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Database: PDB
Entry: 5EG2
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Original site: 5EG2 
HEADER    TRANSFERASE/TRANSCRIPTION FACTOR        26-OCT-15   5EG2              
TITLE     SET7/9 N265A IN COMPLEX WITH ADOHCY AND TAF10 PEPTIDE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD7;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HISTONE H3-K4 METHYLTRANSFERASE SETD7,H3-K4-HMTASE SETD7,   
COMPND   5 LYSINE N-METHYLTRANSFERASE 7,SET DOMAIN-CONTAINING PROTEIN 7,SET7/9; 
COMPND   6 EC: 2.1.1.43;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 10;          
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 186-195;                                      
COMPND  13 SYNONYM: STAF28,TRANSCRIPTION INITIATION FACTOR TFIID 30 KDA SUBUNIT,
COMPND  14 TAFII30;                                                             
COMPND  15 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: SETD7, KIAA1717, KMT7, SET7, SET9;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 BL21(DE3);                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHIS2;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRANSFERASE-TRANSCRIPTION FACTOR COMPLEX                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.M.KRONER,R.J.FICK,R.C.TRIEVEL                                       
REVDAT   4   20-SEP-17 5EG2    1       REMARK                                   
REVDAT   3   30-MAR-16 5EG2    1       JRNL                                     
REVDAT   2   03-FEB-16 5EG2    1       JRNL                                     
REVDAT   1   13-JAN-16 5EG2    0                                                
JRNL        AUTH   R.J.FICK,G.M.KRONER,B.NEPAL,R.MAGNANI,S.HOROWITZ,R.L.HOUTZ,  
JRNL        AUTH 2 S.SCHEINER,R.C.TRIEVEL                                       
JRNL        TITL   SULFUR-OXYGEN CHALCOGEN BONDING MEDIATES ADOMET RECOGNITION  
JRNL        TITL 2 IN THE LYSINE METHYLTRANSFERASE SET7/9.                      
JRNL        REF    ACS CHEM.BIOL.                V.  11   748 2016              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   26713889                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.5B00852                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 56152                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.148                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.171                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2817                            
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 39.9198 -  4.2030    1.00     2836   154  0.1548 0.1767        
REMARK   3     2  4.2030 -  3.3366    1.00     2723   139  0.1328 0.1576        
REMARK   3     3  3.3366 -  2.9149    1.00     2720   148  0.1591 0.1616        
REMARK   3     4  2.9149 -  2.6485    1.00     2684   143  0.1686 0.1941        
REMARK   3     5  2.6485 -  2.4587    1.00     2679   142  0.1565 0.1708        
REMARK   3     6  2.4587 -  2.3137    1.00     2665   137  0.1479 0.1817        
REMARK   3     7  2.3137 -  2.1979    1.00     2667   142  0.1402 0.1463        
REMARK   3     8  2.1979 -  2.1022    1.00     2683   144  0.1396 0.1681        
REMARK   3     9  2.1022 -  2.0213    1.00     2637   139  0.1387 0.1738        
REMARK   3    10  2.0213 -  1.9515    1.00     2673   138  0.1442 0.1988        
REMARK   3    11  1.9515 -  1.8905    1.00     2637   137  0.1341 0.1684        
REMARK   3    12  1.8905 -  1.8365    1.00     2663   140  0.1316 0.1755        
REMARK   3    13  1.8365 -  1.7881    1.00     2638   139  0.1339 0.1700        
REMARK   3    14  1.7881 -  1.7445    1.00     2663   140  0.1301 0.1751        
REMARK   3    15  1.7445 -  1.7048    1.00     2651   141  0.1308 0.1522        
REMARK   3    16  1.7048 -  1.6686    1.00     2609   139  0.1409 0.1631        
REMARK   3    17  1.6686 -  1.6352    1.00     2660   140  0.1429 0.1890        
REMARK   3    18  1.6352 -  1.6043    1.00     2613   135  0.1440 0.1681        
REMARK   3    19  1.6043 -  1.5757    1.00     2646   141  0.1499 0.1808        
REMARK   3    20  1.5757 -  1.5490    0.99     2588   139  0.1567 0.2043        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.310           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.16                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.57                          
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      :  0.009           2023                                  
REMARK   3   ANGLE     :  1.182           2765                                  
REMARK   3   CHIRALITY :  0.052            302                                  
REMARK   3   PLANARITY :  0.006            358                                  
REMARK   3   DIHEDRAL  : 12.808            728                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5EG2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214636.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97903                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 V706                      
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000 V706                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56195                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.90                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.90400                            
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 2.5.6                                          
REMARK 200 STARTING MODEL: 4J83                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 RATIO OF PROTEIN SOLUTION TO         
REMARK 280  CRYSTALLIZATION SOLUTION. PROTEIN SOLUTION: 4.0-8.0 MG/ML           
REMARK 280  PROTEIN, 2.5 MM ADOMET, 2.0 MM TAF10 PEPTIDE, AND 2.0 MM TCEP       
REMARK 280  CRYSTALLANT SOLUTION: 0.99 - 1.02 M SODIUM CITRATE, 12 - 22 MM      
REMARK 280  NICKEL (II) CHLORIDE, AND 100 MM IMIDAZOLE PH 8.4, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.90600            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.95300            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.95300            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       63.90600            
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: 1140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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     GLY A   105                                                      
REMARK 465     ALA A   106                                                      
REMARK 465     MET A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     TYR A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     ASN A   113                                                      
REMARK 465     ILE A   114                                                      
REMARK 465     ARG A   115                                                      
REMARK 465     HIS A   116                                                      
REMARK 465     PRO A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     GLN A   365                                                      
REMARK 465     LYS A   366                                                      
REMARK 465     LYS B   192                                                      
REMARK 465     TYR B   193                                                      
REMARK 465     THR B   194                                                      
REMARK 465     LEU B   195                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 135    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 152    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 271    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 272    CG   CD   OE1  OE2                                  
REMARK 470     SER A 340    OG                                                  
REMARK 470     LYS A 358    CG   CD   CE   NZ                                   
REMARK 470     GLN A 364    CG   CD   OE1  NE2                                  
REMARK 470     SER B 186    OG                                                  
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     ARG B 191    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   717     O    HOH A   776              2.12            
REMARK 500   O    HOH B   208     O    HOH B   209              2.13            
REMARK 500   O    HOH A   536     O    HOH A   760              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   639     O    HOH A   639     4645     1.91            
REMARK 500   O    HOH A   511     O    HOH A   659     5665     2.17            
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    ARG A 152      -43.75   -143.09                                   
REMARK 500    ASP A 194       56.65   -151.73                                   
REMARK 500    THR A 197     -168.08   -119.91                                   
REMARK 500    SER A 202      146.08   -174.75                                   
REMARK 500    CYS A 288       21.22   -142.83                                   
REMARK 500    ILE A 316     -159.99   -139.19                                   
REMARK 500    LYS B 187       44.76    -84.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 801        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A 802        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A 803        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH A 804        DISTANCE =  6.74 ANGSTROMS                       
REMARK 525    HOH A 805        DISTANCE =  6.80 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 126   O                                                      
REMARK 620 2 SER A 128   OG  113.7                                              
REMARK 620 3 VAL A 147   O   101.8  81.1                                        
REMARK 620 4 TYR A 148   O    94.9 135.9  59.9                                  
REMARK 620 5 HOH A 607   O   125.0  78.2 133.1 112.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 402                  
DBREF  5EG2 A  110   366  UNP    Q8WTS6   SETD7_HUMAN    110    366             
DBREF  5EG2 B  186   195  UNP    Q12962   TAF10_HUMAN    186    195             
SEQADV 5EG2 GLY A  105  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5EG2 ALA A  106  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5EG2 MET A  107  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5EG2 GLY A  108  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5EG2 SER A  109  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 5EG2 ALA A  265  UNP  Q8WTS6    ASN   265 ENGINEERED MUTATION            
SEQRES   1 A  262  GLY ALA MET GLY SER TYR LYS ASP ASN ILE ARG HIS GLY          
SEQRES   2 A  262  VAL CYS TRP ILE TYR TYR PRO ASP GLY GLY SER LEU VAL          
SEQRES   3 A  262  GLY GLU VAL ASN GLU ASP GLY GLU MET THR GLY GLU LYS          
SEQRES   4 A  262  ILE ALA TYR VAL TYR PRO ASP GLU ARG THR ALA LEU TYR          
SEQRES   5 A  262  GLY LYS PHE ILE ASP GLY GLU MET ILE GLU GLY LYS LEU          
SEQRES   6 A  262  ALA THR LEU MET SER THR GLU GLU GLY ARG PRO HIS PHE          
SEQRES   7 A  262  GLU LEU MET PRO GLY ASN SER VAL TYR HIS PHE ASP LYS          
SEQRES   8 A  262  SER THR SER SER CYS ILE SER THR ASN ALA LEU LEU PRO          
SEQRES   9 A  262  ASP PRO TYR GLU SER GLU ARG VAL TYR VAL ALA GLU SER          
SEQRES  10 A  262  LEU ILE SER SER ALA GLY GLU GLY LEU PHE SER LYS VAL          
SEQRES  11 A  262  ALA VAL GLY PRO ASN THR VAL MET SER PHE TYR ASN GLY          
SEQRES  12 A  262  VAL ARG ILE THR HIS GLN GLU VAL ASP SER ARG ASP TRP          
SEQRES  13 A  262  ALA LEU ASN GLY ALA THR LEU SER LEU ASP GLU GLU THR          
SEQRES  14 A  262  VAL ILE ASP VAL PRO GLU PRO TYR ASN HIS VAL SER LYS          
SEQRES  15 A  262  TYR CYS ALA SER LEU GLY HIS LYS ALA ASN HIS SER PHE          
SEQRES  16 A  262  THR PRO ASN CYS ILE TYR ASP MET PHE VAL HIS PRO ARG          
SEQRES  17 A  262  PHE GLY PRO ILE LYS CYS ILE ARG THR LEU ARG ALA VAL          
SEQRES  18 A  262  GLU ALA ASP GLU GLU LEU THR VAL ALA TYR GLY TYR ASP          
SEQRES  19 A  262  HIS SER PRO PRO GLY LYS SER GLY PRO GLU ALA PRO GLU          
SEQRES  20 A  262  TRP TYR GLN VAL GLU LEU LYS ALA PHE GLN ALA THR GLN          
SEQRES  21 A  262  GLN LYS                                                      
SEQRES   1 B   10  SER LYS SER MLZ ASP ARG LYS TYR THR LEU                      
MODRES 5EG2 MLZ B  189  LYS  MODIFIED RESIDUE                                   
HET    MLZ  B 189      10                                                       
HET    SAH  A 401      26                                                       
HET     NA  A 402       1                                                       
HETNAM     MLZ N-METHYL-LYSINE                                                  
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM      NA SODIUM ION                                                       
FORMUL   2  MLZ    C7 H16 N2 O2                                                 
FORMUL   3  SAH    C14 H20 N6 O5 S                                              
FORMUL   4   NA    NA 1+                                                        
FORMUL   5  HOH   *316(H2 O)                                                    
HELIX    1 AA1 ASP A  209  GLU A  214  1                                   6    
HELIX    2 AA2 THR A  251  SER A  257  1                                   7    
HELIX    3 AA3 ASP A  259  ASN A  263  5                                   5    
HELIX    4 AA4 LEU A  291  ALA A  295  5                                   5    
HELIX    5 AA5 PRO A  350  GLN A  364  1                                  15    
SHEET    1 AA1 6 VAL A 118  TYR A 122  0                                        
SHEET    2 AA1 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3 AA1 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4 AA1 6 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    5 AA1 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6 AA1 6 ARG A 179  LEU A 184 -1  O  HIS A 181   N  MET A 173           
SHEET    1 AA2 6 VAL A 118  TYR A 122  0                                        
SHEET    2 AA2 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3 AA2 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4 AA2 6 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    5 AA2 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6 AA2 6 VAL A 190  TYR A 191 -1  O  TYR A 191   N  GLY A 167           
SHEET    1 AA3 4 VAL A 216  GLU A 220  0                                        
SHEET    2 AA3 4 GLU A 228  SER A 232 -1  O  GLY A 229   N  ALA A 219           
SHEET    3 AA3 4 GLU A 330  VAL A 333 -1  O  LEU A 331   N  LEU A 230           
SHEET    4 AA3 4 ASN A 296  HIS A 297  1  N  ASN A 296   O  VAL A 333           
SHEET    1 AA4 3 VAL A 241  TYR A 245  0                                        
SHEET    2 AA4 3 GLY A 314  THR A 321 -1  O  ILE A 319   N  MET A 242           
SHEET    3 AA4 3 CYS A 303  HIS A 310 -1  N  ASP A 306   O  CYS A 318           
SHEET    1 AA5 3 VAL A 248  ILE A 250  0                                        
SHEET    2 AA5 3 VAL A 274  ASP A 276 -1  O  VAL A 274   N  ILE A 250           
SHEET    3 AA5 3 LEU A 267  SER A 268 -1  N  LEU A 267   O  ILE A 275           
LINK         O   GLY A 126                NA    NA A 402     1555   1555  2.79  
LINK         OG  SER A 128                NA    NA A 402     1555   1555  2.96  
LINK         O   VAL A 147                NA    NA A 402     1555   1555  3.11  
LINK         O   TYR A 148                NA    NA A 402     1555   1555  3.18  
LINK         C   SER B 188                 N   MLZ B 189     1555   1555  1.33  
LINK         C   MLZ B 189                 N   ASP B 190     1555   1555  1.34  
LINK        NA    NA A 402                 O   HOH A 607     1555   1555  2.78  
CISPEP   1 GLU A  279    PRO A  280          0         3.55                     
SITE     1 AC1 18 ALA A 226  GLU A 228  GLY A 264  HIS A 293                    
SITE     2 AC1 18 LYS A 294  ASN A 296  HIS A 297  TYR A 335                    
SITE     3 AC1 18 TRP A 352  GLU A 356  HOH A 515  HOH A 518                    
SITE     4 AC1 18 HOH A 584  HOH A 642  HOH A 653  HOH A 662                    
SITE     5 AC1 18 HOH A 695  MLZ B 189                                          
SITE     1 AC2  7 TYR A 122  GLY A 126  GLY A 127  SER A 128                    
SITE     2 AC2  7 VAL A 147  TYR A 148  HOH A 607                               
CRYST1   83.198   83.198   95.859  90.00  90.00 120.00 P 32 2 1      6          
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      0.012020  0.006939  0.000000        0.00000                         
SCALE2      0.000000  0.013879  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010432        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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