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Database: PDB
Entry: 2VQQ
LinkDB: 2VQQ
Original site: 2VQQ 
HEADER    HYDROLASE                               18-MAR-08   2VQQ              
TITLE     STRUCTURE OF HDAC4 CATALYTIC DOMAIN (A DOUBLE CYSTEINE-TO-            
TITLE    2 ALANINE MUTANT) BOUND TO A TRIFLUOROMETHYLKETONE INHBITOR            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE DEACETYLASE 4;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 648-1057;                       
COMPND   5 SYNONYM: HD4;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PETM-11 (OBTAINED FROM EMBL-              
SOURCE   9  HEIDELBERG)                                                         
KEYWDS    INHIBITOR, REPRESSOR, CHROMATIN, COILED COIL, HISTONE                 
KEYWDS   2 DEACETYLASE, TRANSCRIPTION REGULATION, UBL CONJUGATION,              
KEYWDS   3 CHROMATIN REGULATOR, POLYMORPHISM, TRANSCRIPTION,                    
KEYWDS   4 PHOSPHOPROTEIN, HDAC, ZINC, HDACI, NUCLEUS, HYDROLASE,               
KEYWDS   5 CYTOPLASM                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.BOTTOMLEY,P.LO SURDO,P.DI GIOVINE,A.CIRILLO,R.SCARPELLI,          
AUTHOR   2 F.FERRIGNO,P.JONES,P.NEDDERMANN,R.DE FRANCESCO,                      
AUTHOR   3 C.STEINKUHLER,P.GALLINARI,A.CARFI                                    
REVDAT   3   24-FEB-09 2VQQ    1       VERSN                                    
REVDAT   2   30-SEP-08 2VQQ    1       JRNL                                     
REVDAT   1   08-JUL-08 2VQQ    0                                                
JRNL        AUTH   M.J.BOTTOMLEY,P.LO SURDO,P.DI GIOVINE,A.CIRILLO,             
JRNL        AUTH 2 R.SCARPELLI,F.FERRIGNO,P.JONES,P.NEDDERMANN,                 
JRNL        AUTH 3 R.DE FRANCESCO,C.STEINKUHLER,P.GALLINARI,A.CARFI             
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE HUMAN              
JRNL        TITL 2 HDAC4 CATALYTIC DOMAIN REVEALS A REGULATORY                  
JRNL        TITL 3 ZINC-BINDING DOMAIN.                                         
JRNL        REF    J.BIOL.CHEM.                  V. 283 26694 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18614528                                                     
JRNL        DOI    10.1074/JBC.M803514200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.9  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 75011                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3935                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5517                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 292                          
REMARK   3   BIN FREE R VALUE                    : 0.2960                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5530                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 79                                      
REMARK   3   SOLVENT ATOMS            : 609                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.63000                                              
REMARK   3    B22 (A**2) : -0.40000                                             
REMARK   3    B33 (A**2) : 0.67000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.45000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.133         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.123         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.088         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.945         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5745 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3798 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7845 ; 1.240 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9252 ; 0.946 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   755 ; 5.701 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   243 ;33.658 ;23.868       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   910 ;13.751 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;15.744 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   876 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6500 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1150 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1127 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3897 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2714 ; 0.170 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2734 ; 0.083 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   412 ; 0.260 ; 0.200       
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):     7 ; 0.122 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    53 ; 0.289 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.086 ; 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):  3611 ; 0.520 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5797 ; 0.961 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2156 ; 1.351 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2026 ; 2.230 ; 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          
REMARK   3  RIDING POSITIONS. RESIDUES NOT VISIBLE IN DENSITY MAPS INCLUDE      
REMARK   3  23-33, 85-111 IN CHAIN A AND 22-35,85-112 IN CHAIN B.               
REMARK   4                                                                      
REMARK   4 2VQQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-MAR-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-35720.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20692                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.8                                
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.47                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.60                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2VQJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULPHATE, 0.1M MES         
REMARK 280  PH 6.5, 10% DIOXANE 1MM DTT                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.33650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 669 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 700 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 669 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 700 TO ALA                        
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     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     MET A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     CYS A    23                                                      
REMARK 465     THR A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     PRO A    32                                                      
REMARK 465     GLU A    33                                                      
REMARK 465     ASN A    85                                                      
REMARK 465     ARG A    86                                                      
REMARK 465     GLN A    87                                                      
REMARK 465     LYS A    88                                                      
REMARK 465     LEU A    89                                                      
REMARK 465     ASP A    90                                                      
REMARK 465     SER A    91                                                      
REMARK 465     LYS A    92                                                      
REMARK 465     LYS A    93                                                      
REMARK 465     LEU A    94                                                      
REMARK 465     LEU A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     SER A    97                                                      
REMARK 465     LEU A    98                                                      
REMARK 465     ALA A    99                                                      
REMARK 465     SER A   100                                                      
REMARK 465     VAL A   101                                                      
REMARK 465     PHE A   102                                                      
REMARK 465     VAL A   103                                                      
REMARK 465     ARG A   104                                                      
REMARK 465     LEU A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     CYS A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     GLY A   109                                                      
REMARK 465     VAL A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     ASN A   406                                                      
REMARK 465     GLU A   407                                                      
REMARK 465     GLU A   408                                                      
REMARK 465     ALA A   409                                                      
REMARK 465     GLU A   410                                                      
REMARK 465     THR A   411                                                      
REMARK 465     VAL A   412                                                      
REMARK 465     THR A   413                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     MET B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     GLN B    22                                                      
REMARK 465     CYS B    23                                                      
REMARK 465     THR B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     SER B    29                                                      
REMARK 465     SER B    30                                                      
REMARK 465     HIS B    31                                                      
REMARK 465     PRO B    32                                                      
REMARK 465     GLU B    33                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     ALA B    35                                                      
REMARK 465     ASN B    85                                                      
REMARK 465     ARG B    86                                                      
REMARK 465     GLN B    87                                                      
REMARK 465     LYS B    88                                                      
REMARK 465     LEU B    89                                                      
REMARK 465     ASP B    90                                                      
REMARK 465     SER B    91                                                      
REMARK 465     LYS B    92                                                      
REMARK 465     LYS B    93                                                      
REMARK 465     LEU B    94                                                      
REMARK 465     LEU B    95                                                      
REMARK 465     GLY B    96                                                      
REMARK 465     SER B    97                                                      
REMARK 465     LEU B    98                                                      
REMARK 465     ALA B    99                                                      
REMARK 465     SER B   100                                                      
REMARK 465     VAL B   101                                                      
REMARK 465     PHE B   102                                                      
REMARK 465     VAL B   103                                                      
REMARK 465     ARG B   104                                                      
REMARK 465     LEU B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     CYS B   107                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     GLY B   109                                                      
REMARK 465     VAL B   110                                                      
REMARK 465     GLY B   111                                                      
REMARK 465     VAL B   112                                                      
REMARK 465     ASN B   406                                                      
REMARK 465     GLU B   407                                                      
REMARK 465     GLU B   408                                                      
REMARK 465     ALA B   409                                                      
REMARK 465     GLU B   410                                                      
REMARK 465     THR B   411                                                      
REMARK 465     VAL B   412                                                      
REMARK 465     THR B   413                                                      
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   7    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A  34    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 389    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 405    CG   CD   OE1  OE2                                  
REMARK 470     ARG B   7    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B  21    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B 389    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 405    CB   CG   CD   OE1  OE2                             
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 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    THR A 297      -42.61    -10.68                                   
REMARK 500    HIS A 332      -25.26   -144.98                                   
REMARK 500    ALA B 279       65.53     61.41                                   
REMARK 500    THR B 297      -45.22    -15.26                                   
REMARK 500    HIS B 332      -22.53   -147.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG A  389     THR A  390                 -146.72                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR A 297        23.0      L          L   OUTSIDE RANGE           
REMARK 500    THR B 297        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 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 A1408   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 194   O                                                      
REMARK 620 2 ASP A 194   OD1  68.7                                              
REMARK 620 3 HIS A 198   O   160.2  92.4                                        
REMARK 620 4 SER A 217   OG   84.4 116.0 110.2                                  
REMARK 620 5 LEU A 218   O    72.9 132.5 119.9  86.2                            
REMARK 620 6 ASP A 196   O    97.6  94.2  77.3 147.8  64.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A1409   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 207   O                                                      
REMARK 620 2 ASP A 210   O    76.0                                              
REMARK 620 3 VAL A 213   O   123.0  69.8                                        
REMARK 620 4 HOH A2154   O    88.1  96.7 139.0                                  
REMARK 620 5 PHE A 244   O   162.0 116.5  74.8  77.9                            
REMARK 620 6 HOH A2156   O    67.4 143.1 127.6  86.8 100.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B1407   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 217   OG                                                     
REMARK 620 2 HIS B 198   O   111.0                                              
REMARK 620 3 ASP B 194   O    83.0 161.1                                        
REMARK 620 4 LEU B 218   O    86.0 119.0  73.2                                  
REMARK 620 5 ASP B 194   OD1 114.8  93.4  68.6 133.0                            
REMARK 620 6 ASP B 196   O   147.3  77.0  98.3  63.5  95.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B1408   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE B 207   O                                                      
REMARK 620 2 HOH B2209   O    87.8                                              
REMARK 620 3 HOH B2212   O    71.1  89.2                                        
REMARK 620 4 ASP B 210   O    76.0  94.3 146.7                                  
REMARK 620 5 PHE B 244   O   164.9  79.7 100.0 113.1                            
REMARK 620 6 VAL B 213   O   120.7 137.8 127.5  67.2  74.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1411  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TFG A1410   O3                                                     
REMARK 620 2 ASP A 196   OD2  94.5                                              
REMARK 620 3 ASP A 290   OD2 153.3 105.5                                        
REMARK 620 4 TFG A1410   O2   63.6 141.7  89.9                                  
REMARK 620 5 HIS A 198   ND1  98.5 104.0  93.7 109.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1410  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TFG B1409   O3                                                     
REMARK 620 2 HIS B 198   ND1  97.6                                              
REMARK 620 3 ASP B 290   OD2 149.6  93.8                                        
REMARK 620 4 TFG B1409   O2   62.3 109.4  87.3                                  
REMARK 620 5 ASP B 196   OD2  94.6 103.6 109.9 141.6                            
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 SO4 A1406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K A1408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K A1409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TFG A1410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K B1407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K B1408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TFG B1409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1411                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VQW   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF INHIBITOR-FREE HDAC4 CATALYTIC                         
REMARK 900  DOMAIN (WITH GAIN-OF-FUNCTION MUTATION                              
REMARK 900  HIS332TYR)                                                          
REMARK 900 RELATED ID: 2VQO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HDAC4 CATALYTIC DOMAIN WITH A                          
REMARK 900  GAIN-OF-FUNCTION MUATION BOUND TO A                                 
REMARK 900  TRIFLUOROMETHYLKETONE INHBITOR                                      
REMARK 900 RELATED ID: 2VQV   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HDAC4 CATALYTIC DOMAIN WITH A                          
REMARK 900  GAIN-OF-FUNCTION MUATION BOUND TO A                                 
REMARK 900  HYDROXAMIC ACID INHIBITOR                                           
REMARK 900 RELATED ID: 2VQM   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HDAC4 CATALYTIC DOMAIN BOUND TO                        
REMARK 900   A HYDROXAMIC ACID INHBITOR                                         
REMARK 900 RELATED ID: 2VQJ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HDAC4 CATALYTIC DOMAIN BOUND TO                        
REMARK 900   A TRIFLUOROMETHYLKETONE INHBITOR                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 TWO POINT MUTANTS PRESENT INCLUDE C25A AND C56A                      
DBREF  2VQQ A    1     3  PDB    2VQQ     2VQQ             1      3             
DBREF  2VQQ A    4   413  UNP    P56524   HDAC4_HUMAN    648   1057             
DBREF  2VQQ B    1     3  PDB    2VQQ     2VQQ             1      3             
DBREF  2VQQ B    4   413  UNP    P56524   HDAC4_HUMAN    648   1057             
SEQADV 2VQQ ALA A   25  UNP  P56524    CYS   669 ENGINEERED MUTATION            
SEQADV 2VQQ ALA A   56  UNP  P56524    CYS   700 ENGINEERED MUTATION            
SEQADV 2VQQ ALA B   25  UNP  P56524    CYS   669 ENGINEERED MUTATION            
SEQADV 2VQQ ALA B   56  UNP  P56524    CYS   700 ENGINEERED MUTATION            
SEQRES   1 A  413  GLY ALA MET THR LYS PRO ARG PHE THR THR GLY LEU VAL          
SEQRES   2 A  413  TYR ASP THR LEU MET LEU LYS HIS GLN CYS THR ALA GLY          
SEQRES   3 A  413  SER SER SER SER HIS PRO GLU HIS ALA GLY ARG ILE GLN          
SEQRES   4 A  413  SER ILE TRP SER ARG LEU GLN GLU THR GLY LEU ARG GLY          
SEQRES   5 A  413  LYS CYS GLU ALA ILE ARG GLY ARG LYS ALA THR LEU GLU          
SEQRES   6 A  413  GLU LEU GLN THR VAL HIS SER GLU ALA HIS THR LEU LEU          
SEQRES   7 A  413  TYR GLY THR ASN PRO LEU ASN ARG GLN LYS LEU ASP SER          
SEQRES   8 A  413  LYS LYS LEU LEU GLY SER LEU ALA SER VAL PHE VAL ARG          
SEQRES   9 A  413  LEU PRO CYS GLY GLY VAL GLY VAL ASP SER ASP THR ILE          
SEQRES  10 A  413  TRP ASN GLU VAL HIS SER ALA GLY ALA ALA ARG LEU ALA          
SEQRES  11 A  413  VAL GLY CYS VAL VAL GLU LEU VAL PHE LYS VAL ALA THR          
SEQRES  12 A  413  GLY GLU LEU LYS ASN GLY PHE ALA VAL VAL ARG PRO PRO          
SEQRES  13 A  413  GLY HIS HIS ALA GLU GLU SER THR PRO MET GLY PHE CYS          
SEQRES  14 A  413  TYR PHE ASN SER VAL ALA VAL ALA ALA LYS LEU LEU GLN          
SEQRES  15 A  413  GLN ARG LEU SER VAL SER LYS ILE LEU ILE VAL ASP TRP          
SEQRES  16 A  413  ASP VAL HIS HIS GLY ASN GLY THR GLN GLN ALA PHE TYR          
SEQRES  17 A  413  SER ASP PRO SER VAL LEU TYR MET SER LEU HIS ARG TYR          
SEQRES  18 A  413  ASP ASP GLY ASN PHE PHE PRO GLY SER GLY ALA PRO ASP          
SEQRES  19 A  413  GLU VAL GLY THR GLY PRO GLY VAL GLY PHE ASN VAL ASN          
SEQRES  20 A  413  MET ALA PHE THR GLY GLY LEU ASP PRO PRO MET GLY ASP          
SEQRES  21 A  413  ALA GLU TYR LEU ALA ALA PHE ARG THR VAL VAL MET PRO          
SEQRES  22 A  413  ILE ALA SER GLU PHE ALA PRO ASP VAL VAL LEU VAL SER          
SEQRES  23 A  413  SER GLY PHE ASP ALA VAL GLU GLY HIS PRO THR PRO LEU          
SEQRES  24 A  413  GLY GLY TYR ASN LEU SER ALA ARG CYS PHE GLY TYR LEU          
SEQRES  25 A  413  THR LYS GLN LEU MET GLY LEU ALA GLY GLY ARG ILE VAL          
SEQRES  26 A  413  LEU ALA LEU GLU GLY GLY HIS ASP LEU THR ALA ILE CYS          
SEQRES  27 A  413  ASP ALA SER GLU ALA CYS VAL SER ALA LEU LEU GLY ASN          
SEQRES  28 A  413  GLU LEU ASP PRO LEU PRO GLU LYS VAL LEU GLN GLN ARG          
SEQRES  29 A  413  PRO ASN ALA ASN ALA VAL ARG SER MET GLU LYS VAL MET          
SEQRES  30 A  413  GLU ILE HIS SER LYS TYR TRP ARG CYS LEU GLN ARG THR          
SEQRES  31 A  413  THR SER THR ALA GLY ARG SER LEU ILE GLU ALA GLN THR          
SEQRES  32 A  413  CYS GLU ASN GLU GLU ALA GLU THR VAL THR                      
SEQRES   1 B  413  GLY ALA MET THR LYS PRO ARG PHE THR THR GLY LEU VAL          
SEQRES   2 B  413  TYR ASP THR LEU MET LEU LYS HIS GLN CYS THR ALA GLY          
SEQRES   3 B  413  SER SER SER SER HIS PRO GLU HIS ALA GLY ARG ILE GLN          
SEQRES   4 B  413  SER ILE TRP SER ARG LEU GLN GLU THR GLY LEU ARG GLY          
SEQRES   5 B  413  LYS CYS GLU ALA ILE ARG GLY ARG LYS ALA THR LEU GLU          
SEQRES   6 B  413  GLU LEU GLN THR VAL HIS SER GLU ALA HIS THR LEU LEU          
SEQRES   7 B  413  TYR GLY THR ASN PRO LEU ASN ARG GLN LYS LEU ASP SER          
SEQRES   8 B  413  LYS LYS LEU LEU GLY SER LEU ALA SER VAL PHE VAL ARG          
SEQRES   9 B  413  LEU PRO CYS GLY GLY VAL GLY VAL ASP SER ASP THR ILE          
SEQRES  10 B  413  TRP ASN GLU VAL HIS SER ALA GLY ALA ALA ARG LEU ALA          
SEQRES  11 B  413  VAL GLY CYS VAL VAL GLU LEU VAL PHE LYS VAL ALA THR          
SEQRES  12 B  413  GLY GLU LEU LYS ASN GLY PHE ALA VAL VAL ARG PRO PRO          
SEQRES  13 B  413  GLY HIS HIS ALA GLU GLU SER THR PRO MET GLY PHE CYS          
SEQRES  14 B  413  TYR PHE ASN SER VAL ALA VAL ALA ALA LYS LEU LEU GLN          
SEQRES  15 B  413  GLN ARG LEU SER VAL SER LYS ILE LEU ILE VAL ASP TRP          
SEQRES  16 B  413  ASP VAL HIS HIS GLY ASN GLY THR GLN GLN ALA PHE TYR          
SEQRES  17 B  413  SER ASP PRO SER VAL LEU TYR MET SER LEU HIS ARG TYR          
SEQRES  18 B  413  ASP ASP GLY ASN PHE PHE PRO GLY SER GLY ALA PRO ASP          
SEQRES  19 B  413  GLU VAL GLY THR GLY PRO GLY VAL GLY PHE ASN VAL ASN          
SEQRES  20 B  413  MET ALA PHE THR GLY GLY LEU ASP PRO PRO MET GLY ASP          
SEQRES  21 B  413  ALA GLU TYR LEU ALA ALA PHE ARG THR VAL VAL MET PRO          
SEQRES  22 B  413  ILE ALA SER GLU PHE ALA PRO ASP VAL VAL LEU VAL SER          
SEQRES  23 B  413  SER GLY PHE ASP ALA VAL GLU GLY HIS PRO THR PRO LEU          
SEQRES  24 B  413  GLY GLY TYR ASN LEU SER ALA ARG CYS PHE GLY TYR LEU          
SEQRES  25 B  413  THR LYS GLN LEU MET GLY LEU ALA GLY GLY ARG ILE VAL          
SEQRES  26 B  413  LEU ALA LEU GLU GLY GLY HIS ASP LEU THR ALA ILE CYS          
SEQRES  27 B  413  ASP ALA SER GLU ALA CYS VAL SER ALA LEU LEU GLY ASN          
SEQRES  28 B  413  GLU LEU ASP PRO LEU PRO GLU LYS VAL LEU GLN GLN ARG          
SEQRES  29 B  413  PRO ASN ALA ASN ALA VAL ARG SER MET GLU LYS VAL MET          
SEQRES  30 B  413  GLU ILE HIS SER LYS TYR TRP ARG CYS LEU GLN ARG THR          
SEQRES  31 B  413  THR SER THR ALA GLY ARG SER LEU ILE GLU ALA GLN THR          
SEQRES  32 B  413  CYS GLU ASN GLU GLU ALA GLU THR VAL THR                      
HET    SO4  A1406       5                                                       
HET    SO4  A1407       5                                                       
HET      K  A1408       1                                                       
HET      K  A1409       1                                                       
HET    TFG  A1410      29                                                       
HET    SO4  B1406       5                                                       
HET      K  B1407       1                                                       
HET      K  B1408       1                                                       
HET    TFG  B1409      29                                                       
HET     ZN  B1410       1                                                       
HET     ZN  A1411       1                                                       
HETNAM     TFG 2,2,2-TRIFLUORO-1-{5-[(3-PHENYL-5,6-                             
HETNAM   2 TFG  DIHYDROIMIDAZO[1,2-A]PYRAZIN-7(8H)-YL)CARBONYL]                 
HETNAM   3 TFG  THIOPHEN-2-YL}ETHANE-1,1-DIOL                                   
HETNAM       K POTASSIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   3  TFG    2(C19 H16 N3 O3 F3 S1)                                       
FORMUL   4    K    4(K 1+)                                                      
FORMUL   5  SO4    3(O4 S 2-)                                                   
FORMUL   6   ZN    2(ZN 2+)                                                     
FORMUL   7  HOH   *609(H2 O1)                                                   
HELIX    1   1 ASP A   15  LEU A   19  5                                   5    
HELIX    2   2 GLY A   36  GLU A   47  1                                  12    
HELIX    3   3 LEU A   50  CYS A   54  1                                   5    
HELIX    4   4 THR A   63  GLN A   68  1                                   6    
HELIX    5   5 GLU A   73  TYR A   79  1                                   7    
HELIX    6   6 ILE A  117  THR A  143  1                                  27    
HELIX    7   7 ASN A  172  SER A  186  1                                  15    
HELIX    8   8 GLY A  200  PHE A  207  1                                   8    
HELIX    9   9 THR A  238  VAL A  242  5                                   5    
HELIX   10  10 GLY A  259  VAL A  270  1                                  12    
HELIX   11  11 VAL A  270  ALA A  279  1                                  10    
HELIX   12  12 SER A  305  MET A  317  1                                  13    
HELIX   13  14 ASP A  333  LEU A  349  1                                  17    
HELIX   14  15 PRO A  357  GLN A  362  1                                   6    
HELIX   15  16 ASN A  366  SER A  381  1                                  16    
HELIX   16  17 TRP A  384  GLN A  388  5                                   5    
HELIX   17  18 SER A  397  CYS A  404  1                                   8    
HELIX   18  19 ASP B   15  LEU B   19  5                                   5    
HELIX   29  20 GLY B   36  THR B   48  1                                  13    
HELIX   20  21 GLY B   49  CYS B   54  1                                   6    
HELIX   21  22 THR B   63  GLN B   68  1                                   6    
HELIX   22  23 SER B   72  THR B   81  1                                  10    
HELIX   23  24 ILE B  117  THR B  143  1                                  27    
HELIX   24  25 ASN B  172  SER B  186  1                                  15    
HELIX   25  26 GLY B  200  PHE B  207  1                                   8    
HELIX   26  27 ASP B  222  ASN B  225  5                                   4    
HELIX   27  28 THR B  238  VAL B  242  5                                   5    
HELIX   28  29 GLY B  259  VAL B  270  1                                  12    
HELIX   39  30 VAL B  270  ALA B  279  1                                  10    
HELIX   30  31 SER B  305  MET B  317  1                                  13    
HELIX   31  32 GLY B  318  GLY B  322  5                                   5    
HELIX   32  33 ASP B  333  LEU B  349  1                                  17    
HELIX   33  34 PRO B  357  GLN B  362  1                                   6    
HELIX   34  35 ASN B  366  SER B  381  1                                  16    
HELIX   35  36 TRP B  384  GLN B  388  5                                   5    
HELIX   36  37 SER B  397  CYS B  404  1                                   8    
SHEET    1  AA 8 GLU A  55  ILE A  57  0                                        
SHEET    2  AA 8 THR A  10  VAL A  13  1  O  THR A  10   N  GLU A  55           
SHEET    3  AA 8 ASN A 148  ALA A 151  1  O  ASN A 148   N  GLY A  11           
SHEET    4  AA 8 ILE A 324  LEU A 328  1  O  ILE A 324   N  GLY A 149           
SHEET    5  AA 8 VAL A 282  SER A 287  1  O  VAL A 283   N  VAL A 325           
SHEET    6  AA 8 ILE A 190  ASP A 194  1  O  LEU A 191   N  LEU A 284           
SHEET    7  AA 8 VAL A 213  ARG A 220  1  O  LEU A 214   N  ILE A 192           
SHEET    8  AA 8 ASN A 245  PHE A 250  1  O  VAL A 246   N  SER A 217           
SHEET    1  BA 8 GLU B  55  ILE B  57  0                                        
SHEET    2  BA 8 THR B  10  VAL B  13  1  O  THR B  10   N  GLU B  55           
SHEET    3  BA 8 ASN B 148  ALA B 151  1  O  ASN B 148   N  GLY B  11           
SHEET    4  BA 8 ILE B 324  LEU B 328  1  O  ILE B 324   N  GLY B 149           
SHEET    5  BA 8 VAL B 282  SER B 287  1  O  VAL B 283   N  VAL B 325           
SHEET    6  BA 8 ILE B 190  ASP B 194  1  O  LEU B 191   N  LEU B 284           
SHEET    7  BA 8 VAL B 213  ARG B 220  1  O  LEU B 214   N  ILE B 192           
SHEET    8  BA 8 ASN B 245  PHE B 250  1  O  VAL B 246   N  SER B 217           
LINK         K     K A1408                 O   ASP A 194     1555   1555  2.88  
LINK         K     K A1408                 OD1 ASP A 194     1555   1555  2.91  
LINK         K     K A1408                 O   HIS A 198     1555   1555  2.91  
LINK         K     K A1408                 OG  SER A 217     1555   1555  2.78  
LINK         K     K A1408                 O   LEU A 218     1555   1555  2.85  
LINK         K     K A1408                 O   ASP A 196     1555   1555  2.74  
LINK         K     K A1409                 O   PHE A 207     1555   1555  2.69  
LINK         K     K A1409                 O   ASP A 210     1555   1555  2.95  
LINK         K     K A1409                 O   VAL A 213     1555   1555  2.75  
LINK         K     K A1409                 O   HOH A2154     1555   1555  2.74  
LINK         K     K A1409                 O   PHE A 244     1555   1555  3.11  
LINK         K     K A1409                 O   HOH A2156     1555   1555  3.01  
LINK        ZN    ZN A1411                 O3  TFG A1410     1555   1555  2.34  
LINK        ZN    ZN A1411                 OD2 ASP A 196     1555   1555  2.02  
LINK        ZN    ZN A1411                 OD2 ASP A 290     1555   1555  1.89  
LINK        ZN    ZN A1411                 O2  TFG A1410     1555   1555  2.01  
LINK        ZN    ZN A1411                 ND1 HIS A 198     1555   1555  2.23  
LINK         K     K B1407                 O   ASP B 196     1555   1555  2.71  
LINK         K     K B1407                 OD1 ASP B 194     1555   1555  2.93  
LINK         K     K B1407                 O   LEU B 218     1555   1555  2.88  
LINK         K     K B1407                 O   ASP B 194     1555   1555  2.88  
LINK         K     K B1407                 O   HIS B 198     1555   1555  2.81  
LINK         K     K B1407                 OG  SER B 217     1555   1555  2.86  
LINK         K     K B1408                 O   VAL B 213     1555   1555  2.79  
LINK         K     K B1408                 O   PHE B 244     1555   1555  3.13  
LINK         K     K B1408                 O   ASP B 210     1555   1555  3.11  
LINK         K     K B1408                 O   HOH B2212     1555   1555  2.94  
LINK         K     K B1408                 O   HOH B2209     1555   1555  2.78  
LINK         K     K B1408                 O   PHE B 207     1555   1555  2.58  
LINK        ZN    ZN B1410                 ND1 HIS B 198     1555   1555  2.15  
LINK        ZN    ZN B1410                 OD2 ASP B 290     1555   1555  1.97  
LINK        ZN    ZN B1410                 O2  TFG B1409     1555   1555  2.15  
LINK        ZN    ZN B1410                 OD2 ASP B 196     1555   1555  2.03  
LINK        ZN    ZN B1410                 O3  TFG B1409     1555   1555  2.31  
CISPEP   1 ARG A  154    PRO A  155          0        -5.60                     
CISPEP   2 PHE A  227    PRO A  228          0         1.25                     
CISPEP   3 ASP A  255    PRO A  256          0        -5.78                     
CISPEP   4 ARG B  154    PRO B  155          0        -4.73                     
CISPEP   5 PHE B  227    PRO B  228          0        -3.21                     
CISPEP   6 ASP B  255    PRO B  256          0        -3.25                     
SITE     1 AC1  9 LYS A  20  ARG A  37  ILE A  38  ARG A 154                    
SITE     2 AC1  9 HOH A2012  HOH A2266  HOH A2267  HOH A2268                    
SITE     3 AC1  9 HOH B2099                                                     
SITE     1 AC2  4 TRP A  42  GLN A  46  ARG A  51  HOH A2269                    
SITE     1 AC3  5 ASP A 194  ASP A 196  HIS A 198  SER A 217                    
SITE     2 AC3  5 LEU A 218                                                     
SITE     1 AC4  6 PHE A 207  ASP A 210  VAL A 213  PHE A 244                    
SITE     2 AC4  6 HOH A2154  HOH A2156                                          
SITE     1 AC5 18 PRO A 156  HIS A 158  HIS A 159  GLY A 167                    
SITE     2 AC5 18 PHE A 168  ASP A 196  HIS A 198  PHE A 227                    
SITE     3 AC5 18 ASP A 290  GLY A 330   ZN A1411  HOH A2194                    
SITE     4 AC5 18 HOH A2270  LEU B  78  TYR B  79  THR B  81                    
SITE     5 AC5 18 ALA B 124  HOH B2155                                          
SITE     1 AC6  8 LYS B  20  ARG B  37  ILE B  38  ARG B 154                    
SITE     2 AC6  8 HOH B2334  HOH B2335  HOH B2336  HOH B2337                    
SITE     1 AC7  5 ASP B 194  ASP B 196  HIS B 198  SER B 217                    
SITE     2 AC7  5 LEU B 218                                                     
SITE     1 AC8  6 PHE B 207  ASP B 210  VAL B 213  PHE B 244                    
SITE     2 AC8  6 HOH B2209  HOH B2212                                          
SITE     1 AC9 18 LEU A  78  TYR A  79  THR A  81  ALA A 124                    
SITE     2 AC9 18 PRO B 156  HIS B 158  HIS B 159  GLY B 167                    
SITE     3 AC9 18 PHE B 168  ASP B 196  HIS B 198  PHE B 227                    
SITE     4 AC9 18 ASP B 290  GLY B 330   ZN B1410  HOH B2253                    
SITE     5 AC9 18 HOH B2338  HOH B2339                                          
SITE     1 BC1  4 ASP B 196  HIS B 198  ASP B 290  TFG B1409                    
SITE     1 BC2  4 ASP A 196  HIS A 198  ASP A 290  TFG A1410                    
CRYST1   85.605   70.673   88.201  90.00 108.08  90.00 P 1 21 1      4          
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      0.011682  0.000000  0.003814        0.00000                         
SCALE2      0.000000  0.014150  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011927        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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