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Database: PDB
Entry: 5W1Y
LinkDB: 5W1Y
Original site: 5W1Y 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       05-JUN-17   5W1Y              
TITLE     SETD8 IN COMPLEX WITH A COVALENT INHIBITOR                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE KMT5A;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: H4-K20-HMTASE KMT5A,HISTONE-LYSINE N-METHYLTRANSFERASE      
COMPND   5 KMT5A,LYSINE N-METHYLTRANSFERASE 5A,LYSINE-SPECIFIC METHYLASE 5A,    
COMPND   6 PR/SET DOMAIN-CONTAINING PROTEIN 07,PR/SET07,SET DOMAIN-CONTAINING   
COMPND   7 PROTEIN 8;                                                           
COMPND   8 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 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: PHIS2                                     
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,             
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.TEMPEL,W.YU,Y.LI,G.BLUM,M.LUO,F.PITTELLA-SILVA,C.BOUNTRA,           
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM  
AUTHOR   3 (SGC)                                                                
REVDAT   2   12-JUL-17 5W1Y    1       AUTHOR REMARK                            
REVDAT   1   21-JUN-17 5W1Y    0                                                
JRNL        AUTH   W.TEMPEL,W.YU,Y.LI,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,     
JRNL        AUTH 2 P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC)               
JRNL        TITL   SETD8 IN COMPLEX WITH A COVALENT INHIBITOR                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 32998                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1373                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2339                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 98                           
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2461                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 208                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.29000                                             
REMARK   3    B33 (A**2) : 0.35000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.126         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.094         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2652 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2408 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3590 ; 1.616 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5598 ; 0.987 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   337 ; 6.312 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   127 ;32.017 ;24.173       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   476 ;12.734 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;14.722 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   384 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3091 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   543 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1294 ; 1.834 ; 1.884       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1295 ; 1.833 ; 1.884       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1620 ; 2.634 ; 2.822       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: COOT WAS USED FOR INTERACTIVE MODEL       
REMARK   3  BUILDING. MODEL GEOMETRY WAS EVALUATED WITH MOLPROBITY. DENSITY     
REMARK   3  FOR RESIDUE 239 (CHAIN A) RESEMBLES A SERYL SIDE CHAIN WITH         
REMARK   3  ALTERNATE CONFORMATIONS. GEOMETRY RESTRAINTS FOR THE COVALENT       
REMARK   3  LIGAND WERE PREPARED WITH GRADE, WHICH USED MOGUL. THE LENGTH OF    
REMARK   3  THE COVALENT LINK WAS RESTRAINED TO 1.75 A, CONSISTENT WITH THE     
REMARK   3  MEAN LENGTH FOUND IN A MOGUL SEARCH. FOLLOWING ANALYSIS OF          
REMARK   3  MERGING STATISTICS, ONLY MEASUREMENTS ON IMAGES 1..100 WERE         
REMARK   3  INCLUDED IN THE MERGING STEP.                                       
REMARK   4                                                                      
REMARK   4 5W1Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228208.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.32                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34422                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4IJ8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FLUORIDE, 20% PEG-3350,     
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 291K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       29.17400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.94750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.89400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.94750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.17400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       19.89400            
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 300 REMARK: THE MACROMOLECULAR ASSEMBLY WAS NOT A FOCUS OF THIS CRYSTAL  
REMARK 300 STRUCTURE                                                            
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: 2210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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   228                                                      
REMARK 465     ALA A   229                                                      
REMARK 465     MET A   230                                                      
REMARK 465     GLY A   231                                                      
REMARK 465     GLY B   228                                                      
REMARK 465     ALA B   229                                                      
REMARK 465     MET B   230                                                      
REMARK 465     GLY B   231                                                      
REMARK 465     SER B   232                                                      
REMARK 465     ARG B   233                                                      
REMARK 465     LYS B   234                                                      
REMARK 465     SER B   235                                                      
REMARK 465     LYS B   236                                                      
REMARK 465     ALA B   237                                                      
REMARK 465     GLU B   238                                                      
REMARK 465     LEU B   239                                                      
REMARK 465     GLN B   240                                                      
REMARK 465     HIS B   393                                                      
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     ARG A 233    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 236    CE   NZ                                             
REMARK 470     LEU A 239    CG   CD1  CD2                                       
REMARK 470     ARG A 244    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 298    CE   NZ                                             
REMARK 470     LYS A 342    NZ                                                  
REMARK 470     LYS A 349    NZ                                                  
REMARK 470     LYS A 382    NZ                                                  
REMARK 470     LYS B 245    CG   CD   CE   NZ                                   
REMARK 470     LYS B 260    NZ                                                  
REMARK 470     ARG B 279    NE   CZ   NH1  NH2                                  
REMARK 470     GLN B 317    CD   OE1  NE2                                       
REMARK 470     LYS B 321    CE   NZ                                             
REMARK 470     ASN B 332    CG   OD1  ND2                                       
REMARK 470     GLN B 347    CD   OE1  NE2                                       
REMARK 470     LYS B 382    NZ                                                  
REMARK 470     LYS B 392    C    O    CB   CG   CD   CE   NZ                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 333   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A 283      -65.53   -105.29                                   
REMARK 500    LEU A 319     -123.84     54.01                                   
REMARK 500    THR A 331      -69.05   -106.76                                   
REMARK 500    THR A 331     -158.68   -123.11                                   
REMARK 500    SER A 343       52.24   -118.99                                   
REMARK 500    SER A 343       52.41   -118.79                                   
REMARK 500    SER B 320      -23.35     88.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     9SV A  401                                                       
REMARK 610     9SV B  401                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9SV A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 9SV B 401 and CYS B    
REMARK 800  311                                                                 
DBREF  5W1Y A  232   393  UNP    Q9NQR1   KMT5A_HUMAN    232    393             
DBREF  5W1Y B  232   393  UNP    Q9NQR1   KMT5A_HUMAN    232    393             
SEQADV 5W1Y GLY A  228  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5W1Y ALA A  229  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5W1Y MET A  230  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5W1Y GLY A  231  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5W1Y SER A  343  UNP  Q9NQR1    CYS   343 ENGINEERED MUTATION            
SEQADV 5W1Y GLY B  228  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5W1Y ALA B  229  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5W1Y MET B  230  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5W1Y GLY B  231  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 5W1Y SER B  343  UNP  Q9NQR1    CYS   343 ENGINEERED MUTATION            
SEQRES   1 A  166  GLY ALA MET GLY SER ARG LYS SER LYS ALA GLU LEU GLN          
SEQRES   2 A  166  SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU SER          
SEQRES   3 A  166  GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP GLY          
SEQRES   4 A  166  LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER ARG          
SEQRES   5 A  166  GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE GLU          
SEQRES   6 A  166  ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA GLN          
SEQRES   7 A  166  ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN TYR          
SEQRES   8 A  166  LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU THR          
SEQRES   9 A  166  ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS SER GLY          
SEQRES  10 A  166  ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL PRO          
SEQRES  11 A  166  HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA GLY          
SEQRES  12 A  166  GLU GLU LEU LEU TYR ASP TYR GLY ASP ARG SER LYS ALA          
SEQRES  13 A  166  SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                      
SEQRES   1 B  166  GLY ALA MET GLY SER ARG LYS SER LYS ALA GLU LEU GLN          
SEQRES   2 B  166  SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU SER          
SEQRES   3 B  166  GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP GLY          
SEQRES   4 B  166  LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER ARG          
SEQRES   5 B  166  GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE GLU          
SEQRES   6 B  166  ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA GLN          
SEQRES   7 B  166  ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN TYR          
SEQRES   8 B  166  LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU THR          
SEQRES   9 B  166  ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS SER GLY          
SEQRES  10 B  166  ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL PRO          
SEQRES  11 B  166  HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA GLY          
SEQRES  12 B  166  GLU GLU LEU LEU TYR ASP TYR GLY ASP ARG SER LYS ALA          
SEQRES  13 B  166  SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                      
HET    9SV  A 401      19                                                       
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    UNX  A 413       1                                                       
HET    UNX  A 414       1                                                       
HET    UNX  A 415       1                                                       
HET    UNX  A 416       1                                                       
HET    9SV  B 401      19                                                       
HET    UNX  B 402       1                                                       
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                                                       
HET    UNX  B 413       1                                                       
HET    UNX  B 414       1                                                       
HET    UNX  B 415       1                                                       
HET    UNX  B 416       1                                                       
HET    UNX  B 417       1                                                       
HET    UNX  B 418       1                                                       
HET    UNX  B 419       1                                                       
HET    UNX  B 420       1                                                       
HET    UNX  B 421       1                                                       
HET    UNX  B 422       1                                                       
HETNAM     9SV 2-(4-METHYLPIPERAZIN-1-YL)-3-(PHENYLSULFANYL)                    
HETNAM   2 9SV  NAPHTHALENE-1,4-DIONE                                           
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     9SV BOUND FORM                                                       
FORMUL   3  9SV    2(C21 H20 N2 O2 S)                                           
FORMUL   4  UNX    36(X)                                                        
FORMUL  41  HOH   *208(H2 O)                                                    
HELIX    1 AA1 SER A  235  GLY A  254  1                                  20    
HELIX    2 AA2 ILE A  293  ALA A  304  1                                  12    
HELIX    3 AA3 ARG A  333  ILE A  338  5                                   6    
HELIX    4 AA4 TYR A  377  HIS A  388  1                                  12    
HELIX    5 AA5 PRO A  389  HIS A  393  5                                   5    
HELIX    6 AA6 GLU B  243  GLY B  254  1                                  12    
HELIX    7 AA7 ILE B  293  GLN B  305  1                                  13    
HELIX    8 AA8 LEU B  334  ILE B  338  5                                   5    
HELIX    9 AA9 TYR B  377  HIS B  388  1                                  12    
HELIX   10 AB1 PRO B  389  LYS B  392  5                                   4    
SHEET    1 AA1 2 MET A 259  ILE A 264  0                                        
SHEET    2 AA1 2 GLY A 268  ALA A 273 -1  O  GLY A 268   N  ILE A 264           
SHEET    1 AA2 3 PHE A 282  TYR A 286  0                                        
SHEET    2 AA2 3 VAL A 356  ALA A 363 -1  O  LEU A 359   N  TYR A 286           
SHEET    3 AA2 3 CYS A 346  ILE A 353 -1  N  HIS A 351   O  HIS A 358           
SHEET    1 AA3 3 ASP A 289  GLU A 292  0                                        
SHEET    2 AA3 3 LYS A 321  ASP A 326 -1  O  CYS A 324   N  ILE A 291           
SHEET    3 AA3 3 MET A 313  TYR A 318 -1  N  PHE A 316   O  TYR A 323           
SHEET    1 AA4 2 ASN A 339  HIS A 340  0                                        
SHEET    2 AA4 2 LEU A 374  TYR A 375  1  O  TYR A 375   N  ASN A 339           
SHEET    1 AA5 2 MET B 259  ILE B 264  0                                        
SHEET    2 AA5 2 GLY B 268  ALA B 273 -1  O  GLY B 268   N  ILE B 264           
SHEET    1 AA6 3 PHE B 282  GLU B 285  0                                        
SHEET    2 AA6 3 VAL B 356  ALA B 363 -1  O  LEU B 361   N  VAL B 284           
SHEET    3 AA6 3 CYS B 346  ILE B 353 -1  N  HIS B 351   O  HIS B 358           
SHEET    1 AA7 3 ASP B 289  GLU B 292  0                                        
SHEET    2 AA7 3 LYS B 321  ASP B 326 -1  O  CYS B 324   N  ILE B 291           
SHEET    3 AA7 3 MET B 313  TYR B 318 -1  N  PHE B 316   O  TYR B 323           
SHEET    1 AA8 2 ASN B 339  HIS B 340  0                                        
SHEET    2 AA8 2 LEU B 374  TYR B 375  1  O  TYR B 375   N  ASN B 339           
LINK         SG  CYS A 311                 C6  9SV A 401     1555   1555  1.75  
LINK         SG  CYS B 311                 C6  9SV B 401     1555   1555  1.75  
SITE     1 AC1  7 TYR A 303  ASP A 306  THR A 309  GLY A 310                    
SITE     2 AC1  7 CYS A 311  HOH A 501  9SV B 401                               
SITE     1 AC2 12 CYS A 311  9SV A 401  TYR B 303  ASP B 306                    
SITE     2 AC2 12 THR B 309  GLY B 310  TYR B 312  MET B 313                    
SITE     3 AC2 12 ARG B 380  HOH B 504  HOH B 531  HOH B 538                    
CRYST1   58.348   39.788  131.895  90.00  90.00  90.00 P 21 21 21    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      0.017139  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.025133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007582        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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