29  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER C   30  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY D   14  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER D   15  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ HIS D   16  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET D   17  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ALA D   18  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER D   19  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET D   20  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ THR D   21  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY D   22  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY D   23  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN D   24  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN D   25  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET D   26  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY D   27  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ARG D   28  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY D   29  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER D   30  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY E   14  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER E   15  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ HIS E   16  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET E   17  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ALA E   18  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER E   19  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET E   20  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ THR E   21  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY E   22  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY E   23  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN E   24  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN E   25  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET E   26  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY E   27  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ARG E   28  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY E   29  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER E   30  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY F   14  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER F   15  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ HIS F   16  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET F   17  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ALA F   18  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER F   19  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET F   20  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ THR F   21  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY F   22  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY F   23  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN F   24  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN F   25  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET F   26  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY F   27  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ARG F   28  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY F   29  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER F   30  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY G   14  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER G   15  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ HIS G   16  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET G   17  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ALA G   18  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER G   19  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET G   20  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ THR G   21  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY G   22  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY G   23  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN G   24  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN G   25  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET G   26  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY G   27  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ARG G   28  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY G   29  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER G   30  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY H   14  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER H   15  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ HIS H   16  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET H   17  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ALA H   18  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER H   19  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET H   20  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ THR H   21  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY H   22  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY H   23  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN H   24  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLN H   25  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ MET H   26  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY H   27  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ ARG H   28  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ GLY H   29  UNP  P56545              EXPRESSION TAG                 
SEQADV 4LCJ SER H   30  UNP  P56545              EXPRESSION TAG                 
SEQRES   1 A  349  GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET          
SEQRES   2 A  349  GLY ARG GLY SER HIS PRO ARG PRO LEU VAL ALA LEU LEU          
SEQRES   3 A  349  ASP GLY ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS          
SEQRES   4 A  349  ASP LEU ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR          
SEQRES   5 A  349  GLN GLU ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY          
SEQRES   6 A  349  ALA MET MET TYR HIS THR ILE THR LEU THR ARG GLU ASP          
SEQRES   7 A  349  LEU GLU LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE          
SEQRES   8 A  349  GLY SER GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY          
SEQRES   9 A  349  GLU LEU GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA          
SEQRES  10 A  349  VAL GLU GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU          
SEQRES  11 A  349  ASN LEU TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU          
SEQRES  12 A  349  ARG GLU GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG          
SEQRES  13 A  349  GLU VAL ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR          
SEQRES  14 A  349  LEU GLY LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL          
SEQRES  15 A  349  ALA VAL ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE          
SEQRES  16 A  349  TYR ASP PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU          
SEQRES  17 A  349  GLY VAL GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR          
SEQRES  18 A  349  GLN SER ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU          
SEQRES  19 A  349  HIS ASN HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN          
SEQRES  20 A  349  MET ARG GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY          
SEQRES  21 A  349  GLY LEU VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS          
SEQRES  22 A  349  GLU GLY ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU          
SEQRES  23 A  349  SER GLU PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP          
SEQRES  24 A  349  ALA PRO ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR          
SEQRES  25 A  349  SER GLU GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA          
SEQRES  26 A  349  THR GLU ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU          
SEQRES  27 A  349  SER LEU ARG ASN CYS VAL ASN LYS GLU PHE PHE                  
SEQRES   1 B  349  GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET          
SEQRES   2 B  349  GLY ARG GLY SER HIS PRO ARG PRO LEU VAL ALA LEU LEU          
SEQRES   3 B  349  ASP GLY ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS          
SEQRES   4 B  349  ASP LEU ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR          
SEQRES   5 B  349  GLN GLU ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY          
SEQRES   6 B  349  ALA MET MET TYR HIS THR ILE THR LEU THR ARG GLU ASP          
SEQRES   7 B  349  LEU GLU LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE          
SEQRES   8 B  349  GLY SER GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY          
SEQRES   9 B  349  GLU LEU GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA          
SEQRES  10 B  349  VAL GLU GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU          
SEQRES  11 B  349  ASN LEU TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU          
SEQRES  12 B  349  ARG GLU GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG          
SEQRES  13 B  349  GLU VAL ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR          
SEQRES  14 B  349  LEU GLY LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL          
SEQRES  15 B  349  ALA VAL ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE          
SEQRES  16 B  349  TYR ASP PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU          
SEQRES  17 B  349  GLY VAL GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR          
SEQRES  18 B  349  GLN SER ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU          
SEQRES  19 B  349  HIS ASN HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN          
SEQRES  20 B  349  MET ARG GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY          
SEQRES  21 B  349  GLY LEU VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS          
SEQRES  22 B  349  GLU GLY ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU          
SEQRES  23 B  349  SER GLU PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP          
SEQRES  24 B  349  ALA PRO ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR          
SEQRES  25 B  349  SER GLU GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA          
SEQRES  26 B  349  THR GLU ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU          
SEQRES  27 B  349  SER LEU ARG ASN CYS VAL ASN LYS GLU PHE PHE                  
SEQRES   1 C  349  GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET          
SEQRES   2 C  349  GLY ARG GLY SER HIS PRO ARG PRO LEU VAL ALA LEU LEU          
SEQRES   3 C  349  ASP GLY ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS          
SEQRES   4 C  349  ASP LEU ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR          
SEQRES   5 C  349  GLN GLU ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY          
SEQRES   6 C  349  ALA MET MET TYR HIS THR ILE THR LEU THR ARG GLU ASP          
SEQRES   7 C  349  LEU GLU LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE          
SEQRES   8 C  349  GLY SER GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY          
SEQRES   9 C  349  GLU LEU GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA          
SEQRES  10 C  349  VAL GLU GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU          
SEQRES  11 C  349  ASN LEU TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU          
SEQRES  12 C  349  ARG GLU GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG          
SEQRES  13 C  349  GLU VAL ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR          
SEQRES  14 C  349  LEU GLY LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL          
SEQRES  15 C  349  ALA VAL ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE          
SEQRES  16 C  349  TYR ASP PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU          
SEQRES  17 C  349  GLY VAL GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR          
SEQRES  18 C  349  GLN SER ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU          
SEQRES  19 C  349  HIS ASN HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN          
SEQRES  20 C  349  MET ARG GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY          
SEQRES  21 C  349  GLY LEU VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS          
SEQRES  22 C  349  GLU GLY ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU          
SEQRES  23 C  349  SER GLU PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP          
SEQRES  24 C  349  ALA PRO ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR          
SEQRES  25 C  349  SER GLU GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA          
SEQRES  26 C  349  THR GLU ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU          
SEQRES  27 C  349  SER LEU ARG ASN CYS VAL ASN LYS GLU PHE PHE                  
SEQRES   1 D  349  GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET          
SEQRES   2 D  349  GLY ARG GLY SER HIS PRO ARG PRO LEU VAL ALA LEU LEU          
SEQRES   3 D  349  ASP GLY ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS          
SEQRES   4 D  349  ASP LEU ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR          
SEQRES   5 D  349  GLN GLU ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY          
SEQRES   6 D  349  ALA MET MET TYR HIS THR ILE THR LEU THR ARG GLU ASP          
SEQRES   7 D  349  LEU GLU LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE          
SEQRES   8 D  349  GLY SER GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY          
SEQRES   9 D  349  GLU LEU GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA          
SEQRES  10 D  349  VAL GLU GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU          
SEQRES  11 D  349  ASN LEU TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU          
SEQRES  12 D  349  ARG GLU GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG          
SEQRES  13 D  349  GLU VAL ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR          
SEQRES  14 D  349  LEU GLY LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL          
SEQRES  15 D  349  ALA VAL ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE          
SEQRES  16 D  349  TYR ASP PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU          
SEQRES  17 D  349  GLY VAL GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR          
SEQRES  18 D  349  GLN SER ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU          
SEQRES  19 D  349  HIS ASN HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN          
SEQRES  20 D  349  MET ARG GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY          
SEQRES  21 D  349  GLY LEU VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS          
SEQRES  22 D  349  GLU GLY ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU          
SEQRES  23 D  349  SER GLU PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP          
SEQRES  24 D  349  ALA PRO ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR          
SEQRES  25 D  349  SER GLU GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA          
SEQRES  26 D  349  THR GLU ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU          
SEQRES  27 D  349  SER LEU ARG ASN CYS VAL ASN LYS GLU PHE PHE                  
SEQRES   1 E  349  GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET          
SEQRES   2 E  349  GLY ARG GLY SER HIS PRO ARG PRO LEU VAL ALA LEU LEU          
SEQRES   3 E  349  ASP GLY ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS          
SEQRES   4 E  349  ASP LEU ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR          
SEQRES   5 E  349  GLN GLU ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY          
SEQRES   6 E  349  ALA MET MET TYR HIS THR ILE THR LEU THR ARG GLU ASP          
SEQRES   7 E  349  LEU GLU LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE          
SEQRES   8 E  349  GLY SER GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY          
SEQRES   9 E  349  GLU LEU GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA          
SEQRES  10 E  349  VAL GLU GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU          
SEQRES  11 E  349  ASN LEU TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU          
SEQRES  12 E  349  ARG GLU GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG          
SEQRES  13 E  349  GLU VAL ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR          
SEQRES  14 E  349  LEU GLY LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL          
SEQRES  15 E  349  ALA VAL ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE          
SEQRES  16 E  349  TYR ASP PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU          
SEQRES  17 E  349  GLY VAL GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR          
SEQRES  18 E  349  GLN SER ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU          
SEQRES  19 E  349  HIS ASN HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN          
SEQRES  20 E  349  MET ARG GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY          
SEQRES  21 E  349  GLY LEU VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS          
SEQRES  22 E  349  GLU GLY ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU          
SEQRES  23 E  349  SER GLU PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP          
SEQRES  24 E  349  ALA PRO ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR          
SEQRES  25 E  349  SER GLU GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA          
SEQRES  26 E  349  THR GLU ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU          
SEQRES  27 E  349  SER LEU ARG ASN CYS VAL ASN LYS GLU PHE PHE                  
SEQRES   1 F  349  GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET          
SEQRES   2 F  349  GLY ARG GLY SER HIS PRO ARG PRO LEU VAL ALA LEU LEU          
SEQRES   3 F  349  ASP GLY ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS          
SEQRES   4 F  349  ASP LEU ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR          
SEQRES   5 F  349  GLN GLU ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY          
SEQRES   6 F  349  ALA MET MET TYR HIS THR ILE THR LEU THR ARG GLU ASP          
SEQRES   7 F  349  LEU GLU LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE          
SEQRES   8 F  349  GLY SER GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY          
SEQRES   9 F  349  GLU LEU GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA          
SEQRES  10 F  349  VAL GLU GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU          
SEQRES  11 F  349  ASN LEU TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU          
SEQRES  12 F  349  ARG GLU GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG          
SEQRES  13 F  349  GLU VAL ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR          
SEQRES  14 F  349  LEU GLY LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL          
SEQRES  15 F  349  ALA VAL ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE          
SEQRES  16 F  349  TYR ASP PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU          
SEQRES  17 F  349  GLY VAL GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR          
SEQRES  18 F  349  GLN SER ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU          
SEQRES  19 F  349  HIS ASN HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN          
SEQRES  20 F  349  MET ARG GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY          
SEQRES  21 F  349  GLY LEU VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS          
SEQRES  22 F  349  GLU GLY ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU          
SEQRES  23 F  349  SER GLU PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP          
SEQRES  24 F  349  ALA PRO ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR          
SEQRES  25 F  349  SER GLU GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA          
SEQRES  26 F  349  THR GLU ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU          
SEQRES  27 F  349  SER LEU ARG ASN CYS VAL ASN LYS GLU PHE PHE                  
SEQRES   1 G  349  GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET          
SEQRES   2 G  349  GLY ARG GLY SER HIS PRO ARG PRO LEU VAL ALA LEU LEU          
SEQRES   3 G  349  ASP GLY ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS          
SEQRES   4 G  349  ASP LEU ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR          
SEQRES   5 G  349  GLN GLU ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY          
SEQRES   6 G  349  ALA MET MET TYR HIS THR ILE THR LEU THR ARG GLU ASP          
SEQRES   7 G  349  LEU GLU LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE          
SEQRES   8 G  349  GLY SER GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY          
SEQRES   9 G  349  GLU LEU GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA          
SEQRES  10 G  349  VAL GLU GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU          
SEQRES  11 G  349  ASN LEU TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU          
SEQRES  12 G  349  ARG GLU GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG          
SEQRES  13 G  349  GLU VAL ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR          
SEQRES  14 G  349  LEU GLY LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL          
SEQRES  15 G  349  ALA VAL ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE          
SEQRES  16 G  349  TYR ASP PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU          
SEQRES  17 G  349  GLY VAL GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR          
SEQRES  18 G  349  GLN SER ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU          
SEQRES  19 G  349  HIS ASN HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN          
SEQRES  20 G  349  MET ARG GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY          
SEQRES  21 G  349  GLY LEU VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS          
SEQRES  22 G  349  GLU GLY ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU          
SEQRES  23 G  349  SER GLU PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP          
SEQRES  24 G  349  ALA PRO ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR          
SEQRES  25 G  349  SER GLU GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA          
SEQRES  26 G  349  THR GLU ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU          
SEQRES  27 G  349  SER LEU ARG ASN CYS VAL ASN LYS GLU PHE PHE                  
SEQRES   1 H  349  GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET          
SEQRES   2 H  349  GLY ARG GLY SER HIS PRO ARG PRO LEU VAL ALA LEU LEU          
SEQRES   3 H  349  ASP GLY ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS          
SEQRES   4 H  349  ASP LEU ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR          
SEQRES   5 H  349  GLN GLU ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY          
SEQRES   6 H  349  ALA MET MET TYR HIS THR ILE THR LEU THR ARG GLU ASP          
SEQRES   7 H  349  LEU GLU LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE          
SEQRES   8 H  349  GLY SER GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY          
SEQRES   9 H  349  GLU LEU GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA          
SEQRES  10 H  349  VAL GLU GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU          
SEQRES  11 H  349  ASN LEU TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU          
SEQRES  12 H  349  ARG GLU GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG          
SEQRES  13 H  349  GLU VAL ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR          
SEQRES  14 H  349  LEU GLY LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL          
SEQRES  15 H  349  ALA VAL ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE          
SEQRES  16 H  349  TYR ASP PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU          
SEQRES  17 H  349  GLY VAL GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR          
SEQRES  18 H  349  GLN SER ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU          
SEQRES  19 H  349  HIS ASN HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN          
SEQRES  20 H  349  MET ARG GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY          
SEQRES  21 H  349  GLY LEU VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS          
SEQRES  22 H  349  GLU GLY ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU          
SEQRES  23 H  349  SER GLU PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP          
SEQRES  24 H  349  ALA PRO ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR          
SEQRES  25 H  349  SER GLU GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA          
SEQRES  26 H  349  THR GLU ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU          
SEQRES  27 H  349  SER LEU ARG ASN CYS VAL ASN LYS GLU PHE PHE                  
HET    NAD  A 401      44                                                       
HET    KMT  A 402       9                                                       
HET    NAD  B 401      44                                                       
HET    KMT  B 402       9                                                       
HET    NAD  C 401      44                                                       
HET    KMT  C 402       9                                                       
HET    NAD  D 401      44                                                       
HET    KMT  D 402       9                                                       
HET    NAD  E 401      44                                                       
HET    KMT  E 402       9                                                       
HET    NAD  F 401      44                                                       
HET    KMT  F 402       9                                                       
HET    NAD  G 401      44                                                       
HET    KMT  G 402       9                                                       
HET    NAD  H 401      44                                                       
HET    KMT  H 402       9                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     KMT 4-(METHYLSULFANYL)-2-OXOBUTANOIC ACID                            
FORMUL   9  NAD    8(C21 H27 N7 O14 P2)                                         
FORMUL  10  KMT    8(C5 H8 O3 S)                                                
FORMUL  25  HOH   *205(H2 O)                                                    
HELIX    1   1 VAL A   46  LYS A   52  1                                   7    
HELIX    2   2 SER A   64  ILE A   68  5                                   5    
HELIX    3   3 HIS A   69  GLU A   75  1                                   7    
HELIX    4   4 THR A   88  LYS A   94  1                                   7    
HELIX    5   5 ASP A  112  LEU A  119  1                                   8    
HELIX    6   6 ALA A  130  ARG A  148  1                                  19    
HELIX    7   7 ARG A  148  GLU A  158  1                                  11    
HELIX    8   8 SER A  164  ALA A  172  1                                   9    
HELIX    9   9 GLY A  189  LYS A  200  1                                  12    
HELIX   10  10 ALA A  201  GLY A  203  5                                   3    
HELIX   11  11 GLY A  216  LEU A  221  1                                   6    
HELIX   12  12 THR A  228  SER A  236  1                                   9    
HELIX   13  13 ASN A  254  LYS A  259  1                                   6    
HELIX   14  14 ARG A  272  VAL A  276  5                                   5    
HELIX   15  15 ASP A  277  GLU A  287  1                                  11    
HELIX   16  16 SER A  326  GLY A  347  1                                  22    
HELIX   17  17 VAL B   46  LYS B   52  1                                   7    
HELIX   18  18 SER B   64  ILE B   68  5                                   5    
HELIX   19  19 HIS B   69  GLU B   75  1                                   7    
HELIX   20  20 THR B   88  LYS B   94  1                                   7    
HELIX   21  21 ASP B  112  LEU B  119  1                                   8    
HELIX   22  22 ALA B  130  ARG B  148  1                                  19    
HELIX   23  23 ARG B  148  GLU B  158  1                                  11    
HELIX   24  24 SER B  164  ALA B  172  1                                   9    
HELIX   25  25 GLY B  189  LYS B  200  1                                  12    
HELIX   26  26 ALA B  201  GLY B  203  5                                   3    
HELIX   27  27 GLY B  216  LEU B  221  1                                   6    
HELIX   28  28 THR B  228  SER B  236  1                                   9    
HELIX   29  29 ASN B  254  LYS B  259  1                                   6    
HELIX   30  30 ARG B  272  VAL B  276  5                                   5    
HELIX   31  31 ASP B  277  GLU B  287  1                                  11    
HELIX   32  32 SER B  326  GLY B  347  1                                  22    
HELIX   33  33 VAL C   46  LYS C   52  1                                   7    
HELIX   34  34 SER C   64  ILE C   68  5                                   5    
HELIX   35  35 HIS C   69  GLU C   75  1                                   7    
HELIX   36  36 THR C   88  LYS C   94  1                                   7    
HELIX   37  37 ASP C  112  LEU C  119  1                                   8    
HELIX   38  38 ALA C  130  ARG C  148  1                                  19    
HELIX   39  39 ARG C  148  GLU C  158  1                                  11    
HELIX   40  40 SER C  164  ALA C  172  1                                   9    
HELIX   41  41 GLY C  189  LYS C  200  1                                  12    
HELIX   42  42 ALA C  201  GLY C  203  5                                   3    
HELIX   43  43 GLY C  216  LEU C  221  1                                   6    
HELIX   44  44 THR C  228  SER C  236  1                                   9    
HELIX   45  45 ASN C  254  LYS C  259  1                                   6    
HELIX   46  46 ARG C  272  VAL C  276  5                                   5    
HELIX   47  47 ASP C  277  GLU C  287  1                                  11    
HELIX   48  48 SER C  326  GLY C  347  1                                  22    
HELIX   49  49 VAL D   46  LYS D   52  1                                   7    
HELIX   50  50 SER D   64  ILE D   68  5                                   5    
HELIX   51  51 HIS D   69  GLU D   75  1                                   7    
HELIX   52  52 THR D   88  LYS D   94  1                                   7    
HELIX   53  53 ASP D  112  LEU D  119  1                                   8    
HELIX   54  54 ALA D  130  ARG D  148  1                                  19    
HELIX   55  55 ARG D  148  GLU D  158  1                                  11    
HELIX   56  56 SER D  164  ALA D  172  1                                   9    
HELIX   57  57 GLY D  189  LYS D  200  1                                  12    
HELIX   58  58 ALA D  201  GLY D  203  5                                   3    
HELIX   59  59 GLY D  216  LEU D  221  1                                   6    
HELIX   60  60 THR D  228  SER D  236  1                                   9    
HELIX   61  61 ASN D  254  LYS D  259  1                                   6    
HELIX   62  62 ARG D  272  VAL D  276  5                                   5    
HELIX   63  63 ASP D  277  GLU D  287  1                                  11    
HELIX   64  64 SER D  326  GLY D  347  1                                  22    
HELIX   65  65 VAL E   46  ASP E   53  1                                   8    
HELIX   66  66 SER E   64  ILE E   68  5                                   5    
HELIX   67  67 HIS E   69  GLU E   75  1                                   7    
HELIX   68  68 THR E   88  LYS E   94  1                                   7    
HELIX   69  69 ASP E  112  LEU E  119  1                                   8    
HELIX   70  70 ALA E  130  ARG E  148  1                                  19    
HELIX   71  71 ARG E  148  GLU E  158  1                                  11    
HELIX   72  72 SER E  164  ALA E  172  1                                   9    
HELIX   73  73 GLY E  189  LYS E  200  1                                  12    
HELIX   74  74 ALA E  201  GLY E  203  5                                   3    
HELIX   75  75 GLY E  216  LEU E  221  1                                   6    
HELIX   76  76 THR E  228  SER E  236  1                                   9    
HELIX   77  77 ASN E  254  LYS E  259  1                                   6    
HELIX   78  78 ARG E  272  VAL E  276  5                                   5    
HELIX   79  79 ASP E  277  GLU E  287  1                                  11    
HELIX   80  80 SER E  326  GLY E  347  1                                  22    
HELIX   81  81 GLU F   47  LYS F   52  1                                   6    
HELIX   82  82 SER F   64  ILE F   68  5                                   5    
HELIX   83  83 HIS F   69  GLU F   75  1                                   7    
HELIX   84  84 THR F   88  PHE F   95  1                                   8    
HELIX   85  85 ASP F  112  LEU F  119  1                                   8    
HELIX   86  86 ALA F  130  ARG F  148  1                                  19    
HELIX   87  87 ARG F  148  GLU F  158  1                                  11    
HELIX   88  88 SER F  164  ALA F  172  1                                   9    
HELIX   89  89 GLY F  189  LYS F  200  1                                  12    
HELIX   90  90 ALA F  201  GLY F  203  5                                   3    
HELIX   91  91 GLY F  216  LEU F  221  1                                   6    
HELIX   92  92 THR F  228  SER F  236  1                                   9    
HELIX   93  93 ASN F  254  LYS F  259  1                                   6    
HELIX   94  94 ARG F  272  VAL F  276  5                                   5    
HELIX   95  95 ASP F  277  GLU F  287  1                                  11    
HELIX   96  96 SER F  326  GLY F  347  1                                  22    
HELIX   97  97 GLU G   47  LYS G   52  1                                   6    
HELIX   98  98 SER G   64  ILE G   68  5                                   5    
HELIX   99  99 HIS G   69  GLU G   75  1                                   7    
HELIX  100 100 THR G   88  LYS G   94  1                                   7    
HELIX  101 101 ASP G  112  LEU G  119  1                                   8    
HELIX  102 102 ALA G  130  ARG G  148  1                                  19    
HELIX  103 103 ARG G  148  GLU G  158  1                                  11    
HELIX  104 104 SER G  164  ALA G  172  1                                   9    
HELIX  105 105 GLY G  189  LYS G  200  1                                  12    
HELIX  106 106 ALA G  201  GLY G  203  5                                   3    
HELIX  107 107 GLY G  216  LEU G  221  1                                   6    
HELIX  108 108 THR G  228  SER G  236  1                                   9    
HELIX  109 109 ASN G  254  GLN G  260  1                                   7    
HELIX  110 110 ARG G  272  VAL G  276  5                                   5    
HELIX  111 111 ASP G  277  GLU G  287  1                                  11    
HELIX  112 112 SER G  326  THR G  346  1                                  21    
HELIX  113 113 GLU H   47  LYS H   52  1                                   6    
HELIX  114 114 SER H   64  ILE H   68  5                                   5    
HELIX  115 115 HIS H   69  GLU H   75  1                                   7    
HELIX  116 116 THR H   88  PHE H   95  1                                   8    
HELIX  117 117 ASP H  112  LEU H  119  1                                   8    
HELIX  118 118 ALA H  130  ARG H  148  1                                  19    
HELIX  119 119 ARG H  148  GLU H  158  1                                  11    
HELIX  120 120 SER H  164  ALA H  172  1                                   9    
HELIX  121 121 GLY H  189  LYS H  200  1                                  12    
HELIX  122 122 ALA H  201  GLY H  203  5                                   3    
HELIX  123 123 GLY H  216  LEU H  221  1                                   6    
HELIX  124 124 THR H  228  SER H  236  1                                   9    
HELIX  125 125 ASN H  254  LYS H  259  1                                   6    
HELIX  126 126 ARG H  272  VAL H  276  5                                   5    
HELIX  127 127 ASP H  277  GLU H  287  1                                  11    
HELIX  128 128 SER H  326  GLY H  347  1                                  22    
SHEET    1   A 5 THR A  56  PHE A  59  0                                        
SHEET    2   A 5 LEU A  35  LEU A  38  1  N  LEU A  38   O  ALA A  58           
SHEET    3   A 5 ALA A  76  MET A  81  1  O  GLY A  78   N  ALA A  37           
SHEET    4   A 5 VAL A 100  ARG A 103  1  O  VAL A 102   N  ALA A  79           
SHEET    5   A 5 ALA A 122  CYS A 124  1  O  CYS A 124   N  ARG A 103           
SHEET    1   B 7 GLN A 224  ARG A 225  0                                        
SHEET    2   B 7 SER A 205  TYR A 209  1  N  VAL A 206   O  GLN A 224           
SHEET    3   B 7 THR A 182  ILE A 186  1  N  LEU A 183   O  SER A 205           
SHEET    4   B 7 CYS A 238  LEU A 241  1  O  CYS A 238   N  GLY A 184           
SHEET    5   B 7 ALA A 265  ASN A 269  1  O  PHE A 266   N  VAL A 239           
SHEET    6   B 7 ILE A 290  LEU A 295  1  O  ALA A 294   N  ASN A 269           
SHEET    7   B 7 LEU A 316  CYS A 318  1  O  ILE A 317   N  LEU A 295           
SHEET    1   C 5 THR B  56  PHE B  59  0                                        
SHEET    2   C 5 LEU B  35  LEU B  38  1  N  VAL B  36   O  THR B  56           
SHEET    3   C 5 ALA B  76  MET B  81  1  O  MET B  80   N  ALA B  37           
SHEET    4   C 5 VAL B 100  ARG B 103  1  O  VAL B 102   N  ALA B  79           
SHEET    5   C 5 ALA B 122  CYS B 124  1  O  ALA B 122   N  ILE B 101           
SHEET    1   D 7 GLN B 224  ARG B 225  0                                        
SHEET    2   D 7 SER B 205  TYR B 209  1  N  VAL B 206   O  GLN B 224           
SHEET    3   D 7 THR B 182  ILE B 186  1  N  LEU B 185   O  ILE B 207           
SHEET    4   D 7 CYS B 238  LEU B 241  1  O  CYS B 238   N  GLY B 184           
SHEET    5   D 7 ALA B 265  ASN B 269  1  O  VAL B 268   N  VAL B 239           
SHEET    6   D 7 ILE B 290  LEU B 295  1  O  ALA B 294   N  ASN B 269           
SHEET    7   D 7 LEU B 316  CYS B 318  1  O  ILE B 317   N  LEU B 295           
SHEET    1   E 5 THR C  56  PHE C  59  0                                        
SHEET    2   E 5 LEU C  35  LEU C  38  1  N  LEU C  38   O  ALA C  58           
SHEET    3   E 5 ALA C  76  MET C  81  1  O  VAL C  77   N  LEU C  35           
SHEET    4   E 5 VAL C 100  ARG C 103  1  O  VAL C 102   N  ALA C  79           
SHEET    5   E 5 ALA C 122  CYS C 124  1  O  CYS C 124   N  ARG C 103           
SHEET    1   F 7 GLN C 224  ARG C 225  0                                        
SHEET    2   F 7 SER C 205  TYR C 209  1  N  VAL C 206   O  GLN C 224           
SHEET    3   F 7 THR C 182  ILE C 186  1  N  LEU C 185   O  ILE C 207           
SHEET    4   F 7 CYS C 238  LEU C 241  1  O  CYS C 238   N  GLY C 184           
SHEET    5   F 7 ALA C 265  ASN C 269  1  O  PHE C 266   N  VAL C 239           
SHEET    6   F 7 ILE C 290  LEU C 295  1  O  ALA C 294   N  LEU C 267           
SHEET    7   F 7 LEU C 316  CYS C 318  1  O  ILE C 317   N  LEU C 295           
SHEET    1   G 5 THR D  56  PHE D  59  0                                        
SHEET    2   G 5 LEU D  35  LEU D  38  1  N  LEU D  38   O  ALA D  58           
SHEET    3   G 5 ALA D  76  MET D  81  1  O  GLY D  78   N  ALA D  37           
SHEET    4   G 5 VAL D 100  ARG D 103  1  O  VAL D 102   N  ALA D  79           
SHEET    5   G 5 ALA D 122  ASN D 125  1  O  ALA D 122   N  ILE D 101           
SHEET    1   H 7 GLN D 224  ARG D 225  0                                        
SHEET    2   H 7 SER D 205  TYR D 209  1  N  VAL D 206   O  GLN D 224           
SHEET    3   H 7 THR D 182  ILE D 186  1  N  LEU D 185   O  ILE D 207           
SHEET    4   H 7 CYS D 238  LEU D 241  1  O  CYS D 238   N  GLY D 184           
SHEET    5   H 7 ALA D 265  ASN D 269  1  O  PHE D 266   N  VAL D 239           
SHEET    6   H 7 ILE D 290  LEU D 295  1  O  ALA D 294   N  ASN D 269           
SHEET    7   H 7 LEU D 316  CYS D 318  1  O  ILE D 317   N  ALA D 293           
SHEET    1   I 5 THR E  56  PHE E  59  0                                        
SHEET    2   I 5 LEU E  35  LEU E  38  1  N  LEU E  38   O  ALA E  58           
SHEET    3   I 5 ALA E  76  MET E  81  1  O  MET E  80   N  ALA E  37           
SHEET    4   I 5 VAL E 100  ARG E 103  1  O  VAL E 102   N  ALA E  79           
SHEET    5   I 5 ALA E 122  CYS E 124  1  O  ALA E 122   N  ILE E 101           
SHEET    1   J 7 GLN E 224  ARG E 225  0                                        
SHEET    2   J 7 SER E 205  TYR E 209  1  N  VAL E 206   O  GLN E 224           
SHEET    3   J 7 THR E 182  ILE E 186  1  N  LEU E 185   O  ILE E 207           
SHEET    4   J 7 CYS E 238  LEU E 241  1  O  CYS E 238   N  GLY E 184           
SHEET    5   J 7 ALA E 265  ASN E 269  1  O  PHE E 266   N  VAL E 239           
SHEET    6   J 7 ILE E 290  LEU E 295  1  O  ALA E 294   N  ASN E 269           
SHEET    7   J 7 LEU E 316  CYS E 318  1  O  ILE E 317   N  LEU E 295           
SHEET    1   K 5 THR F  56  PHE F  59  0                                        
SHEET    2   K 5 LEU F  35  LEU F  38  1  N  LEU F  38   O  ALA F  58           
SHEET    3   K 5 ALA F  76  MET F  81  1  O  MET F  80   N  ALA F  37           
SHEET    4   K 5 VAL F 100  ARG F 103  1  O  VAL F 100   N  ALA F  79           
SHEET    5   K 5 ALA F 122  CYS F 124  1  O  CYS F 124   N  ARG F 103           
SHEET    1   L 7 GLN F 224  ARG F 225  0                                        
SHEET    2   L 7 SER F 205  TYR F 209  1  N  VAL F 206   O  GLN F 224           
SHEET    3   L 7 THR F 182  ILE F 186  1  N  LEU F 185   O  ILE F 207           
SHEET    4   L 7 CYS F 238  LEU F 241  1  O  CYS F 238   N  GLY F 184           
SHEET    5   L 7 ALA F 265  ASN F 269  1  O  PHE F 266   N  VAL F 239           
SHEET    6   L 7 ILE F 290  LEU F 295  1  O  ALA F 294   N  ASN F 269           
SHEET    7   L 7 LEU F 316  CYS F 318  1  O  ILE F 317   N  LEU F 295           
SHEET    1   M 5 VAL G  57  PHE G  59  0                                        
SHEET    2   M 5 VAL G  36  LEU G  38  1  N  LEU G  38   O  ALA G  58           
SHEET    3   M 5 GLY G  78  MET G  81  1  O  MET G  80   N  ALA G  37           
SHEET    4   M 5 ILE G 101  ARG G 103  1  O  VAL G 102   N  ALA G  79           
SHEET    5   M 5 VAL G 123  CYS G 124  1  O  CYS G 124   N  ARG G 103           
SHEET    1   N 7 GLN G 224  ARG G 225  0                                        
SHEET    2   N 7 SER G 205  TYR G 209  1  N  VAL G 206   O  GLN G 224           
SHEET    3   N 7 THR G 182  ILE G 186  1  N  LEU G 185   O  ILE G 207           
SHEET    4   N 7 CYS G 238  LEU G 241  1  O  CYS G 238   N  GLY G 184           
SHEET    5   N 7 ALA G 265  ASN G 269  1  O  PHE G 266   N  VAL G 239           
SHEET    6   N 7 ILE G 290  LEU G 295  1  O  ALA G 294   N  ASN G 269           
SHEET    7   N 7 LEU G 316  CYS G 318  1  O  ILE G 317   N  LEU G 295           
SHEET    1   O 5 THR H  56  PHE H  59  0                                        
SHEET    2   O 5 LEU H  35  LEU H  38  1  N  LEU H  38   O  ALA H  58           
SHEET    3   O 5 ALA H  76  MET H  81  1  O  VAL H  77   N  LEU H  35           
SHEET    4   O 5 VAL H 100  ARG H 103  1  O  VAL H 102   N  ALA H  79           
SHEET    5   O 5 ALA H 122  CYS H 124  1  O  ALA H 122   N  ILE H 101           
SHEET    1   P 7 GLN H 224  ARG H 225  0                                        
SHEET    2   P 7 SER H 205  TYR H 209  1  N  VAL H 206   O  GLN H 224           
SHEET    3   P 7 THR H 182  ILE H 186  1  N  LEU H 185   O  ILE H 207           
SHEET    4   P 7 CYS H 238  LEU H 241  1  O  CYS H 238   N  GLY H 184           
SHEET    5   P 7 ALA H 265  ASN H 269  1  O  PHE H 266   N  VAL H 239           
SHEET    6   P 7 ILE H 290  LEU H 295  1  O  ALA H 294   N  LEU H 267           
SHEET    7   P 7 LEU H 316  CYS H 318  1  O  ILE H 317   N  LEU H 295           
CISPEP   1 GLU A  301    PRO A  302          0         7.67                     
CISPEP   2 ILE A  349    PRO A  350          0         8.53                     
CISPEP   3 GLU B  301    PRO B  302          0         7.38                     
CISPEP   4 ILE B  349    PRO B  350          0         6.64                     
CISPEP   5 GLU C  301    PRO C  302          0         7.39                     
CISPEP   6 ILE C  349    PRO C  350          0         8.00                     
CISPEP   7 GLU D  301    PRO D  302          0         5.80                     
CISPEP   8 ILE D  349    PRO D  350          0         7.03                     
CISPEP   9 GLU E  301    PRO E  302          0         6.67                     
CISPEP  10 ILE E  349    PRO E  350          0         7.01                     
CISPEP  11 GLU F  301    PRO F  302          0         7.74                     
CISPEP  12 ILE F  349    PRO F  350          0         6.27                     
CISPEP  13 GLU G  301    PRO G  302          0         7.13                     
CISPEP  14 ILE G  349    PRO G  350          0         5.73                     
CISPEP  15 GLU H  301    PRO H  302          0         6.32                     
CISPEP  16 ILE H  349    PRO H  350          0         6.76                     
SITE     1 AC1 25 SER A 106  THR A 134  ILE A 186  GLY A 187                    
SITE     2 AC1 25 GLY A 189  ARG A 190  THR A 191  TYR A 209                    
SITE     3 AC1 25 ASP A 210  PRO A 211  TYR A 212  HIS A 242                    
SITE     4 AC1 25 CYS A 243  ASN A 244  ASN A 246  ASN A 249                    
SITE     5 AC1 25 ALA A 270  ALA A 271  ARG A 272  ASP A 296                    
SITE     6 AC1 25 HIS A 321  ALA A 323  TRP A 324  KMT A 402                    
SITE     7 AC1 25 HOH A 512                                                     
SITE     1 AC2 10 HIS A  83  ARG A 103  ILE A 104  GLY A 105                    
SITE     2 AC2 10 SER A 106  GLY A 107  ARG A 272  HIS A 321                    
SITE     3 AC2 10 TRP A 324  NAD A 401                                          
SITE     1 AC3 26 SER B 106  THR B 134  ILE B 186  GLY B 187                    
SITE     2 AC3 26 GLY B 189  ARG B 190  THR B 191  TYR B 209                    
SITE     3 AC3 26 ASP B 210  PRO B 211  TYR B 212  HIS B 242                    
SITE     4 AC3 26 CYS B 243  ASN B 244  ASN B 246  ASN B 249                    
SITE     5 AC3 26 ALA B 270  ALA B 271  ARG B 272  ASP B 296                    
SITE     6 AC3 26 VAL B 297  HIS B 321  ALA B 323  TRP B 324                    
SITE     7 AC3 26 KMT B 402  HOH B 528                                          
SITE     1 AC4 11 TYR B  82  HIS B  83  ARG B 103  ILE B 104                    
SITE     2 AC4 11 GLY B 105  SER B 106  GLY B 107  ARG B 272                    
SITE     3 AC4 11 HIS B 321  TRP B 324  NAD B 401                               
SITE     1 AC5 26 SER C 106  THR C 134  ILE C 186  GLY C 187                    
SITE     2 AC5 26 GLY C 189  ARG C 190  THR C 191  TYR C 209                    
SITE     3 AC5 26 ASP C 210  PRO C 211  TYR C 212  HIS C 242                    
SITE     4 AC5 26 CYS C 243  ASN C 244  ASN C 246  ASN C 249                    
SITE     5 AC5 26 ALA C 270  ALA C 271  ARG C 272  ASP C 296                    
SITE     6 AC5 26 VAL C 297  HIS C 321  ALA C 323  TRP C 324                    
SITE     7 AC5 26 KMT C 402  HOH C 514                                          
SITE     1 AC6  9 HIS C  83  ARG C 103  ILE C 104  GLY C 105                    
SITE     2 AC6  9 SER C 106  GLY C 107  ARG C 272  HIS C 321                    
SITE     3 AC6  9 NAD C 401                                                     
SITE     1 AC7 23 SER D 106  THR D 134  GLY D 187  GLY D 189                    
SITE     2 AC7 23 ARG D 190  THR D 191  TYR D 209  ASP D 210                    
SITE     3 AC7 23 PRO D 211  TYR D 212  HIS D 242  CYS D 243                    
SITE     4 AC7 23 ASN D 244  ASN D 246  ASN D 249  ALA D 270                    
SITE     5 AC7 23 ALA D 271  ARG D 272  ASP D 296  HIS D 321                    
SITE     6 AC7 23 ALA D 323  TRP D 324  KMT D 402                               
SITE     1 AC8 10 HIS D  83  ARG D 103  ILE D 104  GLY D 105                    
SITE     2 AC8 10 SER D 106  GLY D 107  ARG D 272  HIS D 321                    
SITE     3 AC8 10 TRP D 324  NAD D 401                                          
SITE     1 AC9 26 SER E 106  GLY E 107  THR E 134  GLY E 187                    
SITE     2 AC9 26 GLY E 189  ARG E 190  THR E 191  TYR E 209                    
SITE     3 AC9 26 ASP E 210  PRO E 211  TYR E 212  HIS E 242                    
SITE     4 AC9 26 CYS E 243  ASN E 244  ASN E 246  ASN E 249                    
SITE     5 AC9 26 ALA E 270  ALA E 271  ARG E 272  ASP E 296                    
SITE     6 AC9 26 HIS E 321  ALA E 323  TRP E 324  KMT E 402                    
SITE     7 AC9 26 HOH E 505  HOH E 515                                          
SITE     1 BC1  9 HIS E  83  ARG E 103  ILE E 104  SER E 106                    
SITE     2 BC1  9 GLY E 107  ARG E 272  HIS E 321  TRP E 324                    
SITE     3 BC1  9 NAD E 401                                                     
SITE     1 BC2 25 SER F 106  THR F 134  ILE F 186  GLY F 187                    
SITE     2 BC2 25 GLY F 189  ARG F 190  THR F 191  TYR F 209                    
SITE     3 BC2 25 ASP F 210  PRO F 211  TYR F 212  HIS F 242                    
SITE     4 BC2 25 CYS F 243  ASN F 244  ASN F 246  ALA F 270                    
SITE     5 BC2 25 ALA F 271  ARG F 272  ASP F 296  VAL F 297                    
SITE     6 BC2 25 HIS F 321  ALA F 323  TRP F 324  KMT F 402                    
SITE     7 BC2 25 HOH F 508                                                     
SITE     1 BC3  9 HIS F  83  ARG F 103  ILE F 104  GLY F 105                    
SITE     2 BC3  9 SER F 106  GLY F 107  ARG F 272  HIS F 321                    
SITE     3 BC3  9 NAD F 401                                                     
SITE     1 BC4 25 SER G 106  THR G 134  GLY G 187  GLY G 189                    
SITE     2 BC4 25 ARG G 190  THR G 191  TYR G 209  ASP G 210                    
SITE     3 BC4 25 PRO G 211  TYR G 212  HIS G 242  CYS G 243                    
SITE     4 BC4 25 ASN G 244  ASN G 246  ASN G 249  ALA G 270                    
SITE     5 BC4 25 ALA G 271  ARG G 272  ASP G 296  HIS G 321                    
SITE     6 BC4 25 ALA G 323  TRP G 324  KMT G 402  HOH G 505                    
SITE     7 BC4 25 HOH G 515                                                     
SITE     1 BC5 10 TYR G  82  HIS G  83  ILE G 104  GLY G 105                    
SITE     2 BC5 10 SER G 106  GLY G 107  ARG G 272  HIS G 321                    
SITE     3 BC5 10 TRP G 324  NAD G 401                                          
SITE     1 BC6 25 SER H 106  GLY H 107  THR H 134  GLY H 187                    
SITE     2 BC6 25 GLY H 189  ARG H 190  THR H 191  TYR H 209                    
SITE     3 BC6 25 ASP H 210  PRO H 211  TYR H 212  HIS H 242                    
SITE     4 BC6 25 CYS H 243  ASN H 244  ASN H 246  ASN H 249                    
SITE     5 BC6 25 ALA H 270  ALA H 271  ARG H 272  ASP H 296                    
SITE     6 BC6 25 HIS H 321  TRP H 324  KMT H 402  HOH H 520                    
SITE     7 BC6 25 HOH H 521                                                     
SITE     1 BC7  9 HIS H  83  ARG H 103  ILE H 104  GLY H 105                    
SITE     2 BC7  9 SER H 106  GLY H 107  ARG H 272  HIS H 321                    
SITE     3 BC7  9 NAD H 401                                                     
CRYST1   86.151  140.605  135.126  90.00  97.87  90.00 P 1 21 1     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011608  0.000000  0.001604        0.00000                         
SCALE2      0.000000  0.007112  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007471        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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