GenomeNet

Database: PDB
Entry: 5TUY
LinkDB: 5TUY
Original site: 5TUY 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       07-NOV-16   5TUY              
TITLE     STRUCTURE OF HUMAN G9A SET-DOMAIN (EHMT2) IN COMPLEX WITH INHIBITOR   
TITLE    2 MS0124                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 887-1154;                                     
COMPND   5 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 2,HLA-B-     
COMPND   6 ASSOCIATED TRANSCRIPT 8,HISTONE H3-K9 METHYLTRANSFERASE 3,H3-K9-     
COMPND   7 HMTASE 3,LYSINE N-METHYLTRANSFERASE 1C,PROTEIN G9A;                  
COMPND   8 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   9 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: EHMT2, BAT8, C6ORF30, G9A, KMT1C, NG36;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS RIL;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC                                
KEYWDS    METHYL-TRANSFERASE INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE         
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.BABAULT,Y.XIONG,J.LIU,J.JIN                                         
REVDAT   3   27-SEP-17 5TUY    1       REMARK                                   
REVDAT   2   22-MAR-17 5TUY    1       JRNL                                     
REVDAT   1   22-FEB-17 5TUY    0                                                
JRNL        AUTH   Y.XIONG,F.LI,N.BABAULT,A.DONG,H.ZENG,H.WU,X.CHEN,            
JRNL        AUTH 2 C.H.ARROWSMITH,P.J.BROWN,J.LIU,M.VEDADI,J.JIN                
JRNL        TITL   DISCOVERY OF POTENT AND SELECTIVE INHIBITORS FOR G9A-LIKE    
JRNL        TITL 2 PROTEIN (GLP) LYSINE METHYLTRANSFERASE.                      
JRNL        REF    J. MED. CHEM.                 V.  60  1876 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28135087                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01645                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21071                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.330                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1124                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 56.9837 -  5.1990    1.00     2527   156  0.1334 0.1803        
REMARK   3     2  5.1990 -  4.1270    1.00     2502   146  0.1186 0.1714        
REMARK   3     3  4.1270 -  3.6054    1.00     2506   132  0.1465 0.2328        
REMARK   3     4  3.6054 -  3.2758    1.00     2485   141  0.1771 0.2449        
REMARK   3     5  3.2758 -  3.0410    1.00     2470   156  0.2070 0.2771        
REMARK   3     6  3.0410 -  2.8617    1.00     2464   132  0.2252 0.3099        
REMARK   3     7  2.8617 -  2.7184    1.00     2492   128  0.2398 0.2993        
REMARK   3     8  2.7184 -  2.6001    1.00     2501   133  0.2695 0.3241        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.450           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           4511                                  
REMARK   3   ANGLE     :  1.216           6060                                  
REMARK   3   CHIRALITY :  0.055            637                                  
REMARK   3   PLANARITY :  0.006            788                                  
REMARK   3   DIHEDRAL  : 13.794           1686                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0606  -2.9056  16.4431              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1667 T22:   0.1365                                     
REMARK   3      T33:   0.2134 T12:  -0.0002                                     
REMARK   3      T13:   0.0408 T23:   0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4367 L22:   0.4771                                     
REMARK   3      L33:   2.4712 L12:  -0.1196                                     
REMARK   3      L13:   1.5239 L23:  -0.1119                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0383 S12:   0.0169 S13:  -0.0521                       
REMARK   3      S21:   0.0090 S22:   0.0518 S23:   0.0272                       
REMARK   3      S31:   0.0361 S32:  -0.1365 S33:  -0.0759                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 2486                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5TUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224862.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21095                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
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: 3K5K                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3,350, 0.2 M NAF, 0.1 M    
REMARK 280  BIS-TRIS PROPANE (PH 6.5), VAPOR DIFFUSION, 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       41.15000            
REMARK 290   SMTRY3   2  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: 2270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 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     LYS A  1188                                                      
REMARK 465     ILE B   921                                                      
REMARK 465     ILE B   922                                                      
REMARK 465     ASN B  1091                                                      
REMARK 465     LYS B  1092                                                      
REMARK 465     ASP B  1093                                                      
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   OG   SER B   991     O    HOH B  1601              2.03            
REMARK 500   OE2  GLU B   931     O    HOH B  1602              2.16            
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    CYS A1027   CA  -  CB  -  SG  ANGL. DEV. =   7.9 DEGREES          
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    ASP A 949       35.51    -99.78                                   
REMARK 500    ASP A 978     -153.46    -98.50                                   
REMARK 500    ILE A 992      -42.91     74.04                                   
REMARK 500    ASN A1007       95.39    -68.71                                   
REMARK 500    ASN A1026       31.83    -97.23                                   
REMARK 500    ILE A1064      -62.92    -96.75                                   
REMARK 500    GLU A1095       79.98     57.63                                   
REMARK 500    ASN A1106     -157.45   -110.15                                   
REMARK 500    ASP A1116       79.88   -111.11                                   
REMARK 500    MET A1126      -86.94   -134.78                                   
REMARK 500    ASP B 949       40.22   -101.53                                   
REMARK 500    ASP B 978     -153.66   -102.13                                   
REMARK 500    ILE B 992      -42.64     76.48                                   
REMARK 500    ILE B1064      -61.23    -97.61                                   
REMARK 500    ASN B1106     -158.00   -108.98                                   
REMARK 500    MET B1126      -87.69   -134.64                                   
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 A1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 974   SG                                                     
REMARK 620 2 CYS A 987   SG   96.4                                              
REMARK 620 3 CYS A1017   SG  106.1 115.9                                        
REMARK 620 4 CYS A1021   SG  108.3  92.9 131.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 974   SG                                                     
REMARK 620 2 CYS A 976   SG  106.4                                              
REMARK 620 3 CYS A 980   SG  118.1 117.4                                        
REMARK 620 4 CYS A 985   SG   96.1  93.8 120.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 980   SG                                                     
REMARK 620 2 CYS A1017   SG  105.6                                              
REMARK 620 3 CYS A1023   SG  108.9 103.2                                        
REMARK 620 4 CYS A1027   SG   98.0 111.4 127.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1115   SG                                                     
REMARK 620 2 CYS A1168   SG  119.9                                              
REMARK 620 3 CYS A1170   SG  114.9 110.6                                        
REMARK 620 4 CYS A1175   SG  100.7  97.0 111.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 974   SG                                                     
REMARK 620 2 CYS B 976   SG  109.3                                              
REMARK 620 3 CYS B 980   SG  106.1 104.3                                        
REMARK 620 4 CYS B 985   SG  112.3 104.6 119.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 974   SG                                                     
REMARK 620 2 CYS B 987   SG  112.2                                              
REMARK 620 3 CYS B1017   SG  104.1 119.1                                        
REMARK 620 4 CYS B1021   SG  101.1 107.3 111.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 980   SG                                                     
REMARK 620 2 CYS B1017   SG  113.9                                              
REMARK 620 3 CYS B1023   SG  105.7 104.0                                        
REMARK 620 4 CYS B1027   SG  115.5 107.5 109.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1115   SG                                                     
REMARK 620 2 CYS B1168   SG  113.4                                              
REMARK 620 3 CYS B1170   SG  113.4 106.6                                        
REMARK 620 4 CYS B1175   SG  102.9 107.5 113.1                                  
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 ZN A 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7L6 A 1506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7L6 B 1506                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5TUZ   RELATED DB: PDB                                   
REMARK 900 GLP SET-DOMAIN (EHMT1) IN COMPLEX WITH INHIBITOR MS0124              
DBREF  5TUY A  921  1188  UNP    Q96KQ7   EHMT2_HUMAN    887   1154             
DBREF  5TUY B  921  1188  UNP    Q96KQ7   EHMT2_HUMAN    887   1154             
SEQADV 5TUY LYS A 1188  UNP  Q96KQ7    ARG  1154 CONFLICT                       
SEQADV 5TUY LYS B 1188  UNP  Q96KQ7    ARG  1154 CONFLICT                       
SEQRES   1 A  268  ILE ILE CYS ARG ASP VAL ALA ARG GLY TYR GLU ASN VAL          
SEQRES   2 A  268  PRO ILE PRO CYS VAL ASN GLY VAL ASP GLY GLU PRO CYS          
SEQRES   3 A  268  PRO GLU ASP TYR LYS TYR ILE SER GLU ASN CYS GLU THR          
SEQRES   4 A  268  SER THR MET ASN ILE ASP ARG ASN ILE THR HIS LEU GLN          
SEQRES   5 A  268  HIS CYS THR CYS VAL ASP ASP CYS SER SER SER ASN CYS          
SEQRES   6 A  268  LEU CYS GLY GLN LEU SER ILE ARG CYS TRP TYR ASP LYS          
SEQRES   7 A  268  ASP GLY ARG LEU LEU GLN GLU PHE ASN LYS ILE GLU PRO          
SEQRES   8 A  268  PRO LEU ILE PHE GLU CYS ASN GLN ALA CYS SER CYS TRP          
SEQRES   9 A  268  ARG ASN CYS LYS ASN ARG VAL VAL GLN SER GLY ILE LYS          
SEQRES  10 A  268  VAL ARG LEU GLN LEU TYR ARG THR ALA LYS MET GLY TRP          
SEQRES  11 A  268  GLY VAL ARG ALA LEU GLN THR ILE PRO GLN GLY THR PHE          
SEQRES  12 A  268  ILE CYS GLU TYR VAL GLY GLU LEU ILE SER ASP ALA GLU          
SEQRES  13 A  268  ALA ASP VAL ARG GLU ASP ASP SER TYR LEU PHE ASP LEU          
SEQRES  14 A  268  ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA ARG          
SEQRES  15 A  268  TYR TYR GLY ASN ILE SER ARG PHE ILE ASN HIS LEU CYS          
SEQRES  16 A  268  ASP PRO ASN ILE ILE PRO VAL ARG VAL PHE MET LEU HIS          
SEQRES  17 A  268  GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER SER          
SEQRES  18 A  268  ARG ASP ILE ARG THR GLY GLU GLU LEU GLY PHE ASP TYR          
SEQRES  19 A  268  GLY ASP ARG PHE TRP ASP ILE LYS SER LYS TYR PHE THR          
SEQRES  20 A  268  CYS GLN CYS GLY SER GLU LYS CYS LYS HIS SER ALA GLU          
SEQRES  21 A  268  ALA ILE ALA LEU GLU GLN SER LYS                              
SEQRES   1 B  268  ILE ILE CYS ARG ASP VAL ALA ARG GLY TYR GLU ASN VAL          
SEQRES   2 B  268  PRO ILE PRO CYS VAL ASN GLY VAL ASP GLY GLU PRO CYS          
SEQRES   3 B  268  PRO GLU ASP TYR LYS TYR ILE SER GLU ASN CYS GLU THR          
SEQRES   4 B  268  SER THR MET ASN ILE ASP ARG ASN ILE THR HIS LEU GLN          
SEQRES   5 B  268  HIS CYS THR CYS VAL ASP ASP CYS SER SER SER ASN CYS          
SEQRES   6 B  268  LEU CYS GLY GLN LEU SER ILE ARG CYS TRP TYR ASP LYS          
SEQRES   7 B  268  ASP GLY ARG LEU LEU GLN GLU PHE ASN LYS ILE GLU PRO          
SEQRES   8 B  268  PRO LEU ILE PHE GLU CYS ASN GLN ALA CYS SER CYS TRP          
SEQRES   9 B  268  ARG ASN CYS LYS ASN ARG VAL VAL GLN SER GLY ILE LYS          
SEQRES  10 B  268  VAL ARG LEU GLN LEU TYR ARG THR ALA LYS MET GLY TRP          
SEQRES  11 B  268  GLY VAL ARG ALA LEU GLN THR ILE PRO GLN GLY THR PHE          
SEQRES  12 B  268  ILE CYS GLU TYR VAL GLY GLU LEU ILE SER ASP ALA GLU          
SEQRES  13 B  268  ALA ASP VAL ARG GLU ASP ASP SER TYR LEU PHE ASP LEU          
SEQRES  14 B  268  ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA ARG          
SEQRES  15 B  268  TYR TYR GLY ASN ILE SER ARG PHE ILE ASN HIS LEU CYS          
SEQRES  16 B  268  ASP PRO ASN ILE ILE PRO VAL ARG VAL PHE MET LEU HIS          
SEQRES  17 B  268  GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER SER          
SEQRES  18 B  268  ARG ASP ILE ARG THR GLY GLU GLU LEU GLY PHE ASP TYR          
SEQRES  19 B  268  GLY ASP ARG PHE TRP ASP ILE LYS SER LYS TYR PHE THR          
SEQRES  20 B  268  CYS GLN CYS GLY SER GLU LYS CYS LYS HIS SER ALA GLU          
SEQRES  21 B  268  ALA ILE ALA LEU GLU GLN SER LYS                              
HET     ZN  A1501       1                                                       
HET     ZN  A1502       1                                                       
HET     ZN  A1503       1                                                       
HET     ZN  A1504       1                                                       
HET    SAM  A1505      27                                                       
HET    7L6  A1506      28                                                       
HET     ZN  B1501       1                                                       
HET     ZN  B1502       1                                                       
HET     ZN  B1503       1                                                       
HET     ZN  B1504       1                                                       
HET    SAM  B1505      27                                                       
HET    7L6  B1506      28                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     7L6 6,7-DIMETHOXY-N-(1-METHYLPIPERIDIN-4-YL)-2-(MORPHOLIN-           
HETNAM   2 7L6  4-YL)QUINAZOLIN-4-AMINE                                         
FORMUL   3   ZN    8(ZN 2+)                                                     
FORMUL   7  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   8  7L6    2(C20 H29 N5 O3)                                             
FORMUL  15  HOH   *101(H2 O)                                                    
HELIX    1 AA1 ASN A  967  LEU A  971  5                                   5    
HELIX    2 AA2 CYS A  985  SER A  991  1                                   7    
HELIX    3 AA3 VAL A 1031  GLY A 1035  5                                   5    
HELIX    4 AA4 ASP A 1074  ARG A 1080  1                                   7    
HELIX    5 AA5 ILE A 1107  ILE A 1111  5                                   5    
HELIX    6 AA6 GLY A 1155  SER A 1163  1                                   9    
HELIX    7 AA7 SER A 1178  GLN A 1186  1                                   9    
HELIX    8 AA8 ASN B  967  LEU B  971  5                                   5    
HELIX    9 AA9 CYS B  985  LEU B  990  1                                   6    
HELIX   10 AB1 VAL B 1031  GLY B 1035  5                                   5    
HELIX   11 AB2 ASP B 1074  VAL B 1079  1                                   6    
HELIX   12 AB3 ILE B 1107  ILE B 1111  5                                   5    
HELIX   13 AB4 GLY B 1155  SER B 1163  1                                   9    
HELIX   14 AB5 SER B 1178  LYS B 1188  1                                  11    
SHEET    1 AA1 3 CYS A 937  VAL A 938  0                                        
SHEET    2 AA1 3 LEU A1040  ARG A1044  1  O  LEU A1042   N  VAL A 938           
SHEET    3 AA1 3 TRP A1050  ALA A1054 -1  O  GLY A1051   N  TYR A1043           
SHEET    1 AA2 4 LYS A 951  TYR A 952  0                                        
SHEET    2 AA2 4 TYR A1097  GLY A1105  1  O  TYR A1103   N  LYS A 951           
SHEET    3 AA2 4 GLY A1069  SER A1073 -1  N  ILE A1072   O  CYS A1098           
SHEET    4 AA2 4 CYS A 957  GLU A 958  1  N  CYS A 957   O  LEU A1071           
SHEET    1 AA3 3 LYS A 951  TYR A 952  0                                        
SHEET    2 AA3 3 TYR A1097  GLY A1105  1  O  TYR A1103   N  LYS A 951           
SHEET    3 AA3 3 LEU A1086  LEU A1089 -1  N  PHE A1087   O  ILE A1099           
SHEET    1 AA4 4 ILE A1014  PHE A1015  0                                        
SHEET    2 AA4 4 ILE A1119  PHE A1125  1  O  PHE A1125   N  ILE A1014           
SHEET    3 AA4 4 ARG A1135  SER A1140 -1  O  ALA A1137   N  VAL A1122           
SHEET    4 AA4 4 PHE A1063  TYR A1067 -1  N  ILE A1064   O  PHE A1138           
SHEET    1 AA5 2 ASN A1112  HIS A1113  0                                        
SHEET    2 AA5 2 GLY A1151  PHE A1152  1  O  PHE A1152   N  ASN A1112           
SHEET    1 AA6 3 CYS B 937  VAL B 938  0                                        
SHEET    2 AA6 3 LEU B1040  ARG B1044  1  O  LEU B1042   N  VAL B 938           
SHEET    3 AA6 3 TRP B1050  ALA B1054 -1  O  GLY B1051   N  TYR B1043           
SHEET    1 AA7 3 LYS B 951  TYR B 952  0                                        
SHEET    2 AA7 3 TYR B1097  GLY B1105  1  O  TYR B1103   N  LYS B 951           
SHEET    3 AA7 3 GLY B1069  SER B1073 -1  N  ILE B1072   O  CYS B1098           
SHEET    1 AA8 3 LYS B 951  TYR B 952  0                                        
SHEET    2 AA8 3 TYR B1097  GLY B1105  1  O  TYR B1103   N  LYS B 951           
SHEET    3 AA8 3 LEU B1086  LEU B1089 -1  N  PHE B1087   O  ILE B1099           
SHEET    1 AA9 4 ILE B1014  PHE B1015  0                                        
SHEET    2 AA9 4 ILE B1119  PHE B1125  1  O  PHE B1125   N  ILE B1014           
SHEET    3 AA9 4 ARG B1135  SER B1140 -1  O  PHE B1139   N  ILE B1120           
SHEET    4 AA9 4 PHE B1063  TYR B1067 -1  N  ILE B1064   O  PHE B1138           
SHEET    1 AB1 2 ASN B1112  HIS B1113  0                                        
SHEET    2 AB1 2 GLY B1151  PHE B1152  1  O  PHE B1152   N  ASN B1112           
SSBOND   1 CYS A  937    CYS A  946                          1555   1555  2.04  
SSBOND   2 CYS B  937    CYS B  946                          1555   1555  2.04  
LINK         SG  CYS A 974                ZN    ZN A1502     1555   1555  2.41  
LINK         SG  CYS A 974                ZN    ZN A1503     1555   1555  2.41  
LINK         SG  CYS A 976                ZN    ZN A1503     1555   1555  2.40  
LINK         SG  CYS A 980                ZN    ZN A1503     1555   1555  2.26  
LINK         SG  CYS A 980                ZN    ZN A1501     1555   1555  2.28  
LINK         SG  CYS A 985                ZN    ZN A1503     1555   1555  2.29  
LINK         SG  CYS A 987                ZN    ZN A1502     1555   1555  2.22  
LINK         SG  CYS A1017                ZN    ZN A1502     1555   1555  2.20  
LINK         SG  CYS A1017                ZN    ZN A1501     1555   1555  2.16  
LINK         SG  CYS A1021                ZN    ZN A1502     1555   1555  2.20  
LINK         SG  CYS A1023                ZN    ZN A1501     1555   1555  2.27  
LINK         SG  CYS A1027                ZN    ZN A1501     1555   1555  1.99  
LINK         SG  CYS A1115                ZN    ZN A1504     1555   1555  2.31  
LINK         SG  CYS A1168                ZN    ZN A1504     1555   1555  2.27  
LINK         SG  CYS A1170                ZN    ZN A1504     1555   1555  2.26  
LINK         SG  CYS A1175                ZN    ZN A1504     1555   1555  2.44  
LINK         SG  CYS B 974                ZN    ZN B1503     1555   1555  2.33  
LINK         SG  CYS B 974                ZN    ZN B1502     1555   1555  2.45  
LINK         SG  CYS B 976                ZN    ZN B1503     1555   1555  2.30  
LINK         SG  CYS B 980                ZN    ZN B1503     1555   1555  2.36  
LINK         SG  CYS B 980                ZN    ZN B1501     1555   1555  2.27  
LINK         SG  CYS B 985                ZN    ZN B1503     1555   1555  2.31  
LINK         SG  CYS B 987                ZN    ZN B1502     1555   1555  2.29  
LINK         SG  CYS B1017                ZN    ZN B1502     1555   1555  2.32  
LINK         SG  CYS B1017                ZN    ZN B1501     1555   1555  2.20  
LINK         SG  CYS B1021                ZN    ZN B1502     1555   1555  2.30  
LINK         SG  CYS B1023                ZN    ZN B1501     1555   1555  2.30  
LINK         SG  CYS B1027                ZN    ZN B1501     1555   1555  2.28  
LINK         SG  CYS B1115                ZN    ZN B1504     1555   1555  2.33  
LINK         SG  CYS B1168                ZN    ZN B1504     1555   1555  2.38  
LINK         SG  CYS B1170                ZN    ZN B1504     1555   1555  2.11  
LINK         SG  CYS B1175                ZN    ZN B1504     1555   1555  2.43  
SITE     1 AC1  5 CYS A 980  CYS A1017  CYS A1023  CYS A1027                    
SITE     2 AC1  5  ZN A1503                                                     
SITE     1 AC2  4 CYS A 974  CYS A 987  CYS A1017  CYS A1021                    
SITE     1 AC3  5 CYS A 974  CYS A 976  CYS A 980  CYS A 985                    
SITE     2 AC3  5  ZN A1501                                                     
SITE     1 AC4  4 CYS A1115  CYS A1168  CYS A1170  CYS A1175                    
SITE     1 AC5 10 MET A1048  TRP A1050  SER A1084  TYR A1085                    
SITE     2 AC5 10 ARG A1109  ASN A1112  HIS A1113  TYR A1154                    
SITE     3 AC5 10 PHE A1166  GLN A1169                                          
SITE     1 AC6 10 ASP A1074  ALA A1077  ASP A1078  ARG A1080                    
SITE     2 AC6 10 ASP A1083  LEU A1086  ASP A1088  CYS A1098                    
SITE     3 AC6 10 ARG A1157  PHE A1158                                          
SITE     1 AC7  4 CYS B 980  CYS B1017  CYS B1023  CYS B1027                    
SITE     1 AC8  4 CYS B 974  CYS B 987  CYS B1017  CYS B1021                    
SITE     1 AC9  4 CYS B 974  CYS B 976  CYS B 980  CYS B 985                    
SITE     1 AD1  4 CYS B1115  CYS B1168  CYS B1170  CYS B1175                    
SITE     1 AD2 14 MET B1048  GLY B1049  TRP B1050  SER B1084                    
SITE     2 AD2 14 TYR B1085  ARG B1109  PHE B1110  ASN B1112                    
SITE     3 AD2 14 HIS B1113  TYR B1154  PHE B1166  CYS B1168                    
SITE     4 AD2 14 GLN B1169  HOH B1630                                          
SITE     1 AD3 10 ASP B1074  ALA B1077  ASP B1078  ARG B1080                    
SITE     2 AD3 10 ASP B1083  LEU B1086  ASP B1088  CYS B1098                    
SITE     3 AD3 10 PHE B1158  ILE B1161                                          
CRYST1   56.970   82.300   73.740  90.00  89.97  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017553  0.000000 -0.000009        0.00000                         
SCALE2      0.000000  0.012151  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013561        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system