GenomeNet

Database: PDB
Entry: 3MAX
LinkDB: 3MAX
Original site: 3MAX 
HEADER    HYDROLASE                               24-MAR-10   3MAX              
TITLE     CRYSTAL STRUCTURE OF HUMAN HDAC2 COMPLEXED WITH AN N-(2-AMINOPHENYL)  
TITLE    2 BENZAMIDE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE DEACETYLASE 2;                                     
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: HD2;                                                        
COMPND   5 EC: 3.5.1.98;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HDAC2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PSXB19                                
KEYWDS    CLASS 2, HDAC, FOOT POCKET, HYDROLASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.J.SKENE,A.J.JENNINGS                                                
REVDAT   3   21-FEB-24 3MAX    1       REMARK SEQADV LINK                       
REVDAT   2   19-MAY-10 3MAX    1       JRNL                                     
REVDAT   1   28-APR-10 3MAX    0                                                
JRNL        AUTH   J.C.BRESSI,A.J.JENNINGS,R.SKENE,Y.WU,R.MELKUS,R.DE JONG,     
JRNL        AUTH 2 S.O'CONNELL,C.E.GRIMSHAW,M.NAVRE,A.R.GANGLOFF                
JRNL        TITL   EXPLORATION OF THE HDAC2 FOOT POCKET: SYNTHESIS AND SAR OF   
JRNL        TITL 2 SUBSTITUTED N-(2-AMINOPHENYL)BENZAMIDES.                     
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  20  3142 2010              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   20392638                                                     
JRNL        DOI    10.1016/J.BMCL.2010.03.091                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 75270                          
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3973                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5480                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 244                          
REMARK   3   BIN FREE R VALUE                    : 0.2860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8842                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 624                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.11000                                             
REMARK   3    B22 (A**2) : 3.56000                                              
REMARK   3    B33 (A**2) : -1.45000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.174         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.152         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.101         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.053         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9185 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12400 ; 1.325 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1094 ; 5.136 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   454 ;37.752 ;23.744       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1558 ;13.240 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;18.269 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1270 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7111 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4539 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6302 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   601 ; 0.130 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    15 ; 0.096 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    73 ; 0.200 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.138 ; 0.200       
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):  5438 ; 1.711 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8752 ; 2.668 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3867 ; 2.271 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3648 ; 3.312 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3MAX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000058325.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79353                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.060                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% (V/V) PEG-600, 0.1 MM CHES, PH       
REMARK 280  9.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                
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       46.15550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.42450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.61350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.42450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.15550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.61350            
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, 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     ALA B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     LYS B    14                                                      
REMARK 465     ALA C    12                                                      
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 C  13    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 373   CD    GLU A 373   OE2     0.077                       
REMARK 500    GLU B 373   CD    GLU B 373   OE2     0.080                       
REMARK 500    GLU C 373   CD    GLU C 373   OE2     0.079                       
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    GLU A 103     -101.26   -136.82                                   
REMARK 500    CYS A 105       78.17   -117.24                                   
REMARK 500    PHE A 155       -3.86     75.40                                   
REMARK 500    TYR A 226       -1.71     83.29                                   
REMARK 500    CYS A 266       43.95   -108.89                                   
REMARK 500    GLU B 103     -100.35   -110.82                                   
REMARK 500    CYS B 105       79.60   -111.86                                   
REMARK 500    PHE B 155       -1.66     80.56                                   
REMARK 500    TYR B 226        0.87     81.88                                   
REMARK 500    CYS B 266       44.72   -109.12                                   
REMARK 500    TYR C  72      -52.61   -121.56                                   
REMARK 500    GLU C 103      -98.61   -113.63                                   
REMARK 500    CYS C 105       79.85   -114.43                                   
REMARK 500    PHE C 155       -2.63     80.75                                   
REMARK 500    TYR C 226       -0.49     80.61                                   
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                              CA A 380  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 179   OD1                                                    
REMARK 620 2 ASP A 179   O    71.9                                              
REMARK 620 3 ASP A 181   O   100.2 103.3                                        
REMARK 620 4 HIS A 183   O    90.1 162.0  79.1                                  
REMARK 620 5 SER A 202   OG  102.8  88.6 156.5  95.8                            
REMARK 620 6 PHE A 203   O   144.2  76.2  71.7 121.0  92.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 379  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 181   OD2                                                    
REMARK 620 2 HIS A 183   ND1 105.3                                              
REMARK 620 3 ASP A 269   OD2 104.7 102.4                                        
REMARK 620 4 LLX A 400   N1  100.5 102.2 138.3                                  
REMARK 620 5 LLX A 400   O10 167.8  83.7  80.9  69.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 381  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 192   O                                                      
REMARK 620 2 THR A 195   O    91.2                                              
REMARK 620 3 VAL A 198   O   129.8  88.0                                        
REMARK 620 4 HOH A 396   O    93.4  93.7 136.7                                  
REMARK 620 5 HOH A 425   O    84.7 167.9 103.4  75.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 380  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 179   OD1                                                    
REMARK 620 2 ASP B 179   O    71.1                                              
REMARK 620 3 ASP B 181   O   100.2 105.5                                        
REMARK 620 4 HIS B 183   O    94.5 165.2  80.1                                  
REMARK 620 5 SER B 202   OG  104.2  87.7 155.0  92.5                            
REMARK 620 6 PHE B 203   O   144.8  76.7  74.6 118.1  88.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 379  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 181   OD2                                                    
REMARK 620 2 HIS B 183   ND1 100.4                                              
REMARK 620 3 ASP B 269   OD1 103.6 105.0                                        
REMARK 620 4 LLX B 400   N1  102.0 103.3 137.3                                  
REMARK 620 5 LLX B 400   O10 174.7  82.5  79.8  72.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 381  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE B 192   O                                                      
REMARK 620 2 THR B 195   O    90.5                                              
REMARK 620 3 VAL B 198   O   124.7  88.0                                        
REMARK 620 4 HOH B 385   O    91.6  94.2 143.7                                  
REMARK 620 5 HOH B 441   O    78.5 164.5 107.3  75.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 380  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 179   OD1                                                    
REMARK 620 2 ASP C 179   O    71.0                                              
REMARK 620 3 ASP C 181   O   100.5 103.2                                        
REMARK 620 4 HIS C 183   O    91.7 162.4  82.4                                  
REMARK 620 5 SER C 202   OG  102.5  87.0 156.8  94.1                            
REMARK 620 6 PHE C 203   O   144.7  78.6  69.3 118.9  93.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 379  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 181   OD2                                                    
REMARK 620 2 HIS C 183   ND1 101.2                                              
REMARK 620 3 ASP C 269   OD2 102.8 103.1                                        
REMARK 620 4 LLX C 400   N1   99.9 104.7 139.7                                  
REMARK 620 5 LLX C 400   O10 173.0  85.0  78.9  75.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 381  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE C 192   O                                                      
REMARK 620 2 THR C 195   O    93.4                                              
REMARK 620 3 VAL C 198   O   121.4  87.5                                        
REMARK 620 4 HOH C 389   O    91.9 101.2 145.2                                  
REMARK 620 5 HOH C 464   O    79.3 172.3  98.3  76.9                            
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 ZN A 379                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 380                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 381                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LLX A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A 383                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 379                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 380                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 381                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LLX B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 379                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 380                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 381                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LLX C 400                 
DBREF  3MAX A   13   378  UNP    Q92769   HDAC2_HUMAN      9    374             
DBREF  3MAX B   13   378  UNP    Q92769   HDAC2_HUMAN      9    374             
DBREF  3MAX C   13   378  UNP    Q92769   HDAC2_HUMAN      9    374             
SEQADV 3MAX ALA A   12  UNP  Q92769              EXPRESSION TAG                 
SEQADV 3MAX ALA B   12  UNP  Q92769              EXPRESSION TAG                 
SEQADV 3MAX ALA C   12  UNP  Q92769              EXPRESSION TAG                 
SEQRES   1 A  367  ALA LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE          
SEQRES   2 A  367  GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO          
SEQRES   3 A  367  HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR          
SEQRES   4 A  367  GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS          
SEQRES   5 A  367  ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU          
SEQRES   6 A  367  TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET          
SEQRES   7 A  367  SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY          
SEQRES   8 A  367  GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS          
SEQRES   9 A  367  GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS          
SEQRES  10 A  367  LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA          
SEQRES  11 A  367  GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY          
SEQRES  12 A  367  PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU          
SEQRES  13 A  367  LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE          
SEQRES  14 A  367  ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR          
SEQRES  15 A  367  THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR          
SEQRES  16 A  367  GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE          
SEQRES  17 A  367  GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO          
SEQRES  18 A  367  MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE          
SEQRES  19 A  367  PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN          
SEQRES  20 A  367  PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU          
SEQRES  21 A  367  SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS          
SEQRES  22 A  367  GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN          
SEQRES  23 A  367  LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE          
SEQRES  24 A  367  ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL          
SEQRES  25 A  367  ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN          
SEQRES  26 A  367  ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS          
SEQRES  27 A  367  ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU          
SEQRES  28 A  367  TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU          
SEQRES  29 A  367  ARG MET LEU                                                  
SEQRES   1 B  367  ALA LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE          
SEQRES   2 B  367  GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO          
SEQRES   3 B  367  HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR          
SEQRES   4 B  367  GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS          
SEQRES   5 B  367  ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU          
SEQRES   6 B  367  TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET          
SEQRES   7 B  367  SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY          
SEQRES   8 B  367  GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS          
SEQRES   9 B  367  GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS          
SEQRES  10 B  367  LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA          
SEQRES  11 B  367  GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY          
SEQRES  12 B  367  PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU          
SEQRES  13 B  367  LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE          
SEQRES  14 B  367  ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR          
SEQRES  15 B  367  THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR          
SEQRES  16 B  367  GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE          
SEQRES  17 B  367  GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO          
SEQRES  18 B  367  MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE          
SEQRES  19 B  367  PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN          
SEQRES  20 B  367  PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU          
SEQRES  21 B  367  SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS          
SEQRES  22 B  367  GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN          
SEQRES  23 B  367  LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE          
SEQRES  24 B  367  ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL          
SEQRES  25 B  367  ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN          
SEQRES  26 B  367  ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS          
SEQRES  27 B  367  ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU          
SEQRES  28 B  367  TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU          
SEQRES  29 B  367  ARG MET LEU                                                  
SEQRES   1 C  367  ALA LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE          
SEQRES   2 C  367  GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO          
SEQRES   3 C  367  HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR          
SEQRES   4 C  367  GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS          
SEQRES   5 C  367  ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU          
SEQRES   6 C  367  TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET          
SEQRES   7 C  367  SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY          
SEQRES   8 C  367  GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS          
SEQRES   9 C  367  GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS          
SEQRES  10 C  367  LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA          
SEQRES  11 C  367  GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY          
SEQRES  12 C  367  PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU          
SEQRES  13 C  367  LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE          
SEQRES  14 C  367  ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR          
SEQRES  15 C  367  THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR          
SEQRES  16 C  367  GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE          
SEQRES  17 C  367  GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO          
SEQRES  18 C  367  MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE          
SEQRES  19 C  367  PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN          
SEQRES  20 C  367  PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU          
SEQRES  21 C  367  SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS          
SEQRES  22 C  367  GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN          
SEQRES  23 C  367  LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE          
SEQRES  24 C  367  ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL          
SEQRES  25 C  367  ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN          
SEQRES  26 C  367  ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS          
SEQRES  27 C  367  ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU          
SEQRES  28 C  367  TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU          
SEQRES  29 C  367  ARG MET LEU                                                  
HET     ZN  A 379       1                                                       
HET     CA  A 380       1                                                       
HET     NA  A 381       1                                                       
HET    LLX  A 400      22                                                       
HET    NHE  A 383      19                                                       
HET     ZN  B 379       1                                                       
HET     CA  B 380       1                                                       
HET     NA  B 381       1                                                       
HET    LLX  B 400      22                                                       
HET     ZN  C 379       1                                                       
HET     CA  C 380       1                                                       
HET     NA  C 381       1                                                       
HET    LLX  C 400      22                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM     LLX N-(4-AMINOBIPHENYL-3-YL)BENZAMIDE                                
HETNAM     NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID                        
HETSYN     NHE N-CYCLOHEXYLTAURINE; CHES                                        
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   5   CA    3(CA 2+)                                                     
FORMUL   6   NA    3(NA 1+)                                                     
FORMUL   7  LLX    3(C19 H16 N2 O)                                              
FORMUL   8  NHE    C8 H17 N O3 S                                                
FORMUL  17  HOH   *624(H2 O)                                                    
HELIX    1   1 ASP A   21  TYR A   27  5                                   7    
HELIX    2   2 PRO A   37  TYR A   50  1                                  14    
HELIX    3   3 GLY A   51  MET A   56  5                                   6    
HELIX    4   4 THR A   65  THR A   70  1                                   6    
HELIX    5   5 SER A   74  ILE A   84  1                                  11    
HELIX    6   6 ARG A   85  GLU A   91  5                                   7    
HELIX    7   7 TYR A   92  PHE A   99  1                                   8    
HELIX    8   8 GLY A  110  ARG A  131  1                                  22    
HELIX    9   9 ASN A  159  LEU A  169  1                                  11    
HELIX   10  10 GLY A  185  PHE A  192  1                                   8    
HELIX   11  11 ALA A  221  LYS A  225  5                                   5    
HELIX   12  12 ASP A  238  GLN A  258  1                                  21    
HELIX   13  13 GLY A  267  LEU A  271  5                                   5    
HELIX   14  14 THR A  282  THR A  295  1                                  14    
HELIX   15  15 THR A  309  LEU A  325  1                                  17    
HELIX   16  16 TYR A  338  GLY A  343  5                                   6    
HELIX   17  17 THR A  360  ARG A  376  1                                  17    
HELIX   18  18 ASP B   23  TYR B   27  5                                   5    
HELIX   19  19 PRO B   37  TYR B   50  1                                  14    
HELIX   20  20 GLY B   51  LYS B   55  5                                   5    
HELIX   21  21 THR B   65  THR B   70  1                                   6    
HELIX   22  22 SER B   74  ILE B   84  1                                  11    
HELIX   23  23 ARG B   85  MET B   89  5                                   5    
HELIX   24  24 TYR B   92  ASN B  100  1                                   9    
HELIX   25  25 GLY B  110  ARG B  131  1                                  22    
HELIX   26  26 ASN B  159  LYS B  170  1                                  12    
HELIX   27  27 GLY B  185  PHE B  192  1                                   8    
HELIX   28  28 ALA B  221  LYS B  225  5                                   5    
HELIX   29  29 ASP B  238  GLN B  258  1                                  21    
HELIX   30  30 GLY B  267  LEU B  271  5                                   5    
HELIX   31  31 THR B  282  THR B  295  1                                  14    
HELIX   32  32 THR B  309  LEU B  325  1                                  17    
HELIX   33  33 TYR B  338  GLY B  343  5                                   6    
HELIX   34  34 THR B  360  ARG B  376  1                                  17    
HELIX   35  35 ASP C   23  TYR C   27  5                                   5    
HELIX   36  36 PRO C   37  TYR C   50  1                                  14    
HELIX   37  37 GLY C   51  MET C   56  5                                   6    
HELIX   38  38 THR C   65  THR C   70  1                                   6    
HELIX   39  39 SER C   74  ILE C   84  1                                  11    
HELIX   40  40 ARG C   85  GLU C   91  5                                   7    
HELIX   41  41 TYR C   92  PHE C   99  1                                   8    
HELIX   42  42 GLY C  110  ARG C  131  1                                  22    
HELIX   43  43 ASN C  159  LEU C  169  1                                  11    
HELIX   44  44 GLY C  185  PHE C  192  1                                   8    
HELIX   45  45 ALA C  221  LYS C  225  5                                   5    
HELIX   46  46 ASP C  238  GLN C  258  1                                  21    
HELIX   47  47 GLY C  267  LEU C  271  5                                   5    
HELIX   48  48 THR C  282  THR C  295  1                                  14    
HELIX   49  49 THR C  309  LEU C  325  1                                  17    
HELIX   50  50 TYR C  338  GLY C  343  5                                   6    
HELIX   51  51 THR C  360  ARG C  376  1                                  17    
SHEET    1   A 8 GLU A  57  TYR A  59  0                                        
SHEET    2   A 8 VAL A  16  TYR A  19  1  N  TYR A  18   O  TYR A  59           
SHEET    3   A 8 MET A 136  ASN A 139  1  O  VAL A 138   N  TYR A  19           
SHEET    4   A 8 LEU A 300  LEU A 303  1  O  MET A 302   N  ALA A 137           
SHEET    5   A 8 ALA A 261  GLN A 265  1  N  LEU A 264   O  LEU A 301           
SHEET    6   A 8 VAL A 175  ASP A 179  1  N  ILE A 178   O  GLN A 265           
SHEET    7   A 8 VAL A 198  LYS A 205  1  O  MET A 199   N  TYR A 177           
SHEET    8   A 8 ALA A 228  MET A 233  1  O  PHE A 231   N  SER A 202           
SHEET    1   B 8 GLU B  57  TYR B  59  0                                        
SHEET    2   B 8 VAL B  16  TYR B  19  1  N  TYR B  18   O  TYR B  59           
SHEET    3   B 8 MET B 136  ASN B 139  1  O  VAL B 138   N  TYR B  19           
SHEET    4   B 8 LEU B 300  LEU B 303  1  O  MET B 302   N  ALA B 137           
SHEET    5   B 8 ALA B 261  GLN B 265  1  N  LEU B 264   O  LEU B 301           
SHEET    6   B 8 VAL B 175  ASP B 179  1  N  LEU B 176   O  VAL B 263           
SHEET    7   B 8 VAL B 198  LYS B 205  1  O  MET B 199   N  TYR B 177           
SHEET    8   B 8 ALA B 228  MET B 233  1  O  PHE B 231   N  SER B 202           
SHEET    1   C 8 GLU C  57  TYR C  59  0                                        
SHEET    2   C 8 VAL C  16  TYR C  19  1  N  TYR C  18   O  TYR C  59           
SHEET    3   C 8 MET C 136  ASN C 139  1  O  VAL C 138   N  TYR C  19           
SHEET    4   C 8 LEU C 300  LEU C 303  1  O  MET C 302   N  ALA C 137           
SHEET    5   C 8 ALA C 261  GLN C 265  1  N  LEU C 264   O  LEU C 301           
SHEET    6   C 8 VAL C 175  ASP C 179  1  N  ILE C 178   O  GLN C 265           
SHEET    7   C 8 VAL C 198  LYS C 205  1  O  MET C 199   N  TYR C 177           
SHEET    8   C 8 ALA C 228  MET C 233  1  O  VAL C 229   N  THR C 200           
LINK         OD1 ASP A 179                CA    CA A 380     1555   1555  2.66  
LINK         O   ASP A 179                CA    CA A 380     1555   1555  2.99  
LINK         OD2 ASP A 181                ZN    ZN A 379     1555   1555  2.00  
LINK         O   ASP A 181                CA    CA A 380     1555   1555  2.62  
LINK         ND1 HIS A 183                ZN    ZN A 379     1555   1555  2.19  
LINK         O   HIS A 183                CA    CA A 380     1555   1555  2.69  
LINK         O   PHE A 192                NA    NA A 381     1555   1555  2.18  
LINK         O   THR A 195                NA    NA A 381     1555   1555  2.50  
LINK         O   VAL A 198                NA    NA A 381     1555   1555  2.33  
LINK         OG  SER A 202                CA    CA A 380     1555   1555  2.84  
LINK         O   PHE A 203                CA    CA A 380     1555   1555  2.65  
LINK         OD2 ASP A 269                ZN    ZN A 379     1555   1555  2.05  
LINK        ZN    ZN A 379                 N1  LLX A 400     1555   1555  2.13  
LINK        ZN    ZN A 379                 O10 LLX A 400     1555   1555  2.54  
LINK        NA    NA A 381                 O   HOH A 396     1555   1555  2.41  
LINK        NA    NA A 381                 O   HOH A 425     1555   1555  2.58  
LINK         OD1 ASP B 179                CA    CA B 380     1555   1555  2.59  
LINK         O   ASP B 179                CA    CA B 380     1555   1555  2.90  
LINK         OD2 ASP B 181                ZN    ZN B 379     1555   1555  1.95  
LINK         O   ASP B 181                CA    CA B 380     1555   1555  2.52  
LINK         ND1 HIS B 183                ZN    ZN B 379     1555   1555  2.10  
LINK         O   HIS B 183                CA    CA B 380     1555   1555  2.64  
LINK         O   PHE B 192                NA    NA B 381     1555   1555  2.34  
LINK         O   THR B 195                NA    NA B 381     1555   1555  2.50  
LINK         O   VAL B 198                NA    NA B 381     1555   1555  2.34  
LINK         OG  SER B 202                CA    CA B 380     1555   1555  2.90  
LINK         O   PHE B 203                CA    CA B 380     1555   1555  2.58  
LINK         OD1 ASP B 269                ZN    ZN B 379     1555   1555  1.91  
LINK        ZN    ZN B 379                 N1  LLX B 400     1555   1555  2.08  
LINK        ZN    ZN B 379                 O10 LLX B 400     1555   1555  2.67  
LINK        NA    NA B 381                 O   HOH B 385     1555   1555  2.33  
LINK        NA    NA B 381                 O   HOH B 441     1555   1555  2.52  
LINK         OD1 ASP C 179                CA    CA C 380     1555   1555  2.63  
LINK         O   ASP C 179                CA    CA C 380     1555   1555  2.83  
LINK         OD2 ASP C 181                ZN    ZN C 379     1555   1555  2.15  
LINK         O   ASP C 181                CA    CA C 380     1555   1555  2.57  
LINK         ND1 HIS C 183                ZN    ZN C 379     1555   1555  2.04  
LINK         O   HIS C 183                CA    CA C 380     1555   1555  2.72  
LINK         O   PHE C 192                NA    NA C 381     1555   1555  2.30  
LINK         O   THR C 195                NA    NA C 381     1555   1555  2.38  
LINK         O   VAL C 198                NA    NA C 381     1555   1555  2.33  
LINK         OG  SER C 202                CA    CA C 380     1555   1555  2.86  
LINK         O   PHE C 203                CA    CA C 380     1555   1555  2.62  
LINK         OD2 ASP C 269                ZN    ZN C 379     1555   1555  1.98  
LINK        ZN    ZN C 379                 N1  LLX C 400     1555   1555  2.13  
LINK        ZN    ZN C 379                 O10 LLX C 400     1555   1555  2.61  
LINK        NA    NA C 381                 O   HOH C 389     1555   1555  2.26  
LINK        NA    NA C 381                 O   HOH C 464     1555   1555  2.67  
CISPEP   1 PHE A  210    PRO A  211          0        -3.60                     
CISPEP   2 GLY A  343    PRO A  344          0         4.13                     
CISPEP   3 PHE B  210    PRO B  211          0        -4.24                     
CISPEP   4 GLY B  343    PRO B  344          0         0.28                     
CISPEP   5 PHE C  210    PRO C  211          0        -4.99                     
CISPEP   6 GLY C  343    PRO C  344          0         2.58                     
SITE     1 AC1  4 ASP A 181  HIS A 183  ASP A 269  LLX A 400                    
SITE     1 AC2  5 ASP A 179  ASP A 181  HIS A 183  SER A 202                    
SITE     2 AC2  5 PHE A 203                                                     
SITE     1 AC3  6 PHE A 192  THR A 195  VAL A 198  TYR A 227                    
SITE     2 AC3  6 HOH A 396  HOH A 425                                          
SITE     1 AC4 19 TYR A  29  MET A  35  ARG A  39  GLY A 143                    
SITE     2 AC4 19 LEU A 144  HIS A 145  HIS A 146  GLY A 154                    
SITE     3 AC4 19 PHE A 155  CYS A 156  ASP A 181  HIS A 183                    
SITE     4 AC4 19 PHE A 210  ASP A 269  LEU A 276  GLY A 305                    
SITE     5 AC4 19 GLY A 306  TYR A 308   ZN A 379                               
SITE     1 AC5 11 TYR A  59  LYS A 128  HOH A 537  HOH A 538                    
SITE     2 AC5 11 HOH A 539  ASP B  21  GLY B  22  ASP B  23                    
SITE     3 AC5 11 ARG B  60  GLU B 113  LEU B 117                               
SITE     1 AC6  4 ASP B 181  HIS B 183  ASP B 269  LLX B 400                    
SITE     1 AC7  5 ASP B 179  ASP B 181  HIS B 183  SER B 202                    
SITE     2 AC7  5 PHE B 203                                                     
SITE     1 AC8  6 PHE B 192  THR B 195  VAL B 198  TYR B 227                    
SITE     2 AC8  6 HOH B 385  HOH B 441                                          
SITE     1 AC9 18 TYR B  29  MET B  35  ARG B  39  GLY B 143                    
SITE     2 AC9 18 LEU B 144  HIS B 145  HIS B 146  GLY B 154                    
SITE     3 AC9 18 PHE B 155  CYS B 156  ASP B 181  HIS B 183                    
SITE     4 AC9 18 PHE B 210  ASP B 269  GLY B 305  GLY B 306                    
SITE     5 AC9 18 TYR B 308   ZN B 379                                          
SITE     1 BC1  4 ASP C 181  HIS C 183  ASP C 269  LLX C 400                    
SITE     1 BC2  5 ASP C 179  ASP C 181  HIS C 183  SER C 202                    
SITE     2 BC2  5 PHE C 203                                                     
SITE     1 BC3  6 PHE C 192  THR C 195  VAL C 198  TYR C 227                    
SITE     2 BC3  6 HOH C 389  HOH C 464                                          
SITE     1 BC4 19 TYR C  29  MET C  35  ARG C  39  GLY C 143                    
SITE     2 BC4 19 LEU C 144  HIS C 145  HIS C 146  GLY C 154                    
SITE     3 BC4 19 PHE C 155  CYS C 156  ASP C 181  HIS C 183                    
SITE     4 BC4 19 PHE C 210  ASP C 269  LEU C 276  GLY C 305                    
SITE     5 BC4 19 GLY C 306  TYR C 308   ZN C 379                               
CRYST1   92.311   97.227  138.849  90.00  90.00  90.00 P 21 21 21   12          
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      0.010833  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010285  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007202        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system