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Database: PDB
Entry: 5CCL
LinkDB: 5CCL
Original site: 5CCL 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       02-JUL-15   5CCL              
TITLE     CRYSTAL STRUCTURE OF SMYD3 WITH SAM AND OXINDOLE COMPOUND             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SMYD3;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SET AND MYND DOMAIN-CONTAINING PROTEIN 3,ZINC FINGER MYND   
COMPND   5 DOMAIN-CONTAINING PROTEIN 1;                                         
COMPND   6 EC: 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: SMYD3, ZMYND1, ZNFN3A1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN-INHIBITOR COMPLEX, METHYLTRANSFERASE, EPIGENETICS, DRUG       
KEYWDS   2 DISCOVERY, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.BORIACK-SJODIN                                                    
REVDAT   2   30-MAR-16 5CCL    1       JRNL                                     
REVDAT   1   09-SEP-15 5CCL    0                                                
JRNL        AUTH   L.H.MITCHELL,P.A.BORIACK-SJODIN,S.SMITH,M.THOMENIUS,N.RIOUX, 
JRNL        AUTH 2 M.MUNCHHOF,J.E.MILLS,C.KLAUS,J.TOTMAN,T.V.RIERA,A.RAIMONDI,  
JRNL        AUTH 3 S.L.JACQUES,K.WEST,M.FOLEY,N.J.WATERS,K.W.KUNTZ,T.J.WIGLE,   
JRNL        AUTH 4 M.P.SCOTT,R.A.COPELAND,J.J.SMITH,R.CHESWORTH                 
JRNL        TITL   NOVEL OXINDOLE SULFONAMIDES AND SULFAMIDES: EPZ031686, THE   
JRNL        TITL 2 FIRST ORALLY BIOAVAILABLE SMALL MOLECULE SMYD3 INHIBITOR.    
JRNL        REF    ACS MED.CHEM.LETT.            V.   7   134 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   26985287                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.5B00272                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 59053                          
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) : 0.116                           
REMARK   3   R VALUE            (WORKING SET) : 0.113                           
REMARK   3   FREE R VALUE                     : 0.164                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3081                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4464                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 215                          
REMARK   3   BIN FREE R VALUE                    : 0.1830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3400                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 449                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.61000                                              
REMARK   3    B22 (A**2) : -0.56000                                             
REMARK   3    B33 (A**2) : -0.05000                                             
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): 0.078         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.037         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.113         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.979                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3816 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3680 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5146 ; 1.732 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8506 ; 0.913 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   468 ; 6.110 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   173 ;32.614 ;23.873       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   719 ;14.196 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;19.865 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   555 ; 0.124 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4280 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   859 ; 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):  1839 ; 3.367 ; 1.950       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1839 ; 3.367 ; 1.950       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2318 ; 3.787 ; 2.925       
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):  7496 ; 3.323 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    90 ;23.573 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  7760 ;11.646 ; 5.000       
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 : MASK                                                 
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5CCL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211372.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97907                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62186                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22600                            
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.10 M MAGNESIUM FORMATE, 0.1M TRIS      
REMARK 280  8.0, 14% W/V PEG 3350. CRYSTALS OF SMYD3-SAM WERE PRODUCED AND      
REMARK 280  COMPOUND WAS SOAKED INTO THE PRE-FORMED CRYSTALS, PH 8.0, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
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       29.29700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.98300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.61600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.98300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.29700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.61600            
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 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     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     SER A   428                                                      
REMARK 465     PHE A   429                                                      
REMARK 465     SEC A   430                                                      
REMARK 465     LEU A   431                                                      
REMARK 465     LEU A   432                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   937     O    HOH A   940              1.85            
REMARK 500   NZ   LYS A   140     O    HOH A   601              1.93            
REMARK 500   O    HOH A   846     O    HOH A   939              1.96            
REMARK 500   NH1  ARG A    66     O    HOH A   602              1.96            
REMARK 500   OD1  ASP A   398     O    HOH A   603              2.05            
REMARK 500   OG1  THR A   137     OD1  ASP A   139              2.14            
REMARK 500   O    HOH A   630     O    HOH A   789              2.16            
REMARK 500   OE2  GLU A   247     O    HOH A   604              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE2  GLN A    64     O    HOH A   702     2554     2.14            
REMARK 500   NH2  ARG A    96     O    HOH A   892     4555     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 247   CD    GLU A 247   OE2     0.074                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A  14   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP A  50   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 107   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP A 241   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG A 394   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 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    ASN A  13       15.49   -148.18                                   
REMARK 500    VAL A  67      -53.17   -123.58                                   
REMARK 500    SER A  92      -86.53    -19.73                                   
REMARK 500    LYS A  94      154.99    -47.31                                   
REMARK 500    PRO A  95       65.38    -68.36                                   
REMARK 500    LYS A 271       -6.52     79.32                                   
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 A1049        DISTANCE =  6.76 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  49   SG                                                     
REMARK 620 2 CYS A  52   SG  107.4                                              
REMARK 620 3 CYS A  71   SG  113.3 110.7                                        
REMARK 620 4 CYS A  75   SG  107.7 114.0 103.9                                  
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  62   SG                                                     
REMARK 620 2 CYS A  65   SG  109.0                                              
REMARK 620 3 HIS A  83   NE2 112.7 104.9                                        
REMARK 620 4 CYS A  87   SG  111.5 110.5 108.1                                  
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  62   SG                                                     
REMARK 620 2 CYS A  65   SG  104.6                                              
REMARK 620 3 HIS A  83   NE2 120.7  78.1                                        
REMARK 620 4 CYS A  87   SG  114.7 104.8 121.7                                  
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 208   SG                                                     
REMARK 620 2 CYS A 261   SG  113.4                                              
REMARK 620 3 CYS A 263   SG  106.5 108.3                                        
REMARK 620 4 CYS A 266   SG   98.8 115.5 113.8                                  
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 SAM A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4ZW A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4ZW A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5CCM   RELATED DB: PDB                                   
DBREF  5CCL A    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
SEQADV 5CCL ASN A   13  UNP  Q9H7B4    LYS    13 CONFLICT                       
SEQADV 5CCL PHE A  429  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5CCL SEC A  430  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5CCL LEU A  431  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5CCL LEU A  432  UNP  Q9H7B4              EXPRESSION TAG                 
SEQRES   1 A  432  MET GLU PRO LEU LYS VAL GLU LYS PHE ALA THR ALA ASN          
SEQRES   2 A  432  ARG GLY ASN GLY LEU ARG ALA VAL THR PRO LEU ARG PRO          
SEQRES   3 A  432  GLY GLU LEU LEU PHE ARG SER ASP PRO LEU ALA TYR THR          
SEQRES   4 A  432  VAL CYS LYS GLY SER ARG GLY VAL VAL CYS ASP ARG CYS          
SEQRES   5 A  432  LEU LEU GLY LYS GLU LYS LEU MET ARG CYS SER GLN CYS          
SEQRES   6 A  432  ARG VAL ALA LYS TYR CYS SER ALA LYS CYS GLN LYS LYS          
SEQRES   7 A  432  ALA TRP PRO ASP HIS LYS ARG GLU CYS LYS CYS LEU LYS          
SEQRES   8 A  432  SER CYS LYS PRO ARG TYR PRO PRO ASP SER VAL ARG LEU          
SEQRES   9 A  432  LEU GLY ARG VAL VAL PHE LYS LEU MET ASP GLY ALA PRO          
SEQRES  10 A  432  SER GLU SER GLU LYS LEU TYR SER PHE TYR ASP LEU GLU          
SEQRES  11 A  432  SER ASN ILE ASN LYS LEU THR GLU ASP LYS LYS GLU GLY          
SEQRES  12 A  432  LEU ARG GLN LEU VAL MET THR PHE GLN HIS PHE MET ARG          
SEQRES  13 A  432  GLU GLU ILE GLN ASP ALA SER GLN LEU PRO PRO ALA PHE          
SEQRES  14 A  432  ASP LEU PHE GLU ALA PHE ALA LYS VAL ILE CYS ASN SER          
SEQRES  15 A  432  PHE THR ILE CYS ASN ALA GLU MET GLN GLU VAL GLY VAL          
SEQRES  16 A  432  GLY LEU TYR PRO SER ILE SER LEU LEU ASN HIS SER CYS          
SEQRES  17 A  432  ASP PRO ASN CYS SER ILE VAL PHE ASN GLY PRO HIS LEU          
SEQRES  18 A  432  LEU LEU ARG ALA VAL ARG ASP ILE GLU VAL GLY GLU GLU          
SEQRES  19 A  432  LEU THR ILE CYS TYR LEU ASP MET LEU MET THR SER GLU          
SEQRES  20 A  432  GLU ARG ARG LYS GLN LEU ARG ASP GLN TYR CYS PHE GLU          
SEQRES  21 A  432  CYS ASP CYS PHE ARG CYS GLN THR GLN ASP LYS ASP ALA          
SEQRES  22 A  432  ASP MET LEU THR GLY ASP GLU GLN VAL TRP LYS GLU VAL          
SEQRES  23 A  432  GLN GLU SER LEU LYS LYS ILE GLU GLU LEU LYS ALA HIS          
SEQRES  24 A  432  TRP LYS TRP GLU GLN VAL LEU ALA MET CYS GLN ALA ILE          
SEQRES  25 A  432  ILE SER SER ASN SER GLU ARG LEU PRO ASP ILE ASN ILE          
SEQRES  26 A  432  TYR GLN LEU LYS VAL LEU ASP CYS ALA MET ASP ALA CYS          
SEQRES  27 A  432  ILE ASN LEU GLY LEU LEU GLU GLU ALA LEU PHE TYR GLY          
SEQRES  28 A  432  THR ARG THR MET GLU PRO TYR ARG ILE PHE PHE PRO GLY          
SEQRES  29 A  432  SER HIS PRO VAL ARG GLY VAL GLN VAL MET LYS VAL GLY          
SEQRES  30 A  432  LYS LEU GLN LEU HIS GLN GLY MET PHE PRO GLN ALA MET          
SEQRES  31 A  432  LYS ASN LEU ARG LEU ALA PHE ASP ILE MET ARG VAL THR          
SEQRES  32 A  432  HIS GLY ARG GLU HIS SER LEU ILE GLU ASP LEU ILE LEU          
SEQRES  33 A  432  LEU LEU GLU GLU CYS ASP ALA ASN ILE ARG ALA SER PHE          
SEQRES  34 A  432  SEC LEU LEU                                                  
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       2                                                       
HET    SAM  A 504      27                                                       
HET    4ZW  A 505      19                                                       
HET    4ZW  A 506      19                                                       
HET    EDO  A 507       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     4ZW 2-OXIDANYLIDENE-N-PIPERIDIN-4-YL-1,3-DIHYDROINDOLE-5-            
HETNAM   2 4ZW  CARBOXAMIDE                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  SAM    C15 H22 N6 O5 S                                              
FORMUL   6  4ZW    2(C14 H17 N3 O2)                                             
FORMUL   8  EDO    C2 H6 O2                                                     
FORMUL   9  HOH   *449(H2 O)                                                    
HELIX    1 AA1 LYS A   42  ARG A   45  5                                   4    
HELIX    2 AA2 SER A   72  LYS A   84  1                                  13    
HELIX    3 AA3 GLU A   86  LYS A   94  1                                   9    
HELIX    4 AA4 PRO A   99  GLY A  115  1                                  17    
HELIX    5 AA5 SER A  118  LYS A  122  5                                   5    
HELIX    6 AA6 SER A  125  LEU A  129  5                                   5    
HELIX    7 AA7 ASN A  132  LEU A  136  5                                   5    
HELIX    8 AA8 THR A  137  MET A  155  1                                  19    
HELIX    9 AA9 ASP A  161  LEU A  165  5                                   5    
HELIX   10 AB1 ASP A  170  SER A  182  1                                  13    
HELIX   11 AB2 SER A  200  LEU A  204  5                                   5    
HELIX   12 AB3 THR A  245  CYS A  258  1                                  14    
HELIX   13 AB4 CYS A  263  GLN A  269  1                                   7    
HELIX   14 AB5 LYS A  271  LEU A  276  1                                   6    
HELIX   15 AB6 ASP A  279  HIS A  299  1                                  21    
HELIX   16 AB7 LYS A  301  SER A  314  1                                  14    
HELIX   17 AB8 ASN A  324  LEU A  341  1                                  18    
HELIX   18 AB9 LEU A  343  PHE A  362  1                                  20    
HELIX   19 AC1 HIS A  366  GLN A  383  1                                  18    
HELIX   20 AC2 MET A  385  HIS A  404  1                                  20    
HELIX   21 AC3 HIS A  408  ARG A  426  1                                  19    
SHEET    1 AA1 2 VAL A   6  ALA A  10  0                                        
SHEET    2 AA1 2 ASN A  16  ALA A  20 -1  O  GLY A  17   N  PHE A   9           
SHEET    1 AA2 3 LEU A  29  SER A  33  0                                        
SHEET    2 AA2 3 HIS A 220  ALA A 225 -1  O  LEU A 221   N  SER A  33           
SHEET    3 AA2 3 CYS A 212  ASN A 217 -1  N  ASN A 217   O  HIS A 220           
SHEET    1 AA3 3 ALA A  37  VAL A  40  0                                        
SHEET    2 AA3 3 GLU A 192  LEU A 197 -1  O  LEU A 197   N  ALA A  37           
SHEET    3 AA3 3 PHE A 183  CYS A 186 -1  N  PHE A 183   O  GLY A 196           
SHEET    1 AA4 2 MET A  60  ARG A  61  0                                        
SHEET    2 AA4 2 LYS A  69  TYR A  70 -1  O  TYR A  70   N  MET A  60           
SHEET    1 AA5 2 ASN A 205  HIS A 206  0                                        
SHEET    2 AA5 2 THR A 236  ILE A 237  1  O  ILE A 237   N  ASN A 205           
LINK         SG  CYS A  49                ZN    ZN A 501     1555   1555  2.34  
LINK         SG  CYS A  52                ZN    ZN A 501     1555   1555  2.31  
LINK         SG ACYS A  62                ZN  A ZN A 503     1555   1555  2.30  
LINK         SG BCYS A  62                ZN  B ZN A 503     1555   1555  2.29  
LINK         SG ACYS A  65                ZN  A ZN A 503     1555   1555  2.36  
LINK         SG BCYS A  65                ZN  B ZN A 503     1555   1555  2.40  
LINK         SG  CYS A  71                ZN    ZN A 501     1555   1555  2.32  
LINK         SG  CYS A  75                ZN    ZN A 501     1555   1555  2.32  
LINK         NE2 HIS A  83                ZN  B ZN A 503     1555   1555  1.96  
LINK         NE2 HIS A  83                ZN  A ZN A 503     1555   1555  2.18  
LINK         SG ACYS A  87                ZN  A ZN A 503     1555   1555  2.25  
LINK         SG BCYS A  87                ZN  B ZN A 503     1555   1555  2.29  
LINK         SG  CYS A 208                ZN    ZN A 502     1555   1555  2.38  
LINK         SG  CYS A 261                ZN    ZN A 502     1555   1555  2.34  
LINK         SG  CYS A 263                ZN    ZN A 502     1555   1555  2.32  
LINK         SG  CYS A 266                ZN    ZN A 502     1555   1555  2.31  
CISPEP   1 LYS A   94    PRO A   95          0        -0.98                     
CISPEP   2 LYS A   94    PRO A   95          0        -2.37                     
SITE     1 AC1  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 AC2  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 AC3  5 CYS A  62  CYS A  65  TRP A  80  HIS A  83                    
SITE     2 AC3  5 CYS A  87                                                     
SITE     1 AC4 24 ARG A  14  GLY A  15  ASN A  16  TYR A 124                    
SITE     2 AC4 24 GLU A 130  ASN A 132  CYS A 180  ASN A 181                    
SITE     3 AC4 24 SER A 202  LEU A 203  LEU A 204  ASN A 205                    
SITE     4 AC4 24 HIS A 206  TYR A 239  TYR A 257  PHE A 259                    
SITE     5 AC4 24 4ZW A 505  HOH A 673  HOH A 692  HOH A 723                    
SITE     6 AC4 24 HOH A 738  HOH A 750  HOH A 805  HOH A 809                    
SITE     1 AC5 13 ASN A 181  SER A 182  PHE A 183  THR A 184                    
SITE     2 AC5 13 GLU A 192  SER A 202  TYR A 239  ASP A 241                    
SITE     3 AC5 13 TYR A 257  SAM A 504  HOH A 605  HOH A 725                    
SITE     4 AC5 13 HOH A 760                                                     
SITE     1 AC6  8 ARG A  19  VAL A  21  GLY A 232  MET A 390                    
SITE     2 AC6  8 ARG A 394  ILE A 415  GLU A 419  HOH A 831                    
SITE     1 AC7  5 LEU A 344  HIS A 382  GLN A 383  HOH A 683                    
SITE     2 AC7  5 HOH A 818                                                     
CRYST1   58.594   65.232  105.966  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      0.017067  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015330  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009437        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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