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Database: PDB
Entry: 5EDU
LinkDB: 5EDU
Original site: 5EDU 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           22-OCT-15   5EDU              
TITLE     CRYSTAL STRUCTURE OF HUMAN HISTONE DEACETYLASE 6 CATALYTIC DOMAIN 2 IN
TITLE    2 COMPLEX WITH TRICHOSTATIN A                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MALTOSE-BINDING PERIPLASMIC PROTEIN, HISTONE DEACETYLASE 6 
COMPND   3 CHIMERA;                                                             
COMPND   4 CHAIN: B, A;                                                         
COMPND   5 FRAGMENT: MBP + HD6 CATALYTIC DOMAIN 2 (UNP RESIDUES 479-835);       
COMPND   6 SYNONYM: MBP, MMBP, MALTODEXTRIN-BINDING PROTEIN, HD6;               
COMPND   7 EC: 3.5.1.98;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 562, 9606;                                           
SOURCE   5 GENE: MALE, Z5632, ECS5017, HDAC6, KIAA0901, JM21;                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28LIC                                  
KEYWDS    HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.HAI,D.CHRISTIANSON                                                  
REVDAT   4   13-SEP-17 5EDU    1       REMARK                                   
REVDAT   3   07-SEP-16 5EDU    1       JRNL                                     
REVDAT   2   10-AUG-16 5EDU    1       JRNL                                     
REVDAT   1   27-JUL-16 5EDU    0                                                
JRNL        AUTH   Y.HAI,D.W.CHRISTIANSON                                       
JRNL        TITL   HISTONE DEACETYLASE 6 STRUCTURE AND MOLECULAR BASIS OF       
JRNL        TITL 2 CATALYSIS AND INHIBITION.                                    
JRNL        REF    NAT.CHEM.BIOL.                V.  12   741 2016              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   27454933                                                     
JRNL        DOI    10.1038/NCHEMBIO.2134                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.3_1479                                    
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) : 2.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 87.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 40774                          
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) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2055                            
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 87.5828 -  6.8797    1.00     2782   167  0.1699 0.2299        
REMARK   3     2  6.8797 -  5.4609    1.00     2631   149  0.1928 0.2406        
REMARK   3     3  5.4609 -  4.7707    1.00     2647   122  0.1716 0.2544        
REMARK   3     4  4.7707 -  4.3345    1.00     2610   130  0.1618 0.2037        
REMARK   3     5  4.3345 -  4.0238    1.00     2582   140  0.1795 0.2332        
REMARK   3     6  4.0238 -  3.7866    1.00     2531   151  0.2021 0.2764        
REMARK   3     7  3.7866 -  3.5969    1.00     2571   144  0.2160 0.2684        
REMARK   3     8  3.5969 -  3.4404    1.00     2589   112  0.2404 0.3323        
REMARK   3     9  3.4404 -  3.3079    1.00     2531   130  0.2601 0.3193        
REMARK   3    10  3.3079 -  3.1938    1.00     2597   132  0.2820 0.3217        
REMARK   3    11  3.1938 -  3.0939    1.00     2499   123  0.2829 0.3869        
REMARK   3    12  3.0939 -  3.0054    1.00     2594   117  0.3018 0.3634        
REMARK   3    13  3.0054 -  2.9263    1.00     2489   147  0.2958 0.3868        
REMARK   3    14  2.9263 -  2.8549    1.00     2548   141  0.3002 0.3574        
REMARK   3    15  2.8549 -  2.7900    1.00     2518   150  0.3157 0.3854        
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)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.310           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.003          11395                                  
REMARK   3   ANGLE     :  0.738          15529                                  
REMARK   3   CHIRALITY :  0.026           1720                                  
REMARK   3   PLANARITY :  0.003           2028                                  
REMARK   3   DIHEDRAL  : 14.618           4063                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 473 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.5061 -35.6567  32.6609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5032 T22:   0.3853                                     
REMARK   3      T33:   0.4002 T12:  -0.0309                                     
REMARK   3      T13:  -0.0027 T23:   0.0343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0543 L22:   2.2975                                     
REMARK   3      L33:   1.7495 L12:   0.5136                                     
REMARK   3      L13:   0.5450 L23:   0.6400                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0196 S12:   0.0517 S13:  -0.2082                       
REMARK   3      S21:   0.1211 S22:   0.0462 S23:   0.1043                       
REMARK   3      S31:   0.3235 S32:  -0.0460 S33:  -0.2038                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 474 THROUGH 835 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1763  -3.3987  15.4311              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3232 T22:   0.3660                                     
REMARK   3      T33:   0.3841 T12:   0.0170                                     
REMARK   3      T13:  -0.0324 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1508 L22:   1.8997                                     
REMARK   3      L33:   1.1333 L12:   0.6211                                     
REMARK   3      L13:  -0.1732 L23:  -0.2516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0979 S12:   0.0689 S13:  -0.0847                       
REMARK   3      S21:   0.0306 S22:  -0.0706 S23:  -0.1782                       
REMARK   3      S31:   0.0169 S32:   0.0761 S33:   0.0043                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 114 THROUGH 166 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4436   1.2143  86.1916              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6987 T22:   0.8252                                     
REMARK   3      T33:   0.6202 T12:  -0.1379                                     
REMARK   3      T13:   0.0659 T23:  -0.2695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0076 L22:   0.4448                                     
REMARK   3      L33:   1.7496 L12:   0.4461                                     
REMARK   3      L13:  -0.0278 L23:  -0.6183                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2391 S12:  -0.7435 S13:   0.4164                       
REMARK   3      S21:   0.3792 S22:   0.0270 S23:  -0.3376                       
REMARK   3      S31:  -0.3728 S32:   0.6125 S33:   0.0616                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 167 THROUGH 308 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6298  -7.2245  64.4875              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5687 T22:   0.4893                                     
REMARK   3      T33:   0.5458 T12:   0.0027                                     
REMARK   3      T13:  -0.0409 T23:  -0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3771 L22:   0.9731                                     
REMARK   3      L33:   1.2817 L12:  -0.3163                                     
REMARK   3      L13:  -0.4085 L23:   0.0552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1582 S12:  -0.0905 S13:   0.3375                       
REMARK   3      S21:  -0.3222 S22:  -0.0876 S23:   0.2946                       
REMARK   3      S31:  -0.4321 S32:  -0.0708 S33:   0.0118                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 309 THROUGH 380 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5768  -1.1565  64.6434              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7207 T22:   0.5656                                     
REMARK   3      T33:   0.5547 T12:  -0.0793                                     
REMARK   3      T13:   0.0608 T23:  -0.0952                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8374 L22:   0.4696                                     
REMARK   3      L33:   0.8634 L12:  -0.0660                                     
REMARK   3      L13:  -0.0356 L23:  -0.5257                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1812 S12:  -0.2710 S13:   0.5801                       
REMARK   3      S21:   0.0067 S22:  -0.0952 S23:  -0.0654                       
REMARK   3      S31:  -0.5145 S32:   0.2323 S33:   0.0617                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 381 THROUGH 460 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4562   0.6661  70.0573              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7385 T22:   0.5982                                     
REMARK   3      T33:   0.6362 T12:   0.0006                                     
REMARK   3      T13:   0.0371 T23:  -0.0564                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5920 L22:   0.2846                                     
REMARK   3      L33:   0.7867 L12:  -0.1000                                     
REMARK   3      L13:  -0.2029 L23:  -0.2854                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2256 S12:  -0.0962 S13:   0.3988                       
REMARK   3      S21:  -0.1773 S22:  -0.0883 S23:   0.1967                       
REMARK   3      S31:  -0.6417 S32:   0.1007 S33:   0.0242                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 461 THROUGH 516 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8888 -41.6146  82.3394              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2791 T22:   0.3447                                     
REMARK   3      T33:   0.3668 T12:  -0.0003                                     
REMARK   3      T13:  -0.0015 T23:  -0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8238 L22:   0.6834                                     
REMARK   3      L33:   0.9322 L12:   0.0293                                     
REMARK   3      L13:   0.4300 L23:  -0.3675                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0557 S12:  -0.2002 S13:   0.0595                       
REMARK   3      S21:  -0.0999 S22:   0.0284 S23:   0.0846                       
REMARK   3      S31:   0.0298 S32:   0.0898 S33:  -0.0416                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 517 THROUGH 755 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8811 -34.3773  91.2284              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2234 T22:   0.3388                                     
REMARK   3      T33:   0.3707 T12:  -0.0083                                     
REMARK   3      T13:   0.0160 T23:   0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8067 L22:   0.9802                                     
REMARK   3      L33:   0.9628 L12:  -0.2640                                     
REMARK   3      L13:   0.2162 L23:   0.2010                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0179 S12:   0.0110 S13:   0.0788                       
REMARK   3      S21:   0.0155 S22:   0.0111 S23:  -0.2546                       
REMARK   3      S31:   0.0181 S32:   0.1461 S33:   0.0432                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 756 THROUGH 835 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2810 -25.1703  95.8614              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2890 T22:   0.3517                                     
REMARK   3      T33:   0.4146 T12:   0.0096                                     
REMARK   3      T13:  -0.0073 T23:   0.0330                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6715 L22:   0.4126                                     
REMARK   3      L33:   1.3137 L12:  -0.1715                                     
REMARK   3      L13:   0.3182 L23:   0.0731                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0652 S12:   0.0161 S13:   0.1880                       
REMARK   3      S21:   0.1044 S22:  -0.0075 S23:  -0.1810                       
REMARK   3      S31:  -0.0373 S32:  -0.1376 S33:   0.0126                       
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 5EDU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214751.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9798                             
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(220) SIDE        
REMARK 200                                   BOUNCE                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40864                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 149.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.00                              
REMARK 200  R MERGE                    (I) : 0.20400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.85300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4CBT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM SODIUM TARTRATE, 20%     
REMARK 280  PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
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       24.63100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.16650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.51600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      108.16650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.63100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       74.51600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     MET B    91                                                      
REMARK 465     GLY B    92                                                      
REMARK 465     SER B    93                                                      
REMARK 465     SER B    94                                                      
REMARK 465     HIS B    95                                                      
REMARK 465     HIS B    96                                                      
REMARK 465     HIS B    97                                                      
REMARK 465     HIS B    98                                                      
REMARK 465     HIS B    99                                                      
REMARK 465     HIS B   100                                                      
REMARK 465     GLU B   101                                                      
REMARK 465     ASN B   102                                                      
REMARK 465     LEU B   103                                                      
REMARK 465     TYR B   104                                                      
REMARK 465     PHE B   105                                                      
REMARK 465     GLN B   106                                                      
REMARK 465     GLY B   107                                                      
REMARK 465     SER B   108                                                      
REMARK 465     LYS B   109                                                      
REMARK 465     ILE B   110                                                      
REMARK 465     LEU B   808                                                      
REMARK 465     PRO B   809                                                      
REMARK 465     MET A    91                                                      
REMARK 465     GLY A    92                                                      
REMARK 465     SER A    93                                                      
REMARK 465     SER A    94                                                      
REMARK 465     HIS A    95                                                      
REMARK 465     HIS A    96                                                      
REMARK 465     HIS A    97                                                      
REMARK 465     HIS A    98                                                      
REMARK 465     HIS A    99                                                      
REMARK 465     HIS A   100                                                      
REMARK 465     GLU A   101                                                      
REMARK 465     ASN A   102                                                      
REMARK 465     LEU A   103                                                      
REMARK 465     TYR A   104                                                      
REMARK 465     PHE A   105                                                      
REMARK 465     GLN A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     SER A   108                                                      
REMARK 465     LYS A   109                                                      
REMARK 465     ILE A   110                                                      
REMARK 465     GLU A   111                                                      
REMARK 465     GLU A   112                                                      
REMARK 465     GLY A   113                                                      
REMARK 465     ASP A   138                                                      
REMARK 465     THR A   139                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B 114    CG   CD   CE   NZ                                   
REMARK 470     LYS B 133    CG   CD   CE   NZ                                   
REMARK 470     LYS B 248    CG   CD   CE   NZ                                   
REMARK 470     LYS B 347    CG   CD   CE   NZ                                   
REMARK 470     ARG B 810    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 114    CG   CD   CE   NZ                                   
REMARK 470     LYS A 133    CG   CD   CE   NZ                                   
REMARK 470     LYS A 134    CG   CD   CE   NZ                                   
REMARK 470     GLU A 136    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 137    CG   CD   CE   NZ                                   
REMARK 470     LYS A 150    CG   CD   CE   NZ                                   
REMARK 470     LYS A 154    CG   CD   CE   NZ                                   
REMARK 470     LYS A 245    CG   CD   CE   NZ                                   
REMARK 470     LYS A 347    CG   CD   CE   NZ                                   
REMARK 470     LYS A 381    CG   CD   CE   NZ                                   
REMARK 470     GLU A 382    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 386    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 403    CG   CD   CE   NZ                                   
REMARK 470     GLU A 418    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 421    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU B   280     O    LYS B   283              2.12            
REMARK 500   OH   TYR A   782     O2   TSN A   904              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 379   C   -  N   -  CD  ANGL. DEV. =  19.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS B 114     -164.25   -128.25                                   
REMARK 500    LEU B 115       98.32   -166.24                                   
REMARK 500    THR B 161       31.90    -92.46                                   
REMARK 500    ILE B 216      -56.64   -122.41                                   
REMARK 500    ALA B 276      -89.12    -84.72                                   
REMARK 500    ASN B 281     -128.58     60.36                                   
REMARK 500    LYS B 310       19.54     59.66                                   
REMARK 500    ASP B 317     -165.94   -122.75                                   
REMARK 500    TYR B 391      -32.35   -139.49                                   
REMARK 500    PRO B 442        3.59    -68.20                                   
REMARK 500    PHE B 622      -55.63   -128.48                                   
REMARK 500    ASN B 624       92.92    -68.34                                   
REMARK 500    PRO B 681       31.14    -85.45                                   
REMARK 500    MET B 682       -2.83     73.28                                   
REMARK 500    ALA B 694     -134.74     56.49                                   
REMARK 500    PRO B 708     -159.13    -86.22                                   
REMARK 500    LEU B 722      -63.86   -137.04                                   
REMARK 500    ASN B 731       73.08     53.59                                   
REMARK 500    SER B 738       85.11    -69.73                                   
REMARK 500    GLU B 779     -101.54   -121.57                                   
REMARK 500    LEU B 806     -169.22   -124.20                                   
REMARK 500    GLU A 136       14.22    104.59                                   
REMARK 500    LYS A 191       42.28    -72.67                                   
REMARK 500    ALA A 192      -46.93   -136.93                                   
REMARK 500    ILE A 216      -75.04    -92.90                                   
REMARK 500    LYS A 252     -170.35     58.75                                   
REMARK 500    ALA A 276      -78.47    -83.69                                   
REMARK 500    ASN A 293     -176.95    -69.60                                   
REMARK 500    ASP A 317     -156.67    -99.24                                   
REMARK 500    ASN A 375     -158.83    -70.69                                   
REMARK 500    SER A 378     -153.81     70.77                                   
REMARK 500    ASP A 404      -64.46    -94.26                                   
REMARK 500    ALA A 409       97.77    -65.08                                   
REMARK 500    HIS A 492      107.49    -55.55                                   
REMARK 500    SER A 568       71.16     55.17                                   
REMARK 500    PHE A 622      -49.75   -132.39                                   
REMARK 500    ALA A 694     -129.24     51.68                                   
REMARK 500    ASN A 706       66.39   -112.34                                   
REMARK 500    PRO A 708     -156.39    -86.97                                   
REMARK 500    ARG A 709       48.09     39.88                                   
REMARK 500    LEU A 722      -64.19   -137.91                                   
REMARK 500    ASN A 731       70.34     53.21                                   
REMARK 500    GLU A 779     -110.85   -128.68                                   
REMARK 500    LEU A 808       79.03   -119.54                                   
REMARK 500    SER A 833       -3.97   -143.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A  378     PRO A  379                  -31.81                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B2504   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 647   O                                                      
REMARK 620 2 ASP B 647   OD1  70.4                                              
REMARK 620 3 ASP B 649   O    93.9  97.3                                        
REMARK 620 4 HIS B 651   O   156.7  88.7  78.3                                  
REMARK 620 5 SER B 670   OG   85.1 109.3 151.2 112.3                            
REMARK 620 6 LEU B 671   O    77.5 138.2  58.3 115.0  93.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 649   OD1                                                    
REMARK 620 2 HIS B 651   ND1  97.4                                              
REMARK 620 3 ASP B 742   OD2  90.8  81.2                                        
REMARK 620 4 TSN B2501   O1   95.5 118.7 158.0                                  
REMARK 620 5 TSN B2501   O2  170.4  90.4  95.8  75.8                            
REMARK 620 6 TSN B2501   N1  120.1  93.0 149.1  32.1  53.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B2503   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE B 660   O                                                      
REMARK 620 2 ASP B 663   O    73.6                                              
REMARK 620 3 VAL B 666   O   106.2  68.9                                        
REMARK 620 4 PHE B 699   O   153.1 133.2  89.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 902   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 647   O                                                      
REMARK 620 2 ASP A 647   OD1  73.7                                              
REMARK 620 3 ASP A 649   O    95.3  97.4                                        
REMARK 620 4 HIS A 651   O   157.9  85.9  78.5                                  
REMARK 620 5 SER A 670   OG   83.9 107.6 153.5 111.0                            
REMARK 620 6 LEU A 671   O    73.8 137.4  59.2 118.8  95.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 649   OD1                                                    
REMARK 620 2 HIS A 651   ND1 102.4                                              
REMARK 620 3 ASP A 742   OD2  89.9 108.0                                        
REMARK 620 4 TSN A 904   O2  158.4  94.6  97.6                                  
REMARK 620 5 TSN A 904   O1   96.5  97.2 152.0  67.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 903   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 660   O                                                      
REMARK 620 2 ASP A 663   O    74.0                                              
REMARK 620 3 VAL A 666   O   107.9  69.8                                        
REMARK 620 4 PHE A 699   O   158.1 124.5  90.9                                  
REMARK 620 5 HOH A1003   O    84.7  98.3 158.4  81.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TSN B 2501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 2503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 2504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MAL B 2505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 902                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 903                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TSN A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MAL A 905                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EEF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EEI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EEK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EEM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EEN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EF7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EF8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EFB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EFG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EFH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EFJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EFK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EFN   RELATED DB: PDB                                   
DBREF  5EDU B  109   474  UNP    P0AEY0   MALE_ECO57      27    392             
DBREF  5EDU B  479   835  UNP    Q9UBN7   HDAC6_HUMAN    479    835             
DBREF  5EDU A  109   474  UNP    P0AEY0   MALE_ECO57      27    392             
DBREF  5EDU A  479   835  UNP    Q9UBN7   HDAC6_HUMAN    479    835             
SEQADV 5EDU MET B   91  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU GLY B   92  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU SER B   93  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU SER B   94  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS B   95  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS B   96  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS B   97  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS B   98  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS B   99  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS B  100  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU GLU B  101  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU ASN B  102  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU LEU B  103  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU TYR B  104  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU PHE B  105  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU GLN B  106  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU GLY B  107  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU SER B  108  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU ALA B  467  UNP  P0AEY0    GLU   385 CONFLICT                       
SEQADV 5EDU ALA B  470  UNP  P0AEY0    LYS   388 CONFLICT                       
SEQADV 5EDU ALA B  471  UNP  P0AEY0    ASP   389 CONFLICT                       
SEQADV 5EDU ASN B  475  UNP  P0AEY0              LINKER                         
SEQADV 5EDU ALA B  476  UNP  P0AEY0              LINKER                         
SEQADV 5EDU ALA B  477  UNP  P0AEY0              LINKER                         
SEQADV 5EDU ALA B  478  UNP  P0AEY0              LINKER                         
SEQADV 5EDU MET A   91  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU GLY A   92  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU SER A   93  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU SER A   94  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS A   95  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS A   96  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS A   97  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS A   98  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS A   99  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU HIS A  100  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU GLU A  101  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU ASN A  102  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU LEU A  103  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU TYR A  104  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU PHE A  105  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU GLN A  106  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU GLY A  107  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU SER A  108  UNP  P0AEY0              EXPRESSION TAG                 
SEQADV 5EDU ALA A  467  UNP  P0AEY0    GLU   385 CONFLICT                       
SEQADV 5EDU ALA A  470  UNP  P0AEY0    LYS   388 CONFLICT                       
SEQADV 5EDU ALA A  471  UNP  P0AEY0    ASP   389 CONFLICT                       
SEQADV 5EDU ASN A  475  UNP  P0AEY0              LINKER                         
SEQADV 5EDU ALA A  476  UNP  P0AEY0              LINKER                         
SEQADV 5EDU ALA A  477  UNP  P0AEY0              LINKER                         
SEQADV 5EDU ALA A  478  UNP  P0AEY0              LINKER                         
SEQRES   1 B  745  MET GLY SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU          
SEQRES   2 B  745  TYR PHE GLN GLY SER LYS ILE GLU GLU GLY LYS LEU VAL          
SEQRES   3 B  745  ILE TRP ILE ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA          
SEQRES   4 B  745  GLU VAL GLY LYS LYS PHE GLU LYS ASP THR GLY ILE LYS          
SEQRES   5 B  745  VAL THR VAL GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE          
SEQRES   6 B  745  PRO GLN VAL ALA ALA THR GLY ASP GLY PRO ASP ILE ILE          
SEQRES   7 B  745  PHE TRP ALA HIS ASP ARG PHE GLY GLY TYR ALA GLN SER          
SEQRES   8 B  745  GLY LEU LEU ALA GLU ILE THR PRO ASP LYS ALA PHE GLN          
SEQRES   9 B  745  ASP LYS LEU TYR PRO PHE THR TRP ASP ALA VAL ARG TYR          
SEQRES  10 B  745  ASN GLY LYS LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA          
SEQRES  11 B  745  LEU SER LEU ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO          
SEQRES  12 B  745  PRO LYS THR TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU          
SEQRES  13 B  745  LEU LYS ALA LYS GLY LYS SER ALA LEU MET PHE ASN LEU          
SEQRES  14 B  745  GLN GLU PRO TYR PHE THR TRP PRO LEU ILE ALA ALA ASP          
SEQRES  15 B  745  GLY GLY TYR ALA PHE LYS TYR GLU ASN GLY LYS TYR ASP          
SEQRES  16 B  745  ILE LYS ASP VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA          
SEQRES  17 B  745  GLY LEU THR PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS          
SEQRES  18 B  745  MET ASN ALA ASP THR ASP TYR SER ILE ALA GLU ALA ALA          
SEQRES  19 B  745  PHE ASN LYS GLY GLU THR ALA MET THR ILE ASN GLY PRO          
SEQRES  20 B  745  TRP ALA TRP SER ASN ILE ASP THR SER LYS VAL ASN TYR          
SEQRES  21 B  745  GLY VAL THR VAL LEU PRO THR PHE LYS GLY GLN PRO SER          
SEQRES  22 B  745  LYS PRO PHE VAL GLY VAL LEU SER ALA GLY ILE ASN ALA          
SEQRES  23 B  745  ALA SER PRO ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU          
SEQRES  24 B  745  ASN TYR LEU LEU THR ASP GLU GLY LEU GLU ALA VAL ASN          
SEQRES  25 B  745  LYS ASP LYS PRO LEU GLY ALA VAL ALA LEU LYS SER TYR          
SEQRES  26 B  745  GLU GLU GLU LEU ALA LYS ASP PRO ARG ILE ALA ALA THR          
SEQRES  27 B  745  MET GLU ASN ALA GLN LYS GLY GLU ILE MET PRO ASN ILE          
SEQRES  28 B  745  PRO GLN MET SER ALA PHE TRP TYR ALA VAL ARG THR ALA          
SEQRES  29 B  745  VAL ILE ASN ALA ALA SER GLY ARG GLN THR VAL ASP ALA          
SEQRES  30 B  745  ALA LEU ALA ALA ALA GLN THR ASN ALA ALA ALA SER ARG          
SEQRES  31 B  745  THR GLY LEU VAL TYR ASP GLN ASN MET MET ASN HIS CYS          
SEQRES  32 B  745  ASN LEU TRP ASP SER HIS HIS PRO GLU VAL PRO GLN ARG          
SEQRES  33 B  745  ILE LEU ARG ILE MET CYS ARG LEU GLU GLU LEU GLY LEU          
SEQRES  34 B  745  ALA GLY ARG CYS LEU THR LEU THR PRO ARG PRO ALA THR          
SEQRES  35 B  745  GLU ALA GLU LEU LEU THR CYS HIS SER ALA GLU TYR VAL          
SEQRES  36 B  745  GLY HIS LEU ARG ALA THR GLU LYS MET LYS THR ARG GLU          
SEQRES  37 B  745  LEU HIS ARG GLU SER SER ASN PHE ASP SER ILE TYR ILE          
SEQRES  38 B  745  CYS PRO SER THR PHE ALA CYS ALA GLN LEU ALA THR GLY          
SEQRES  39 B  745  ALA ALA CYS ARG LEU VAL GLU ALA VAL LEU SER GLY GLU          
SEQRES  40 B  745  VAL LEU ASN GLY ALA ALA VAL VAL ARG PRO PRO GLY HIS          
SEQRES  41 B  745  HIS ALA GLU GLN ASP ALA ALA CYS GLY PHE CYS PHE PHE          
SEQRES  42 B  745  ASN SER VAL ALA VAL ALA ALA ARG HIS ALA GLN THR ILE          
SEQRES  43 B  745  SER GLY HIS ALA LEU ARG ILE LEU ILE VAL ASP TRP ASP          
SEQRES  44 B  745  VAL HIS HIS GLY ASN GLY THR GLN HIS MET PHE GLU ASP          
SEQRES  45 B  745  ASP PRO SER VAL LEU TYR VAL SER LEU HIS ARG TYR ASP          
SEQRES  46 B  745  HIS GLY THR PHE PHE PRO MET GLY ASP GLU GLY ALA SER          
SEQRES  47 B  745  SER GLN ILE GLY ARG ALA ALA GLY THR GLY PHE THR VAL          
SEQRES  48 B  745  ASN VAL ALA TRP ASN GLY PRO ARG MET GLY ASP ALA ASP          
SEQRES  49 B  745  TYR LEU ALA ALA TRP HIS ARG LEU VAL LEU PRO ILE ALA          
SEQRES  50 B  745  TYR GLU PHE ASN PRO GLU LEU VAL LEU VAL SER ALA GLY          
SEQRES  51 B  745  PHE ASP ALA ALA ARG GLY ASP PRO LEU GLY GLY CYS GLN          
SEQRES  52 B  745  VAL SER PRO GLU GLY TYR ALA HIS LEU THR HIS LEU LEU          
SEQRES  53 B  745  MET GLY LEU ALA SER GLY ARG ILE ILE LEU ILE LEU GLU          
SEQRES  54 B  745  GLY GLY TYR ASN LEU THR SER ILE SER GLU SER MET ALA          
SEQRES  55 B  745  ALA CYS THR ARG SER LEU LEU GLY ASP PRO PRO PRO LEU          
SEQRES  56 B  745  LEU THR LEU PRO ARG PRO PRO LEU SER GLY ALA LEU ALA          
SEQRES  57 B  745  SER ILE THR GLU THR ILE GLN VAL HIS ARG ARG TYR TRP          
SEQRES  58 B  745  ARG SER LEU ARG                                              
SEQRES   1 A  745  MET GLY SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU          
SEQRES   2 A  745  TYR PHE GLN GLY SER LYS ILE GLU GLU GLY LYS LEU VAL          
SEQRES   3 A  745  ILE TRP ILE ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA          
SEQRES   4 A  745  GLU VAL GLY LYS LYS PHE GLU LYS ASP THR GLY ILE LYS          
SEQRES   5 A  745  VAL THR VAL GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE          
SEQRES   6 A  745  PRO GLN VAL ALA ALA THR GLY ASP GLY PRO ASP ILE ILE          
SEQRES   7 A  745  PHE TRP ALA HIS ASP ARG PHE GLY GLY TYR ALA GLN SER          
SEQRES   8 A  745  GLY LEU LEU ALA GLU ILE THR PRO ASP LYS ALA PHE GLN          
SEQRES   9 A  745  ASP LYS LEU TYR PRO PHE THR TRP ASP ALA VAL ARG TYR          
SEQRES  10 A  745  ASN GLY LYS LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA          
SEQRES  11 A  745  LEU SER LEU ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO          
SEQRES  12 A  745  PRO LYS THR TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU          
SEQRES  13 A  745  LEU LYS ALA LYS GLY LYS SER ALA LEU MET PHE ASN LEU          
SEQRES  14 A  745  GLN GLU PRO TYR PHE THR TRP PRO LEU ILE ALA ALA ASP          
SEQRES  15 A  745  GLY GLY TYR ALA PHE LYS TYR GLU ASN GLY LYS TYR ASP          
SEQRES  16 A  745  ILE LYS ASP VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA          
SEQRES  17 A  745  GLY LEU THR PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS          
SEQRES  18 A  745  MET ASN ALA ASP THR ASP TYR SER ILE ALA GLU ALA ALA          
SEQRES  19 A  745  PHE ASN LYS GLY GLU THR ALA MET THR ILE ASN GLY PRO          
SEQRES  20 A  745  TRP ALA TRP SER ASN ILE ASP THR SER LYS VAL ASN TYR          
SEQRES  21 A  745  GLY VAL THR VAL LEU PRO THR PHE LYS GLY GLN PRO SER          
SEQRES  22 A  745  LYS PRO PHE VAL GLY VAL LEU SER ALA GLY ILE ASN ALA          
SEQRES  23 A  745  ALA SER PRO ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU          
SEQRES  24 A  745  ASN TYR LEU LEU THR ASP GLU GLY LEU GLU ALA VAL ASN          
SEQRES  25 A  745  LYS ASP LYS PRO LEU GLY ALA VAL ALA LEU LYS SER TYR          
SEQRES  26 A  745  GLU GLU GLU LEU ALA LYS ASP PRO ARG ILE ALA ALA THR          
SEQRES  27 A  745  MET GLU ASN ALA GLN LYS GLY GLU ILE MET PRO ASN ILE          
SEQRES  28 A  745  PRO GLN MET SER ALA PHE TRP TYR ALA VAL ARG THR ALA          
SEQRES  29 A  745  VAL ILE ASN ALA ALA SER GLY ARG GLN THR VAL ASP ALA          
SEQRES  30 A  745  ALA LEU ALA ALA ALA GLN THR ASN ALA ALA ALA SER ARG          
SEQRES  31 A  745  THR GLY LEU VAL TYR ASP GLN ASN MET MET ASN HIS CYS          
SEQRES  32 A  745  ASN LEU TRP ASP SER HIS HIS PRO GLU VAL PRO GLN ARG          
SEQRES  33 A  745  ILE LEU ARG ILE MET CYS ARG LEU GLU GLU LEU GLY LEU          
SEQRES  34 A  745  ALA GLY ARG CYS LEU THR LEU THR PRO ARG PRO ALA THR          
SEQRES  35 A  745  GLU ALA GLU LEU LEU THR CYS HIS SER ALA GLU TYR VAL          
SEQRES  36 A  745  GLY HIS LEU ARG ALA THR GLU LYS MET LYS THR ARG GLU          
SEQRES  37 A  745  LEU HIS ARG GLU SER SER ASN PHE ASP SER ILE TYR ILE          
SEQRES  38 A  745  CYS PRO SER THR PHE ALA CYS ALA GLN LEU ALA THR GLY          
SEQRES  39 A  745  ALA ALA CYS ARG LEU VAL GLU ALA VAL LEU SER GLY GLU          
SEQRES  40 A  745  VAL LEU ASN GLY ALA ALA VAL VAL ARG PRO PRO GLY HIS          
SEQRES  41 A  745  HIS ALA GLU GLN ASP ALA ALA CYS GLY PHE CYS PHE PHE          
SEQRES  42 A  745  ASN SER VAL ALA VAL ALA ALA ARG HIS ALA GLN THR ILE          
SEQRES  43 A  745  SER GLY HIS ALA LEU ARG ILE LEU ILE VAL ASP TRP ASP          
SEQRES  44 A  745  VAL HIS HIS GLY ASN GLY THR GLN HIS MET PHE GLU ASP          
SEQRES  45 A  745  ASP PRO SER VAL LEU TYR VAL SER LEU HIS ARG TYR ASP          
SEQRES  46 A  745  HIS GLY THR PHE PHE PRO MET GLY ASP GLU GLY ALA SER          
SEQRES  47 A  745  SER GLN ILE GLY ARG ALA ALA GLY THR GLY PHE THR VAL          
SEQRES  48 A  745  ASN VAL ALA TRP ASN GLY PRO ARG MET GLY ASP ALA ASP          
SEQRES  49 A  745  TYR LEU ALA ALA TRP HIS ARG LEU VAL LEU PRO ILE ALA          
SEQRES  50 A  745  TYR GLU PHE ASN PRO GLU LEU VAL LEU VAL SER ALA GLY          
SEQRES  51 A  745  PHE ASP ALA ALA ARG GLY ASP PRO LEU GLY GLY CYS GLN          
SEQRES  52 A  745  VAL SER PRO GLU GLY TYR ALA HIS LEU THR HIS LEU LEU          
SEQRES  53 A  745  MET GLY LEU ALA SER GLY ARG ILE ILE LEU ILE LEU GLU          
SEQRES  54 A  745  GLY GLY TYR ASN LEU THR SER ILE SER GLU SER MET ALA          
SEQRES  55 A  745  ALA CYS THR ARG SER LEU LEU GLY ASP PRO PRO PRO LEU          
SEQRES  56 A  745  LEU THR LEU PRO ARG PRO PRO LEU SER GLY ALA LEU ALA          
SEQRES  57 A  745  SER ILE THR GLU THR ILE GLN VAL HIS ARG ARG TYR TRP          
SEQRES  58 A  745  ARG SER LEU ARG                                              
HET    TSN  B2501      22                                                       
HET     ZN  B2502       1                                                       
HET      K  B2503       1                                                       
HET      K  B2504       1                                                       
HET    MAL  B2505      23                                                       
HET     ZN  A 901       1                                                       
HET      K  A 902       1                                                       
HET      K  A 903       1                                                       
HET    TSN  A 904      22                                                       
HET    MAL  A 905      23                                                       
HETNAM     TSN TRICHOSTATIN A                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM       K POTASSIUM ION                                                    
HETNAM     MAL MALTOSE                                                          
HETSYN     TSN 7-[4-(DIMETHYLAMINO)PHENYL]-N-HYDROXY-4,6-DIMETHYL-7-            
HETSYN   2 TSN  OXO-2,4-HEPTADIENAMIDE                                          
FORMUL   3  TSN    2(C17 H22 N2 O3)                                             
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   5    K    4(K 1+)                                                      
FORMUL   7  MAL    2(C12 H22 O11)                                               
FORMUL  13  HOH   *58(H2 O)                                                     
HELIX    1 AA1 GLY B  124  GLY B  140  1                                  17    
HELIX    2 AA2 LYS B  150  THR B  161  1                                  12    
HELIX    3 AA3 ARG B  174  SER B  181  1                                   8    
HELIX    4 AA4 ASP B  190  ASP B  195  1                                   6    
HELIX    5 AA5 TYR B  198  VAL B  205  1                                   8    
HELIX    6 AA6 THR B  236  GLU B  238  5                                   3    
HELIX    7 AA7 GLU B  239  ALA B  249  1                                  11    
HELIX    8 AA8 THR B  265  ALA B  270  1                                   6    
HELIX    9 AA9 ASN B  293  ASN B  309  1                                  17    
HELIX   10 AB1 ASP B  317  LYS B  327  1                                  11    
HELIX   11 AB2 GLY B  336  TRP B  338  5                                   3    
HELIX   12 AB3 ALA B  339  SER B  346  1                                   8    
HELIX   13 AB4 ASN B  380  TYR B  391  1                                  12    
HELIX   14 AB5 THR B  394  LYS B  405  1                                  12    
HELIX   15 AB6 LEU B  412  ALA B  420  1                                   9    
HELIX   16 AB7 ASP B  422  GLY B  435  1                                  14    
HELIX   17 AB8 GLN B  443  ALA B  459  1                                  17    
HELIX   18 AB9 THR B  464  THR B  474  1                                  11    
HELIX   19 AC1 ASP B  486  ASN B  491  5                                   6    
HELIX   20 AC2 PRO B  504  LEU B  517  1                                  14    
HELIX   21 AC3 THR B  532  LEU B  537  1                                   6    
HELIX   22 AC4 SER B  541  THR B  551  1                                  11    
HELIX   23 AC5 GLU B  552  MET B  554  5                                   3    
HELIX   24 AC6 LYS B  555  SER B  564  1                                  10    
HELIX   25 AC7 SER B  574  LEU B  594  1                                  21    
HELIX   26 AC8 ASN B  624  GLY B  638  1                                  15    
HELIX   27 AC9 GLY B  653  PHE B  660  1                                   8    
HELIX   28 AD1 ARG B  693  THR B  697  5                                   5    
HELIX   29 AD2 GLY B  711  LEU B  722  1                                  12    
HELIX   30 AD3 LEU B  722  ASN B  731  1                                  10    
HELIX   31 AD4 SER B  755  MET B  767  1                                  13    
HELIX   32 AD5 GLY B  768  GLY B  772  5                                   5    
HELIX   33 AD6 ASN B  783  LEU B  799  1                                  17    
HELIX   34 AD7 LEU B  813  ARG B  828  1                                  16    
HELIX   35 AD8 GLY A  124  GLY A  132  1                                   9    
HELIX   36 AD9 LYS A  150  ALA A  160  1                                  11    
HELIX   37 AE1 ARG A  174  GLY A  182  1                                   9    
HELIX   38 AE2 TYR A  198  ASP A  203  1                                   6    
HELIX   39 AE3 THR A  236  GLU A  238  5                                   3    
HELIX   40 AE4 GLU A  239  LYS A  248  1                                  10    
HELIX   41 AE5 ALA A  249  GLY A  251  5                                   3    
HELIX   42 AE6 THR A  265  ALA A  270  1                                   6    
HELIX   43 AE7 ASN A  293  ASN A  309  1                                  17    
HELIX   44 AE8 ASP A  317  LYS A  327  1                                  11    
HELIX   45 AE9 GLY A  336  TRP A  338  5                                   3    
HELIX   46 AF1 ALA A  339  THR A  345  1                                   7    
HELIX   47 AF2 ASN A  380  LEU A  392  1                                  13    
HELIX   48 AF3 THR A  394  LYS A  403  1                                  10    
HELIX   49 AF4 LEU A  412  GLU A  417  1                                   6    
HELIX   50 AF5 ASP A  422  LYS A  434  1                                  13    
HELIX   51 AF6 GLN A  443  SER A  460  1                                  18    
HELIX   52 AF7 THR A  464  ALA A  477  1                                  14    
HELIX   53 AF8 ASP A  486  ASN A  491  5                                   6    
HELIX   54 AF9 PRO A  504  LEU A  517  1                                  14    
HELIX   55 AG1 GLY A  518  CYS A  523  1                                   6    
HELIX   56 AG2 THR A  532  LEU A  537  1                                   6    
HELIX   57 AG3 SER A  541  ALA A  550  1                                  10    
HELIX   58 AG4 THR A  551  MET A  554  5                                   4    
HELIX   59 AG5 LYS A  555  SER A  564  1                                  10    
HELIX   60 AG6 SER A  574  SER A  595  1                                  22    
HELIX   61 AG7 ASN A  624  ILE A  636  1                                  13    
HELIX   62 AG8 GLY A  653  PHE A  660  1                                   8    
HELIX   63 AG9 ASP A  675  THR A  678  5                                   4    
HELIX   64 AH1 ARG A  693  THR A  697  5                                   5    
HELIX   65 AH2 GLY A  711  LEU A  722  1                                  12    
HELIX   66 AH3 LEU A  722  ASN A  731  1                                  10    
HELIX   67 AH4 SER A  755  MET A  767  1                                  13    
HELIX   68 AH5 GLY A  768  GLY A  772  5                                   5    
HELIX   69 AH6 ASN A  783  LEU A  799  1                                  17    
HELIX   70 AH7 LEU A  813  HIS A  827  1                                  15    
SHEET    1 AA1 6 VAL B 143  GLU B 146  0                                        
SHEET    2 AA1 6 LEU B 115  TRP B 118  1  N  ILE B 117   O  THR B 144           
SHEET    3 AA1 6 ILE B 167  ALA B 171  1  O  ILE B 167   N  TRP B 118           
SHEET    4 AA1 6 PHE B 366  ILE B 374 -1  O  SER B 371   N  TRP B 170           
SHEET    5 AA1 6 TYR B 214  GLU B 219 -1  N  TYR B 214   O  ALA B 372           
SHEET    6 AA1 6 ALA B 409  VAL B 410 -1  O  ALA B 409   N  VAL B 218           
SHEET    1 AA2 5 VAL B 143  GLU B 146  0                                        
SHEET    2 AA2 5 LEU B 115  TRP B 118  1  N  ILE B 117   O  THR B 144           
SHEET    3 AA2 5 ILE B 167  ALA B 171  1  O  ILE B 167   N  TRP B 118           
SHEET    4 AA2 5 PHE B 366  ILE B 374 -1  O  SER B 371   N  TRP B 170           
SHEET    5 AA2 5 GLU B 436  ILE B 437  1  O  GLU B 436   N  VAL B 367           
SHEET    1 AA3 2 ARG B 206  TYR B 207  0                                        
SHEET    2 AA3 2 LYS B 210  LEU B 211 -1  O  LYS B 210   N  TYR B 207           
SHEET    1 AA4 4 SER B 253  LEU B 255  0                                        
SHEET    2 AA4 4 THR B 330  ASN B 335  1  O  MET B 332   N  ALA B 254           
SHEET    3 AA4 4 SER B 222  ASN B 226 -1  N  ASN B 226   O  ALA B 331           
SHEET    4 AA4 4 TYR B 350  THR B 353 -1  O  GLY B 351   N  TYR B 225           
SHEET    1 AA5 2 TYR B 275  GLU B 280  0                                        
SHEET    2 AA5 2 LYS B 283  GLY B 290 -1  O  GLY B 290   N  TYR B 275           
SHEET    1 AA6 8 LEU B 524  LEU B 526  0                                        
SHEET    2 AA6 8 THR B 481  VAL B 484  1  N  LEU B 483   O  LEU B 526           
SHEET    3 AA6 8 ASN B 600  ALA B 603  1  O  ASN B 600   N  GLY B 482           
SHEET    4 AA6 8 ILE B 774  LEU B 778  1  O  LEU B 776   N  ALA B 603           
SHEET    5 AA6 8 LEU B 734  ALA B 739  1  N  VAL B 737   O  ILE B 775           
SHEET    6 AA6 8 ILE B 643  ASP B 647  1  N  LEU B 644   O  LEU B 736           
SHEET    7 AA6 8 VAL B 666  ARG B 673  1  O  VAL B 669   N  ILE B 645           
SHEET    8 AA6 8 THR B 700  TRP B 705  1  O  TRP B 705   N  HIS B 672           
SHEET    1 AA7 6 VAL A 143  GLU A 146  0                                        
SHEET    2 AA7 6 LEU A 115  TRP A 118  1  N  ILE A 117   O  GLU A 146           
SHEET    3 AA7 6 ILE A 167  ALA A 171  1  O  PHE A 169   N  TRP A 118           
SHEET    4 AA7 6 GLY A 368  ILE A 374 -1  O  GLY A 373   N  ILE A 168           
SHEET    5 AA7 6 TYR A 214  GLU A 219 -1  N  ILE A 216   O  LEU A 370           
SHEET    6 AA7 6 ALA A 409  VAL A 410 -1  O  ALA A 409   N  VAL A 218           
SHEET    1 AA8 2 ARG A 206  TYR A 207  0                                        
SHEET    2 AA8 2 LYS A 210  LEU A 211 -1  O  LYS A 210   N  TYR A 207           
SHEET    1 AA9 4 SER A 253  LEU A 255  0                                        
SHEET    2 AA9 4 THR A 330  ASN A 335  1  O  ALA A 331   N  SER A 253           
SHEET    3 AA9 4 SER A 222  ASN A 226 -1  N  ILE A 224   O  THR A 333           
SHEET    4 AA9 4 TYR A 350  THR A 353 -1  O  THR A 353   N  LEU A 223           
SHEET    1 AB1 2 TYR A 275  GLU A 280  0                                        
SHEET    2 AB1 2 LYS A 283  GLY A 290 -1  O  ASP A 285   N  LYS A 278           
SHEET    1 AB2 8 LEU A 524  LEU A 526  0                                        
SHEET    2 AB2 8 THR A 481  VAL A 484  1  N  THR A 481   O  LEU A 524           
SHEET    3 AB2 8 ASN A 600  ALA A 603  1  O  ASN A 600   N  GLY A 482           
SHEET    4 AB2 8 ILE A 774  LEU A 778  1  O  LEU A 776   N  ALA A 603           
SHEET    5 AB2 8 LEU A 734  ALA A 739  1  N  VAL A 737   O  ILE A 777           
SHEET    6 AB2 8 ILE A 643  ASP A 647  1  N  LEU A 644   O  LEU A 736           
SHEET    7 AB2 8 VAL A 666  ARG A 673  1  O  VAL A 669   N  ASP A 647           
SHEET    8 AB2 8 THR A 700  TRP A 705  1  O  VAL A 701   N  TYR A 668           
LINK         O   ASP B 647                 K     K B2504     1555   1555  2.77  
LINK         OD1 ASP B 647                 K     K B2504     1555   1555  2.80  
LINK         O   ASP B 649                 K     K B2504     1555   1555  2.79  
LINK         OD1 ASP B 649                ZN    ZN B2502     1555   1555  2.16  
LINK         O   HIS B 651                 K     K B2504     1555   1555  2.79  
LINK         ND1 HIS B 651                ZN    ZN B2502     1555   1555  2.20  
LINK         O   PHE B 660                 K     K B2503     1555   1555  2.79  
LINK         O   ASP B 663                 K     K B2503     1555   1555  3.16  
LINK         O   VAL B 666                 K     K B2503     1555   1555  2.87  
LINK         OG  SER B 670                 K     K B2504     1555   1555  2.78  
LINK         O   LEU B 671                 K     K B2504     1555   1555  3.01  
LINK         O   PHE B 699                 K     K B2503     1555   1555  2.77  
LINK         OD2 ASP B 742                ZN    ZN B2502     1555   1555  2.06  
LINK         O   ASP A 647                 K     K A 902     1555   1555  2.83  
LINK         OD1 ASP A 647                 K     K A 902     1555   1555  2.79  
LINK         O   ASP A 649                 K     K A 902     1555   1555  2.79  
LINK         OD1 ASP A 649                ZN    ZN A 901     1555   1555  2.18  
LINK         O   HIS A 651                 K     K A 902     1555   1555  2.85  
LINK         ND1 HIS A 651                ZN    ZN A 901     1555   1555  2.11  
LINK         O   PHE A 660                 K     K A 903     1555   1555  2.69  
LINK         O   ASP A 663                 K     K A 903     1555   1555  3.07  
LINK         O   VAL A 666                 K     K A 903     1555   1555  2.78  
LINK         OG  SER A 670                 K     K A 902     1555   1555  2.79  
LINK         O   LEU A 671                 K     K A 902     1555   1555  2.94  
LINK         O   PHE A 699                 K     K A 903     1555   1555  2.75  
LINK         OD2 ASP A 742                ZN    ZN A 901     1555   1555  2.06  
LINK         O1  TSN B2501                ZN    ZN B2502     1555   1555  2.02  
LINK         O2  TSN B2501                ZN    ZN B2502     1555   1555  2.30  
LINK         N1  TSN B2501                ZN    ZN B2502     1555   1555  2.60  
LINK        ZN    ZN A 901                 O2  TSN A 904     1555   1555  2.59  
LINK        ZN    ZN A 901                 O1  TSN A 904     1555   1555  2.17  
LINK         K     K A 903                 O   HOH A1003     1555   1555  3.05  
CISPEP   1 ARG B  606    PRO B  607          0         3.20                     
CISPEP   2 PHE B  680    PRO B  681          0         5.36                     
CISPEP   3 ARG A  606    PRO A  607          0         1.86                     
CISPEP   4 PHE A  680    PRO A  681          0         3.27                     
SITE     1 AC1 11 PRO B 501  HIS B 610  HIS B 611  PHE B 620                    
SITE     2 AC1 11 ASP B 649  HIS B 651  PHE B 680  ASP B 742                    
SITE     3 AC1 11 LEU B 749  TYR B 782   ZN B2502                               
SITE     1 AC2  4 ASP B 649  HIS B 651  ASP B 742  TSN B2501                    
SITE     1 AC3  4 PHE B 660  ASP B 663  VAL B 666  PHE B 699                    
SITE     1 AC4  5 ASP B 647  ASP B 649  HIS B 651  SER B 670                    
SITE     2 AC4  5 LEU B 671                                                     
SITE     1 AC5 12 ASN B 120  ASP B 122  LYS B 123  TRP B 170                    
SITE     2 AC5 12 ALA B 171  ASP B 173  ARG B 174  GLU B 219                    
SITE     3 AC5 12 GLU B 261  PRO B 262  TYR B 263  TRP B 448                    
SITE     1 AC6  4 ASP A 649  HIS A 651  ASP A 742  TSN A 904                    
SITE     1 AC7  5 ASP A 647  ASP A 649  HIS A 651  SER A 670                    
SITE     2 AC7  5 LEU A 671                                                     
SITE     1 AC8  5 PHE A 660  ASP A 663  VAL A 666  PHE A 699                    
SITE     2 AC8  5 HOH A1003                                                     
SITE     1 AC9 12 HIS A 500  PRO A 501  HIS A 610  HIS A 611                    
SITE     2 AC9 12 PHE A 620  ASP A 649  HIS A 651  PHE A 680                    
SITE     3 AC9 12 ASP A 742  TYR A 782  PRO A 809   ZN A 901                    
SITE     1 AD1 11 LYS A 123  TRP A 170  ALA A 171  ASP A 173                    
SITE     2 AD1 11 ARG A 174  GLU A 219  GLU A 261  PRO A 262                    
SITE     3 AD1 11 TYR A 263  TRP A 338  TRP A 448                               
CRYST1   49.262  149.032  216.333  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020300  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006710  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004623        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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