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Database: PDB
Entry: 5JJ0
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Original site: 5JJ0 
HEADER    TRANSFERASE                             22-APR-16   5JJ0              
TITLE     STRUCTURE OF G9A SET-DOMAIN WITH HISTONE H3K9M PEPTIDE AND EXCESS SAH 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SET DOMAIN OF HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2 G9A,
COMPND   5 UNP RESIDUES 882-1155;                                               
COMPND   6 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 2,HLA-B-     
COMPND   7 ASSOCIATED TRANSCRIPT 8,HISTONE H3-K9 METHYLTRANSFERASE 3,H3-K9-     
COMPND   8 HMTASE 3,LYSINE N-METHYLTRANSFERASE 1C,PROTEIN G9A;                  
COMPND   9 EC: 2.1.1.-,2.1.1.43;                                                
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: HISTONE H3K9M MUTANT PEPTIDE;                              
COMPND  13 CHAIN: F, G;                                                         
COMPND  14 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: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SET-DOMAIN, HISTONE METHYL TRANSFERASE, HISTONE PEPTIDE, TRANSFERASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.JAYARAM,S.F.BELLON,F.POY                                            
REVDAT   1   06-JUL-16 5JJ0    0                                                
JRNL        AUTH   H.JAYARAM,D.HOELPER,S.U.JAIN,N.CANTONE,S.M.LUNDGREN,F.POY,   
JRNL        AUTH 2 C.D.ALLIS,R.CUMMINGS,S.BELLON,P.W.LEWIS                      
JRNL        TITL   S-ADENOSYL METHIONINE IS NECESSARY FOR INHIBITION OF THE     
JRNL        TITL 2 METHYLTRANSFERASE G9A BY THE LYSINE 9 TO METHIONINE MUTATION 
JRNL        TITL 3 ON HISTONE H3.                                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 113  6182 2016              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   27185940                                                     
JRNL        DOI    10.1073/PNAS.1605523113                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.72 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.91                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 63270                          
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3380                            
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) : 1.72                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4111                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.49                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 246                          
REMARK   3   BIN FREE R VALUE                    : 0.2990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4488                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.09000                                             
REMARK   3    B22 (A**2) : 0.64000                                              
REMARK   3    B33 (A**2) : 0.43000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.58000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.125         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.121         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.105         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.309         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4694 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4302 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6336 ; 1.879 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9876 ; 1.155 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   560 ; 6.332 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   242 ;31.205 ;23.719       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   805 ;14.853 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;15.571 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   674 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5320 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1133 ; 0.002 ; 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):  2246 ; 2.577 ; 2.901       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2245 ; 2.576 ; 2.900       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2801 ; 3.548 ; 4.333       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2802 ; 3.547 ; 4.334       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2448 ; 3.434 ; 3.308       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2449 ; 3.433 ; 3.308       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3535 ; 5.280 ; 4.801       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5188 ; 6.782 ;23.253       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5155 ; 6.756 ;23.206       
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 : NULL                                                 
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 5JJ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220679.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 178                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0010                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63270                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.720                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.910                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.1300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: 2O8J                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M TRI-AMMONIUM CITRATE PH 7 AND      
REMARK 280  20% W/V POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  TEMPERATURE 298K                                                    
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       39.15550            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, B, G                            
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     LEU A  1189                                                      
REMARK 465     THR F     3                                                      
REMARK 465     GLY F    12                                                      
REMARK 465     GLY F    13                                                      
REMARK 465     ILE B   916                                                      
REMARK 465     ARG B   917                                                      
REMARK 465     THR B   918                                                      
REMARK 465     ASN B  1091                                                      
REMARK 465     LYS B  1092                                                      
REMARK 465     ASP B  1093                                                      
REMARK 465     GLY B  1094                                                      
REMARK 465     GLY G    12                                                      
REMARK 465     GLY G    13                                                      
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 925      101.21   -164.29                                   
REMARK 500    ASP A 978     -168.48    -74.13                                   
REMARK 500    ILE A 992      -55.61     76.03                                   
REMARK 500    ASN A1106     -169.61   -115.41                                   
REMARK 500    ASP A1116       78.46   -107.68                                   
REMARK 500    MET A1126      -88.63   -132.26                                   
REMARK 500    ASP B 925      100.18   -160.51                                   
REMARK 500    ASP B 949       38.56    -91.23                                   
REMARK 500    ASP B 949       32.44    -86.77                                   
REMARK 500    ASP B 978     -148.24   -105.63                                   
REMARK 500    ILE B 992      -49.45     68.88                                   
REMARK 500    ARG B1030       38.38   -144.93                                   
REMARK 500    ASN B1106     -165.77   -126.53                                   
REMARK 500    ASP B1116       76.88   -111.25                                   
REMARK 500    MET B1126      -89.98   -136.94                                   
REMARK 500    PHE B1158      -62.11    -93.73                                   
REMARK 500    SER B1187       71.12    -62.99                                   
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 A1202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 974   SG                                                     
REMARK 620 2 CYS A 976   SG  106.3                                              
REMARK 620 3 CYS A 980   SG  106.8 106.4                                        
REMARK 620 4 CYS A 985   SG  111.7 105.1 119.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 974   SG                                                     
REMARK 620 2 CYS A 987   SG  113.5                                              
REMARK 620 3 CYS A1017   SG  109.5 110.5                                        
REMARK 620 4 CYS A1021   SG  105.2 100.9 117.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1203  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 980   SG                                                     
REMARK 620 2 CYS A1017   SG  111.3                                              
REMARK 620 3 CYS A1023   SG  108.6 108.2                                        
REMARK 620 4 CYS A1027   SG  113.4 107.8 107.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1204  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1115   SG                                                     
REMARK 620 2 CYS A1168   SG  115.6                                              
REMARK 620 3 CYS A1170   SG  108.7 105.8                                        
REMARK 620 4 CYS A1175   SG  102.0 111.1 113.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1203  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 974   SG                                                     
REMARK 620 2 CYS B 976   SG  106.7                                              
REMARK 620 3 CYS B 980   SG  107.7 107.0                                        
REMARK 620 4 CYS B 985   SG  109.2 104.7 120.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 974   SG                                                     
REMARK 620 2 CYS B 987   SG  113.1                                              
REMARK 620 3 CYS B1017   SG  108.3 112.4                                        
REMARK 620 4 CYS B1021   SG  106.2 102.1 114.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 980   SG                                                     
REMARK 620 2 CYS B1017   SG  112.8                                              
REMARK 620 3 CYS B1023   SG  109.0 108.0                                        
REMARK 620 4 CYS B1027   SG  112.7 105.0 109.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1204  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1115   SG                                                     
REMARK 620 2 CYS B1168   SG  116.8                                              
REMARK 620 3 CYS B1170   SG  107.6 105.1                                        
REMARK 620 4 CYS B1175   SG  102.8 108.0 117.2                                  
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 1201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 1205                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5JHN   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF G9A WITH H3K9ALA MUTANT PEPTIDE PART OF THE SAME STUDY  
REMARK 900 RELATED ID: 5JIN   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF G9A WITH H3K9MET MUTANT PEPTIDE PART OF THE SAME STUDY  
REMARK 900 RELATED ID: 5JIY   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF G9A WITH H3K9NORLEU MUTANT PEPTIDE PART OF THE SAME     
REMARK 900 STUDY                                                                
DBREF  5JJ0 A  916  1189  UNP    Q96KQ7   EHMT2_HUMAN    882   1155             
DBREF  5JJ0 F    3    13  PDB    5JJ0     5JJ0             3     13             
DBREF  5JJ0 B  916  1189  UNP    Q96KQ7   EHMT2_HUMAN    882   1155             
DBREF  5JJ0 G    3    13  PDB    5JJ0     5JJ0             3     13             
SEQRES   1 A  274  ILE ARG THR GLU LYS ILE ILE CYS ARG ASP VAL ALA ARG          
SEQRES   2 A  274  GLY TYR GLU ASN VAL PRO ILE PRO CYS VAL ASN GLY VAL          
SEQRES   3 A  274  ASP GLY GLU PRO CYS PRO GLU ASP TYR LYS TYR ILE SER          
SEQRES   4 A  274  GLU ASN CYS GLU THR SER THR MET ASN ILE ASP ARG ASN          
SEQRES   5 A  274  ILE THR HIS LEU GLN HIS CYS THR CYS VAL ASP ASP CYS          
SEQRES   6 A  274  SER SER SER ASN CYS LEU CYS GLY GLN LEU SER ILE ARG          
SEQRES   7 A  274  CYS TRP TYR ASP LYS ASP GLY ARG LEU LEU GLN GLU PHE          
SEQRES   8 A  274  ASN LYS ILE GLU PRO PRO LEU ILE PHE GLU CYS ASN GLN          
SEQRES   9 A  274  ALA CYS SER CYS TRP ARG ASN CYS LYS ASN ARG VAL VAL          
SEQRES  10 A  274  GLN SER GLY ILE LYS VAL ARG LEU GLN LEU TYR ARG THR          
SEQRES  11 A  274  ALA LYS MET GLY TRP GLY VAL ARG ALA LEU GLN THR ILE          
SEQRES  12 A  274  PRO GLN GLY THR PHE ILE CYS GLU TYR VAL GLY GLU LEU          
SEQRES  13 A  274  ILE SER ASP ALA GLU ALA ASP VAL ARG GLU ASP ASP SER          
SEQRES  14 A  274  TYR LEU PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR          
SEQRES  15 A  274  CYS ILE ASP ALA ARG TYR TYR GLY ASN ILE SER ARG PHE          
SEQRES  16 A  274  ILE ASN HIS LEU CYS ASP PRO ASN ILE ILE PRO VAL ARG          
SEQRES  17 A  274  VAL PHE MET LEU HIS GLN ASP LEU ARG PHE PRO ARG ILE          
SEQRES  18 A  274  ALA PHE PHE SER SER ARG ASP ILE ARG THR GLY GLU GLU          
SEQRES  19 A  274  LEU GLY PHE ASP TYR GLY ASP ARG PHE TRP ASP ILE LYS          
SEQRES  20 A  274  SER LYS TYR PHE THR CYS GLN CYS GLY SER GLU LYS CYS          
SEQRES  21 A  274  LYS HIS SER ALA GLU ALA ILE ALA LEU GLU GLN SER ARG          
SEQRES  22 A  274  LEU                                                          
SEQRES   1 F   11  THR LYS GLN THR ALA ARG MET SER THR GLY GLY                  
SEQRES   1 B  274  ILE ARG THR GLU LYS ILE ILE CYS ARG ASP VAL ALA ARG          
SEQRES   2 B  274  GLY TYR GLU ASN VAL PRO ILE PRO CYS VAL ASN GLY VAL          
SEQRES   3 B  274  ASP GLY GLU PRO CYS PRO GLU ASP TYR LYS TYR ILE SER          
SEQRES   4 B  274  GLU ASN CYS GLU THR SER THR MET ASN ILE ASP ARG ASN          
SEQRES   5 B  274  ILE THR HIS LEU GLN HIS CYS THR CYS VAL ASP ASP CYS          
SEQRES   6 B  274  SER SER SER ASN CYS LEU CYS GLY GLN LEU SER ILE ARG          
SEQRES   7 B  274  CYS TRP TYR ASP LYS ASP GLY ARG LEU LEU GLN GLU PHE          
SEQRES   8 B  274  ASN LYS ILE GLU PRO PRO LEU ILE PHE GLU CYS ASN GLN          
SEQRES   9 B  274  ALA CYS SER CYS TRP ARG ASN CYS LYS ASN ARG VAL VAL          
SEQRES  10 B  274  GLN SER GLY ILE LYS VAL ARG LEU GLN LEU TYR ARG THR          
SEQRES  11 B  274  ALA LYS MET GLY TRP GLY VAL ARG ALA LEU GLN THR ILE          
SEQRES  12 B  274  PRO GLN GLY THR PHE ILE CYS GLU TYR VAL GLY GLU LEU          
SEQRES  13 B  274  ILE SER ASP ALA GLU ALA ASP VAL ARG GLU ASP ASP SER          
SEQRES  14 B  274  TYR LEU PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR          
SEQRES  15 B  274  CYS ILE ASP ALA ARG TYR TYR GLY ASN ILE SER ARG PHE          
SEQRES  16 B  274  ILE ASN HIS LEU CYS ASP PRO ASN ILE ILE PRO VAL ARG          
SEQRES  17 B  274  VAL PHE MET LEU HIS GLN ASP LEU ARG PHE PRO ARG ILE          
SEQRES  18 B  274  ALA PHE PHE SER SER ARG ASP ILE ARG THR GLY GLU GLU          
SEQRES  19 B  274  LEU GLY PHE ASP TYR GLY ASP ARG PHE TRP ASP ILE LYS          
SEQRES  20 B  274  SER LYS TYR PHE THR CYS GLN CYS GLY SER GLU LYS CYS          
SEQRES  21 B  274  LYS HIS SER ALA GLU ALA ILE ALA LEU GLU GLN SER ARG          
SEQRES  22 B  274  LEU                                                          
SEQRES   1 G   11  THR LYS GLN THR ALA ARG MET SER THR GLY GLY                  
HET     ZN  A1201       1                                                       
HET     ZN  A1202       1                                                       
HET     ZN  A1203       1                                                       
HET     ZN  A1204       1                                                       
HET    SAM  A1205      27                                                       
HET     ZN  B1201       1                                                       
HET     ZN  B1202       1                                                       
HET     ZN  B1203       1                                                       
HET     ZN  B1204       1                                                       
HET    SAM  B1205      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL   9  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL  15  HOH   *130(H2 O)                                                    
HELIX    1 AA1 ASN A  967  LEU A  971  5                                   5    
HELIX    2 AA2 CYS A  985  LEU A  990  1                                   6    
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  ARG A 1188  1                                  11    
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  SER B 1187  1                                  10    
SHEET    1 AA1 4 LYS A 920  CYS A 923  0                                        
SHEET    2 AA1 4 CYS A 937  ASN A 939 -1  O  ASN A 939   N  LYS A 920           
SHEET    3 AA1 4 LEU A1040  ARG A1044  1  O  LEU A1042   N  VAL A 938           
SHEET    4 AA1 4 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  GLU A1070   O  ASP A1100           
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  ASP A1088 -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  ARG A1123   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 4 LYS B 920  CYS B 923  0                                        
SHEET    2 AA6 4 CYS B 937  ASN B 939 -1  O  CYS B 937   N  CYS B 923           
SHEET    3 AA6 4 LEU B1040  ARG B1044  1  O  LEU B1042   N  VAL B 938           
SHEET    4 AA6 4 TRP B1050  ALA B1054 -1  O  GLY B1051   N  TYR B1043           
SHEET    1 AA7 4 LYS B 951  TYR B 952  0                                        
SHEET    2 AA7 4 TYR B1097  GLY B1105  1  O  TYR B1103   N  LYS B 951           
SHEET    3 AA7 4 GLY B1069  SER B1073 -1  N  ILE B1072   O  CYS B1098           
SHEET    4 AA7 4 CYS B 957  GLU B 958  1  N  CYS B 957   O  LEU B1071           
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  ALA B1137   N  VAL B1122           
SHEET    4 AA9 4 PHE B1063  TYR B1067 -1  N  CYS B1065   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           
LINK         SG  CYS A 974                ZN    ZN A1202     1555   1555  2.34  
LINK         SG  CYS A 974                ZN    ZN A1201     1555   1555  2.37  
LINK         SG  CYS A 976                ZN    ZN A1202     1555   1555  2.39  
LINK         SG  CYS A 980                ZN    ZN A1202     1555   1555  2.26  
LINK         SG  CYS A 980                ZN    ZN A1203     1555   1555  2.43  
LINK         SG  CYS A 985                ZN    ZN A1202     1555   1555  2.29  
LINK         SG  CYS A 987                ZN    ZN A1201     1555   1555  2.29  
LINK         SG  CYS A1017                ZN    ZN A1201     1555   1555  2.33  
LINK         SG  CYS A1017                ZN    ZN A1203     1555   1555  2.37  
LINK         SG  CYS A1021                ZN    ZN A1201     1555   1555  2.29  
LINK         SG  CYS A1023                ZN    ZN A1203     1555   1555  2.26  
LINK         SG  CYS A1027                ZN    ZN A1203     1555   1555  2.28  
LINK         SG  CYS A1115                ZN    ZN A1204     1555   1555  2.30  
LINK         SG  CYS A1168                ZN    ZN A1204     1555   1555  2.31  
LINK         SG  CYS A1170                ZN    ZN A1204     1555   1555  2.35  
LINK         SG  CYS A1175                ZN    ZN A1204     1555   1555  2.34  
LINK         SG  CYS B 974                ZN    ZN B1203     1555   1555  2.31  
LINK         SG  CYS B 974                ZN    ZN B1201     1555   1555  2.40  
LINK         SG  CYS B 976                ZN    ZN B1203     1555   1555  2.36  
LINK         SG  CYS B 980                ZN    ZN B1202     1555   1555  2.33  
LINK         SG  CYS B 980                ZN    ZN B1203     1555   1555  2.29  
LINK         SG  CYS B 985                ZN    ZN B1203     1555   1555  2.30  
LINK         SG  CYS B 987                ZN    ZN B1201     1555   1555  2.26  
LINK         SG  CYS B1017                ZN    ZN B1202     1555   1555  2.36  
LINK         SG  CYS B1017                ZN    ZN B1201     1555   1555  2.39  
LINK         SG  CYS B1021                ZN    ZN B1201     1555   1555  2.28  
LINK         SG  CYS B1023                ZN    ZN B1202     1555   1555  2.24  
LINK         SG  CYS B1027                ZN    ZN B1202     1555   1555  2.35  
LINK         SG  CYS B1115                ZN    ZN B1204     1555   1555  2.30  
LINK         SG  CYS B1168                ZN    ZN B1204     1555   1555  2.34  
LINK         SG  CYS B1170                ZN    ZN B1204     1555   1555  2.31  
LINK         SG  CYS B1175                ZN    ZN B1204     1555   1555  2.31  
SITE     1 AC1  4 CYS A 974  CYS A 987  CYS A1017  CYS A1021                    
SITE     1 AC2  4 CYS A 974  CYS A 976  CYS A 980  CYS A 985                    
SITE     1 AC3  4 CYS A 980  CYS A1017  CYS A1023  CYS A1027                    
SITE     1 AC4  4 CYS A1115  CYS A1168  CYS A1170  CYS A1175                    
SITE     1 AC5 15 MET A1048  TRP A1050  SER A1084  TYR A1085                    
SITE     2 AC5 15 ARG A1109  PHE A1110  ASN A1112  HIS A1113                    
SITE     3 AC5 15 TYR A1154  PHE A1158  PHE A1166  THR A1167                    
SITE     4 AC5 15 CYS A1168  GLN A1169  MET F   9                               
SITE     1 AC6  4 CYS B 974  CYS B 987  CYS B1017  CYS B1021                    
SITE     1 AC7  4 CYS B 980  CYS B1017  CYS B1023  CYS B1027                    
SITE     1 AC8  4 CYS B 974  CYS B 976  CYS B 980  CYS B 985                    
SITE     1 AC9  4 CYS B1115  CYS B1168  CYS B1170  CYS B1175                    
SITE     1 AD1 13 MET B1048  TRP B1050  SER B1084  TYR B1085                    
SITE     2 AD1 13 ARG B1109  PHE B1110  ASN B1112  HIS B1113                    
SITE     3 AD1 13 TYR B1154  PHE B1166  THR B1167  CYS B1168                    
SITE     4 AD1 13 GLN B1169                                                     
CRYST1   56.667   78.311   73.056  90.00  90.20  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      0.017647  0.000000  0.000063        0.00000                         
SCALE2      0.000000  0.012770  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013688        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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