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Database: PDB
Entry: 4YND
LinkDB: 4YND
Original site: 4YND 
HEADER    TRANFERASE/TRANSFERASE INHIBITOR        09-MAR-15   4YND              
TITLE     THE DISCOVERY OF A-893, A NEW CELL-ACTIVE BENZOXAZINONE INHIBITOR OF  
TITLE    2 LYSINE METHYLTRANSFERASE SMYD2                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE SMYD2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HSKM-B,HISTONE METHYLTRANSFERASE SMYD2,LYSINE N-            
COMPND   5 METHYLTRANSFERASE 3C,SET AND MYND DOMAIN-CONTAINING PROTEIN 2;       
COMPND   6 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   7 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: SMYD2, KMT3C;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    EPIGENETICS, SMYD2, H3K36, P53, METHYLTRANSFERASE, LYSINE,            
KEYWDS   2 TRANFERASE-TRANSFERASE INHIBITOR COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.F.SWEIS,Z.WANG,M.ALGIRE,C.H.ARROWSMITH,P.J.BROWN,G.C.CHIANG,J.GUO,  
AUTHOR   2 C.G.JAKOB,S.KENNEDY,F.LI,N.B.SONI,M.VEDADI,W.N.PAPPANO               
REVDAT   2   08-JUL-15 4YND    1       JRNL                                     
REVDAT   1   20-MAY-15 4YND    0                                                
JRNL        AUTH   R.F.SWEIS,Z.WANG,M.ALGIRE,C.H.ARROWSMITH,P.J.BROWN,          
JRNL        AUTH 2 G.G.CHIANG,J.GUO,C.G.JAKOB,S.KENNEDY,F.LI,D.MAAG,B.SHAW,     
JRNL        AUTH 3 N.B.SONI,M.VEDADI,W.N.PAPPANO                                
JRNL        TITL   DISCOVERY OF A-893, A NEW CELL-ACTIVE BENZOXAZINONE          
JRNL        TITL 2 INHIBITOR OF LYSINE METHYLTRANSFERASE SMYD2.                 
JRNL        REF    ACS MED.CHEM.LETT.            V.   6   695 2015              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   26101576                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.5B00124                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.6                                        
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) : 2.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 11691                          
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)  : 0.200                          
REMARK   3   R VALUE            (WORKING SET)  : 0.198                          
REMARK   3   FREE R VALUE                      : 0.253                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.720                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 552                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 6                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.79                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.06                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.89                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2739                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2186                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2599                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2168                   
REMARK   3   BIN FREE R VALUE                        : 0.2512                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.11                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 140                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3433                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 131                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.64                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.73070                                             
REMARK   3    B22 (A**2) : 5.33120                                              
REMARK   3    B33 (A**2) : -1.60050                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.324               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.397               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.906                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.832                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3582   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4831   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1268   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 90     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 529    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3582   ; 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   : 443    ; 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   : 4039   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.007                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.93                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.96                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.50                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4YND COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000207750.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11772                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 118.938                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.15500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
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: 3S7B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN LIGAND COMPLEX WAS MADE      
REMARK 280  USING A SLIGHT MOLAR EXCESS OF S ADENOMETHIONINE (SAM) AND A-893    
REMARK 280  FROM CONCENTRATED DMSO STOCKS. CO-CRYSTALS WERE GROWN USING THE     
REMARK 280  HANGING DROP FORMAT WITH A 1:1 V/V DROP COMPOSITION OF THE          
REMARK 280  PROTEIN COMPLEX: WELL SOLUTION (20% W/V PEG 10,000, 0.1 HEPES PH    
REMARK 280  7.5) AT 17C., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K       
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       26.39800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.46500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.65050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.46500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.39800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.65050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 20640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 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     MET A   -27                                                      
REMARK 465     SER A   -26                                                      
REMARK 465     TYR A   -25                                                      
REMARK 465     TYR A   -24                                                      
REMARK 465     HIS A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     ASP A   -17                                                      
REMARK 465     TYR A   -16                                                      
REMARK 465     ASP A   -15                                                      
REMARK 465     ILE A   -14                                                      
REMARK 465     PRO A   -13                                                      
REMARK 465     THR A   -12                                                      
REMARK 465     THR A   -11                                                      
REMARK 465     GLU A   -10                                                      
REMARK 465     ASN A    -9                                                      
REMARK 465     LEU A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     PHE A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     PRO A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     GLU A   431                                                      
REMARK 465     SER A   432                                                      
REMARK 465     HIS A   433                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  98    CG   CD   OE1  OE2                                  
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    HIS A 119       77.86   -118.27                                   
REMARK 500    CYS A 210       74.14   -118.91                                   
REMARK 500    VAL A 277       58.83   -106.54                                   
REMARK 500    ASP A 284       78.90   -119.33                                   
REMARK 500    TYR A 311      -36.21   -134.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 731        DISTANCE =  6.91 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  55   SG  103.5                                              
REMARK 620 3 CYS A  74   SG   99.3  93.0                                        
REMARK 620 4 CYS A  78   SG  112.6 121.1 123.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  65   SG                                                     
REMARK 620 2 CYS A  68   SG  112.1                                              
REMARK 620 3 HIS A  86   NE2 103.4 111.6                                        
REMARK 620 4 CYS A  90   SG  107.5 120.7  99.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 209   SG                                                     
REMARK 620 2 CYS A 262   SG  115.5                                              
REMARK 620 3 CYS A 264   SG  110.6  97.1                                        
REMARK 620 4 CYS A 267   SG  102.4 112.7 119.1                                  
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4GQ A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 505                 
DBREF  4YND A    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
SEQADV 4YND MET A  -27  UNP  Q9NRG4              INITIATING METHIONINE          
SEQADV 4YND SER A  -26  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND TYR A  -25  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND TYR A  -24  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND HIS A  -23  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND HIS A  -22  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND HIS A  -21  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND HIS A  -20  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND HIS A  -19  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND HIS A  -18  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND ASP A  -17  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND TYR A  -16  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND ASP A  -15  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND ILE A  -14  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND PRO A  -13  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND THR A  -12  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND THR A  -11  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND GLU A  -10  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND ASN A   -9  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND LEU A   -8  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND TYR A   -7  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND PHE A   -6  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND GLN A   -5  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND GLY A   -4  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND ALA A   -3  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND MET A   -2  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND ASP A   -1  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 4YND PRO A    0  UNP  Q9NRG4              EXPRESSION TAG                 
SEQRES   1 A  461  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 A  461  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET          
SEQRES   3 A  461  ASP PRO MET ARG ALA GLU GLY LEU GLY GLY LEU GLU ARG          
SEQRES   4 A  461  PHE CYS SER PRO GLY LYS GLY ARG GLY LEU ARG ALA LEU          
SEQRES   5 A  461  GLN PRO PHE GLN VAL GLY ASP LEU LEU PHE SER CYS PRO          
SEQRES   6 A  461  ALA TYR ALA TYR VAL LEU THR VAL ASN GLU ARG GLY ASN          
SEQRES   7 A  461  HIS CYS GLU TYR CYS PHE THR ARG LYS GLU GLY LEU SER          
SEQRES   8 A  461  LYS CYS GLY ARG CYS LYS GLN ALA PHE TYR CYS ASN VAL          
SEQRES   9 A  461  GLU CYS GLN LYS GLU ASP TRP PRO MET HIS LYS LEU GLU          
SEQRES  10 A  461  CYS SER PRO MET VAL VAL PHE GLY GLU ASN TRP ASN PRO          
SEQRES  11 A  461  SER GLU THR VAL ARG LEU THR ALA ARG ILE LEU ALA LYS          
SEQRES  12 A  461  GLN LYS ILE HIS PRO GLU ARG THR PRO SER GLU LYS LEU          
SEQRES  13 A  461  LEU ALA VAL LYS GLU PHE GLU SER HIS LEU ASP LYS LEU          
SEQRES  14 A  461  ASP ASN GLU LYS LYS ASP LEU ILE GLN SER ASP ILE ALA          
SEQRES  15 A  461  ALA LEU HIS HIS PHE TYR SER LYS HIS LEU GLY PHE PRO          
SEQRES  16 A  461  ASP ASN ASP SER LEU VAL VAL LEU PHE ALA GLN VAL ASN          
SEQRES  17 A  461  CYS ASN GLY PHE THR ILE GLU ASP GLU GLU LEU SER HIS          
SEQRES  18 A  461  LEU GLY SER ALA ILE PHE PRO ASP VAL ALA LEU MET ASN          
SEQRES  19 A  461  HIS SER CYS CYS PRO ASN VAL ILE VAL THR TYR LYS GLY          
SEQRES  20 A  461  THR LEU ALA GLU VAL ARG ALA VAL GLN GLU ILE LYS PRO          
SEQRES  21 A  461  GLY GLU GLU VAL PHE THR SER TYR ILE ASP LEU LEU TYR          
SEQRES  22 A  461  PRO THR GLU ASP ARG ASN ASP ARG LEU ARG ASP SER TYR          
SEQRES  23 A  461  PHE PHE THR CYS GLU CYS GLN GLU CYS THR THR LYS ASP          
SEQRES  24 A  461  LYS ASP LYS ALA LYS VAL GLU ILE ARG LYS LEU SER ASP          
SEQRES  25 A  461  PRO PRO LYS ALA GLU ALA ILE ARG ASP MET VAL ARG TYR          
SEQRES  26 A  461  ALA ARG ASN VAL ILE GLU GLU PHE ARG ARG ALA LYS HIS          
SEQRES  27 A  461  TYR LYS SER PRO SER GLU LEU LEU GLU ILE CYS GLU LEU          
SEQRES  28 A  461  SER GLN GLU LYS MET SER SER VAL PHE GLU ASP SER ASN          
SEQRES  29 A  461  VAL TYR MET LEU HIS MET MET TYR GLN ALA MET GLY VAL          
SEQRES  30 A  461  CYS LEU TYR MET GLN ASP TRP GLU GLY ALA LEU GLN TYR          
SEQRES  31 A  461  GLY GLN LYS ILE ILE LYS PRO TYR SER LYS HIS TYR PRO          
SEQRES  32 A  461  LEU TYR SER LEU ASN VAL ALA SER MET TRP LEU LYS LEU          
SEQRES  33 A  461  GLY ARG LEU TYR MET GLY LEU GLU HIS LYS ALA ALA GLY          
SEQRES  34 A  461  GLU LYS ALA LEU LYS LYS ALA ILE ALA ILE MET GLU VAL          
SEQRES  35 A  461  ALA HIS GLY LYS ASP HIS PRO TYR ILE SER GLU ILE LYS          
SEQRES  36 A  461  GLN GLU ILE GLU SER HIS                                      
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET    4GQ  A 504      39                                                       
HET    SAM  A 505      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     4GQ N-CYCLOHEXYL-N~3~-[2-(3,4-DICHLOROPHENYL)ETHYL]-N-(2-            
HETNAM   2 4GQ  {[(2R)-2-HYDROXY-2-(3-OXO-3,4-DIHYDRO-2H-1,4-                   
HETNAM   3 4GQ  BENZOXAZIN-8-YL)ETHYL]AMINO}ETHYL)-BETA-ALANINAMIDE             
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  4GQ    C29 H38 CL2 N4 O4                                            
FORMUL   6  SAM    C15 H22 N6 O5 S                                              
FORMUL   7  HOH   *131(H2 O)                                                    
HELIX    1 AA1 VAL A   45  ARG A   48  5                                   4    
HELIX    2 AA2 ASN A   75  GLY A   97  1                                  23    
HELIX    3 AA3 GLU A   98  TRP A  100  5                                   3    
HELIX    4 AA4 SER A  103  HIS A  119  1                                  17    
HELIX    5 AA5 ALA A  130  PHE A  134  5                                   5    
HELIX    6 AA6 ASP A  142  SER A  161  1                                  20    
HELIX    7 AA7 ASP A  168  GLY A  183  1                                  16    
HELIX    8 AA8 ASP A  201  MET A  205  5                                   5    
HELIX    9 AA9 PRO A  246  TYR A  258  1                                  13    
HELIX   10 AB1 CYS A  264  LYS A  270  1                                   7    
HELIX   11 AB2 LYS A  272  VAL A  277  1                                   6    
HELIX   12 AB3 LYS A  287  LYS A  309  1                                  23    
HELIX   13 AB4 SER A  313  SER A  329  1                                  17    
HELIX   14 AB5 ASN A  336  MET A  353  1                                  18    
HELIX   15 AB6 ASP A  355  TYR A  374  1                                  20    
HELIX   16 AB7 SER A  378  LEU A  395  1                                  18    
HELIX   17 AB8 HIS A  397  HIS A  416  1                                  20    
HELIX   18 AB9 HIS A  420  ILE A  430  1                                  11    
SHEET    1 AA1 2 LEU A   9  SER A  14  0                                        
SHEET    2 AA1 2 GLY A  18  ALA A  23 -1  O  GLY A  20   N  PHE A  12           
SHEET    1 AA2 3 LEU A  32  PRO A  37  0                                        
SHEET    2 AA2 3 LEU A 221  ALA A 226 -1  O  ALA A 222   N  CYS A  36           
SHEET    3 AA2 3 VAL A 213  LYS A 218 -1  N  THR A 216   O  GLU A 223           
SHEET    1 AA3 3 ALA A  40  LEU A  43  0                                        
SHEET    2 AA3 3 HIS A 193  ILE A 198 -1  O  SER A 196   N  VAL A  42           
SHEET    3 AA3 3 PHE A 184  GLU A 187 -1  N  PHE A 184   O  ALA A 197           
SHEET    1 AA4 2 SER A  63  LYS A  64  0                                        
SHEET    2 AA4 2 PHE A  72  TYR A  73 -1  O  TYR A  73   N  SER A  63           
SHEET    1 AA5 2 ASN A 206  HIS A 207  0                                        
SHEET    2 AA5 2 PHE A 237  THR A 238  1  O  THR A 238   N  ASN A 206           
LINK         SG  CYS A  52                ZN    ZN A 501     1555   1555  2.42  
LINK         SG  CYS A  55                ZN    ZN A 501     1555   1555  2.33  
LINK         SG  CYS A  65                ZN    ZN A 503     1555   1555  2.36  
LINK         SG  CYS A  68                ZN    ZN A 503     1555   1555  2.29  
LINK         SG  CYS A  74                ZN    ZN A 501     1555   1555  2.63  
LINK         SG  CYS A  78                ZN    ZN A 501     1555   1555  2.33  
LINK         NE2 HIS A  86                ZN    ZN A 503     1555   1555  2.21  
LINK         SG  CYS A  90                ZN    ZN A 503     1555   1555  2.33  
LINK         SG  CYS A 209                ZN    ZN A 502     1555   1555  2.35  
LINK         SG  CYS A 262                ZN    ZN A 502     1555   1555  2.38  
LINK         SG  CYS A 264                ZN    ZN A 502     1555   1555  2.51  
LINK         SG  CYS A 267                ZN    ZN A 502     1555   1555  2.35  
SITE     1 AC1  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC2  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
SITE     1 AC3  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC4 16 THR A 105  LEU A 141  LYS A 145  ILE A 149                    
SITE     2 AC4 16 VAL A 179  ASN A 180  ASN A 182  GLY A 183                    
SITE     3 AC4 16 PHE A 184  ALA A 203  SER A 239  TYR A 240                    
SITE     4 AC4 16 SER A 257  TYR A 258  SAM A 505  HOH A 614                    
SITE     1 AC5 14 GLY A  16  LYS A  17  ARG A  19  HIS A 137                    
SITE     2 AC5 14 CYS A 181  ASN A 182  ALA A 203  LEU A 204                    
SITE     3 AC5 14 ASN A 206  HIS A 207  TYR A 240  TYR A 258                    
SITE     4 AC5 14 PHE A 260  4GQ A 504                                          
CRYST1   52.796   71.301  118.930  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018941  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014025  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008408        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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