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Database: PDB
Entry: 4LY1
LinkDB: 4LY1
Original site: 4LY1 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           30-JUL-13   4LY1              
TITLE     STRUCTURE OF HUMAN HDAC2 IN COMPLEX WITH INHIBITOR 4-(ACETYLAMINO)-N- 
TITLE    2 [2-AMINO-5-(THIOPHEN-2-YL)PHENYL]BENZAMIDE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE DEACETYLASE 2;                                     
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: CORE DOMAIN (UNP RESIDUES 8-376);                          
COMPND   5 SYNONYM: HD2;                                                        
COMPND   6 EC: 3.5.1.98;                                                        
COMPND   7 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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    DEACETYLASE, HISTONE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.FONG,P.J.LUPARDUS                                                   
REVDAT   3   20-SEP-23 4LY1    1       REMARK LINK                              
REVDAT   2   02-OCT-13 4LY1    1       JRNL                                     
REVDAT   1   21-AUG-13 4LY1    0                                                
JRNL        AUTH   B.E.LAUFFER,R.MINTZER,R.FONG,S.MUKUND,C.TAM,I.ZILBERLEYB,    
JRNL        AUTH 2 B.FLICKE,A.RITSCHER,G.FEDOROWICZ,R.VALLERO,D.F.ORTWINE,      
JRNL        AUTH 3 J.GUNZNER,Z.MODRUSAN,L.NEUMANN,C.M.KOTH,P.J.LUPARDUS,        
JRNL        AUTH 4 J.S.KAMINKER,C.E.HEISE,P.STEINER                             
JRNL        TITL   HISTONE DEACETYLASE (HDAC) INHIBITOR KINETIC RATE CONSTANTS  
JRNL        TITL 2 CORRELATE WITH CELLULAR HISTONE ACETYLATION BUT NOT          
JRNL        TITL 3 TRANSCRIPTION AND CELL VIABILITY.                            
JRNL        REF    J.BIOL.CHEM.                  V. 288 26926 2013              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   23897821                                                     
JRNL        DOI    10.1074/JBC.M113.490706                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.57 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 174095                         
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)  : 0.170                          
REMARK   3   R VALUE            (WORKING SET)  : 0.169                          
REMARK   3   FREE R VALUE                      : 0.187                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 8703                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.57                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.61                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.94                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 12661                    
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2179                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 12015                    
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2170                   
REMARK   3   BIN FREE R VALUE                        : 0.2347                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.10                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 646                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8869                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 201                                     
REMARK   3   SOLVENT ATOMS            : 846                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.36860                                              
REMARK   3    B22 (A**2) : -6.58640                                             
REMARK   3    B33 (A**2) : 3.21780                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.163               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.073               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 9480   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 12784  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3329   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 227    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1389   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 9480   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1117   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 12225  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.70                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.66                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4LY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000081228.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-AUG-11                          
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               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 174095                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.570                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
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 3MAX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CHES, PH 9.5, 40% PEG-600, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
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       46.01700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.46100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.74500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.46100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.01700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.74500            
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     HIS A   380                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     HIS B   380                                                      
REMARK 465     GLY C    12                                                      
REMARK 465     PRO C   379                                                      
REMARK 465     HIS C   380                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B  13    CG   CD   CE   NZ                                   
REMARK 470     LYS C  13    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   781     O    HOH A   795              2.19            
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    TYR A  72      -58.58   -129.39                                   
REMARK 500    GLU A 103      -91.99   -114.11                                   
REMARK 500    CYS A 105       75.59   -116.15                                   
REMARK 500    PHE A 155       -3.25     79.61                                   
REMARK 500    TYR A 226        2.78     87.73                                   
REMARK 500    TYR B  72      -56.63   -126.85                                   
REMARK 500    GLU B 103     -102.63   -110.45                                   
REMARK 500    CYS B 105       78.52   -115.00                                   
REMARK 500    TYR B 226        2.26     86.97                                   
REMARK 500    TYR C  72      -53.78   -126.17                                   
REMARK 500    GLU C 103     -102.36   -111.17                                   
REMARK 500    CYS C 105       78.11   -115.64                                   
REMARK 500    TYR C 226        5.77     82.05                                   
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 402  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   100.3 104.2                                        
REMARK 620 4 HIS A 183   O    91.8 163.1  82.9                                  
REMARK 620 5 SER A 202   OG  101.1  88.0 157.9  90.7                            
REMARK 620 6 PHE A 203   O   145.9  78.1  71.6 118.8  93.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 181   OD2                                                    
REMARK 620 2 HIS A 183   ND1 100.4                                              
REMARK 620 3 ASP A 269   OD2 106.7 104.2                                        
REMARK 620 4 20Y A 407   N20  93.2 107.2 138.8                                  
REMARK 620 5 20Y A 407   N20  96.1 103.8 139.6   4.1                            
REMARK 620 6 20Y A 407   O12 173.0  84.2  76.9  80.4  77.6                      
REMARK 620 7 20Y A 407   O12 167.1  86.5  81.8  74.3  71.6   6.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 192   O                                                      
REMARK 620 2 THR A 195   O    77.6                                              
REMARK 620 3 VAL A 198   O   117.6  83.2                                        
REMARK 620 4 TYR A 227   O   156.0 121.6  81.4                                  
REMARK 620 5 HOH A 520   O    90.3  92.0 149.6  75.7                            
REMARK 620 6 HOH A 521   O    74.8 151.9 114.5  83.9  82.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 179   OD1                                                    
REMARK 620 2 ASP B 179   O    72.1                                              
REMARK 620 3 ASP B 181   O   101.0 103.8                                        
REMARK 620 4 HIS B 183   O    92.3 164.0  82.4                                  
REMARK 620 5 SER B 202   OG  102.5  88.0 156.0  91.9                            
REMARK 620 6 PHE B 203   O   146.3  78.5  70.2 117.5  92.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  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 103.7 103.9                                        
REMARK 620 4 20Y B 408   N20  97.5 105.7 139.5                                  
REMARK 620 5 20Y B 408   N20  97.6 107.5 137.9   1.9                            
REMARK 620 6 20Y B 408   O12 171.3  85.0  81.3  74.4  74.2                      
REMARK 620 7 20Y B 408   O12 174.0  84.4  78.5  77.6  77.4   3.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE B 192   O                                                      
REMARK 620 2 THR B 195   O    79.5                                              
REMARK 620 3 VAL B 198   O   119.6  83.7                                        
REMARK 620 4 TYR B 227   O   155.8 120.0  79.2                                  
REMARK 620 5 HOH B 514   O    89.8  91.9 148.6  76.2                            
REMARK 620 6 HOH B 535   O    72.8 151.5 115.5  85.7  81.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 179   OD1                                                    
REMARK 620 2 ASP C 179   O    70.9                                              
REMARK 620 3 ASP C 181   O   100.7 103.8                                        
REMARK 620 4 HIS C 183   O    93.3 163.7  82.6                                  
REMARK 620 5 SER C 202   OG  103.2  89.2 155.5  90.6                            
REMARK 620 6 PHE C 203   O   145.5  78.6  71.0 117.7  91.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 181   OD2                                                    
REMARK 620 2 HIS C 183   ND1 100.2                                              
REMARK 620 3 ASP C 269   OD2 104.2 103.0                                        
REMARK 620 4 20Y C 406   N20  95.4 108.8 138.8                                  
REMARK 620 5 20Y C 406   N20 100.5 103.0 140.0   7.0                            
REMARK 620 6 20Y C 406   O12 171.7  86.3  79.2  77.5  72.8                      
REMARK 620 7 20Y C 406   O12 172.5  83.6  81.1  77.2  72.2   3.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 403  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE C 192   O                                                      
REMARK 620 2 THR C 195   O    80.1                                              
REMARK 620 3 VAL C 198   O   115.6  80.1                                        
REMARK 620 4 TYR C 227   O   155.7 119.1  84.0                                  
REMARK 620 5 HOH C 501   O    88.1  92.9 153.2  76.9                            
REMARK 620 6 HOH C 503   O    72.9 152.6 116.1  85.8  81.4                      
REMARK 620 N                    1     2     3     4     5                       
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 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 20Y A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 20Y B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 20Y C 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LXZ   RELATED DB: PDB                                   
DBREF  4LY1 A   12   380  UNP    Q92769   HDAC2_HUMAN      8    376             
DBREF  4LY1 B   12   380  UNP    Q92769   HDAC2_HUMAN      8    376             
DBREF  4LY1 C   12   380  UNP    Q92769   HDAC2_HUMAN      8    376             
SEQRES   1 A  369  GLY LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE          
SEQRES   2 A  369  GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO          
SEQRES   3 A  369  HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR          
SEQRES   4 A  369  GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS          
SEQRES   5 A  369  ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU          
SEQRES   6 A  369  TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET          
SEQRES   7 A  369  SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY          
SEQRES   8 A  369  GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS          
SEQRES   9 A  369  GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS          
SEQRES  10 A  369  LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA          
SEQRES  11 A  369  GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY          
SEQRES  12 A  369  PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU          
SEQRES  13 A  369  LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE          
SEQRES  14 A  369  ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR          
SEQRES  15 A  369  THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR          
SEQRES  16 A  369  GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE          
SEQRES  17 A  369  GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO          
SEQRES  18 A  369  MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE          
SEQRES  19 A  369  PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN          
SEQRES  20 A  369  PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU          
SEQRES  21 A  369  SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS          
SEQRES  22 A  369  GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN          
SEQRES  23 A  369  LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE          
SEQRES  24 A  369  ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL          
SEQRES  25 A  369  ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN          
SEQRES  26 A  369  ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS          
SEQRES  27 A  369  ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU          
SEQRES  28 A  369  TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU          
SEQRES  29 A  369  ARG MET LEU PRO HIS                                          
SEQRES   1 B  369  GLY LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE          
SEQRES   2 B  369  GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO          
SEQRES   3 B  369  HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR          
SEQRES   4 B  369  GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS          
SEQRES   5 B  369  ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU          
SEQRES   6 B  369  TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET          
SEQRES   7 B  369  SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY          
SEQRES   8 B  369  GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS          
SEQRES   9 B  369  GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS          
SEQRES  10 B  369  LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA          
SEQRES  11 B  369  GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY          
SEQRES  12 B  369  PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU          
SEQRES  13 B  369  LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE          
SEQRES  14 B  369  ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR          
SEQRES  15 B  369  THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR          
SEQRES  16 B  369  GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE          
SEQRES  17 B  369  GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO          
SEQRES  18 B  369  MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE          
SEQRES  19 B  369  PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN          
SEQRES  20 B  369  PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU          
SEQRES  21 B  369  SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS          
SEQRES  22 B  369  GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN          
SEQRES  23 B  369  LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE          
SEQRES  24 B  369  ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL          
SEQRES  25 B  369  ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN          
SEQRES  26 B  369  ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS          
SEQRES  27 B  369  ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU          
SEQRES  28 B  369  TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU          
SEQRES  29 B  369  ARG MET LEU PRO HIS                                          
SEQRES   1 C  369  GLY LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE          
SEQRES   2 C  369  GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO          
SEQRES   3 C  369  HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR          
SEQRES   4 C  369  GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS          
SEQRES   5 C  369  ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU          
SEQRES   6 C  369  TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET          
SEQRES   7 C  369  SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY          
SEQRES   8 C  369  GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS          
SEQRES   9 C  369  GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS          
SEQRES  10 C  369  LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA          
SEQRES  11 C  369  GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY          
SEQRES  12 C  369  PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU          
SEQRES  13 C  369  LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE          
SEQRES  14 C  369  ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR          
SEQRES  15 C  369  THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR          
SEQRES  16 C  369  GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE          
SEQRES  17 C  369  GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO          
SEQRES  18 C  369  MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE          
SEQRES  19 C  369  PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN          
SEQRES  20 C  369  PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU          
SEQRES  21 C  369  SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS          
SEQRES  22 C  369  GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN          
SEQRES  23 C  369  LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE          
SEQRES  24 C  369  ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL          
SEQRES  25 C  369  ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN          
SEQRES  26 C  369  ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS          
SEQRES  27 C  369  ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU          
SEQRES  28 C  369  TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU          
SEQRES  29 C  369  ARG MET LEU PRO HIS                                          
HET     ZN  A 401       1                                                       
HET     CA  A 402       1                                                       
HET     NA  A 403       1                                                       
HET    PG4  A 404      13                                                       
HET    PG4  A 405      13                                                       
HET    PG4  A 406      13                                                       
HET    20Y  A 407      50                                                       
HET     ZN  B 401       1                                                       
HET     CA  B 402       1                                                       
HET     NA  B 403       1                                                       
HET    NHE  B 404      13                                                       
HET    PG4  B 405      13                                                       
HET    PG4  B 406      13                                                       
HET    PG4  B 407      13                                                       
HET    20Y  B 408      50                                                       
HET     ZN  C 401       1                                                       
HET     CA  C 402       1                                                       
HET     NA  C 403       1                                                       
HET    PG4  C 404      13                                                       
HET    PG4  C 405      13                                                       
HET    20Y  C 406      50                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     20Y 4-(ACETYLAMINO)-N-[2-AMINO-5-(THIOPHEN-2-YL)                     
HETNAM   2 20Y  PHENYL]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  PG4    8(C8 H18 O5)                                                 
FORMUL  10  20Y    3(C19 H17 N3 O2 S)                                           
FORMUL  14  NHE    C8 H17 N O3 S                                                
FORMUL  25  HOH   *846(H2 O)                                                    
HELIX    1   1 ASP A   23  TYR A   27  5                                   5    
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 ASN A   88  GLU A   91  5                                   4    
HELIX    7   7 TYR A   92  ASN A  100  1                                   9    
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  PHE A  296  1                                  15    
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  MET B   56  5                                   6    
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  LEU B  169  1                                  11    
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  LYS C   55  5                                   5    
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  ASN C  100  1                                   9    
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  ASP C  326  1                                  18    
HELIX   50  50 TYR C  338  GLY C  343  5                                   6    
HELIX   51  51 THR C  360  MET C  377  1                                  18    
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  VAL A 229   N  THR A 200           
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  ILE B 178   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  GLU C  57           
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  PHE C 231   N  SER C 202           
LINK         OD1 ASP A 179                CA    CA A 402     1555   1555  2.57  
LINK         O   ASP A 179                CA    CA A 402     1555   1555  2.91  
LINK         OD2 ASP A 181                ZN    ZN A 401     1555   1555  2.03  
LINK         O   ASP A 181                CA    CA A 402     1555   1555  2.63  
LINK         ND1 HIS A 183                ZN    ZN A 401     1555   1555  2.05  
LINK         O   HIS A 183                CA    CA A 402     1555   1555  2.70  
LINK         O   PHE A 192                NA    NA A 403     1555   1555  2.55  
LINK         O   THR A 195                NA    NA A 403     1555   1555  2.77  
LINK         O   VAL A 198                NA    NA A 403     1555   1555  2.53  
LINK         OG  SER A 202                CA    CA A 402     1555   1555  2.93  
LINK         O   PHE A 203                CA    CA A 402     1555   1555  2.61  
LINK         O   TYR A 227                NA    NA A 403     1555   1555  3.08  
LINK         OD2 ASP A 269                ZN    ZN A 401     1555   1555  1.92  
LINK        ZN    ZN A 401                 N20A20Y A 407     1555   1555  1.91  
LINK        ZN    ZN A 401                 N20B20Y A 407     1555   1555  2.29  
LINK        ZN    ZN A 401                 O12A20Y A 407     1555   1555  2.56  
LINK        ZN    ZN A 401                 O12B20Y A 407     1555   1555  2.59  
LINK        NA    NA A 403                 O   HOH A 520     1555   1555  2.50  
LINK        NA    NA A 403                 O   HOH A 521     1555   1555  2.95  
LINK         OD1 ASP B 179                CA    CA B 402     1555   1555  2.60  
LINK         O   ASP B 179                CA    CA B 402     1555   1555  2.94  
LINK         OD2 ASP B 181                ZN    ZN B 401     1555   1555  1.98  
LINK         O   ASP B 181                CA    CA B 402     1555   1555  2.60  
LINK         ND1 HIS B 183                ZN    ZN B 401     1555   1555  2.02  
LINK         O   HIS B 183                CA    CA B 402     1555   1555  2.68  
LINK         O   PHE B 192                NA    NA B 403     1555   1555  2.58  
LINK         O   THR B 195                NA    NA B 403     1555   1555  2.75  
LINK         O   VAL B 198                NA    NA B 403     1555   1555  2.52  
LINK         OG  SER B 202                CA    CA B 402     1555   1555  2.87  
LINK         O   PHE B 203                CA    CA B 402     1555   1555  2.60  
LINK         O   TYR B 227                NA    NA B 403     1555   1555  3.03  
LINK         OD1 ASP B 269                ZN    ZN B 401     1555   1555  1.97  
LINK        ZN    ZN B 401                 N20B20Y B 408     1555   1555  2.03  
LINK        ZN    ZN B 401                 N20A20Y B 408     1555   1555  2.19  
LINK        ZN    ZN B 401                 O12A20Y B 408     1555   1555  2.58  
LINK        ZN    ZN B 401                 O12B20Y B 408     1555   1555  2.66  
LINK        NA    NA B 403                 O   HOH B 514     1555   1555  2.55  
LINK        NA    NA B 403                 O   HOH B 535     1555   1555  2.87  
LINK         OD1 ASP C 179                CA    CA C 402     1555   1555  2.57  
LINK         O   ASP C 179                CA    CA C 402     1555   1555  2.89  
LINK         OD2 ASP C 181                ZN    ZN C 401     1555   1555  2.05  
LINK         O   ASP C 181                CA    CA C 402     1555   1555  2.58  
LINK         ND1 HIS C 183                ZN    ZN C 401     1555   1555  2.06  
LINK         O   HIS C 183                CA    CA C 402     1555   1555  2.70  
LINK         O   PHE C 192                NA    NA C 403     1555   1555  2.55  
LINK         O   THR C 195                NA    NA C 403     1555   1555  2.76  
LINK         O   VAL C 198                NA    NA C 403     1555   1555  2.49  
LINK         OG  SER C 202                CA    CA C 402     1555   1555  2.91  
LINK         O   PHE C 203                CA    CA C 402     1555   1555  2.61  
LINK         O   TYR C 227                NA    NA C 403     1555   1555  3.08  
LINK         OD2 ASP C 269                ZN    ZN C 401     1555   1555  1.99  
LINK        ZN    ZN C 401                 N20B20Y C 406     1555   1555  2.04  
LINK        ZN    ZN C 401                 N20A20Y C 406     1555   1555  2.19  
LINK        ZN    ZN C 401                 O12B20Y C 406     1555   1555  2.50  
LINK        ZN    ZN C 401                 O12A20Y C 406     1555   1555  2.62  
LINK        NA    NA C 403                 O   HOH C 501     1555   1555  2.53  
LINK        NA    NA C 403                 O   HOH C 503     1555   1555  2.95  
CISPEP   1 PHE A  210    PRO A  211          0        -3.99                     
CISPEP   2 GLY A  343    PRO A  344          0         1.28                     
CISPEP   3 PHE B  210    PRO B  211          0        -2.64                     
CISPEP   4 GLY B  343    PRO B  344          0         2.65                     
CISPEP   5 PHE C  210    PRO C  211          0        -4.18                     
CISPEP   6 GLY C  343    PRO C  344          0         2.91                     
SITE     1 AC1  4 ASP A 181  HIS A 183  ASP A 269  20Y A 407                    
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 520  HOH A 521                                          
SITE     1 AC4  3 LYS A  71  ALA A 191  PHE A 192                               
SITE     1 AC5  5 ARG A 311  GLU A 340  TYR A 341  GLY A 343                    
SITE     2 AC5  5 HOH A 791                                                     
SITE     1 AC6  3 ASP A  23  ASN A  26  TYR A  27                               
SITE     1 AC7 20 TYR A  29  MET A  35  ARG A  39  GLY A 143                    
SITE     2 AC7 20 LEU A 144  HIS A 145  HIS A 146  GLY A 154                    
SITE     3 AC7 20 PHE A 155  CYS A 156  ASP A 181  HIS A 183                    
SITE     4 AC7 20 PHE A 210  ASP A 269  LEU A 276  GLY A 305                    
SITE     5 AC7 20 GLY A 306  TYR A 308   ZN A 401  HOH A 593                    
SITE     1 AC8  4 ASP B 181  HIS B 183  ASP B 269  20Y B 408                    
SITE     1 AC9  5 ASP B 179  ASP B 181  HIS B 183  SER B 202                    
SITE     2 AC9  5 PHE B 203                                                     
SITE     1 BC1  6 PHE B 192  THR B 195  VAL B 198  TYR B 227                    
SITE     2 BC1  6 HOH B 514  HOH B 535                                          
SITE     1 BC2 10 TYR A  59  LYS A 128  HOH A 583  ASP B  21                    
SITE     2 BC2 10 ASP B  23  TYR B  27  ARG B  60  LYS B  63                    
SITE     3 BC2 10 GLU B 113  PG4 B 407                                          
SITE     1 BC3  6 HOH A 783  ARG B 311  GLU B 340  TYR B 341                    
SITE     2 BC3  6 GLY B 343  HOH B 714                                          
SITE     1 BC4  6 LYS B 284  GLU B 328  ASN B 331  HIS B 349                    
SITE     2 BC4  6 GLU C  67  THR C  70                                          
SITE     1 BC5 10 ARG A 131  HOH A 631  ASP B  23  ASN B  26                    
SITE     2 BC5 10 TYR B  27  ASP B 109  NHE B 404  HOH B 736                    
SITE     3 BC5 10 HOH B 748  HOH B 822                                          
SITE     1 BC6 21 TYR B  29  MET B  35  ARG B  39  GLY B 143                    
SITE     2 BC6 21 LEU B 144  HIS B 145  HIS B 146  GLY B 154                    
SITE     3 BC6 21 PHE B 155  CYS B 156  ASP B 181  HIS B 183                    
SITE     4 BC6 21 PHE B 210  ASP B 269  GLY B 305  GLY B 306                    
SITE     5 BC6 21 TYR B 308   ZN B 401  HOH B 602  HOH B 617                    
SITE     6 BC6 21 HOH B 639                                                     
SITE     1 BC7  4 ASP C 181  HIS C 183  ASP C 269  20Y C 406                    
SITE     1 BC8  5 ASP C 179  ASP C 181  HIS C 183  SER C 202                    
SITE     2 BC8  5 PHE C 203                                                     
SITE     1 BC9  6 PHE C 192  THR C 195  VAL C 198  TYR C 227                    
SITE     2 BC9  6 HOH C 501  HOH C 503                                          
SITE     1 CC1  5 ASP B 345  ALA C 191  ARG C 197  HOH C 558                    
SITE     2 CC1  5 HOH C 576                                                     
SITE     1 CC2  7 ASN B 354  LEU C 169  LYS C 170  TYR C 171                    
SITE     2 CC2  7 GLN C 173  ARG C 197  HOH C 687                               
SITE     1 CC3 20 TYR C  29  MET C  35  ARG C  39  GLY C 143                    
SITE     2 CC3 20 LEU C 144  HIS C 145  HIS C 146  GLY C 154                    
SITE     3 CC3 20 PHE C 155  CYS C 156  ASP C 181  HIS C 183                    
SITE     4 CC3 20 PHE C 210  ASP C 269  GLY C 305  GLY C 306                    
SITE     5 CC3 20 TYR C 308   ZN C 401  HOH C 583  HOH C 586                    
CRYST1   92.034   97.490  138.922  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      0.010866  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010257  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007198        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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