GenomeNet

Database: PDB
Entry: 4MN3
LinkDB: 4MN3
Original site: 4MN3 
HEADER    TRANSCRIPTION REGULATOR                 09-SEP-13   4MN3              
TITLE     CHROMODOMAIN ANTAGONISTS THAT TARGET THE POLYCOMB-GROUP METHYLLYSINE  
TITLE    2 READER PROTEIN CHROMOBOX HOMOLOG 7 (CBX7)                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHROMOBOX PROTEIN HOMOLOG 7;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PROTEIN;                                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PEPTIDE;                                                   
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: PEPTIDE;                                                   
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CBX7;                                                          
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: SYNTHETIC PEPTIDE;                              
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    CHROMOBOX DOMAIN 7, TRANSCRIPTION REGULATOR                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CHAKRAVARTHI,K.DAZE,S.DOUGLAS,T.QUON,A.DEV,F.PENG,M.HELLER,         
AUTHOR   2 M.J.BOULANGER,J.WULFF,F.HOF                                          
REVDAT   3   08-OCT-14 4MN3    1       AUTHOR                                   
REVDAT   2   18-JUN-14 4MN3    1       JRNL                                     
REVDAT   1   02-APR-14 4MN3    0                                                
JRNL        AUTH   C.SIMHADRI,K.D.DAZE,S.F.DOUGLAS,T.T.QUON,A.DEV,M.C.GIGNAC,   
JRNL        AUTH 2 F.PENG,M.HELLER,M.J.BOULANGER,J.E.WULFF,F.HOF                
JRNL        TITL   CHROMODOMAIN ANTAGONISTS THAT TARGET THE POLYCOMB-GROUP      
JRNL        TITL 2 METHYLLYSINE READER PROTEIN CHROMOBOX HOMOLOG 7 (CBX7).      
JRNL        REF    J.MED.CHEM.                   V.  57  2874 2014              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   24625057                                                     
JRNL        DOI    10.1021/JM401487X                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 1.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 8664                           
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 431                             
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) : 1.54                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.58                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 606                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 25                           
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 531                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 40                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : -0.01000                                             
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): 0.086         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.090         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.058         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.600         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   565 ; 0.022 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):   562 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):   747 ; 2.139 ; 1.999       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1302 ; 1.018 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    59 ; 7.046 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    26 ;31.068 ;23.077       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   100 ;18.225 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;13.894 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):    71 ; 0.163 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   572 ; 0.013 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   122 ; 0.003 ; 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):   243 ; 2.249 ; 1.897       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   242 ; 2.178 ; 1.893       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   299 ; 3.354 ; 2.851       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   300 ; 3.357 ; 2.851       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   322 ; 3.550 ; 2.343       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   322 ; 3.531 ; 2.342       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):   449 ; 5.017 ; 3.282       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):   642 ; 6.791 ;16.246       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):   643 ; 6.787 ;16.280       
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 4MN3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB082117.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SIDE SCATTERING BENT CUBE-ROOT I   
REMARK 200                                   -BEAM SINGLE CRYSTAL; ASYMMETRIC   
REMARK 200                                   CUT 4.965 DEGS                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8874                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.540                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.1                               
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% ETHYLENE GLYCOL, 0.1M HEPES PH       
REMARK 280  7.5, 5% PEG 3000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       31.64500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       15.93000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       31.64500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       15.93000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 1370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 4600 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 MG    MG A 104  LIES ON A SPECIAL POSITION.                          
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    LYS A  17       46.24     35.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     P33 A  105                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 104                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P33 A 105                 
DBREF  4MN3 A    1    56  UNP    O95931   CBX7_HUMAN       7     62             
DBREF  4MN3 B    1     7  PDB    4MN3     4MN3             1      7             
SEQRES   1 A   56  GLY GLU GLN VAL PHE ALA VAL GLU SER ILE ARG LYS LYS          
SEQRES   2 A   56  ARG VAL ARG LYS GLY LYS VAL GLU TYR LEU VAL LYS TRP          
SEQRES   3 A   56  LYS GLY TRP PRO PRO LYS TYR SER THR TRP GLU PRO GLU          
SEQRES   4 A   56  GLU HIS ILE LEU ASP PRO ARG LEU VAL MET ALA TYR GLU          
SEQRES   5 A   56  GLU LYS GLU GLU                                              
SEQRES   1 B    7  ACE PHE ALA TYR M3L SER NH2                                  
MODRES 4MN3 M3L B    5  LYS  N-TRIMETHYLLYSINE                                  
HET    ACE  B   1       3                                                       
HET    M3L  B   5      12                                                       
HET    NH2  B   7       1                                                       
HET    EDO  A 101       4                                                       
HET    EDO  A 102       4                                                       
HET    EDO  A 103       4                                                       
HET     MG  A 104       1                                                       
HET    P33  A 105      13                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     M3L N-TRIMETHYLLYSINE                                                
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL                          
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     P33 HEPTAETHYLENE GLYCOL, PEG330                                     
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   2  M3L    C9 H21 N2 O2 1+                                              
FORMUL   2  NH2    H2 N                                                         
FORMUL   3  EDO    3(C2 H6 O2)                                                  
FORMUL   6   MG    MG 2+                                                        
FORMUL   7  P33    C14 H30 O8                                                   
FORMUL   8  HOH   *40(H2 O)                                                     
HELIX    1   1 PRO A   30  SER A   34  5                                   5    
HELIX    2   2 GLU A   40  ILE A   42  5                                   3    
HELIX    3   3 ASP A   44  GLU A   55  1                                  12    
SHEET    1   A 2 VAL A   4  PHE A   5  0                                        
SHEET    2   A 2 ALA B   3  TYR B   4 -1  O  ALA B   3   N  PHE A   5           
SHEET    1   B 3 VAL A   7  ARG A  16  0                                        
SHEET    2   B 3 LYS A  19  TRP A  26 -1  O  LYS A  19   N  ARG A  16           
SHEET    3   B 3 THR A  35  PRO A  38 -1  O  THR A  35   N  VAL A  24           
LINK         C   ACE B   1                 N   PHE B   2     1555   1555  1.58  
LINK         C   TYR B   4                 N   M3L B   5     1555   1555  1.32  
LINK         C   M3L B   5                 N   SER B   6     1555   1555  1.32  
LINK         C   SER B   6                 N   NH2 B   7     1555   1555  1.58  
LINK         OE1 GLU A   2                MG    MG A 104     1555   1555  2.48  
SITE     1 AC1  3 LYS A  25  TRP A  29  PRO A  30                               
SITE     1 AC2  5 LYS A  32  MET A  49  GLU A  52  HOH A 203                    
SITE     2 AC2  5 HOH A 232                                                     
SITE     1 AC3  4 LYS A  27  TRP A  29  PRO A  45  HOH B 103                    
SITE     1 AC4  2 GLU A   2  HIS A  41                                          
SITE     1 AC5  8 LYS A  12  LYS A  13  VAL A  15  LEU A  23                    
SITE     2 AC5  8 PRO A  31  SER A  34  GLU A  55  HOH A 222                    
CRYST1   63.290   31.860   38.390  90.00 119.02  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015800  0.000000  0.008765        0.00000                         
SCALE2      0.000000  0.031387  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029788        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system