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Database: PDB
Entry: 4X3S
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Original site: 4X3S 
HEADER    TRANSCRIPTION                           01-DEC-14   4X3S              
TITLE     CRYSTAL STRUCTURE OF CHROMOBOX HOMOLOGY 7 (CBX7) WITH SETDB1-1170ME3  
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHROMOBOX PROTEIN HOMOLOG 7;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 7-66;                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SETDB1-1170ME3 PEPTIDE;                                    
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 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;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606                                                 
KEYWDS    CBX7, CHROMODOMAIN, TRANSCRIPTION                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.REN,A.N.PLOTNIKOV,M.M.ZHOU                                          
REVDAT   1   04-MAR-15 4X3S    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.    1.60 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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.26                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 22009                          
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) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1195                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1567                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 91                           
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1185                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 189                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.22000                                              
REMARK   3    B22 (A**2) : -0.10000                                             
REMARK   3    B33 (A**2) : -1.12000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.106         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.093         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.057         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.606         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1281 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1231 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1725 ; 1.737 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2839 ; 0.818 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   139 ; 5.719 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    62 ;26.645 ;21.613       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   232 ;13.120 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;16.645 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   167 ; 0.116 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1363 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   293 ; 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):  2512 ; 7.448 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    48 ;24.363 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2629 ;13.157 ; 5.000       
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 4X3S 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_1000205013.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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   : 23204                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 42.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: 3I91                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% JEFFAMINE M-600, 0.1 M NA CITRATE    
REMARK 280  PH 5.6, 0.01 M FECL3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  290K                                                                
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       23.01350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.39850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.02000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.39850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.01350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       23.02000            
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                                                    
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: 1960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 5540 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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: 1970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 5570 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     ALA B    66                                                      
REMARK 465     GLY C  1174                                                      
REMARK 465     GLY D  1174                                                      
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     MET A   6    CG   SD   CE                                        
REMARK 470     MET B   6    CG   SD   CE                                        
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 B   251     O    HOH C  1205              2.02            
REMARK 500   O    HOH A   207     O    HOH A   208              2.10            
REMARK 500   NH2  ARG A    17     O    HOH A   201              2.10            
REMARK 500   O    HOH B   252     O    HOH B   269              2.12            
REMARK 500   O    HOH B   206     O    HOH B   234              2.13            
REMARK 500   O    HOH A   249     O    HOH D  1207              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  22   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A  22   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG B  52   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 283        DISTANCE =  6.28 ANGSTROMS                       
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                              FE A 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT B 102   O7                                                     
REMARK 620 2 CIT B 102   O6   77.5                                              
REMARK 620 3 CIT A 102   O7   96.5  91.5                                        
REMARK 620 4 CIT B 102   O4   87.2  92.2 175.2                                  
REMARK 620 5 CIT A 102   O4  173.3  96.7  86.9  89.7                            
REMARK 620 6 CIT A 102   O5   99.8 170.7  79.9  96.5  86.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT B 102   O1                                                     
REMARK 620 2 CIT B 102   O7   57.0                                              
REMARK 620 3 CIT A 102   O1  128.7 156.6                                        
REMARK 620 4 CIT A 102   O7  105.8  96.2 102.5                                  
REMARK 620 5 CIT A 102   O5  144.3  87.6  85.1  71.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT A 103   O1                                                     
REMARK 620 2 CIT A 103   O7   61.2                                              
REMARK 620 3 HOH A 224   O    90.9  79.2                                        
REMARK 620 4 CIT B 103   O2  128.2 162.1  85.2                                  
REMARK 620 5 CIT B 103   O7  107.3  94.5 155.2  96.1                            
REMARK 620 6 CIT B 103   O5  146.7  85.7  86.7  84.7  68.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT A 103   O7                                                     
REMARK 620 2 CIT A 103   O3   87.8                                              
REMARK 620 3 CIT A 103   O5   78.8  92.3                                        
REMARK 620 4 CIT B 103   O7   96.2 173.6  93.3                                  
REMARK 620 5 CIT B 103   O5   98.2  95.7 171.4  78.9                            
REMARK 620 6 CIT B 103   O3  172.2  87.3  95.2  89.2  88.4                      
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 FE A 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE B 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT B 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT B 103                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4X3T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4X3U   RELATED DB: PDB                                   
DBREF  4X3S A    7    66  UNP    Q8VDS3   CBX7_MOUSE       7     66             
DBREF  4X3S B    7    66  UNP    Q8VDS3   CBX7_MOUSE       7     66             
DBREF  4X3S C 1165  1174  PDB    4X3S     4X3S          1165   1174             
DBREF  4X3S D 1165  1174  PDB    4X3S     4X3S          1165   1174             
SEQADV 4X3S GLY A    3  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3S SER A    4  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3S HIS A    5  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3S MET A    6  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3S GLY B    3  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3S SER B    4  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3S HIS B    5  UNP  Q8VDS3              EXPRESSION TAG                 
SEQADV 4X3S MET B    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   10  ARG GLY PHE ALA LEU M3L SER THR HIS GLY                      
SEQRES   1 D   10  ARG GLY PHE ALA LEU M3L SER THR HIS GLY                      
HET    M3L  C1170      12                                                       
HET    M3L  D1170      12                                                       
HET     FE  A 101       2                                                       
HET    CIT  A 102      13                                                       
HET    CIT  A 103      13                                                       
HET     FE  B 101       2                                                       
HET    CIT  B 102      13                                                       
HET    CIT  B 103      13                                                       
HETNAM     M3L N-TRIMETHYLLYSINE                                                
HETNAM      FE FE (III) ION                                                     
HETNAM     CIT CITRIC ACID                                                      
FORMUL   3  M3L    2(C9 H21 N2 O2 1+)                                           
FORMUL   5   FE    2(FE 3+)                                                     
FORMUL   6  CIT    4(C6 H8 O7)                                                  
FORMUL  11  HOH   *189(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  ARG A   65  1                                  16    
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  ASP B   64  1                                  15    
SHEET    1 AA1 4 THR A  41  PRO A  44  0                                        
SHEET    2 AA1 4 LYS A  25  TRP A  32 -1  N  VAL A  30   O  THR A  41           
SHEET    3 AA1 4 GLY A   7  ARG A  22 -1  N  ARG A  20   O  GLU A  27           
SHEET    4 AA1 4 PHE D1167  THR D1172 -1  O  M3L D1170   N  GLN A   9           
SHEET    1 AA2 4 THR B  41  PRO B  44  0                                        
SHEET    2 AA2 4 LYS B  25  TRP B  32 -1  N  VAL B  30   O  THR B  41           
SHEET    3 AA2 4 GLY B   7  ARG B  22 -1  N  SER B  15   O  LYS B  31           
SHEET    4 AA2 4 PHE C1167  THR C1172 -1  O  M3L C1170   N  GLN B   9           
LINK         C   LEU C1169                 N   M3L C1170     1555   1555  1.33  
LINK         C   M3L C1170                 N   SER C1171     1555   1555  1.33  
LINK         C   LEU D1169                 N   M3L D1170     1555   1555  1.32  
LINK         C   M3L D1170                 N   SER D1171     1555   1555  1.32  
LINK        FE  A FE A 101                 O7  CIT B 102     1555   1555  2.06  
LINK        FE  A FE A 101                 O6  CIT B 102     1555   1555  2.08  
LINK        FE  A FE A 101                 O7  CIT A 102     1555   1555  1.94  
LINK        FE  A FE A 101                 O4  CIT B 102     1555   1555  2.06  
LINK        FE  A FE A 101                 O4  CIT A 102     1555   1555  2.02  
LINK        FE  A FE A 101                 O5  CIT A 102     1555   1555  2.07  
LINK        FE  B FE A 101                 O1  CIT B 102     1555   1555  2.69  
LINK        FE  B FE A 101                 O7  CIT B 102     1555   1555  2.11  
LINK        FE  B FE A 101                 O1  CIT A 102     1555   1555  2.29  
LINK        FE  B FE A 101                 O7  CIT A 102     1555   1555  1.90  
LINK        FE  B FE A 101                 O5  CIT A 102     1555   1555  2.44  
LINK         O1  CIT A 103                FE  B FE B 101     1555   1555  2.60  
LINK         O7  CIT A 103                FE  A FE B 101     1555   1555  2.00  
LINK         O7  CIT A 103                FE  B FE B 101     1555   1555  2.03  
LINK         O3  CIT A 103                FE  A FE B 101     1555   1555  2.02  
LINK         O5  CIT A 103                FE  A FE B 101     1555   1555  2.06  
LINK        FE  A FE B 101                 O7  CIT B 103     1555   1555  1.91  
LINK        FE  A FE B 101                 O5  CIT B 103     1555   1555  2.09  
LINK        FE  A FE B 101                 O3  CIT B 103     1555   1555  2.02  
LINK        FE  B FE B 101                 O   HOH A 224     1555   1555  2.32  
LINK        FE  B FE B 101                 O2  CIT B 103     1555   1555  2.33  
LINK        FE  B FE B 101                 O7  CIT B 103     1555   1555  1.94  
LINK        FE  B FE B 101                 O5  CIT B 103     1555   1555  2.49  
SITE     1 AC1  2 CIT A 102  CIT B 102                                          
SITE     1 AC2 12 ARG A  20  ARG A  22  TRP A  42   FE A 101                    
SITE     2 AC2 12 HOH A 217  HOH A 273  HOH A 275  HOH A 291                    
SITE     3 AC2 12 LYS B  23  ARG B  52  CIT B 102  ARG C1165                    
SITE     1 AC3 15 VAL A  21  ARG A  22  LYS A  23  GLY A  24                    
SITE     2 AC3 15 LEU A  49  ASP A  50  HOH A 221  HOH A 224                    
SITE     3 AC3 15 ARG B  22   FE B 101  CIT B 103  HOH B 228                    
SITE     4 AC3 15 ARG D1165  GLY D1166  PHE D1167                               
SITE     1 AC4  3 CIT A 103  HOH A 224  CIT B 103                               
SITE     1 AC5 13 ARG A  22   FE A 101  CIT A 102  VAL B  21                    
SITE     2 AC5 13 ARG B  22  LYS B  23  GLY B  24  LEU B  49                    
SITE     3 AC5 13 ASP B  50  HOH B 217  ARG C1165  GLY C1166                    
SITE     4 AC5 13 PHE C1167                                                     
SITE     1 AC6 13 LYS A  23  ARG A  52  CIT A 103  ARG B  20                    
SITE     2 AC6 13 ARG B  22  TRP B  42   FE B 101  HOH B 211                    
SITE     3 AC6 13 HOH B 220  HOH B 229  HOH B 261  HOH B 268                    
SITE     4 AC6 13 HOH B 281                                                     
CRYST1   46.027   46.040   80.797  90.00  90.00  90.00 P 21 21 21    8          
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      0.021726  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.021720  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012377        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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