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Database: PDB
Entry: 3ZNR
LinkDB: 3ZNR
Original site: 3ZNR 
HEADER    HYDROLASE                               15-FEB-13   3ZNR              
TITLE     HDAC7 BOUND WITH INHIBITOR TMP269                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE DEACETYLASE 7;                                     
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 482-903;                        
COMPND   5 SYNONYM: HDAC7, HD7, HISTONE DEACETYLASE 7A, HD7A;                   
COMPND   6 EC: 3.5.1.98;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: LIGAND IS A TFMO INHIBITOR                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, CLASS IIA HDACS, TFMO                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.LOBERA,K.MADAUSS,D.POHLHAUS,R.TRUMP,M.NOLAN                         
REVDAT   3   01-MAY-13 3ZNR    1       JRNL   HETATM                            
REVDAT   2   03-APR-13 3ZNR    1       JRNL                                     
REVDAT   1   27-MAR-13 3ZNR    0                                                
JRNL        AUTH   M.LOBERA,K.P.MADAUSS,D.T.POHLHAUS,Q.G.WRIGHT,M.TROCHA,       
JRNL        AUTH 2 D.R.SCHMIDT,E.BALOGLU,R.P.TRUMP,M.S.HEAD,G.A.HOFMANN,        
JRNL        AUTH 3 M.MURRAY-THOMPSON,B.SCHWARTZ,S.CHAKRAVORTY,Z.WU,P.K.MANDER,  
JRNL        AUTH 4 L.KRUIDENIER,R.A.REID,W.BURKHART,B.J.TURUNEN,J.X.RONG,       
JRNL        AUTH 5 C.WAGNER,M.B.MOYER,C.WELLS,X.HONG,J.T.MOORE,J.D.WILLIAMS,    
JRNL        AUTH 6 D.SOLER,S.GHOSH,M.A.NOLAN                                    
JRNL        TITL   SELECTIVE CLASS IIA HISTONE DEACETYLASE INHIBITION VIA A     
JRNL        TITL 2 NON-CHELATING ZINC BINDING GROUP                             
JRNL        REF    NAT.CHEM.BIOL.                V.   9   319 2013              
JRNL        REFN                   ISSN 1552-4450                               
JRNL        PMID   23524983                                                     
JRNL        DOI    10.1038/NCHEMBIO.1223                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.33                          
REMARK   3   NUMBER OF REFLECTIONS             : 40790                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.21385                         
REMARK   3   R VALUE            (WORKING SET) : 0.21235                         
REMARK   3   FREE R VALUE                     : 0.24102                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2165                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.400                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.462                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3017                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.304                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 156                          
REMARK   3   BIN FREE R VALUE                    : 0.344                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8362                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 44                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.375                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.27                                                 
REMARK   3    B22 (A**2) : 2.27                                                 
REMARK   3    B33 (A**2) : -3.40                                                
REMARK   3    B12 (A**2) : 1.13                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.572         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.269         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.222         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.381        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8605 ; 0.005 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  5670 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11691 ; 0.812 ; 1.938       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13765 ; 0.765 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1106 ; 4.545 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   389 ;35.540 ;23.753       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1295 ;12.279 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;12.384 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1258 ; 0.045 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9867 ; 0.002 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1786 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5474 ; 0.130 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2279 ; 0.014 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8694 ; 0.245 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3131 ; 0.277 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2995 ; 0.467 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS.COMPLETE LIGAND DENISTY NOT SEEN IN ALL SUBUNITS.        
REMARK   4                                                                      
REMARK   4 3ZNR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-FEB-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-55844.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MX-300)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40790                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.35                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.4                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.60                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.10                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.51000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       49.75500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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   481                                                      
REMARK 465     SER A   482                                                      
REMARK 465     ARG A   483                                                      
REMARK 465     ALA A   484                                                      
REMARK 465     GLN A   485                                                      
REMARK 465     SER A   486                                                      
REMARK 465     SER A   487                                                      
REMARK 465     PRO A   488                                                      
REMARK 465     ALA A   489                                                      
REMARK 465     ALA A   490                                                      
REMARK 465     PRO A   491                                                      
REMARK 465     ALA A   492                                                      
REMARK 465     SER A   493                                                      
REMARK 465     LEU A   494                                                      
REMARK 465     SER A   495                                                      
REMARK 465     ALA A   496                                                      
REMARK 465     PRO A   497                                                      
REMARK 465     GLU A   498                                                      
REMARK 465     PRO A   499                                                      
REMARK 465     ALA A   500                                                      
REMARK 465     SER A   501                                                      
REMARK 465     GLN A   502                                                      
REMARK 465     ALA A   503                                                      
REMARK 465     ARG A   504                                                      
REMARK 465     VAL A   505                                                      
REMARK 465     LEU A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     SER A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     GLU A   510                                                      
REMARK 465     THR A   511                                                      
REMARK 465     PRO A   512                                                      
REMARK 465     ALA A   513                                                      
REMARK 465     ARG A   514                                                      
REMARK 465     THR A   515                                                      
REMARK 465     ARG A   596                                                      
REMARK 465     LEU A   597                                                      
REMARK 465     LYS A   598                                                      
REMARK 465     LEU A   599                                                      
REMARK 465     ASP A   600                                                      
REMARK 465     ASN A   601                                                      
REMARK 465     GLY A   602                                                      
REMARK 465     LYS A   603                                                      
REMARK 465     LEU A   604                                                      
REMARK 465     ALA A   605                                                      
REMARK 465     GLY A   606                                                      
REMARK 465     LEU A   607                                                      
REMARK 465     LEU A   608                                                      
REMARK 465     ALA A   609                                                      
REMARK 465     GLN A   610                                                      
REMARK 465     ARG A   611                                                      
REMARK 465     MET A   612                                                      
REMARK 465     PHE A   613                                                      
REMARK 465     ALA A   902                                                      
REMARK 465     SER A   903                                                      
REMARK 465     GLY B   481                                                      
REMARK 465     SER B   482                                                      
REMARK 465     ARG B   483                                                      
REMARK 465     ALA B   484                                                      
REMARK 465     GLN B   485                                                      
REMARK 465     SER B   486                                                      
REMARK 465     SER B   487                                                      
REMARK 465     PRO B   488                                                      
REMARK 465     ALA B   489                                                      
REMARK 465     ALA B   490                                                      
REMARK 465     PRO B   491                                                      
REMARK 465     ALA B   492                                                      
REMARK 465     SER B   493                                                      
REMARK 465     LEU B   494                                                      
REMARK 465     SER B   495                                                      
REMARK 465     ALA B   496                                                      
REMARK 465     PRO B   497                                                      
REMARK 465     GLU B   498                                                      
REMARK 465     PRO B   499                                                      
REMARK 465     ALA B   500                                                      
REMARK 465     SER B   501                                                      
REMARK 465     GLN B   502                                                      
REMARK 465     ALA B   503                                                      
REMARK 465     ARG B   504                                                      
REMARK 465     VAL B   505                                                      
REMARK 465     LEU B   506                                                      
REMARK 465     SER B   507                                                      
REMARK 465     SER B   508                                                      
REMARK 465     SER B   509                                                      
REMARK 465     GLU B   510                                                      
REMARK 465     THR B   511                                                      
REMARK 465     PRO B   512                                                      
REMARK 465     ALA B   513                                                      
REMARK 465     ARG B   514                                                      
REMARK 465     THR B   515                                                      
REMARK 465     LEU B   516                                                      
REMARK 465     ARG B   611                                                      
REMARK 465     MET B   612                                                      
REMARK 465     PHE B   613                                                      
REMARK 465     LEU B   901                                                      
REMARK 465     ALA B   902                                                      
REMARK 465     SER B   903                                                      
REMARK 465     GLY C   481                                                      
REMARK 465     SER C   482                                                      
REMARK 465     ARG C   483                                                      
REMARK 465     ALA C   484                                                      
REMARK 465     GLN C   485                                                      
REMARK 465     SER C   486                                                      
REMARK 465     SER C   487                                                      
REMARK 465     PRO C   488                                                      
REMARK 465     ALA C   489                                                      
REMARK 465     ALA C   490                                                      
REMARK 465     PRO C   491                                                      
REMARK 465     ALA C   492                                                      
REMARK 465     SER C   493                                                      
REMARK 465     LEU C   494                                                      
REMARK 465     SER C   495                                                      
REMARK 465     ALA C   496                                                      
REMARK 465     PRO C   497                                                      
REMARK 465     GLU C   498                                                      
REMARK 465     PRO C   499                                                      
REMARK 465     ALA C   500                                                      
REMARK 465     SER C   501                                                      
REMARK 465     GLN C   502                                                      
REMARK 465     ALA C   503                                                      
REMARK 465     ARG C   504                                                      
REMARK 465     VAL C   505                                                      
REMARK 465     LEU C   506                                                      
REMARK 465     SER C   507                                                      
REMARK 465     SER C   508                                                      
REMARK 465     SER C   509                                                      
REMARK 465     GLU C   510                                                      
REMARK 465     THR C   511                                                      
REMARK 465     PRO C   512                                                      
REMARK 465     ALA C   513                                                      
REMARK 465     ARG C   514                                                      
REMARK 465     THR C   515                                                      
REMARK 465     LEU C   516                                                      
REMARK 465     PRO C   517                                                      
REMARK 465     PHE C   518                                                      
REMARK 465     LEU C   594                                                      
REMARK 465     SER C   595                                                      
REMARK 465     ARG C   596                                                      
REMARK 465     LEU C   597                                                      
REMARK 465     LYS C   598                                                      
REMARK 465     LEU C   599                                                      
REMARK 465     ASP C   600                                                      
REMARK 465     ASN C   601                                                      
REMARK 465     GLY C   602                                                      
REMARK 465     LYS C   603                                                      
REMARK 465     LEU C   604                                                      
REMARK 465     ALA C   605                                                      
REMARK 465     GLY C   606                                                      
REMARK 465     LEU C   607                                                      
REMARK 465     LEU C   608                                                      
REMARK 465     ALA C   609                                                      
REMARK 465     GLN C   610                                                      
REMARK 465     ARG C   611                                                      
REMARK 465     MET C   612                                                      
REMARK 465     PHE C   613                                                      
REMARK 465     VAL C   614                                                      
REMARK 465     MET C   615                                                      
REMARK 465     ARG C   900                                                      
REMARK 465     LEU C   901                                                      
REMARK 465     ALA C   902                                                      
REMARK 465     SER C   903                                                      
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 568    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 583    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 584    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 867    CG   CD1  CD2                                       
REMARK 470     GLU A 870    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 875    CG   CD   CE   NZ                                   
REMARK 470     ARG A 889    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B 517    CG   CD                                             
REMARK 470     ARG B 596    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS B 598    CG   CD   CE   NZ                                   
REMARK 470     ARG B 655    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 818    CD   CE   NZ                                        
REMARK 470     ARG B 900    NE   CZ   NH1  NH2                                  
REMARK 470     GLU C 575    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 697    CG   CD   CE   NZ                                   
REMARK 470     GLN C 716    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 870    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 873    CG   CD   CE   NZ                                   
REMARK 470     LYS C 875    CG   CD   CE   NZ                                   
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    HIS A 531       98.64    -69.61                                   
REMARK 500    PHE A 681      -53.34   -127.09                                   
REMARK 500    ASN A 736       44.36    -96.22                                   
REMARK 500    SER A 790       70.29     58.95                                   
REMARK 500    PRO A 809       44.36    -97.43                                   
REMARK 500    GLU A 840      -99.57   -120.53                                   
REMARK 500    HIS B 531       93.14    -68.09                                   
REMARK 500    ARG B 596       33.02    -97.84                                   
REMARK 500    LYS B 598       56.16    -93.33                                   
REMARK 500    PHE B 681      -53.53   -126.08                                   
REMARK 500    SER B 790       70.01     60.40                                   
REMARK 500    GLU B 840     -106.37   -116.58                                   
REMARK 500    HIS B 843      -52.47   -120.65                                   
REMARK 500    ASN C 736       40.19   -104.82                                   
REMARK 500    SER C 790       73.41     61.58                                   
REMARK 500    PRO C 809       34.14    -93.36                                   
REMARK 500    GLU C 840     -105.66   -119.28                                   
REMARK 500    SER C 868       33.65    -98.83                                   
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 A 201   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 705   OD1                                                    
REMARK 620 2 ASP A 705   O    65.9                                              
REMARK 620 3 SER A 728   OG  114.2  82.8                                        
REMARK 620 4 ASP A 707   O    91.9  98.2 151.3                                  
REMARK 620 5 HIS A 709   O    96.0 160.4 112.9  73.9                            
REMARK 620 6 LEU A 729   O   130.5  75.3  89.1  63.8 115.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 202   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 718   O                                                      
REMARK 620 2 HOH A2015   O    75.7                                              
REMARK 620 3 VAL A 724   O   112.8 111.0                                        
REMARK 620 4 HOH A2014   O    69.7  95.2 153.6                                  
REMARK 620 5 PHE A 755   O   161.6  86.2  76.8 109.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 201   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 728   OG                                                     
REMARK 620 2 ASP B 705   OD1 113.3                                              
REMARK 620 3 ASP B 707   O   151.2  93.2                                        
REMARK 620 4 HIS B 709   O   112.6  98.2  72.3                                  
REMARK 620 5 ASP B 705   O    82.3  66.7  99.2 162.7                            
REMARK 620 6 LEU B 729   O    88.6 131.1  64.6 113.5  74.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 202   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 721   O                                                      
REMARK 620 2 VAL B 724   O    74.2                                              
REMARK 620 3 PHE B 718   O    86.7 132.3                                        
REMARK 620 4 HOH B2018   O   152.1  88.3  89.4                                  
REMARK 620 5 PHE B 755   O   130.4  74.0 142.3  61.5                            
REMARK 620 6 HOH B2017   O   103.5 144.0  82.4 103.4  81.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C 201   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU C 729   O                                                      
REMARK 620 2 ASP C 705   O    77.1                                              
REMARK 620 3 ASP C 705   OD1 128.3  62.6                                        
REMARK 620 4 ASP C 707   O    62.8  97.4  90.6                                  
REMARK 620 5 HIS C 709   O   115.4 155.3  94.4  72.5                            
REMARK 620 6 SER C 728   OG   95.9  85.9 111.1 156.7 112.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C 202   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE C 755   O                                                      
REMARK 620 2 HOH C2003   O   116.3                                              
REMARK 620 3 PHE C 718   O   162.3  68.5                                        
REMARK 620 4 VAL C 724   O    75.6 152.8 108.2                                  
REMARK 620 5 HOH C2004   O    86.2  92.8  76.4 113.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 709   ND1                                                    
REMARK 620 2 ASP A 801   OD2  93.0                                              
REMARK 620 3 NU9 A1000   O09 102.8  89.6                                        
REMARK 620 4 ASP A 707   OD1  99.8  97.0 156.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 541   NE2                                                    
REMARK 620 2 CYS A 618   SG  113.0                                              
REMARK 620 3 CYS A 533   SG  101.4 112.8                                        
REMARK 620 4 CYS A 535   SG  103.4 118.9 105.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 707   OD1                                                    
REMARK 620 2 HIS B 709   ND1 105.6                                              
REMARK 620 3 ASP B 801   OD2  97.5  98.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 618   SG                                                     
REMARK 620 2 CYS B 533   SG  108.7                                              
REMARK 620 3 CYS B 535   SG  120.4 102.8                                        
REMARK 620 4 HIS B 541   NE2 118.9 101.5 101.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 709   ND1                                                    
REMARK 620 2 ASP C 801   OD2  90.7                                              
REMARK 620 3 ASP C 707   OD1  99.3  90.1                                        
REMARK 620 4 ASP C 707   OD2 151.9  87.6  52.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 535   SG                                                     
REMARK 620 2 CYS C 618   SG  121.2                                              
REMARK 620 3 CYS C 533   SG  106.4 101.3                                        
REMARK 620 4 HIS C 541   NE2 106.2 118.3 100.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NU9 A1000                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZNS   RELATED DB: PDB                                   
REMARK 900  HDAC7 BOUND WITH TFMO INHIBITOR TMP942                              
DBREF  3ZNR A  482   903  UNP    Q8WUI4   HDAC7_HUMAN    482    903             
DBREF  3ZNR B  482   903  UNP    Q8WUI4   HDAC7_HUMAN    482    903             
DBREF  3ZNR C  482   903  UNP    Q8WUI4   HDAC7_HUMAN    482    903             
SEQADV 3ZNR GLY A  481  UNP  Q8WUI4              EXPRESSION TAG                 
SEQADV 3ZNR GLY B  481  UNP  Q8WUI4              EXPRESSION TAG                 
SEQADV 3ZNR GLY C  481  UNP  Q8WUI4              EXPRESSION TAG                 
SEQRES   1 A  423  GLY SER ARG ALA GLN SER SER PRO ALA ALA PRO ALA SER          
SEQRES   2 A  423  LEU SER ALA PRO GLU PRO ALA SER GLN ALA ARG VAL LEU          
SEQRES   3 A  423  SER SER SER GLU THR PRO ALA ARG THR LEU PRO PHE THR          
SEQRES   4 A  423  THR GLY LEU ILE TYR ASP SER VAL MET LEU LYS HIS GLN          
SEQRES   5 A  423  CYS SER CYS GLY ASP ASN SER ARG HIS PRO GLU HIS ALA          
SEQRES   6 A  423  GLY ARG ILE GLN SER ILE TRP SER ARG LEU GLN GLU ARG          
SEQRES   7 A  423  GLY LEU ARG SER GLN CYS GLU CYS LEU ARG GLY ARG LYS          
SEQRES   8 A  423  ALA SER LEU GLU GLU LEU GLN SER VAL HIS SER GLU ARG          
SEQRES   9 A  423  HIS VAL LEU LEU TYR GLY THR ASN PRO LEU SER ARG LEU          
SEQRES  10 A  423  LYS LEU ASP ASN GLY LYS LEU ALA GLY LEU LEU ALA GLN          
SEQRES  11 A  423  ARG MET PHE VAL MET LEU PRO CYS GLY GLY VAL GLY VAL          
SEQRES  12 A  423  ASP THR ASP THR ILE TRP ASN GLU LEU HIS SER SER ASN          
SEQRES  13 A  423  ALA ALA ARG TRP ALA ALA GLY SER VAL THR ASP LEU ALA          
SEQRES  14 A  423  PHE LYS VAL ALA SER ARG GLU LEU LYS ASN GLY PHE ALA          
SEQRES  15 A  423  VAL VAL ARG PRO PRO GLY HIS HIS ALA ASP HIS SER THR          
SEQRES  16 A  423  ALA MET GLY PHE CYS PHE PHE ASN SER VAL ALA ILE ALA          
SEQRES  17 A  423  CYS ARG GLN LEU GLN GLN GLN SER LYS ALA SER LYS ILE          
SEQRES  18 A  423  LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY ASN GLY THR          
SEQRES  19 A  423  GLN GLN THR PHE TYR GLN ASP PRO SER VAL LEU TYR ILE          
SEQRES  20 A  423  SER LEU HIS ARG HIS ASP ASP GLY ASN PHE PHE PRO GLY          
SEQRES  21 A  423  SER GLY ALA VAL ASP GLU VAL GLY ALA GLY SER GLY GLU          
SEQRES  22 A  423  GLY PHE ASN VAL ASN VAL ALA TRP ALA GLY GLY LEU ASP          
SEQRES  23 A  423  PRO PRO MET GLY ASP PRO GLU TYR LEU ALA ALA PHE ARG          
SEQRES  24 A  423  ILE VAL VAL MET PRO ILE ALA ARG GLU PHE SER PRO ASP          
SEQRES  25 A  423  LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA GLU GLY          
SEQRES  26 A  423  HIS PRO ALA PRO LEU GLY GLY TYR HIS VAL SER ALA LYS          
SEQRES  27 A  423  CYS PHE GLY TYR MET THR GLN GLN LEU MET ASN LEU ALA          
SEQRES  28 A  423  GLY GLY ALA VAL VAL LEU ALA LEU GLU GLY GLY HIS ASP          
SEQRES  29 A  423  LEU THR ALA ILE CYS ASP ALA SER GLU ALA CYS VAL ALA          
SEQRES  30 A  423  ALA LEU LEU GLY ASN ARG VAL ASP PRO LEU SER GLU GLU          
SEQRES  31 A  423  GLY TRP LYS GLN LYS PRO ASN LEU ASN ALA ILE ARG SER          
SEQRES  32 A  423  LEU GLU ALA VAL ILE ARG VAL HIS SER LYS TYR TRP GLY          
SEQRES  33 A  423  CYS MET GLN ARG LEU ALA SER                                  
SEQRES   1 B  423  GLY SER ARG ALA GLN SER SER PRO ALA ALA PRO ALA SER          
SEQRES   2 B  423  LEU SER ALA PRO GLU PRO ALA SER GLN ALA ARG VAL LEU          
SEQRES   3 B  423  SER SER SER GLU THR PRO ALA ARG THR LEU PRO PHE THR          
SEQRES   4 B  423  THR GLY LEU ILE TYR ASP SER VAL MET LEU LYS HIS GLN          
SEQRES   5 B  423  CYS SER CYS GLY ASP ASN SER ARG HIS PRO GLU HIS ALA          
SEQRES   6 B  423  GLY ARG ILE GLN SER ILE TRP SER ARG LEU GLN GLU ARG          
SEQRES   7 B  423  GLY LEU ARG SER GLN CYS GLU CYS LEU ARG GLY ARG LYS          
SEQRES   8 B  423  ALA SER LEU GLU GLU LEU GLN SER VAL HIS SER GLU ARG          
SEQRES   9 B  423  HIS VAL LEU LEU TYR GLY THR ASN PRO LEU SER ARG LEU          
SEQRES  10 B  423  LYS LEU ASP ASN GLY LYS LEU ALA GLY LEU LEU ALA GLN          
SEQRES  11 B  423  ARG MET PHE VAL MET LEU PRO CYS GLY GLY VAL GLY VAL          
SEQRES  12 B  423  ASP THR ASP THR ILE TRP ASN GLU LEU HIS SER SER ASN          
SEQRES  13 B  423  ALA ALA ARG TRP ALA ALA GLY SER VAL THR ASP LEU ALA          
SEQRES  14 B  423  PHE LYS VAL ALA SER ARG GLU LEU LYS ASN GLY PHE ALA          
SEQRES  15 B  423  VAL VAL ARG PRO PRO GLY HIS HIS ALA ASP HIS SER THR          
SEQRES  16 B  423  ALA MET GLY PHE CYS PHE PHE ASN SER VAL ALA ILE ALA          
SEQRES  17 B  423  CYS ARG GLN LEU GLN GLN GLN SER LYS ALA SER LYS ILE          
SEQRES  18 B  423  LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY ASN GLY THR          
SEQRES  19 B  423  GLN GLN THR PHE TYR GLN ASP PRO SER VAL LEU TYR ILE          
SEQRES  20 B  423  SER LEU HIS ARG HIS ASP ASP GLY ASN PHE PHE PRO GLY          
SEQRES  21 B  423  SER GLY ALA VAL ASP GLU VAL GLY ALA GLY SER GLY GLU          
SEQRES  22 B  423  GLY PHE ASN VAL ASN VAL ALA TRP ALA GLY GLY LEU ASP          
SEQRES  23 B  423  PRO PRO MET GLY ASP PRO GLU TYR LEU ALA ALA PHE ARG          
SEQRES  24 B  423  ILE VAL VAL MET PRO ILE ALA ARG GLU PHE SER PRO ASP          
SEQRES  25 B  423  LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA GLU GLY          
SEQRES  26 B  423  HIS PRO ALA PRO LEU GLY GLY TYR HIS VAL SER ALA LYS          
SEQRES  27 B  423  CYS PHE GLY TYR MET THR GLN GLN LEU MET ASN LEU ALA          
SEQRES  28 B  423  GLY GLY ALA VAL VAL LEU ALA LEU GLU GLY GLY HIS ASP          
SEQRES  29 B  423  LEU THR ALA ILE CYS ASP ALA SER GLU ALA CYS VAL ALA          
SEQRES  30 B  423  ALA LEU LEU GLY ASN ARG VAL ASP PRO LEU SER GLU GLU          
SEQRES  31 B  423  GLY TRP LYS GLN LYS PRO ASN LEU ASN ALA ILE ARG SER          
SEQRES  32 B  423  LEU GLU ALA VAL ILE ARG VAL HIS SER LYS TYR TRP GLY          
SEQRES  33 B  423  CYS MET GLN ARG LEU ALA SER                                  
SEQRES   1 C  423  GLY SER ARG ALA GLN SER SER PRO ALA ALA PRO ALA SER          
SEQRES   2 C  423  LEU SER ALA PRO GLU PRO ALA SER GLN ALA ARG VAL LEU          
SEQRES   3 C  423  SER SER SER GLU THR PRO ALA ARG THR LEU PRO PHE THR          
SEQRES   4 C  423  THR GLY LEU ILE TYR ASP SER VAL MET LEU LYS HIS GLN          
SEQRES   5 C  423  CYS SER CYS GLY ASP ASN SER ARG HIS PRO GLU HIS ALA          
SEQRES   6 C  423  GLY ARG ILE GLN SER ILE TRP SER ARG LEU GLN GLU ARG          
SEQRES   7 C  423  GLY LEU ARG SER GLN CYS GLU CYS LEU ARG GLY ARG LYS          
SEQRES   8 C  423  ALA SER LEU GLU GLU LEU GLN SER VAL HIS SER GLU ARG          
SEQRES   9 C  423  HIS VAL LEU LEU TYR GLY THR ASN PRO LEU SER ARG LEU          
SEQRES  10 C  423  LYS LEU ASP ASN GLY LYS LEU ALA GLY LEU LEU ALA GLN          
SEQRES  11 C  423  ARG MET PHE VAL MET LEU PRO CYS GLY GLY VAL GLY VAL          
SEQRES  12 C  423  ASP THR ASP THR ILE TRP ASN GLU LEU HIS SER SER ASN          
SEQRES  13 C  423  ALA ALA ARG TRP ALA ALA GLY SER VAL THR ASP LEU ALA          
SEQRES  14 C  423  PHE LYS VAL ALA SER ARG GLU LEU LYS ASN GLY PHE ALA          
SEQRES  15 C  423  VAL VAL ARG PRO PRO GLY HIS HIS ALA ASP HIS SER THR          
SEQRES  16 C  423  ALA MET GLY PHE CYS PHE PHE ASN SER VAL ALA ILE ALA          
SEQRES  17 C  423  CYS ARG GLN LEU GLN GLN GLN SER LYS ALA SER LYS ILE          
SEQRES  18 C  423  LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY ASN GLY THR          
SEQRES  19 C  423  GLN GLN THR PHE TYR GLN ASP PRO SER VAL LEU TYR ILE          
SEQRES  20 C  423  SER LEU HIS ARG HIS ASP ASP GLY ASN PHE PHE PRO GLY          
SEQRES  21 C  423  SER GLY ALA VAL ASP GLU VAL GLY ALA GLY SER GLY GLU          
SEQRES  22 C  423  GLY PHE ASN VAL ASN VAL ALA TRP ALA GLY GLY LEU ASP          
SEQRES  23 C  423  PRO PRO MET GLY ASP PRO GLU TYR LEU ALA ALA PHE ARG          
SEQRES  24 C  423  ILE VAL VAL MET PRO ILE ALA ARG GLU PHE SER PRO ASP          
SEQRES  25 C  423  LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA GLU GLY          
SEQRES  26 C  423  HIS PRO ALA PRO LEU GLY GLY TYR HIS VAL SER ALA LYS          
SEQRES  27 C  423  CYS PHE GLY TYR MET THR GLN GLN LEU MET ASN LEU ALA          
SEQRES  28 C  423  GLY GLY ALA VAL VAL LEU ALA LEU GLU GLY GLY HIS ASP          
SEQRES  29 C  423  LEU THR ALA ILE CYS ASP ALA SER GLU ALA CYS VAL ALA          
SEQRES  30 C  423  ALA LEU LEU GLY ASN ARG VAL ASP PRO LEU SER GLU GLU          
SEQRES  31 C  423  GLY TRP LYS GLN LYS PRO ASN LEU ASN ALA ILE ARG SER          
SEQRES  32 C  423  LEU GLU ALA VAL ILE ARG VAL HIS SER LYS TYR TRP GLY          
SEQRES  33 C  423  CYS MET GLN ARG LEU ALA SER                                  
HET     ZN  A 101       1                                                       
HET     ZN  A 102       1                                                       
HET      K  A 201       1                                                       
HET      K  A 202       1                                                       
HET     ZN  B 101       1                                                       
HET     ZN  B 102       1                                                       
HET      K  B 201       1                                                       
HET      K  B 202       1                                                       
HET     ZN  C 101       1                                                       
HET     ZN  C 102       1                                                       
HET      K  C 201       1                                                       
HET      K  C 202       1                                                       
HET    NU9  A1000      36                                                       
HETNAM     NU9 N-{[4-(4-PHENYL-1,3-THIAZOL-2-YL)TETRAHYDRO-                     
HETNAM   2 NU9  2H-PYRAN-4-YL]METHYL}-3-[5-(TRIFLUOROMETHYL)-                   
HETNAM   3 NU9  1,2,4-OXADIAZOL-3-YL]BENZAMIDE                                  
HETNAM       K POTASSIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
FORMUL   4  NU9    C25 H21 F3 N4 O3 S                                           
FORMUL   5    K    6(K 1+)                                                      
FORMUL   6   ZN    6(ZN 2+)                                                     
FORMUL   7  HOH   *44(H2 O)                                                     
HELIX    1   1 ASP A  525  HIS A  531  5                                   7    
HELIX    2   2 ALA A  545  ARG A  558  1                                  14    
HELIX    3   3 SER A  573  SER A  579  1                                   7    
HELIX    4   4 SER A  582  THR A  591  1                                  10    
HELIX    5   5 HIS A  633  SER A  654  1                                  22    
HELIX    6   6 ASN A  683  GLN A  695  1                                  13    
HELIX    7   7 GLY A  711  PHE A  718  1                                   8    
HELIX    8   8 ASP A  733  ASN A  736  5                                   4    
HELIX    9   9 ALA A  749  GLU A  753  5                                   5    
HELIX   10  10 GLY A  770  VAL A  781  1                                  12    
HELIX   11  11 VAL A  781  SER A  790  1                                  10    
HELIX   12  12 SER A  816  MET A  828  1                                  13    
HELIX   13  13 ASN A  829  GLY A  833  5                                   5    
HELIX   14  14 ASP A  844  GLY A  861  1                                  18    
HELIX   15  15 ASP A  865  GLU A  869  5                                   5    
HELIX   16  16 ASN A  877  SER A  892  1                                  16    
HELIX   17  17 TRP A  895  GLN A  899  5                                   5    
HELIX   18  18 ASP B  525  HIS B  531  5                                   7    
HELIX   19  19 ALA B  545  ARG B  558  1                                  14    
HELIX   20  20 LEU B  560  SER B  562  5                                   3    
HELIX   21  21 SER B  573  GLN B  578  1                                   6    
HELIX   22  22 SER B  582  THR B  591  1                                  10    
HELIX   23  23 ASP B  600  LEU B  608  1                                   9    
HELIX   24  24 HIS B  633  SER B  654  1                                  22    
HELIX   25  25 ASN B  683  SER B  696  1                                  14    
HELIX   26  26 GLY B  711  PHE B  718  1                                   8    
HELIX   27  27 ALA B  749  GLU B  753  5                                   5    
HELIX   28  28 GLY B  770  VAL B  781  1                                  12    
HELIX   29  29 VAL B  781  SER B  790  1                                  10    
HELIX   30  30 SER B  816  MET B  828  1                                  13    
HELIX   31  31 ASN B  829  GLY B  833  5                                   5    
HELIX   32  32 ASP B  844  GLY B  861  1                                  18    
HELIX   33  33 ASP B  865  GLU B  869  5                                   5    
HELIX   34  34 GLU B  870  GLN B  874  5                                   5    
HELIX   35  35 ASN B  877  SER B  892  1                                  16    
HELIX   36  36 TRP B  895  GLN B  899  5                                   5    
HELIX   37  37 ASP C  525  HIS C  531  5                                   7    
HELIX   38  38 ALA C  545  ARG C  558  1                                  14    
HELIX   39  39 SER C  573  SER C  579  1                                   7    
HELIX   40  40 SER C  582  THR C  591  1                                  10    
HELIX   41  41 HIS C  633  SER C  654  1                                  22    
HELIX   42  42 ASN C  683  GLN C  695  1                                  13    
HELIX   43  43 GLY C  711  PHE C  718  1                                   8    
HELIX   44  44 ALA C  749  GLU C  753  5                                   5    
HELIX   45  45 GLY C  770  VAL C  781  1                                  12    
HELIX   46  46 VAL C  781  SER C  790  1                                  10    
HELIX   47  47 SER C  816  ASN C  829  1                                  14    
HELIX   48  48 LEU C  830  GLY C  833  5                                   4    
HELIX   49  49 ASP C  844  LEU C  860  1                                  17    
HELIX   50  50 ASP C  865  GLU C  869  5                                   5    
HELIX   51  51 ASN C  877  SER C  892  1                                  16    
HELIX   52  52 TRP C  895  GLN C  899  5                                   5    
SHEET    1  AA 8 GLU A 565  LEU A 567  0                                        
SHEET    2  AA 8 THR A 520  ILE A 523  1  O  THR A 520   N  GLU A 565           
SHEET    3  AA 8 ASN A 659  ALA A 662  1  O  ASN A 659   N  GLY A 521           
SHEET    4  AA 8 VAL A 835  LEU A 839  1  O  VAL A 835   N  GLY A 660           
SHEET    5  AA 8 LEU A 793  ALA A 798  1  O  VAL A 794   N  VAL A 836           
SHEET    6  AA 8 ILE A 701  ASP A 705  1  O  LEU A 702   N  LEU A 795           
SHEET    7  AA 8 VAL A 724  ARG A 731  1  O  LEU A 725   N  ILE A 703           
SHEET    8  AA 8 ASN A 756  TRP A 761  1  O  VAL A 757   N  SER A 728           
SHEET    1  BA 8 CYS B 564  LEU B 567  0                                        
SHEET    2  BA 8 THR B 520  ILE B 523  1  O  THR B 520   N  GLU B 565           
SHEET    3  BA 8 ASN B 659  ALA B 662  1  O  ASN B 659   N  GLY B 521           
SHEET    4  BA 8 VAL B 835  LEU B 839  1  O  VAL B 835   N  GLY B 660           
SHEET    5  BA 8 LEU B 793  ALA B 798  1  O  VAL B 794   N  VAL B 836           
SHEET    6  BA 8 ILE B 701  ASP B 705  1  O  LEU B 702   N  LEU B 795           
SHEET    7  BA 8 VAL B 724  ARG B 731  1  O  LEU B 725   N  ILE B 703           
SHEET    8  BA 8 ASN B 756  TRP B 761  1  O  VAL B 757   N  SER B 728           
SHEET    1  BB 2 VAL B 621  GLY B 622  0                                        
SHEET    2  BB 2 ILE B 628  TRP B 629 -1  N  TRP B 629   O  VAL B 621           
SHEET    1  CA 8 GLU C 565  LEU C 567  0                                        
SHEET    2  CA 8 THR C 520  ILE C 523  1  O  THR C 520   N  GLU C 565           
SHEET    3  CA 8 ASN C 659  ALA C 662  1  O  ASN C 659   N  GLY C 521           
SHEET    4  CA 8 VAL C 835  LEU C 839  1  O  VAL C 835   N  GLY C 660           
SHEET    5  CA 8 LEU C 793  ALA C 798  1  O  VAL C 794   N  VAL C 836           
SHEET    6  CA 8 ILE C 701  ASP C 705  1  O  LEU C 702   N  LEU C 795           
SHEET    7  CA 8 VAL C 724  ARG C 731  1  O  LEU C 725   N  ILE C 703           
SHEET    8  CA 8 ASN C 756  TRP C 761  1  O  VAL C 757   N  SER C 728           
LINK        ZN    ZN A 101                 ND1 HIS A 709     1555   1555  2.13  
LINK        ZN    ZN A 101                 OD2 ASP A 801     1555   1555  1.92  
LINK        ZN    ZN A 101                 OD1 ASP A 707     1555   1555  2.09  
LINK        ZN    ZN A 102                 NE2 HIS A 541     1555   1555  2.02  
LINK        ZN    ZN A 102                 SG  CYS A 618     1555   1555  2.29  
LINK        ZN    ZN A 102                 SG  CYS A 533     1555   1555  2.37  
LINK        ZN    ZN A 102                 SG  CYS A 535     1555   1555  2.07  
LINK         K     K A 201                 OD1 ASP A 705     1555   1555  3.11  
LINK         K     K A 201                 O   ASP A 705     1555   1555  2.86  
LINK         K     K A 201                 OG  SER A 728     1555   1555  2.78  
LINK         K     K A 201                 O   ASP A 707     1555   1555  2.61  
LINK         K     K A 201                 O   HIS A 709     1555   1555  2.77  
LINK         K     K A 201                 O   LEU A 729     1555   1555  3.01  
LINK         K     K A 202                 O   PHE A 718     1555   1555  2.75  
LINK         K     K A 202                 O   HOH A2015     1555   1555  2.53  
LINK         K     K A 202                 O   VAL A 724     1555   1555  2.93  
LINK         K     K A 202                 O   HOH A2014     1555   1555  2.92  
LINK         K     K A 202                 O   PHE A 755     1555   1555  3.08  
LINK         O09 NU9 A1000                ZN    ZN A 101     1555   1555  2.68  
LINK        ZN    ZN B 101                 OD2 ASP B 801     1555   1555  1.92  
LINK        ZN    ZN B 101                 ND1 HIS B 709     1555   1555  2.06  
LINK        ZN    ZN B 101                 OD1 ASP B 707     1555   1555  2.03  
LINK        ZN    ZN B 102                 NE2 HIS B 541     1555   1555  2.11  
LINK        ZN    ZN B 102                 SG  CYS B 535     1555   1555  2.18  
LINK        ZN    ZN B 102                 SG  CYS B 533     1555   1555  2.36  
LINK        ZN    ZN B 102                 SG  CYS B 618     1555   1555  2.12  
LINK         K     K B 201                 O   ASP B 705     1555   1555  2.84  
LINK         K     K B 201                 O   HIS B 709     1555   1555  2.82  
LINK         K     K B 201                 OD1 ASP B 705     1555   1555  3.10  
LINK         K     K B 201                 OG  SER B 728     1555   1555  2.75  
LINK         K     K B 201                 O   ASP B 707     1555   1555  2.68  
LINK         K     K B 201                 O   LEU B 729     1555   1555  2.95  
LINK         K     K B 202                 O   ASP B 721     1555   1555  2.70  
LINK         K     K B 202                 O   HOH B2017     1555   1555  2.43  
LINK         K     K B 202                 O   PHE B 755     1555   1555  3.39  
LINK         K     K B 202                 O   HOH B2018     1555   1555  2.36  
LINK         K     K B 202                 O   PHE B 718     1555   1555  2.53  
LINK         K     K B 202                 O   VAL B 724     1555   1555  2.67  
LINK        ZN    ZN C 101                 OD2 ASP C 707     1555   1555  2.65  
LINK        ZN    ZN C 101                 ND1 HIS C 709     1555   1555  2.02  
LINK        ZN    ZN C 101                 OD2 ASP C 801     1555   1555  1.94  
LINK        ZN    ZN C 101                 OD1 ASP C 707     1555   1555  2.20  
LINK        ZN    ZN C 102                 SG  CYS C 535     1555   1555  2.05  
LINK        ZN    ZN C 102                 SG  CYS C 618     1555   1555  2.52  
LINK        ZN    ZN C 102                 SG  CYS C 533     1555   1555  2.43  
LINK        ZN    ZN C 102                 NE2 HIS C 541     1555   1555  2.06  
LINK         K     K C 201                 OG  SER C 728     1555   1555  2.87  
LINK         K     K C 201                 O   HIS C 709     1555   1555  2.88  
LINK         K     K C 201                 O   ASP C 707     1555   1555  2.71  
LINK         K     K C 201                 OD1 ASP C 705     1555   1555  3.29  
LINK         K     K C 201                 O   ASP C 705     1555   1555  2.79  
LINK         K     K C 201                 O   LEU C 729     1555   1555  3.04  
LINK         K     K C 202                 O   HOH C2004     1555   1555  2.65  
LINK         K     K C 202                 O   VAL C 724     1555   1555  3.10  
LINK         K     K C 202                 O   PHE C 718     1555   1555  2.74  
LINK         K     K C 202                 O   HOH C2003     1555   1555  2.97  
LINK         K     K C 202                 O   PHE C 755     1555   1555  3.08  
CISPEP   1 ARG A  665    PRO A  666          0        -0.83                     
CISPEP   2 PHE A  738    PRO A  739          0        -0.17                     
CISPEP   3 ASP A  766    PRO A  767          0        -1.37                     
CISPEP   4 ALA A  808    PRO A  809          0        -0.83                     
CISPEP   5 PRO B  593    LEU B  594          0        -2.92                     
CISPEP   6 ARG B  665    PRO B  666          0        -1.84                     
CISPEP   7 PHE B  738    PRO B  739          0        -0.10                     
CISPEP   8 ASP B  766    PRO B  767          0        -0.67                     
CISPEP   9 ASN C  592    PRO C  593          0        -8.49                     
CISPEP  10 ARG C  665    PRO C  666          0        -0.78                     
CISPEP  11 PHE C  738    PRO C  739          0         1.18                     
CISPEP  12 ASP C  766    PRO C  767          0         1.28                     
CISPEP  13 ALA C  808    PRO C  809          0         3.96                     
SITE     1 AC1  4 ASP A 707  HIS A 709  ASP A 801  NU9 A1000                    
SITE     1 AC2  4 CYS A 533  CYS A 535  HIS A 541  CYS A 618                    
SITE     1 AC3  5 ASP A 705  ASP A 707  HIS A 709  SER A 728                    
SITE     2 AC3  5 LEU A 729                                                     
SITE     1 AC4  6 PHE A 718  ASP A 721  VAL A 724  PHE A 755                    
SITE     2 AC4  6 HOH A2014  HOH A2015                                          
SITE     1 AC5  3 ASP B 707  HIS B 709  ASP B 801                               
SITE     1 AC6  4 CYS B 533  CYS B 535  HIS B 541  CYS B 618                    
SITE     1 AC7  5 ASP B 705  ASP B 707  HIS B 709  SER B 728                    
SITE     2 AC7  5 LEU B 729                                                     
SITE     1 AC8  6 PHE B 718  ASP B 721  VAL B 724  PHE B 755                    
SITE     2 AC8  6 HOH B2017  HOH B2018                                          
SITE     1 AC9  3 ASP C 707  HIS C 709  ASP C 801                               
SITE     1 BC1  4 CYS C 533  CYS C 535  HIS C 541  CYS C 618                    
SITE     1 BC2  5 ASP C 705  ASP C 707  HIS C 709  SER C 728                    
SITE     2 BC2  5 LEU C 729                                                     
SITE     1 BC3  5 PHE C 718  VAL C 724  PHE C 755  HOH C2003                    
SITE     2 BC3  5 HOH C2004                                                     
SITE     1 BC4 18  ZN A 101  PRO A 542  GLU A 543  PRO A 667                    
SITE     2 BC4 18 HIS A 669  HIS A 670  GLY A 678  PHE A 679                    
SITE     3 BC4 18 CYS A 680  ASP A 707  HIS A 709  PHE A 738                    
SITE     4 BC4 18 ASP A 801  PRO A 809  LEU A 810  GLU A 840                    
SITE     5 BC4 18 GLY A 841  HIS A 843                                          
CRYST1   81.393   81.393  149.265  90.00  90.00 120.00 P 32          9          
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      0.012286  0.007093  0.000000        0.00000                         
SCALE2      0.000000  0.014187  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006699        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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