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Database: PDB
Entry: 4X3T
LinkDB: 4X3T
Original site: 4X3T 
HEADER    TRANSCRIPTION                           01-DEC-14   4X3T              
TITLE     CRYSTAL STRUCTURE OF CHROMOBOX HOMOLOG 7 (CBX7) CHROMODOMAIN WITH     
TITLE    2 MS37452                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHROMOBOX PROTEIN HOMOLOG 7;                               
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 7-66;                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: CBX7, D15ERTD417E;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CBX7, CHROMODOMAIN, MS37452, INHIBITOR, TRANSCRIPTION                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.REN,J.JAKONCIC,M.M.ZHOU                                             
REVDAT   1   04-MAR-15 4X3T    0                                                
JRNL        AUTH   C.REN,K.MOROHASHI,A.N.PLOTNIKOV,J.JAKONCIC,S.G.SMITH,J.LI,   
JRNL        AUTH 2 L.ZENG,Y.RODRIGUEZ,V.STOJANOFF,M.WALSH,M.M.ZHOU              
JRNL        TITL   SMALL-MOLECULE MODULATORS OF METHYL-LYSINE BINDING FOR THE   
JRNL        TITL 2 CBX7 CHROMODOMAIN.                                           
JRNL        REF    CHEM.BIOL.                    V.  22   161 2015              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   25660273                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2014.11.021                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.14 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 28452                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1517                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.14                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.20                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1899                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3038                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 187                                     
REMARK   3   SOLVENT ATOMS            : 283                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.17000                                              
REMARK   3    B22 (A**2) : -1.04000                                             
REMARK   3    B33 (A**2) : 0.84000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.10000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.219         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.197         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.144         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.656         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3316 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3203 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4455 ; 1.804 ; 2.013       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7396 ; 0.850 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   347 ; 6.095 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   154 ;27.163 ;22.532       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   614 ;14.130 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;16.462 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   407 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3528 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   755 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4X3T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205020.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30060                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.140                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.610                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M ZINC ACETATE, 20% PEG 3350,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K                     
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       38.65450            
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, 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8940 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8480 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -116.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8280 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     ARG B    65                                                      
REMARK 465     ALA B    66                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     GLY E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     ALA E    56                                                      
REMARK 465     TYR E    57                                                      
REMARK 465     GLU E    58                                                      
REMARK 465     GLU E    59                                                      
REMARK 465     LYS E    60                                                      
REMARK 465     GLU E    61                                                      
REMARK 465     GLU E    62                                                      
REMARK 465     ARG E    63                                                      
REMARK 465     ASP E    64                                                      
REMARK 465     ARG E    65                                                      
REMARK 465     ALA E    66                                                      
REMARK 465     GLY F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     GLU F    61                                                      
REMARK 465     GLU F    62                                                      
REMARK 465     ARG F    63                                                      
REMARK 465     ASP F    64                                                      
REMARK 465     ARG F    65                                                      
REMARK 465     ALA F    66                                                      
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 C   225     O    HOH F   217              1.89            
REMARK 500   O    HOH F   201     O    HOH F   218              1.93            
REMARK 500   O    HOH A   252     O    HOH B   247              1.98            
REMARK 500   OE2  GLU B    14     O    HOH B   232              2.06            
REMARK 500   OD2  ASP B    50     O    HOH B   235              2.10            
REMARK 500   O    HOH A   250     O    HOH A   255              2.11            
REMARK 500   OE1  GLU C    62     O    HOH C   201              2.13            
REMARK 500   N    HIS B     5     O    HOH B   201              2.18            
REMARK 500   O    HOH E   207     O    HOH E   223              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   224     O    HOH D   212     2646     2.14            
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    MET A   6     -154.00    -94.68                                   
REMARK 500    LYS B  23       48.13     32.98                                   
REMARK 500    PRO B  36      172.08    -54.35                                   
REMARK 500    ARG B  63       -3.41    -55.57                                   
REMARK 500    LYS D  60      -90.64   -113.96                                   
REMARK 500    GLU F  59     -111.12   -164.41                                   
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 D   65     ALA D   66                 -147.40                    
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                              ZN A 103  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A   5   N                                                      
REMARK 620 2 HIS A   5   ND1  98.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  47   NE2                                                    
REMARK 620 2 HIS B  47   NE2 102.6                                              
REMARK 620 3 HOH B 249   O   167.4  89.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B   5   N                                                      
REMARK 620 2 HIS B   5   ND1 100.5                                              
REMARK 620 3 HOH A 252   O   140.8 117.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 103  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C   5   N                                                      
REMARK 620 2 HIS C   5   ND1  93.9                                              
REMARK 620 3 HOH F 212   O   144.9 113.5                                        
REMARK 620 4 HOH C 225   O    88.6 170.5  60.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  47   NE2                                                    
REMARK 620 2 HIS F  47   NE2 104.6                                              
REMARK 620 3 HOH C 224   O    95.0  98.2                                        
REMARK 620 4 HOH F 213   O   157.6  97.6  85.3                                  
REMARK 620 5 HOH C 219   O    77.5 176.1  84.9  80.2                            
REMARK 620 6 HOH F 215   O   101.2  98.3 153.2  71.7  78.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 103  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D   5   N                                                      
REMARK 620 2 HIS D   5   ND1  99.0                                              
REMARK 620 3 HOH D 243   O   176.1  77.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  47   NE2                                                    
REMARK 620 2 HIS E  47   NE2 175.0                                              
REMARK 620 3 HOH D 221   O    95.3  83.7                                        
REMARK 620 4 HOH E 227   O    82.5  98.6 177.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F   5   N                                                      
REMARK 620 2 HIS F   5   ND1  97.3                                              
REMARK 620 3 HOH F 201   O    70.1 163.5                                        
REMARK 620 4 HOH C 223   O   155.3 107.3  86.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 45E A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 45E B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 45E C 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 45E D 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 45E E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 45E F 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 103                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4X3S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4X3U   RELATED DB: PDB                                   
DBREF  4X3T A    7    66  UNP    Q8VDS3   CBX7_MOUSE       7     66             
DBREF  4X3T B    7    66  UNP    Q8VDS3   CBX7_MOUSE       7     66             
DBREF  4X3T C    7    66  UNP    Q8VDS3   CBX7_MOUSE       7     66             
DBREF  4X3T D    7    66  UNP    Q8VDS3   CBX7_MOUSE       7     66             
DBREF  4X3T E    7    66  UNP    Q8VDS3   CBX7_MOUSE       7     66             
DBREF  4X3T F    7    66  UNP    Q8VDS3   CBX7_MOUSE       7     66             
SEQADV 4X3T GLY A    3  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T SER A    4  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T HIS A    5  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T MET A    6  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T GLY B    3  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T SER B    4  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T HIS B    5  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T MET B    6  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T GLY C    3  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T SER C    4  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T HIS C    5  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T MET C    6  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T GLY D    3  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T SER D    4  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T HIS D    5  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T MET D    6  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T GLY E    3  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T SER E    4  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T HIS E    5  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T MET E    6  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T GLY F    3  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T SER F    4  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T HIS F    5  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3T MET F    6  UNP  Q8VDS3              EXPRESSION TAG                 
SEQRES   1 A   64  GLY SER HIS MET GLY GLU GLN VAL PHE ALA VAL GLU SER          
SEQRES   2 A   64  ILE ARG LYS LYS ARG VAL ARG LYS GLY LYS VAL GLU TYR          
SEQRES   3 A   64  LEU VAL LYS TRP LYS GLY TRP PRO PRO LYS TYR SER THR          
SEQRES   4 A   64  TRP GLU PRO GLU GLU HIS ILE LEU ASP PRO ARG LEU VAL          
SEQRES   5 A   64  MET ALA TYR GLU GLU LYS GLU GLU ARG ASP ARG ALA              
SEQRES   1 B   64  GLY SER HIS MET GLY GLU GLN VAL PHE ALA VAL GLU SER          
SEQRES   2 B   64  ILE ARG LYS LYS ARG VAL ARG LYS GLY LYS VAL GLU TYR          
SEQRES   3 B   64  LEU VAL LYS TRP LYS GLY TRP PRO PRO LYS TYR SER THR          
SEQRES   4 B   64  TRP GLU PRO GLU GLU HIS ILE LEU ASP PRO ARG LEU VAL          
SEQRES   5 B   64  MET ALA TYR GLU GLU LYS GLU GLU ARG ASP ARG ALA              
SEQRES   1 C   64  GLY SER HIS MET GLY GLU GLN VAL PHE ALA VAL GLU SER          
SEQRES   2 C   64  ILE ARG LYS LYS ARG VAL ARG LYS GLY LYS VAL GLU TYR          
SEQRES   3 C   64  LEU VAL LYS TRP LYS GLY TRP PRO PRO LYS TYR SER THR          
SEQRES   4 C   64  TRP GLU PRO GLU GLU HIS ILE LEU ASP PRO ARG LEU VAL          
SEQRES   5 C   64  MET ALA TYR GLU GLU LYS GLU GLU ARG ASP ARG ALA              
SEQRES   1 D   64  GLY SER HIS MET GLY GLU GLN VAL PHE ALA VAL GLU SER          
SEQRES   2 D   64  ILE ARG LYS LYS ARG VAL ARG LYS GLY LYS VAL GLU TYR          
SEQRES   3 D   64  LEU VAL LYS TRP LYS GLY TRP PRO PRO LYS TYR SER THR          
SEQRES   4 D   64  TRP GLU PRO GLU GLU HIS ILE LEU ASP PRO ARG LEU VAL          
SEQRES   5 D   64  MET ALA TYR GLU GLU LYS GLU GLU ARG ASP ARG ALA              
SEQRES   1 E   64  GLY SER HIS MET GLY GLU GLN VAL PHE ALA VAL GLU SER          
SEQRES   2 E   64  ILE ARG LYS LYS ARG VAL ARG LYS GLY LYS VAL GLU TYR          
SEQRES   3 E   64  LEU VAL LYS TRP LYS GLY TRP PRO PRO LYS TYR SER THR          
SEQRES   4 E   64  TRP GLU PRO GLU GLU HIS ILE LEU ASP PRO ARG LEU VAL          
SEQRES   5 E   64  MET ALA TYR GLU GLU LYS GLU GLU ARG ASP ARG ALA              
SEQRES   1 F   64  GLY SER HIS MET GLY GLU GLN VAL PHE ALA VAL GLU SER          
SEQRES   2 F   64  ILE ARG LYS LYS ARG VAL ARG LYS GLY LYS VAL GLU TYR          
SEQRES   3 F   64  LEU VAL LYS TRP LYS GLY TRP PRO PRO LYS TYR SER THR          
SEQRES   4 F   64  TRP GLU PRO GLU GLU HIS ILE LEU ASP PRO ARG LEU VAL          
SEQRES   5 F   64  MET ALA TYR GLU GLU LYS GLU GLU ARG ASP ARG ALA              
HET    45E  A 101      29                                                       
HET     ZN  A 102       1                                                       
HET     ZN  A 103       1                                                       
HET    45E  B 101      29                                                       
HET     ZN  B 102       1                                                       
HET    45E  C 101      29                                                       
HET     ZN  C 102       1                                                       
HET     ZN  C 103       1                                                       
HET    45E  D 101      29                                                       
HET     ZN  D 102       1                                                       
HET     ZN  D 103       1                                                       
HET    45E  E 101      29                                                       
HET     ZN  E 102       1                                                       
HET    45E  F 101      29                                                       
HET     ZN  F 102       1                                                       
HET    EDO  F 103       4                                                       
HETNAM     45E 1-[4-(2,3-DIMETHOXYBENZOYL)PIPERAZIN-1-YL]-2-(3-                 
HETNAM   2 45E  METHYLPHENOXY)ETHANONE                                          
HETNAM      ZN ZINC ION                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   7  45E    6(C22 H26 N2 O5)                                             
FORMUL   8   ZN    9(ZN 2+)                                                     
FORMUL  22  EDO    C2 H6 O2                                                     
FORMUL  23  HOH   *283(H2 O)                                                    
HELIX    1 AA1 PRO A   36  SER A   40  5                                   5    
HELIX    2 AA2 GLU A   46  ILE A   48  5                                   3    
HELIX    3 AA3 ASP A   50  GLU A   62  1                                  13    
HELIX    4 AA4 PRO B   36  SER B   40  5                                   5    
HELIX    5 AA5 GLU B   46  ILE B   48  5                                   3    
HELIX    6 AA6 ASP B   50  ARG B   63  1                                  14    
HELIX    7 AA7 PRO C   36  SER C   40  5                                   5    
HELIX    8 AA8 GLU C   46  ILE C   48  5                                   3    
HELIX    9 AA9 ASP C   50  GLU C   62  1                                  13    
HELIX   10 AB1 HIS D    5  GLN D    9  5                                   5    
HELIX   11 AB2 PRO D   36  SER D   40  5                                   5    
HELIX   12 AB3 GLU D   45  LEU D   49  1                                   5    
HELIX   13 AB4 ASP D   50  LYS D   60  1                                  11    
HELIX   14 AB5 HIS E    5  VAL E   10  5                                   6    
HELIX   15 AB6 PRO E   36  SER E   40  5                                   5    
HELIX   16 AB7 GLU E   45  LEU E   49  1                                   5    
HELIX   17 AB8 ASP E   50  VAL E   54  5                                   5    
HELIX   18 AB9 PRO F   36  SER F   40  5                                   5    
HELIX   19 AC1 GLU F   46  ILE F   48  5                                   3    
HELIX   20 AC2 PRO F   51  GLU F   58  1                                   8    
SHEET    1 AA1 3 VAL A  13  ARG A  22  0                                        
SHEET    2 AA1 3 LYS A  25  TRP A  32 -1  O  GLU A  27   N  ARG A  20           
SHEET    3 AA1 3 THR A  41  PRO A  44 -1  O  THR A  41   N  VAL A  30           
SHEET    1 AA2 3 VAL B  13  ARG B  22  0                                        
SHEET    2 AA2 3 LYS B  25  TRP B  32 -1  O  GLU B  27   N  ARG B  20           
SHEET    3 AA2 3 THR B  41  PRO B  44 -1  O  THR B  41   N  VAL B  30           
SHEET    1 AA3 3 VAL C  13  ARG C  22  0                                        
SHEET    2 AA3 3 LYS C  25  TRP C  32 -1  O  LEU C  29   N  ARG C  17           
SHEET    3 AA3 3 THR C  41  PRO C  44 -1  O  GLU C  43   N  TYR C  28           
SHEET    1 AA4 3 VAL D  13  ARG D  22  0                                        
SHEET    2 AA4 3 LYS D  25  TRP D  32 -1  O  LYS D  31   N  GLU D  14           
SHEET    3 AA4 3 THR D  41  PRO D  44 -1  O  THR D  41   N  VAL D  30           
SHEET    1 AA5 3 VAL E  13  ARG E  22  0                                        
SHEET    2 AA5 3 LYS E  25  TRP E  32 -1  O  GLU E  27   N  ARG E  20           
SHEET    3 AA5 3 THR E  41  PRO E  44 -1  O  GLU E  43   N  TYR E  28           
SHEET    1 AA6 3 VAL F  13  ARG F  22  0                                        
SHEET    2 AA6 3 LYS F  25  TRP F  32 -1  O  LYS F  31   N  GLU F  14           
SHEET    3 AA6 3 THR F  41  PRO F  44 -1  O  THR F  41   N  VAL F  30           
LINK         N   HIS A   5                ZN    ZN A 103     1555   1555  2.45  
LINK         ND1 HIS A   5                ZN    ZN A 103     1555   1555  2.00  
LINK         NE2 HIS A  47                ZN    ZN A 102     1555   1555  2.12  
LINK         N   HIS B   5                ZN    ZN B 102     1555   1555  2.47  
LINK         ND1 HIS B   5                ZN    ZN B 102     1555   1555  2.04  
LINK         NE2 HIS B  47                ZN    ZN A 102     1555   1555  2.16  
LINK         N   HIS C   5                ZN    ZN C 103     1555   1555  2.60  
LINK         ND1 HIS C   5                ZN    ZN C 103     1555   1555  1.94  
LINK         NE2 HIS C  47                ZN    ZN C 102     1555   1555  2.01  
LINK         N   HIS D   5                ZN    ZN D 103     1555   1555  2.25  
LINK         ND1 HIS D   5                ZN    ZN D 103     1555   1555  1.97  
LINK         NE2 HIS D  47                ZN    ZN D 102     1555   1555  2.17  
LINK         N   HIS E   5                ZN    ZN E 102     1555   1555  2.06  
LINK         NE2 HIS E  47                ZN    ZN D 102     1555   1555  2.22  
LINK         N   HIS F   5                ZN    ZN F 102     1555   1555  2.30  
LINK         ND1 HIS F   5                ZN    ZN F 102     1555   1555  1.86  
LINK         NE2 HIS F  47                ZN    ZN C 102     1555   1555  1.95  
LINK        ZN    ZN A 102                 O   HOH B 249     1555   1555  2.28  
LINK        ZN    ZN B 102                 O   HOH A 252     1555   1555  2.26  
LINK        ZN    ZN C 102                 O   HOH C 224     1555   1555  2.31  
LINK        ZN    ZN C 102                 O   HOH F 213     1555   1555  2.13  
LINK        ZN    ZN C 102                 O   HOH C 219     1555   1555  1.81  
LINK        ZN    ZN C 102                 O   HOH F 215     1555   1555  2.15  
LINK        ZN    ZN C 103                 O   HOH F 212     1555   1555  2.37  
LINK        ZN    ZN C 103                 O   HOH C 225     1555   1555  2.03  
LINK        ZN    ZN D 102                 O   HOH D 221     1555   1555  2.29  
LINK        ZN    ZN D 102                 O   HOH E 227     1555   1555  2.34  
LINK        ZN    ZN D 103                 O   HOH D 243     1555   1555  2.24  
LINK        ZN    ZN F 102                 O   HOH F 201     1555   1555  1.92  
LINK        ZN    ZN F 102                 O   HOH C 223     1555   1555  2.37  
SITE     1 AC1 13 MET A   6  VAL A  13  TRP A  32  TRP A  35                    
SITE     2 AC1 13 TYR A  39  THR A  41  GLU A  43  HIS A  47                    
SITE     3 AC1 13 HOH A 224  HOH A 226  GLU B  46  LEU B  49                    
SITE     4 AC1 13 45E C 101                                                     
SITE     1 AC2  3 HIS A  47  HIS B  47  HOH B 249                               
SITE     1 AC3  2 HIS A   5  MET A   6                                          
SITE     1 AC4 10 GLU A  46  LEU A  49  PHE B  11  TRP B  32                    
SITE     2 AC4 10 TYR B  39  THR B  41  GLU B  43  HIS B  47                    
SITE     3 AC4 10 HOH B 213  HOH B 246                                          
SITE     1 AC5  3 HOH A 252  HIS B   5  HOH B 247                               
SITE     1 AC6 14 TYR A  39  45E A 101  MET C   6  PHE C  11                    
SITE     2 AC6 14 VAL C  13  TRP C  32  TRP C  35  TYR C  39                    
SITE     3 AC6 14 THR C  41  GLU C  43  HIS C  47  HOH C 218                    
SITE     4 AC6 14 GLU F  46  LEU F  49                                          
SITE     1 AC7  6 HIS C  47  HOH C 219  HOH C 224  HIS F  47                    
SITE     2 AC7  6 HOH F 213  HOH F 215                                          
SITE     1 AC8  3 HIS C   5  HOH C 225  HOH F 212                               
SITE     1 AC9 14 VAL D  10  PHE D  11  TRP D  32  TRP D  35                    
SITE     2 AC9 14 TYR D  39  GLU D  43   ZN D 102  HOH D 221                    
SITE     3 AC9 14 HOH D 232  TRP E  32  GLU E  46  HIS E  47                    
SITE     4 AC9 14 ILE E  48  45E E 101                                          
SITE     1 AD1  6 HIS D  47  45E D 101  HOH D 221  HIS E  47                    
SITE     2 AD1  6 45E E 101  HOH E 227                                          
SITE     1 AD2  3 HIS D   5  HOH D 229  HOH D 243                               
SITE     1 AD3 16 VAL A  21  VAL D  13  GLU D  46  HIS D  47                    
SITE     2 AD3 16 PRO D  51  45E D 101   ZN D 102  PHE E  11                    
SITE     3 AD3 16 TRP E  32  TRP E  35  TYR E  39  GLU E  43                    
SITE     4 AD3 16 HOH E 206  HOH E 210  HOH E 217  HOH E 227                    
SITE     1 AD4  2 HIS E   5  MET E   6                                          
SITE     1 AD5 12 GLU C  46  LEU C  49  HOH C 220  MET F   6                    
SITE     2 AD5 12 PHE F  11  VAL F  13  TRP F  32  TRP F  35                    
SITE     3 AD5 12 THR F  41  GLU F  43  HIS F  47  HOH F 221                    
SITE     1 AD6  5 HOH C 223  HIS F   5  HOH F 201  HOH F 204                    
SITE     2 AD6  5 HOH F 218                                                     
SITE     1 AD7  8 LEU C  49  VAL F  13  HIS F  47  ILE F  48                    
SITE     2 AD7  8 LEU F  49  ASP F  50  HOH F 214  HOH F 223                    
CRYST1   54.004   77.309   66.842  90.00  95.55  90.00 P 1 21 1     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      0.018517  0.000000  0.001800        0.00000                         
SCALE2      0.000000  0.012935  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015031        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system