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Database: PDB
Entry: 5TH7
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Original site: 5TH7 
HEADER    TRANSFERASE                             29-SEP-16   5TH7              
TITLE     COMPLEX OF SETD8 WITH MS453                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE KMT5A;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 234-380;                                      
COMPND   5 SYNONYM: H4-K20-HMTASE KMT5A,HISTONE-LYSINE N-METHYLTRANSFERASE      
COMPND   6 KMT5A,LYSINE N-METHYLTRANSFERASE 5A,LYSINE-SPECIFIC METHYLASE 5A,    
COMPND   7 PR/SET DOMAIN-CONTAINING PROTEIN 07,PR/SET07,SET DOMAIN-CONTAINING   
COMPND   8 PROTEIN 8;                                                           
COMPND   9 EC: 2.1.1.-,2.1.1.43;                                                
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KMT5A, PRSET7, SET07, SET8, SETD8;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;                           
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28MHL                                  
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.YU,W.TEMPEL,N.BABAULT,A.MA,K.V.BUTLER,J.JIN,C.H.ARROWSMITH,         
AUTHOR   2 C.BOUNTRA,A.M.EDWARDS,P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC) 
REVDAT   2   23-MAY-18 5TH7    1       JRNL   REMARK                            
REVDAT   1   09-NOV-16 5TH7    0                                                
JRNL        AUTH   K.V.BUTLER,A.MA,W.YU,F.LI,W.TEMPEL,N.BABAULT,                
JRNL        AUTH 2 F.PITTELLA-SILVA,J.SHAO,J.WANG,M.LUO,M.VEDADI,P.J.BROWN,     
JRNL        AUTH 3 C.H.ARROWSMITH,J.JIN                                         
JRNL        TITL   STRUCTURE-BASED DESIGN OF A COVALENT INHIBITOR OF THE SET    
JRNL        TITL 2 DOMAIN-CONTAINING PROTEIN 8 (SETD8) LYSINE                   
JRNL        TITL 3 METHYLTRANSFERASE.                                           
JRNL        REF    J. MED. CHEM.                 V.  59  9881 2016              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   27804297                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01244                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT 2.10.2                                    
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 21340                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : THIN SHELLS (SFTOOLS)          
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.192                          
REMARK   3   R VALUE            (WORKING SET)  : 0.189                          
REMARK   3   FREE R VALUE                      : 0.237                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1066                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 11                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.95                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.04                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.32                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2688                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2574                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2200                   
REMARK   3   BIN FREE R VALUE                        : 0.2450                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.24                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 114                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2142                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 96                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.03                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.34000                                              
REMARK   3    B22 (A**2) : 0.65370                                              
REMARK   3    B33 (A**2) : -0.99370                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.79090                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.000               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.166               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.153               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.165               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.154               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2293   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3105   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 802    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 53     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 383    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2293   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 306    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2656   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.05                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.47                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.56                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|236 - A|378 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.5484   -3.0160  150.6877           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0472 T22:   -0.0750                                    
REMARK   3     T33:   -0.0636 T12:    0.0023                                    
REMARK   3     T13:    0.0136 T23:    0.0112                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4729 L22:    1.2982                                    
REMARK   3     L33:    2.6899 L12:    0.0391                                    
REMARK   3     L13:    0.6103 L23:    0.6202                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0590 S12:   -0.1172 S13:   -0.0753                     
REMARK   3     S21:    0.1361 S22:    0.0507 S23:   -0.0565                     
REMARK   3     S31:   -0.0538 S32:    0.1970 S33:    0.0083                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|236 - B|378 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -38.0425   -2.7789  128.7814           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1196 T22:   -0.0458                                    
REMARK   3     T33:   -0.1539 T12:   -0.0376                                    
REMARK   3     T13:   -0.0114 T23:    0.0057                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.0858 L22:    2.6305                                    
REMARK   3     L33:    1.4251 L12:    2.0417                                    
REMARK   3     L13:    0.7441 L23:    0.3328                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2664 S12:    0.7495 S13:    0.0494                     
REMARK   3     S21:   -0.2770 S22:    0.2698 S23:    0.2519                     
REMARK   3     S31:    0.0209 S32:   -0.0796 S33:   -0.0034                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: GEOMETRY RESTRAINTS FOR THE COVALENT      
REMARK   3  INHIBITOR WERE PREPARED WITH PRODRG AND GRADE.                      
REMARK   4                                                                      
REMARK   4 5TH7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221213.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794535                          
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.25                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21342                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.84200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
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: UNPUBLISHED CRYSTALLOGRAPHIC MODEL OF HUMAN SETD8    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-3350, 0.2 M AMMONIUM FLUORIDE,   
REMARK 280  0.1 M SODIUM CACODYLATE, PH 5.2, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       41.57500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       15.82000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       41.57500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       15.82000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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   233                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     SER A   235                                                      
REMARK 465     ASP A   379                                                      
REMARK 465     ARG A   380                                                      
REMARK 465     GLY B   233                                                      
REMARK 465     LYS B   234                                                      
REMARK 465     SER B   235                                                      
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     LYS A 236    N    CB   CG   CD   CE   NZ                         
REMARK 470     GLU A 238    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 239    CG   CD1  CD2                                       
REMARK 470     SER A 241    OG                                                  
REMARK 470     GLU A 242    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 243    OE1  OE2                                            
REMARK 470     LYS A 245    CG   CD   CE   NZ                                   
REMARK 470     ARG A 246    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 249    CD   OE1  OE2                                       
REMARK 470     LYS A 255    CE   NZ                                             
REMARK 470     LYS A 260    CE   NZ                                             
REMARK 470     LYS A 275    NZ                                                  
REMARK 470     GLU A 292    CD   OE1  OE2                                       
REMARK 470     SER A 320    OG                                                  
REMARK 470     LYS A 321    CE   NZ                                             
REMARK 470     ARG A 329    CZ   NH1  NH2                                       
REMARK 470     GLU A 330    CD   OE1  OE2                                       
REMARK 470     LYS A 342    CE   NZ                                             
REMARK 470     SER A 343    OG                                                  
REMARK 470     LYS A 349    CE   NZ                                             
REMARK 470     GLY A 378    C    O                                              
REMARK 470     LYS B 236    CG   CD   CE   NZ                                   
REMARK 470     GLU B 238    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 239    CG   CD1  CD2                                       
REMARK 470     GLN B 240    CG   CD   OE1  NE2                                  
REMARK 470     SER B 241    OG                                                  
REMARK 470     GLU B 243    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 244    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 245    CG   CD   CE   NZ                                   
REMARK 470     ARG B 246    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 249    CD   OE1  OE2                                       
REMARK 470     LEU B 250    CG   CD1  CD2                                       
REMARK 470     GLU B 252    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 255    CG   CD   CE   NZ                                   
REMARK 470     GLU B 257    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 260    NZ                                                  
REMARK 470     LEU B 263    CG   CD1  CD2                                       
REMARK 470     LYS B 267    CG   CD   CE   NZ                                   
REMARK 470     GLU B 292    CD   OE1  OE2                                       
REMARK 470     LEU B 302    CG   CD1  CD2                                       
REMARK 470     SER B 320    OG                                                  
REMARK 470     LYS B 321    CE   NZ                                             
REMARK 470     ARG B 329    NH1  NH2                                            
REMARK 470     GLU B 330    CD   OE1  OE2                                       
REMARK 470     ASN B 332    CG   OD1  ND2                                       
REMARK 470     LYS B 342    CG   CD   CE   NZ                                   
REMARK 470     GLN B 347    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 349    CE   NZ                                             
REMARK 470     ARG B 380    C    O    CB   CG   CD   NE   CZ                    
REMARK 470     ARG B 380    NH1  NH2                                            
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    VAL A 283      -63.71   -103.06                                   
REMARK 500    ALA A 304       25.80     49.78                                   
REMARK 500    LEU A 319     -123.16     61.81                                   
REMARK 500    SER A 320      -10.86     81.76                                   
REMARK 500    LYS B 267      -71.10   -135.82                                   
REMARK 500    THR B 331     -169.50   -109.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 401                 
DBREF  5TH7 A  234   380  UNP    Q9NQR1   KMT5A_HUMAN    234    380             
DBREF  5TH7 B  234   380  UNP    Q9NQR1   KMT5A_HUMAN    234    380             
SEQADV 5TH7 GLY A  233  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5TH7 SER A  343  UNP  Q9NQR1    CYS   343 ENGINEERED MUTATION            
SEQADV 5TH7 GLY B  233  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5TH7 SER B  343  UNP  Q9NQR1    CYS   343 ENGINEERED MUTATION            
SEQRES   1 A  148  GLY LYS SER LYS ALA GLU LEU GLN SER GLU GLU ARG LYS          
SEQRES   2 A  148  ARG ILE ASP GLU LEU ILE GLU SER GLY LYS GLU GLU GLY          
SEQRES   3 A  148  MET LYS ILE ASP LEU ILE ASP GLY LYS GLY ARG GLY VAL          
SEQRES   4 A  148  ILE ALA THR LYS GLN PHE SER ARG GLY ASP PHE VAL VAL          
SEQRES   5 A  148  GLU TYR HIS GLY ASP LEU ILE GLU ILE THR ASP ALA LYS          
SEQRES   6 A  148  LYS ARG GLU ALA LEU TYR ALA GLN ASP PRO SER THR GLY          
SEQRES   7 A  148  CYS TYR MET TYR TYR PHE GLN TYR LEU SER LYS THR TYR          
SEQRES   8 A  148  CYS VAL ASP ALA THR ARG GLU THR ASN ARG LEU GLY ARG          
SEQRES   9 A  148  LEU ILE ASN HIS SER LYS SER GLY ASN CYS GLN THR LYS          
SEQRES  10 A  148  LEU HIS ASP ILE ASP GLY VAL PRO HIS LEU ILE LEU ILE          
SEQRES  11 A  148  ALA SER ARG ASP ILE ALA ALA GLY GLU GLU LEU LEU TYR          
SEQRES  12 A  148  ASP TYR GLY ASP ARG                                          
SEQRES   1 B  148  GLY LYS SER LYS ALA GLU LEU GLN SER GLU GLU ARG LYS          
SEQRES   2 B  148  ARG ILE ASP GLU LEU ILE GLU SER GLY LYS GLU GLU GLY          
SEQRES   3 B  148  MET LYS ILE ASP LEU ILE ASP GLY LYS GLY ARG GLY VAL          
SEQRES   4 B  148  ILE ALA THR LYS GLN PHE SER ARG GLY ASP PHE VAL VAL          
SEQRES   5 B  148  GLU TYR HIS GLY ASP LEU ILE GLU ILE THR ASP ALA LYS          
SEQRES   6 B  148  LYS ARG GLU ALA LEU TYR ALA GLN ASP PRO SER THR GLY          
SEQRES   7 B  148  CYS TYR MET TYR TYR PHE GLN TYR LEU SER LYS THR TYR          
SEQRES   8 B  148  CYS VAL ASP ALA THR ARG GLU THR ASN ARG LEU GLY ARG          
SEQRES   9 B  148  LEU ILE ASN HIS SER LYS SER GLY ASN CYS GLN THR LYS          
SEQRES  10 B  148  LEU HIS ASP ILE ASP GLY VAL PRO HIS LEU ILE LEU ILE          
SEQRES  11 B  148  ALA SER ARG ASP ILE ALA ALA GLY GLU GLU LEU LEU TYR          
SEQRES  12 B  148  ASP TYR GLY ASP ARG                                          
HET    7BY  A 401      28                                                       
HET    UNX  A 402       1                                                       
HET    UNX  A 403       1                                                       
HET    UNX  A 404       1                                                       
HET    UNX  A 405       1                                                       
HET    UNX  A 406       1                                                       
HET    UNX  A 407       1                                                       
HET    UNX  A 408       1                                                       
HET    UNX  A 409       1                                                       
HET    UNX  A 410       1                                                       
HET    UNX  A 411       1                                                       
HET    UNX  A 412       1                                                       
HET    EDO  B 401       4                                                       
HET    7BY  B 402      28                                                       
HET    UNX  B 403       1                                                       
HET    UNX  B 404       1                                                       
HET    UNX  B 405       1                                                       
HET    UNX  B 406       1                                                       
HET    UNX  B 407       1                                                       
HET    UNX  B 408       1                                                       
HET    UNX  B 409       1                                                       
HET    UNX  B 410       1                                                       
HET    UNX  B 411       1                                                       
HET    UNX  B 412       1                                                       
HETNAM     7BY N-(3-{[6,7-DIMETHOXY-2-(PYRROLIDIN-1-YL)QUINAZOLIN-4-            
HETNAM   2 7BY  YL]AMINO}PROPYL)PROPANAMIDE                                     
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  7BY    2(C20 H29 N5 O3)                                             
FORMUL   4  UNX    21(X)                                                        
FORMUL  15  EDO    C2 H6 O2                                                     
FORMUL  27  HOH   *96(H2 O)                                                     
HELIX    1 AA1 LYS A  236  GLY A  254  1                                  19    
HELIX    2 AA2 ILE A  293  ALA A  304  1                                  12    
HELIX    3 AA3 ASP A  306  GLY A  310  5                                   5    
HELIX    4 AA4 LEU A  334  ILE A  338  5                                   5    
HELIX    5 AA5 ALA B  237  GLU B  252  1                                  16    
HELIX    6 AA6 GLU B  292  ALA B  304  1                                  13    
HELIX    7 AA7 ASP B  306  GLY B  310  5                                   5    
HELIX    8 AA8 LEU B  334  ILE B  338  5                                   5    
SHEET    1 AA1 4 MET A 259  ILE A 264  0                                        
SHEET    2 AA1 4 GLY A 268  ALA A 273 -1  O  GLY A 268   N  ILE A 264           
SHEET    3 AA1 4 GLU A 372  TYR A 375 -1  O  LEU A 373   N  VAL A 271           
SHEET    4 AA1 4 ASN A 339  HIS A 340  1  N  ASN A 339   O  TYR A 375           
SHEET    1 AA2 3 PHE A 282  GLU A 285  0                                        
SHEET    2 AA2 3 VAL A 356  ALA A 363 -1  O  LEU A 361   N  VAL A 284           
SHEET    3 AA2 3 CYS A 346  ILE A 353 -1  N  ILE A 353   O  VAL A 356           
SHEET    1 AA3 3 ASP A 289  GLU A 292  0                                        
SHEET    2 AA3 3 LYS A 321  ASP A 326 -1  O  ASP A 326   N  ASP A 289           
SHEET    3 AA3 3 MET A 313  TYR A 318 -1  N  TYR A 318   O  LYS A 321           
SHEET    1 AA4 2 MET B 259  ILE B 264  0                                        
SHEET    2 AA4 2 GLY B 268  ALA B 273 -1  O  ILE B 272   N  LYS B 260           
SHEET    1 AA5 5 PHE B 282  GLU B 285  0                                        
SHEET    2 AA5 5 VAL B 356  ALA B 363 -1  O  LEU B 361   N  VAL B 284           
SHEET    3 AA5 5 CYS B 346  ILE B 353 -1  N  HIS B 351   O  HIS B 358           
SHEET    4 AA5 5 LEU B 374  ASP B 376  1  O  LEU B 374   N  CYS B 346           
SHEET    5 AA5 5 ASN B 339  HIS B 340  1  N  ASN B 339   O  TYR B 375           
SHEET    1 AA6 3 ASP B 289  ILE B 291  0                                        
SHEET    2 AA6 3 LYS B 321  ASP B 326 -1  O  CYS B 324   N  ILE B 291           
SHEET    3 AA6 3 MET B 313  TYR B 318 -1  N  PHE B 316   O  TYR B 323           
LINK         SG  CYS A 311                 CAA 7BY B 402     1555   1555  1.80  
LINK         SG  CYS B 311                 CAA 7BY A 401     1555   1555  1.82  
SITE     1 AC1  6 MET A 313  TYR A 315  MET B 313  TYR B 315                    
SITE     2 AC1  6 HOH B 512  HOH B 540                                          
CRYST1   83.150   31.640  114.890  90.00 105.23  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012026  0.000000  0.003274        0.00000                         
SCALE2      0.000000  0.031606  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009021        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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