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Database: PDB
Entry: 5WBV
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Original site: 5WBV 
HEADER    TRANSFERASE/INHIBITOR                   29-JUN-17   5WBV              
TITLE     CRYSTAL STRUCTURE OF THE SET DOMAIN OF HUMAN SUV420H1 IN COMPLEX WITH 
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE KMT5B;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SET DOMAIN, UNP RESIDUES 63-335;                           
COMPND   5 SYNONYM: LYSINE N-METHYLTRANSFERASE 5B,LYSINE-SPECIFIC               
COMPND   6 METHYLTRANSFERASE 5B,SUPPRESSOR OF VARIEGATION 4-20 HOMOLOG 1,SUV4-  
COMPND   7 20H1;                                                                
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KMT5B, SUV420H1, CGI-85;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-V3R-PRARE2;                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    SET DOMAIN, METHYLTRANSFERASE, PROTEIN-INHIBITOR COMPLEX, SGC,        
KEYWDS   2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, TRANSFERASE,    
KEYWDS   3 TRANSFERASE-INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.HALABELIAN,W.TEMPEL,P.J.BROWN,C.BOUNTRA,A.M.EDWARDS,C.H.ARROWSMITH, 
AUTHOR   2 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   1   19-JUL-17 5WBV    0                                                
JRNL        AUTH   L.HALABELIAN,W.TEMPEL,P.J.BROWN,C.BOUNTRA,A.M.EDWARDS,       
JRNL        AUTH 2 C.H.ARROWSMITH,STRUCTURAL GENOMICS CONSORTIUM (SGC)          
JRNL        TITL   CRYSTAL STRUCTURE OF THE SET DOMAIN OF HUMAN SUV420H1 IN     
JRNL        TITL 2 COMPLEX WITH INHIBITOR                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26949                          
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)  : 0.236                          
REMARK   3   R VALUE            (WORKING SET)  : 0.234                          
REMARK   3   FREE R VALUE                      : 0.269                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.010                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1351                           
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               : 14                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.39                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 92.94                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2717                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2510                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2587                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2490                   
REMARK   3   BIN FREE R VALUE                        : 0.2900                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.78                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 130                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3396                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 31                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.33                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.76300                                             
REMARK   3    B22 (A**2) : -4.34880                                             
REMARK   3    B33 (A**2) : -8.41420                                             
REMARK   3    B12 (A**2) : -3.95350                                             
REMARK   3    B13 (A**2) : 3.20260                                              
REMARK   3    B23 (A**2) : -1.10170                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.380               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.271               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.219               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.290               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.228               
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      : 0.889                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.867                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3618   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4913   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1207   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 85     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 627    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3618   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 481    ; 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   : 4028   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.13                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.01                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.28                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    6.1288   44.1614    7.5616           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1885 T22:   -0.1695                                    
REMARK   3     T33:   -0.0551 T12:   -0.0031                                    
REMARK   3     T13:    0.0733 T23:   -0.0469                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.2627 L22:    2.6140                                    
REMARK   3     L33:    2.2532 L12:    0.1839                                    
REMARK   3     L13:    0.5118 L23:   -0.9663                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0337 S12:   -0.2405 S13:    0.0026                     
REMARK   3     S21:    0.1346 S22:   -0.0174 S23:   -0.1058                     
REMARK   3     S31:   -0.0369 S32:    0.1160 S33:    0.0511                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    4.2996   18.4688  -18.0052           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2482 T22:   -0.1871                                    
REMARK   3     T33:   -0.0842 T12:   -0.0348                                    
REMARK   3     T13:    0.0943 T23:   -0.1141                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9964 L22:    3.8530                                    
REMARK   3     L33:    3.0571 L12:   -0.2589                                    
REMARK   3     L13:    0.4856 L23:    1.9128                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0633 S12:    0.2578 S13:   -0.0970                     
REMARK   3     S21:    0.0004 S22:   -0.1731 S23:    0.3387                     
REMARK   3     S31:   -0.0356 S32:   -0.1062 S33:    0.2364                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5WBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228753.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN A200                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.32                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26973                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43500                            
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 3S8P                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-12% ETOH, 100MM TRIS PH 8.0, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLN A    63                                                      
REMARK 465     SER A    64                                                      
REMARK 465     ARG A    65                                                      
REMARK 465     TYR A    66                                                      
REMARK 465     VAL A    67                                                      
REMARK 465     PRO A    68                                                      
REMARK 465     SER A    69                                                      
REMARK 465     SER A    70                                                      
REMARK 465     GLY A    71                                                      
REMARK 465     THR A   102                                                      
REMARK 465     SER A   103                                                      
REMARK 465     ALA A   104                                                      
REMARK 465     PHE A   105                                                      
REMARK 465     PRO A   106                                                      
REMARK 465     SER A   107                                                      
REMARK 465     ARG A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     SER A   110                                                      
REMARK 465     ARG A   111                                                      
REMARK 465     HIS A   112                                                      
REMARK 465     PHE A   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     LYS A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     ASP A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     PHE A   119                                                      
REMARK 465     SER A   120                                                      
REMARK 465     HIS A   121                                                      
REMARK 465     ASN A   122                                                      
REMARK 465     ASN A   123                                                      
REMARK 465     PRO A   124                                                      
REMARK 465     VAL A   125                                                      
REMARK 465     ARG A   126                                                      
REMARK 465     PHE A   127                                                      
REMARK 465     ARG A   128                                                      
REMARK 465     PRO A   129                                                      
REMARK 465     ILE A   130                                                      
REMARK 465     SER A   334                                                      
REMARK 465     ARG A   335                                                      
REMARK 465     GLN B    63                                                      
REMARK 465     SER B    64                                                      
REMARK 465     ARG B    65                                                      
REMARK 465     TYR B    66                                                      
REMARK 465     VAL B    67                                                      
REMARK 465     PRO B    68                                                      
REMARK 465     SER B    69                                                      
REMARK 465     SER B    70                                                      
REMARK 465     THR B   102                                                      
REMARK 465     SER B   103                                                      
REMARK 465     ALA B   104                                                      
REMARK 465     PHE B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     SER B   107                                                      
REMARK 465     ARG B   108                                                      
REMARK 465     SER B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     ARG B   111                                                      
REMARK 465     HIS B   112                                                      
REMARK 465     PHE B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     LYS B   115                                                      
REMARK 465     SER B   116                                                      
REMARK 465     ASP B   117                                                      
REMARK 465     SER B   118                                                      
REMARK 465     PHE B   119                                                      
REMARK 465     SER B   120                                                      
REMARK 465     HIS B   121                                                      
REMARK 465     ASN B   122                                                      
REMARK 465     ASN B   123                                                      
REMARK 465     PRO B   124                                                      
REMARK 465     VAL B   125                                                      
REMARK 465     ARG B   126                                                      
REMARK 465     PHE B   127                                                      
REMARK 465     ARG B   128                                                      
REMARK 465     PRO B   129                                                      
REMARK 465     ILE B   130                                                      
REMARK 465     GLY B   160                                                      
REMARK 465     GLU B   161                                                      
REMARK 465     TRP B   162                                                      
REMARK 465     ALA B   163                                                      
REMARK 465     ARG B   164                                                      
REMARK 465     HIS B   165                                                      
REMARK 465     TYR B   166                                                      
REMARK 465     SER B   334                                                      
REMARK 465     ARG B   335                                                      
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  75    CG   CD   CE   NZ                                   
REMARK 470     GLU A  79    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
REMARK 470     ARG A 133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 134    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 135    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 136    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 138    CG   CD   CE   NZ                                   
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 141    CG1  CG2  CD1                                       
REMARK 470     GLU A 142    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     GLU A 148    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 150    CG   CD1  CD2                                       
REMARK 470     LYS A 152    CG   CD   CE   NZ                                   
REMARK 470     LYS A 155    CD   CE   NZ                                        
REMARK 470     GLU A 161    CG   CD   OE1  OE2                                  
REMARK 470     TRP A 162    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 162    CZ3  CH2                                            
REMARK 470     ARG A 164    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 165    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR A 166    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE A 167    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 168    CG   CD1  CD2                                       
REMARK 470     ASN A 169    CG   OD1  ND2                                       
REMARK 470     LYS A 170    CG   CD   CE   NZ                                   
REMARK 470     LYS A 176    CG   CD   CE   NZ                                   
REMARK 470     LYS A 179    CG   CD   CE   NZ                                   
REMARK 470     GLU A 180    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 192    CG   OD1  OD2                                       
REMARK 470     GLN A 207    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 217    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 219    CD   CE   NZ                                        
REMARK 470     LYS A 223    CD   CE   NZ                                        
REMARK 470     GLU A 233    CG   CD   OE1  OE2                                  
REMARK 470     MET A 241    CG   SD   CE                                        
REMARK 470     ARG A 276    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 286    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 298    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 314    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 327    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 332    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 333    CG   CD   CE   NZ                                   
REMARK 470     LYS B  75    CD   CE   NZ                                        
REMARK 470     LYS B 131    CG   CD   CE   NZ                                   
REMARK 470     ARG B 133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 134    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 138    CG   CD   CE   NZ                                   
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 470     GLU B 148    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 151    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 155    CG   CD   CE   NZ                                   
REMARK 470     LEU B 157    CG   CD1  CD2                                       
REMARK 470     PHE B 167    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B 168    CG   CD1  CD2                                       
REMARK 470     ASN B 169    OD1  ND2                                            
REMARK 470     LYS B 170    CG   CD   CE   NZ                                   
REMARK 470     GLN B 174    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 176    CG   CD   CE   NZ                                   
REMARK 470     LYS B 179    CD   CE   NZ                                        
REMARK 470     ASN B 201    CG   OD1  ND2                                       
REMARK 470     GLN B 207    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 211    CE   NZ                                             
REMARK 470     GLU B 217    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 219    CE   NZ                                             
REMARK 470     ARG B 276    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 286    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 287    CG   OD1  OD2                                       
REMARK 470     GLU B 298    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 314    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 315    CG   OD1  ND2                                       
REMARK 470     PHE B 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 326    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 327    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 329    OG1  CG2                                            
REMARK 470     PHE B 332    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 333    CG   CD   CE   NZ                                   
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    ASN A 169       41.90    -89.09                                   
REMARK 500    ASN A 221       -2.19     83.81                                   
REMARK 500    PHE A 312       59.23   -107.40                                   
REMARK 500    GLU B 148       33.84     39.15                                   
REMARK 500    ASN B 169       39.03    -88.06                                   
REMARK 500    ASN B 221       -3.28     82.82                                   
REMARK 500    PHE B 312       53.43   -107.12                                   
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 A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 275   SG                                                     
REMARK 620 2 CYS A 319   SG  113.1                                              
REMARK 620 3 CYS A 321   SG  114.3  97.1                                        
REMARK 620 4 CYS A 324   SG  113.7 103.2 113.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 275   SG                                                     
REMARK 620 2 CYS B 319   SG  112.1                                              
REMARK 620 3 CYS B 321   SG  112.4 101.8                                        
REMARK 620 4 CYS B 324   SG  112.3 107.1 110.5                                  
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 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9ZY A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9ZY B 403                 
DBREF  5WBV A   63   335  UNP    Q4FZB7   KMT5B_HUMAN     63    335             
DBREF  5WBV B   63   335  UNP    Q4FZB7   KMT5B_HUMAN     63    335             
SEQRES   1 A  273  GLN SER ARG TYR VAL PRO SER SER GLY MET SER ALA LYS          
SEQRES   2 A  273  GLU LEU CYS GLU ASN ASP ASP LEU ALA THR SER LEU VAL          
SEQRES   3 A  273  LEU ASP PRO TYR LEU GLY PHE GLN THR HIS LYS MET ASN          
SEQRES   4 A  273  THR SER ALA PHE PRO SER ARG SER SER ARG HIS PHE SER          
SEQRES   5 A  273  LYS SER ASP SER PHE SER HIS ASN ASN PRO VAL ARG PHE          
SEQRES   6 A  273  ARG PRO ILE LYS GLY ARG GLN GLU GLU LEU LYS GLU VAL          
SEQRES   7 A  273  ILE GLU ARG PHE LYS LYS ASP GLU HIS LEU GLU LYS ALA          
SEQRES   8 A  273  PHE LYS CYS LEU THR SER GLY GLU TRP ALA ARG HIS TYR          
SEQRES   9 A  273  PHE LEU ASN LYS ASN LYS MET GLN GLU LYS LEU PHE LYS          
SEQRES  10 A  273  GLU HIS VAL PHE ILE TYR LEU ARG MET PHE ALA THR ASP          
SEQRES  11 A  273  SER GLY PHE GLU ILE LEU PRO CYS ASN ARG TYR SER SER          
SEQRES  12 A  273  GLU GLN ASN GLY ALA LYS ILE VAL ALA THR LYS GLU TRP          
SEQRES  13 A  273  LYS ARG ASN ASP LYS ILE GLU LEU LEU VAL GLY CYS ILE          
SEQRES  14 A  273  ALA GLU LEU SER GLU ILE GLU GLU ASN MET LEU LEU ARG          
SEQRES  15 A  273  HIS GLY GLU ASN ASP PHE SER VAL MET TYR SER THR ARG          
SEQRES  16 A  273  LYS ASN CYS ALA GLN LEU TRP LEU GLY PRO ALA ALA PHE          
SEQRES  17 A  273  ILE ASN HIS ASP CYS ARG PRO ASN CYS LYS PHE VAL SER          
SEQRES  18 A  273  THR GLY ARG ASP THR ALA CYS VAL LYS ALA LEU ARG ASP          
SEQRES  19 A  273  ILE GLU PRO GLY GLU GLU ILE SER CYS TYR TYR GLY ASP          
SEQRES  20 A  273  GLY PHE PHE GLY GLU ASN ASN GLU PHE CYS GLU CYS TYR          
SEQRES  21 A  273  THR CYS GLU ARG ARG GLY THR GLY ALA PHE LYS SER ARG          
SEQRES   1 B  273  GLN SER ARG TYR VAL PRO SER SER GLY MET SER ALA LYS          
SEQRES   2 B  273  GLU LEU CYS GLU ASN ASP ASP LEU ALA THR SER LEU VAL          
SEQRES   3 B  273  LEU ASP PRO TYR LEU GLY PHE GLN THR HIS LYS MET ASN          
SEQRES   4 B  273  THR SER ALA PHE PRO SER ARG SER SER ARG HIS PHE SER          
SEQRES   5 B  273  LYS SER ASP SER PHE SER HIS ASN ASN PRO VAL ARG PHE          
SEQRES   6 B  273  ARG PRO ILE LYS GLY ARG GLN GLU GLU LEU LYS GLU VAL          
SEQRES   7 B  273  ILE GLU ARG PHE LYS LYS ASP GLU HIS LEU GLU LYS ALA          
SEQRES   8 B  273  PHE LYS CYS LEU THR SER GLY GLU TRP ALA ARG HIS TYR          
SEQRES   9 B  273  PHE LEU ASN LYS ASN LYS MET GLN GLU LYS LEU PHE LYS          
SEQRES  10 B  273  GLU HIS VAL PHE ILE TYR LEU ARG MET PHE ALA THR ASP          
SEQRES  11 B  273  SER GLY PHE GLU ILE LEU PRO CYS ASN ARG TYR SER SER          
SEQRES  12 B  273  GLU GLN ASN GLY ALA LYS ILE VAL ALA THR LYS GLU TRP          
SEQRES  13 B  273  LYS ARG ASN ASP LYS ILE GLU LEU LEU VAL GLY CYS ILE          
SEQRES  14 B  273  ALA GLU LEU SER GLU ILE GLU GLU ASN MET LEU LEU ARG          
SEQRES  15 B  273  HIS GLY GLU ASN ASP PHE SER VAL MET TYR SER THR ARG          
SEQRES  16 B  273  LYS ASN CYS ALA GLN LEU TRP LEU GLY PRO ALA ALA PHE          
SEQRES  17 B  273  ILE ASN HIS ASP CYS ARG PRO ASN CYS LYS PHE VAL SER          
SEQRES  18 B  273  THR GLY ARG ASP THR ALA CYS VAL LYS ALA LEU ARG ASP          
SEQRES  19 B  273  ILE GLU PRO GLY GLU GLU ILE SER CYS TYR TYR GLY ASP          
SEQRES  20 B  273  GLY PHE PHE GLY GLU ASN ASN GLU PHE CYS GLU CYS TYR          
SEQRES  21 B  273  THR CYS GLU ARG ARG GLY THR GLY ALA PHE LYS SER ARG          
HET     ZN  A 401       1                                                       
HET    SAM  A 402      27                                                       
HET    9ZY  A 403      27                                                       
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     ZN  B 401       1                                                       
HET    SAM  B 402      27                                                       
HET    9ZY  B 403      27                                                       
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                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     9ZY 2-CHLORO-5-(4-METHYL-6-OXO-3-PHENYLPYRANO[2,3-                   
HETNAM   2 9ZY  C]PYRAZOL-1(6H)-YL)BENZOIC ACID                                 
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   5  9ZY    2(C20 H13 CL N2 O4)                                          
FORMUL   6  UNX    12(X)                                                        
FORMUL  21  HOH   *31(H2 O)                                                     
HELIX    1 AA1 SER A   73  LEU A   89  1                                  17    
HELIX    2 AA2 LEU A   89  GLY A   94  1                                   6    
HELIX    3 AA3 GLY A  132  GLU A  148  1                                  17    
HELIX    4 AA4 HIS A  149  THR A  158  1                                  10    
HELIX    5 AA5 GLY A  160  PHE A  167  1                                   8    
HELIX    6 AA6 ASN A  171  MET A  188  1                                  18    
HELIX    7 AA7 SER A  235  LEU A  243  1                                   9    
HELIX    8 AA8 GLY A  266  ILE A  271  5                                   6    
HELIX    9 AA9 GLY A  313  GLU A  317  5                                   5    
HELIX   10 AB1 CYS A  321  ARG A  327  1                                   7    
HELIX   11 AB2 SER B   73  LEU B   89  1                                  17    
HELIX   12 AB3 LEU B   89  GLY B   94  1                                   6    
HELIX   13 AB4 GLY B  132  GLU B  148  1                                  17    
HELIX   14 AB5 HIS B  149  THR B  158  1                                  10    
HELIX   15 AB6 ASN B  171  MET B  188  1                                  18    
HELIX   16 AB7 SER B  235  LEU B  243  1                                   9    
HELIX   17 AB8 GLY B  266  ILE B  271  5                                   6    
HELIX   18 AB9 GLY B  313  GLU B  317  5                                   5    
HELIX   19 AC1 CYS B  321  ARG B  327  1                                   7    
HELIX   20 AC2 THR B  329  LYS B  333  5                                   5    
SHEET    1 AA1 2 PHE A 195  CYS A 200  0                                        
SHEET    2 AA1 2 GLY A 209  ALA A 214 -1  O  VAL A 213   N  GLU A 196           
SHEET    1 AA2 5 VAL A 252  SER A 255  0                                        
SHEET    2 AA2 5 CYS A 260  LEU A 265 -1  O  GLN A 262   N  MET A 253           
SHEET    3 AA2 5 LYS A 223  LEU A 234 -1  N  LEU A 234   O  ALA A 261           
SHEET    4 AA2 5 THR A 288  ALA A 293 -1  O  VAL A 291   N  ILE A 224           
SHEET    5 AA2 5 CYS A 279  SER A 283 -1  N  VAL A 282   O  CYS A 290           
SHEET    1 AA3 2 ASN A 272  HIS A 273  0                                        
SHEET    2 AA3 2 SER A 304  CYS A 305  1  O  CYS A 305   N  ASN A 272           
SHEET    1 AA4 2 PHE B 195  CYS B 200  0                                        
SHEET    2 AA4 2 GLY B 209  ALA B 214 -1  O  VAL B 213   N  GLU B 196           
SHEET    1 AA5 5 VAL B 252  SER B 255  0                                        
SHEET    2 AA5 5 CYS B 260  LEU B 265 -1  O  GLN B 262   N  MET B 253           
SHEET    3 AA5 5 LYS B 223  LEU B 234 -1  N  LEU B 234   O  ALA B 261           
SHEET    4 AA5 5 THR B 288  ALA B 293 -1  O  VAL B 291   N  ILE B 224           
SHEET    5 AA5 5 CYS B 279  SER B 283 -1  N  VAL B 282   O  CYS B 290           
SHEET    1 AA6 2 ASN B 272  HIS B 273  0                                        
SHEET    2 AA6 2 SER B 304  CYS B 305  1  O  CYS B 305   N  ASN B 272           
LINK         SG  CYS A 275                ZN    ZN A 401     1555   1555  2.28  
LINK         SG  CYS A 319                ZN    ZN A 401     1555   1555  2.49  
LINK         SG  CYS A 321                ZN    ZN A 401     1555   1555  2.36  
LINK         SG  CYS A 324                ZN    ZN A 401     1555   1555  2.45  
LINK         SG  CYS B 275                ZN    ZN B 401     1555   1555  2.28  
LINK         SG  CYS B 319                ZN    ZN B 401     1555   1555  2.32  
LINK         SG  CYS B 321                ZN    ZN B 401     1555   1555  2.43  
LINK         SG  CYS B 324                ZN    ZN B 401     1555   1555  2.48  
SITE     1 AC1  4 CYS A 275  CYS A 319  CYS A 321  CYS A 324                    
SITE     1 AC2 18 HIS A  98  TYR A 203  SER A 205  GLU A 206                    
SITE     2 AC2 18 GLY A 209  ALA A 210  PHE A 250  ALA A 269                    
SITE     3 AC2 18 PHE A 270  ILE A 271  ASN A 272  HIS A 273                    
SITE     4 AC2 18 TYR A 307  PHE A 312  CYS A 319  GLU A 320                    
SITE     5 AC2 18 CYS A 321  ARG B 257                                          
SITE     1 AC3 13 GLY A 229  VAL A 252  MET A 253  TRP A 264                    
SITE     2 AC3 13 ALA A 268  ALA A 269  PHE A 281  ALA A 289                    
SITE     3 AC3 13 TYR A 307  PHE A 311  HOH A 512  ARG B 244                    
SITE     4 AC3 13 HIS B 245                                                     
SITE     1 AC4  4 CYS B 275  CYS B 319  CYS B 321  CYS B 324                    
SITE     1 AC5 20 ARG A 257  HOH A 510  HIS B  98  TYR B 203                    
SITE     2 AC5 20 SER B 205  GLU B 206  GLY B 209  ALA B 210                    
SITE     3 AC5 20 PHE B 250  ALA B 269  PHE B 270  ILE B 271                    
SITE     4 AC5 20 ASN B 272  HIS B 273  TYR B 307  PHE B 312                    
SITE     5 AC5 20 CYS B 319  GLU B 320  CYS B 321  HOH B 508                    
SITE     1 AC6 12 ARG A 244  HIS A 245  GLY B 229  VAL B 252                    
SITE     2 AC6 12 MET B 253  TRP B 264  ALA B 268  ALA B 269                    
SITE     3 AC6 12 PHE B 281  ALA B 289  TYR B 307  PHE B 311                    
CRYST1   46.324   50.559   74.818 101.26 107.51  89.67 P 1           2          
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      0.021587 -0.000124  0.006929        0.00000                         
SCALE2      0.000000  0.019779  0.004099        0.00000                         
SCALE3      0.000000  0.000000  0.014313        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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