GenomeNet

Database: PDB
Entry: 5ARG
LinkDB: 5ARG
Original site: 5ARG 
HEADER    TRANSFERASE                             24-SEP-15   5ARG              
TITLE     SMYD2 IN COMPLEX WITH SGC PROBE BAY-598                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE SMYD2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SET DOMAIN, UNP RESIDUES 2-433;                            
COMPND   5 SYNONYM: HSKM-B, HISTONE METHYLTRANSFERASE SMYD2, LYSINE N-          
COMPND   6 METHYLTRANSFERASE 3C, SET AND MYND DOMAIN-CONTAINING PROTEIN 2;      
COMPND   7 EC: 2.1.1.-, 2.1.1.43;                                               
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9                                     
KEYWDS    TRANSFERASE, OXIDOREDUCTASE, METHYLTRANSFERASE, SET DOMAIN, SMALL     
KEYWDS   2 MOLECULE INHIBITOR, SGC PROBE, DRUG TARGET                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.C.HILLIG,V.BADOCK,N.BARAK,T.STELLFELD,E.EGGERT,A.TER LAAK,J.WEISKE, 
AUTHOR   2 C.D.CHRIST,S.KOEHR,D.STOECKIGT,J.MOWAT,T.MUELLER,A.E.FERNANDEZ-      
AUTHOR   3 MONTALVAN,I.V.HARTUNG,C.STRESEMANN,T.BRUMBY,H.WEINMANN               
REVDAT   4   03-APR-19 5ARG    1       REMARK                                   
REVDAT   3   13-SEP-17 5ARG    1       REMARK                                   
REVDAT   2   08-JUN-16 5ARG    1       JRNL                                     
REVDAT   1   27-APR-16 5ARG    0                                                
JRNL        AUTH   E.EGGERT,R.C.HILLIG,S.KOHR,D.STOCKIGT,J.WEISKE,N.BARAK,      
JRNL        AUTH 2 J.MOWAT,T.BRUMBY,C.D.CHRIST,A.TER LAAK,T.LANG,               
JRNL        AUTH 3 A.E.FERNANDEZ-MONTALVAN,V.BADOCK,H.WEINMANN,I.V.HARTUNG,     
JRNL        AUTH 4 D.BARSYTE-LOVEJOY,M.SZEWCZYK,S.KENNEDY,F.LI,M.VEDADI,        
JRNL        AUTH 5 P.J.BROWN,V.SANTHAKUMAR,C.H.ARROWSMITH,T.STELLFELD,          
JRNL        AUTH 6 C.STRESEMANN                                                 
JRNL        TITL   DISCOVERY AND CHARACTERIZATION OF A HIGHLY POTENT AND        
JRNL        TITL 2 SELECTIVE AMINOPYRAZOLINE-BASED IN VIVO PROBE (BAY-598) FOR  
JRNL        TITL 3 THE PROTEIN LYSINE METHYLTRANSFERASE SMYD2.                  
JRNL        REF    J.MED.CHEM.                   V.  59  4578 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   27075367                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B01890                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 31972                          
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) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1683                            
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) : 1.99                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.04                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2294                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 120                          
REMARK   3   BIN FREE R VALUE                    : 0.3810                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3428                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 71                                      
REMARK   3   SOLVENT ATOMS            : 137                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.09                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.24000                                             
REMARK   3    B22 (A**2) : 0.05000                                              
REMARK   3    B33 (A**2) : 2.18000                                              
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): 0.215         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.188         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.198         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.313        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3641 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3445 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4919 ; 2.033 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7940 ; 0.900 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   441 ; 6.604 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   170 ;38.541 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   658 ;18.929 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;17.422 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   522 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4060 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   826 ; 0.001 ; 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):  1725 ; 3.533 ; 1.406       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1725 ; 3.519 ; 1.406       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2158 ; 4.576 ; 3.140       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1916 ; 5.015 ; 1.844       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    18        A   271                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.0830   7.7350 -19.7210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3683 T22:   0.0454                                     
REMARK   3      T33:   0.0964 T12:  -0.0095                                     
REMARK   3      T13:   0.1058 T23:  -0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9032 L22:   7.9542                                     
REMARK   3      L33:   4.5122 L12:  -0.6868                                     
REMARK   3      L13:  -0.1579 L23:  -4.0574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4017 S12:   0.0466 S13:  -0.0337                       
REMARK   3      S21:   0.3478 S22:   0.0318 S23:   0.7051                       
REMARK   3      S31:  -0.7253 S32:   0.2019 S33:  -0.4335                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   272        A   430                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5060  -8.2930  -1.7630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4800 T22:   0.1979                                     
REMARK   3      T33:   0.0665 T12:  -0.1371                                     
REMARK   3      T13:  -0.0716 T23:   0.0324                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1383 L22:   7.3592                                     
REMARK   3      L33:   4.4377 L12:  -0.6555                                     
REMARK   3      L13:  -0.2266 L23:  -3.2550                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0923 S12:  -0.2470 S13:   0.1593                       
REMARK   3      S21:   1.4530 S22:  -0.4230 S23:  -0.5790                       
REMARK   3      S31:  -0.7808 S32:   0.8156 S33:   0.3307                       
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. B FACTORS WITH TLS ADDED.                                
REMARK   4                                                                      
REMARK   4 5ARG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290065088.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JAN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918409                           
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          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33656                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.990                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.610                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.580                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.3900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.82000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.410                              
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: PDB ENTRY 3TG5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 3350, 100 MMOL HEPES PH 7.0.     
REMARK 280  CRYO BUFFER CONTAINS AN ADDTIONAL 20% GLYCEROL AND 1 MMOL           
REMARK 280  LIGAND. OTHER CRYSTALISATION REMARKS:4 MILLIMOLAR COFACTOR SAM      
REMARK 280  ADDED AND MIXTURE INCUBATED FOR 2 HOURS AT 4 DEGREE CELSIUS         
REMARK 280  PRIOR TO CRYSTALLIZATION. CO- COMPLEX WITH BAY-598 FORMED BY        
REMARK 280  SOAKING SMYD2-SAM CRYSTALS WITH 5 MILLIMOLAR LIGAND FOR 4 DAYS.,    
REMARK 280  TEMPERATURE 277K                                                    
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       26.17150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.55750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.80000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.55750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.17150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.80000            
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     GLY A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     SER A   432                                                      
REMARK 465     HIS A   433                                                      
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   OG   SER A   313     OE1  GLU A   316              2.10            
REMARK 500   ND2  ASN A   180     O    HOH A  2045              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    CYS A 267   CB    CYS A 267   SG      0.103                       
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 111   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP A 242   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    CYS A 267   CB  -  CA  -  C   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    CYS A 267   CA  -  CB  -  SG  ANGL. DEV. =  11.2 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    CYS A  13       50.16    -94.87                                   
REMARK 500    CYS A  13       49.87    -94.33                                   
REMARK 500    SER A  14      129.11    -37.98                                   
REMARK 500    GLN A  70       23.88   -142.11                                   
REMARK 500    ASN A  75      172.49    179.94                                   
REMARK 500    ASN A 101       56.62   -157.92                                   
REMARK 500    HIS A 310      -17.25    -49.00                                   
REMARK 500    TYR A 311      -34.72   -165.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H41 A 1432                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1433                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 1434                
DBREF  5ARG A    2   433  UNP    Q9NRG4   SMYD2_HUMAN      2    433             
SEQADV 5ARG GLY A    1  UNP  Q9NRG4              EXPRESSION TAG                 
SEQRES   1 A  433  GLY ARG ALA GLU GLY LEU GLY GLY LEU GLU ARG PHE CYS          
SEQRES   2 A  433  SER PRO GLY LYS GLY ARG GLY LEU ARG ALA LEU GLN PRO          
SEQRES   3 A  433  PHE GLN VAL GLY ASP LEU LEU PHE SER CYS PRO ALA TYR          
SEQRES   4 A  433  ALA TYR VAL LEU THR VAL ASN GLU ARG GLY ASN HIS CYS          
SEQRES   5 A  433  GLU TYR CYS PHE THR ARG LYS GLU GLY LEU SER LYS CYS          
SEQRES   6 A  433  GLY ARG CYS LYS GLN ALA PHE TYR CYS ASN VAL GLU CYS          
SEQRES   7 A  433  GLN LYS GLU ASP TRP PRO MET HIS LYS LEU GLU CYS SER          
SEQRES   8 A  433  PRO MET VAL VAL PHE GLY GLU ASN TRP ASN PRO SER GLU          
SEQRES   9 A  433  THR VAL ARG LEU THR ALA ARG ILE LEU ALA LYS GLN LYS          
SEQRES  10 A  433  ILE HIS PRO GLU ARG THR PRO SER GLU LYS LEU LEU ALA          
SEQRES  11 A  433  VAL LYS GLU PHE GLU SER HIS LEU ASP LYS LEU ASP ASN          
SEQRES  12 A  433  GLU LYS LYS ASP LEU ILE GLN SER ASP ILE ALA ALA LEU          
SEQRES  13 A  433  HIS HIS PHE TYR SER LYS HIS LEU GLY PHE PRO ASP ASN          
SEQRES  14 A  433  ASP SER LEU VAL VAL LEU PHE ALA GLN VAL ASN CYS ASN          
SEQRES  15 A  433  GLY PHE THR ILE GLU ASP GLU GLU LEU SER HIS LEU GLY          
SEQRES  16 A  433  SER ALA ILE PHE PRO ASP VAL ALA LEU MET ASN HIS SER          
SEQRES  17 A  433  CYS CYS PRO ASN VAL ILE VAL THR TYR LYS GLY THR LEU          
SEQRES  18 A  433  ALA GLU VAL ARG ALA VAL GLN GLU ILE LYS PRO GLY GLU          
SEQRES  19 A  433  GLU VAL PHE THR SER TYR ILE ASP LEU LEU TYR PRO THR          
SEQRES  20 A  433  GLU ASP ARG ASN ASP ARG LEU ARG ASP SER TYR PHE PHE          
SEQRES  21 A  433  THR CYS GLU CYS GLN GLU CYS THR THR LYS ASP LYS ASP          
SEQRES  22 A  433  LYS ALA LYS VAL GLU ILE ARG LYS LEU SER ASP PRO PRO          
SEQRES  23 A  433  LYS ALA GLU ALA ILE ARG ASP MET VAL ARG TYR ALA ARG          
SEQRES  24 A  433  ASN VAL ILE GLU GLU PHE ARG ARG ALA LYS HIS TYR LYS          
SEQRES  25 A  433  SER PRO SER GLU LEU LEU GLU ILE CYS GLU LEU SER GLN          
SEQRES  26 A  433  GLU LYS MET SER SER VAL PHE GLU ASP SER ASN VAL TYR          
SEQRES  27 A  433  MET LEU HIS MET MET TYR GLN ALA MET GLY VAL CYS LEU          
SEQRES  28 A  433  TYR MET GLN ASP TRP GLU GLY ALA LEU GLN TYR GLY GLN          
SEQRES  29 A  433  LYS ILE ILE LYS PRO TYR SER LYS HIS TYR PRO LEU TYR          
SEQRES  30 A  433  SER LEU ASN VAL ALA SER MET TRP LEU LYS LEU GLY ARG          
SEQRES  31 A  433  LEU TYR MET GLY LEU GLU HIS LYS ALA ALA GLY GLU LYS          
SEQRES  32 A  433  ALA LEU LYS LYS ALA ILE ALA ILE MET GLU VAL ALA HIS          
SEQRES  33 A  433  GLY LYS ASP HIS PRO TYR ILE SER GLU ILE LYS GLN GLU          
SEQRES  34 A  433  ILE GLU SER HIS                                              
HET     ZN  A1003       1                                                       
HET     ZN  A1004       1                                                       
HET     ZN  A1005       1                                                       
HET    H41  A1432      35                                                       
HET    GOL  A1433       6                                                       
HET    SAM  A1434      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     H41 N-[1-(N'-CYANO-N-[3-(DIFLUOROMETHOXY)                            
HETNAM   2 H41  PHENYL]CARBAMIMIDOYL)-3-(3,4-DICHLOROPHENYL)-4,5-               
HETNAM   3 H41  DIHYDRO-1H-PYRAZOL-4-YL]-N-ETHYL-2-HYDROXYACETAMIDE             
HETNAM     GOL GLYCEROL                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  H41    C22 H20 CL2 F2 N6 O3                                         
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7  SAM    C15 H22 N6 O5 S                                              
FORMUL   8  HOH   *137(H2 O)                                                    
HELIX    1   1 VAL A   45  ARG A   48  5                                   4    
HELIX    2   2 ASN A   75  LYS A   87  1                                  13    
HELIX    3   3 GLU A   89  GLY A   97  1                                   9    
HELIX    4   4 GLU A   98  TRP A  100  5                                   3    
HELIX    5   5 SER A  103  HIS A  119  1                                  17    
HELIX    6   6 ALA A  130  PHE A  134  5                                   5    
HELIX    7   7 HIS A  137  LEU A  141  5                                   5    
HELIX    8   8 ASP A  142  SER A  161  1                                  20    
HELIX    9   9 ASP A  168  ASN A  182  1                                  15    
HELIX   10  10 ASP A  201  MET A  205  5                                   5    
HELIX   11  11 PRO A  246  PHE A  259  1                                  14    
HELIX   12  12 CYS A  264  LYS A  270  1                                   7    
HELIX   13  13 LYS A  272  VAL A  277  1                                   6    
HELIX   14  14 LYS A  287  HIS A  310  1                                  24    
HELIX   15  15 SER A  313  SER A  329  1                                  17    
HELIX   16  16 ASN A  336  MET A  353  1                                  18    
HELIX   17  17 ASP A  355  TYR A  374  1                                  20    
HELIX   18  18 SER A  378  LEU A  395  1                                  18    
HELIX   19  19 HIS A  397  HIS A  416  1                                  20    
HELIX   20  20 HIS A  420  ILE A  430  1                                  11    
SHEET    1  AA 2 LEU A   9  PHE A  12  0                                        
SHEET    2  AA 2 GLY A  20  ALA A  23 -1  O  GLY A  20   N  PHE A  12           
SHEET    1  AB 3 LEU A  32  PRO A  37  0                                        
SHEET    2  AB 3 LEU A 221  ALA A 226 -1  O  ALA A 222   N  CYS A  36           
SHEET    3  AB 3 VAL A 213  LYS A 218 -1  O  ILE A 214   N  ARG A 225           
SHEET    1  AC 3 ALA A  40  LEU A  43  0                                        
SHEET    2  AC 3 HIS A 193  ILE A 198 -1  O  SER A 196   N  VAL A  42           
SHEET    3  AC 3 GLY A 183  GLU A 187 -1  O  PHE A 184   N  ALA A 197           
SHEET    1  AD 2 SER A  63  LYS A  64  0                                        
SHEET    2  AD 2 PHE A  72  TYR A  73 -1  O  TYR A  73   N  SER A  63           
SHEET    1  AE 2 ASN A 206  HIS A 207  0                                        
SHEET    2  AE 2 PHE A 237  THR A 238  1  N  THR A 238   O  ASN A 206           
SSBOND   1 CYS A  209    CYS A  267                          1555   1555  2.33  
SITE     1 AC1  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
SITE     1 AC2  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC3  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC4 17 GLU A 104  THR A 105  LEU A 108  VAL A 179                    
SITE     2 AC4 17 ASN A 182  GLY A 183  PHE A 184  THR A 185                    
SITE     3 AC4 17 SER A 196  VAL A 202  ALA A 203  TYR A 217                    
SITE     4 AC4 17 TYR A 240  TYR A 258  SAM A1434  HOH A2080                    
SITE     5 AC4 17 HOH A2089                                                     
SITE     1 AC5  8 CYS A 209  LEU A 243  GLU A 266  LYS A 272                    
SITE     2 AC5  8 LYS A 276  HIS A 373  TYR A 374  PRO A 375                    
SITE     1 AC6 14 GLY A  16  LYS A  17  ARG A  19  HIS A 137                    
SITE     2 AC6 14 CYS A 181  ASN A 182  ALA A 203  ASN A 206                    
SITE     3 AC6 14 HIS A 207  TYR A 240  TYR A 258  PHE A 260                    
SITE     4 AC6 14 H41 A1432  HOH A2002                                          
CRYST1   52.343   69.600  131.115  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      0.019105  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014368  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007627        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system