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Database: PDB
Entry: 4NJ5
LinkDB: 4NJ5
Original site: 4NJ5 
HEADER    METAL BINDING PROTEIN                   08-NOV-13   4NJ5              
TITLE     CRYSTAL STRUCTURE OF SUVH9                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9   
COMPND   3 SPECIFIC SUVH9;                                                      
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 134-650;                                      
COMPND   6 SYNONYM: HISTONE H3-K9 METHYLTRANSFERASE 9, H3-K9-HMTASE 9, PROTEIN  
COMPND   7 SET DOMAIN GROUP 22, SUPPRESSOR OF VARIEGATION 3-9 HOMOLOG PROTEIN 9,
COMPND   8 SU(VAR)3-9 HOMOLOG PROTEIN 9;                                        
COMPND   9 EC: 2.1.1.43;                                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;                        
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 STRAIN: COLUMBIA-0;                                                  
SOURCE   6 GENE: AT4G13460, SDG22, SET22, SUVH9, T6G15.10;                      
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HI5;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HTB                              
KEYWDS    SET DOMAIN, ZINC BINDING MOTIF, ZINC BINDING, METAL BINDING PROTEIN   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.DU,D.J.PATEL                                                        
REVDAT   2   12-MAR-14 4NJ5    1       JRNL                                     
REVDAT   1   22-JAN-14 4NJ5    0                                                
JRNL        AUTH   L.M.JOHNSON,J.DU,C.J.HALE,S.BISCHOF,S.FENG,R.K.CHODAVARAPU,  
JRNL        AUTH 2 X.ZHONG,G.MARSON,M.PELLEGRINI,D.J.SEGAL,D.J.PATEL,           
JRNL        AUTH 3 S.E.JACOBSEN                                                 
JRNL        TITL   SRA- AND SET-DOMAIN-CONTAINING PROTEINS LINK RNA POLYMERASE  
JRNL        TITL 2 V OCCUPANCY TO DNA METHYLATION.                              
JRNL        REF    NATURE                        V. 507   124 2014              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   24463519                                                     
JRNL        DOI    10.1038/NATURE12931                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 20230                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.150                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1099                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.6901 -  5.9158    1.00     2563   126  0.1746 0.1934        
REMARK   3     2  5.9158 -  4.6967    1.00     2534   157  0.1517 0.1828        
REMARK   3     3  4.6967 -  4.1034    1.00     2557   140  0.1377 0.1499        
REMARK   3     4  4.1034 -  3.7283    0.97     2454   137  0.1743 0.2156        
REMARK   3     5  3.7283 -  3.4612    0.72     1847   109  0.2366 0.2694        
REMARK   3     6  3.4612 -  3.2571    1.00     2533   146  0.2011 0.2450        
REMARK   3     7  3.2571 -  3.0940    1.00     2532   162  0.1998 0.2622        
REMARK   3     8  3.0940 -  2.9594    1.00     2587   122  0.2056 0.2710        
REMARK   3     9  2.9594 -  2.8455    1.00     2535   138  0.2035 0.2324        
REMARK   3    10  2.8455 -  2.7473    1.00     2573   109  0.2043 0.2460        
REMARK   3    11  2.7473 -  2.6614    1.00     2549   178  0.2104 0.2488        
REMARK   3    12  2.6614 -  2.5853    1.00     2557   118  0.2214 0.3014        
REMARK   3    13  2.5853 -  2.5173    1.00     2580   134  0.2222 0.2775        
REMARK   3    14  2.5173 -  2.4558    1.00     2505   124  0.2383 0.2584        
REMARK   3    15  2.4558 -  2.4000    1.00     2578   136  0.2518 0.3213        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.770           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           3875                                  
REMARK   3   ANGLE     :  0.961           5224                                  
REMARK   3   CHIRALITY :  0.076            548                                  
REMARK   3   PLANARITY :  0.004            690                                  
REMARK   3   DIHEDRAL  : 15.121           1447                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 138 through 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5239  65.0340  65.8814              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2719 T22:   0.2096                                     
REMARK   3      T33:   0.2383 T12:  -0.0348                                     
REMARK   3      T13:  -0.0050 T23:   0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9243 L22:   2.7404                                     
REMARK   3      L33:   1.7950 L12:  -1.7223                                     
REMARK   3      L13:  -1.3409 L23:   1.6018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0394 S12:   0.0159 S13:   0.2861                       
REMARK   3      S21:   0.0141 S22:   0.1354 S23:  -0.4187                       
REMARK   3      S31:  -0.2056 S32:   0.0309 S33:  -0.1454                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 273 through 352 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0106  70.5862  75.2403              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2102 T22:   0.1821                                     
REMARK   3      T33:   0.1802 T12:  -0.0206                                     
REMARK   3      T13:  -0.0148 T23:   0.0457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7832 L22:   2.7672                                     
REMARK   3      L33:   2.3531 L12:  -1.4355                                     
REMARK   3      L13:  -1.0847 L23:   1.5512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0723 S12:   0.0923 S13:   0.0128                       
REMARK   3      S21:  -0.0967 S22:  -0.0788 S23:   0.1591                       
REMARK   3      S31:  -0.2043 S32:  -0.1251 S33:   0.0328                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 353 through 429 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8227  39.7592  54.2508              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1844 T22:   0.2524                                     
REMARK   3      T33:   0.1924 T12:  -0.0201                                     
REMARK   3      T13:   0.0133 T23:  -0.0485                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9051 L22:   2.9134                                     
REMARK   3      L33:   1.2016 L12:  -0.8113                                     
REMARK   3      L13:  -1.0026 L23:   1.2430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1125 S12:   0.3268 S13:  -0.3430                       
REMARK   3      S21:   0.1863 S22:  -0.2080 S23:   0.4784                       
REMARK   3      S31:   0.0498 S32:  -0.2825 S33:   0.3245                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 430 through 637 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3215  38.8062  52.9377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1999 T22:   0.2124                                     
REMARK   3      T33:   0.1865 T12:   0.0032                                     
REMARK   3      T13:   0.0434 T23:   0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7310 L22:   1.5800                                     
REMARK   3      L33:   1.4718 L12:  -0.2425                                     
REMARK   3      L13:   0.5353 L23:   0.7042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0186 S12:   0.1441 S13:   0.0140                       
REMARK   3      S21:  -0.1635 S22:   0.0234 S23:  -0.1150                       
REMARK   3      S31:   0.0608 S32:   0.0943 S33:   0.0026                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4NJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB083268.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2823                             
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE CRYSTAL      
REMARK 200                                   SAGITTAL FOCUSING MONOCHROMATOR    
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          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21408                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 14.000                             
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 35.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.69800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.69800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM THIOCYANATE, 0.1 M BIS   
REMARK 280  -TRIS PROPANE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE   
REMARK 280  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       31.83950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.67950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.09850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.67950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.83950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.09850            
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     SER A   133                                                      
REMARK 465     THR A   134                                                      
REMARK 465     ASP A   135                                                      
REMARK 465     VAL A   136                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     ASN A   170                                                      
REMARK 465     GLY A   171                                                      
REMARK 465     VAL A   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     ARG A   175                                                      
REMARK 465     TYR A   259                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     ASP A   261                                                      
REMARK 465     ASP A   262                                                      
REMARK 465     ASP A   263                                                      
REMARK 465     ASP A   264                                                      
REMARK 465     GLN A   265                                                      
REMARK 465     GLY A   266                                                      
REMARK 465     VAL A   425                                                      
REMARK 465     GLN A   426                                                      
REMARK 465     GLN A   427                                                      
REMARK 465     SER A   428                                                      
REMARK 465     VAL A   638                                                      
REMARK 465     VAL A   639                                                      
REMARK 465     ASP A   640                                                      
REMARK 465     ASP A   641                                                      
REMARK 465     TRP A   642                                                      
REMARK 465     ASN A   643                                                      
REMARK 465     ALA A   644                                                      
REMARK 465     LYS A   645                                                      
REMARK 465     LEU A   646                                                      
REMARK 465     ALA A   647                                                      
REMARK 465     ILE A   648                                                      
REMARK 465     CYS A   649                                                      
REMARK 465     ASN A   650                                                      
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    HIS A 608   NE2   HIS A 608   CD2    -0.074                       
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    LYS A 201       12.82     59.24                                   
REMARK 500    LEU A 242      -88.97   -130.42                                   
REMARK 500    SER A 244     -172.24     78.97                                   
REMARK 500    ASN A 373       67.98   -155.17                                   
REMARK 500    ASP A 386       93.55   -160.35                                   
REMARK 500    ASP A 403     -155.66   -144.66                                   
REMARK 500    ASN A 484       30.64    -99.11                                   
REMARK 500    ILE A 519      -64.64    -99.60                                   
REMARK 500    LYS A 585      -50.79   -124.58                                   
REMARK 500    ASP A 598       72.68   -117.26                                   
REMARK 500    HIS A 608      -58.91   -140.09                                   
REMARK 500    MET A 629       -1.07     82.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 440   SG                                                     
REMARK 620 2 CYS A 478   SG  139.0                                              
REMARK 620 3 CYS A 482   SG   99.1 108.9                                        
REMARK 620 4 CYS A 472   SG   93.8  95.9 121.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 440   SG                                                     
REMARK 620 2 CYS A 436   SG  121.0                                              
REMARK 620 3 CYS A 444   SG  114.8 105.1                                        
REMARK 620 4 CYS A 434   SG   93.3 108.6 113.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 446   SG                                                     
REMARK 620 2 CYS A 434   SG  108.1                                              
REMARK 620 3 CYS A 472   SG  117.4 115.6                                        
REMARK 620 4 CYS A 476   SG   95.4 107.6 110.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 803                  
DBREF  4NJ5 A  134   650  UNP    Q9T0G7   SUVH9_ARATH    134    650             
SEQADV 4NJ5 SER A  133  UNP  Q9T0G7              EXPRESSION TAG                 
SEQRES   1 A  518  SER THR ASP VAL GLY PRO GLU SER GLU ARG GLN PHE ARG          
SEQRES   2 A  518  GLU HIS VAL ARG LYS THR ARG MET ILE TYR ASP SER LEU          
SEQRES   3 A  518  ARG MET PHE LEU MET MET GLU GLU ALA LYS ARG ASN GLY          
SEQRES   4 A  518  VAL GLY GLY ARG ARG ALA ARG ALA ASP GLY LYS ALA GLY          
SEQRES   5 A  518  LYS ALA GLY SER MET MET ARG ASP CYS MET LEU TRP MET          
SEQRES   6 A  518  ASN ARG ASP LYS ARG ILE VAL GLY SER ILE PRO GLY VAL          
SEQRES   7 A  518  GLN VAL GLY ASP ILE PHE PHE PHE ARG PHE GLU LEU CYS          
SEQRES   8 A  518  VAL MET GLY LEU HIS GLY HIS PRO GLN SER GLY ILE ASP          
SEQRES   9 A  518  PHE LEU THR GLY SER LEU SER SER ASN GLY GLU PRO ILE          
SEQRES  10 A  518  ALA THR SER VAL ILE VAL SER GLY GLY TYR GLU ASP ASP          
SEQRES  11 A  518  ASP ASP GLN GLY ASP VAL ILE MET TYR THR GLY GLN GLY          
SEQRES  12 A  518  GLY GLN ASP ARG LEU GLY ARG GLN ALA GLU HIS GLN ARG          
SEQRES  13 A  518  LEU GLU GLY GLY ASN LEU ALA MET GLU ARG SER MET TYR          
SEQRES  14 A  518  TYR GLY ILE GLU VAL ARG VAL ILE ARG GLY LEU LYS TYR          
SEQRES  15 A  518  GLU ASN GLU VAL SER SER ARG VAL TYR VAL TYR ASP GLY          
SEQRES  16 A  518  LEU PHE ARG ILE VAL ASP SER TRP PHE ASP VAL GLY LYS          
SEQRES  17 A  518  SER GLY PHE GLY VAL PHE LYS TYR ARG LEU GLU ARG ILE          
SEQRES  18 A  518  GLU GLY GLN ALA GLU MET GLY SER SER VAL LEU LYS PHE          
SEQRES  19 A  518  ALA ARG THR LEU LYS THR ASN PRO LEU SER VAL ARG PRO          
SEQRES  20 A  518  ARG GLY TYR ILE ASN PHE ASP ILE SER ASN GLY LYS GLU          
SEQRES  21 A  518  ASN VAL PRO VAL TYR LEU PHE ASN ASP ILE ASP SER ASP          
SEQRES  22 A  518  GLN GLU PRO LEU TYR TYR GLU TYR LEU ALA GLN THR SER          
SEQRES  23 A  518  PHE PRO PRO GLY LEU PHE VAL GLN GLN SER GLY ASN ALA          
SEQRES  24 A  518  SER GLY CYS ASP CYS VAL ASN GLY CYS GLY SER GLY CYS          
SEQRES  25 A  518  LEU CYS GLU ALA LYS ASN SER GLY GLU ILE ALA TYR ASP          
SEQRES  26 A  518  TYR ASN GLY THR LEU ILE ARG GLN LYS PRO LEU ILE HIS          
SEQRES  27 A  518  GLU CYS GLY SER ALA CYS GLN CYS PRO PRO SER CYS ARG          
SEQRES  28 A  518  ASN ARG VAL THR GLN LYS GLY LEU ARG ASN ARG LEU GLU          
SEQRES  29 A  518  VAL PHE ARG SER LEU GLU THR GLY TRP GLY VAL ARG SER          
SEQRES  30 A  518  LEU ASP VAL LEU HIS ALA GLY ALA PHE ILE CYS GLU TYR          
SEQRES  31 A  518  ALA GLY VAL ALA LEU THR ARG GLU GLN ALA ASN ILE LEU          
SEQRES  32 A  518  THR MET ASN GLY ASP THR LEU VAL TYR PRO ALA ARG PHE          
SEQRES  33 A  518  SER SER ALA ARG TRP GLU ASP TRP GLY ASP LEU SER GLN          
SEQRES  34 A  518  VAL LEU ALA ASP PHE GLU ARG PRO SER TYR PRO ASP ILE          
SEQRES  35 A  518  PRO PRO VAL ASP PHE ALA MET ASP VAL SER LYS MET ARG          
SEQRES  36 A  518  ASN VAL ALA CYS TYR ILE SER HIS SER THR ASP PRO ASN          
SEQRES  37 A  518  VAL ILE VAL GLN PHE VAL LEU HIS ASP HIS ASN SER LEU          
SEQRES  38 A  518  MET PHE PRO ARG VAL MET LEU PHE ALA ALA GLU ASN ILE          
SEQRES  39 A  518  PRO PRO MET THR GLU LEU SER LEU ASP TYR GLY VAL VAL          
SEQRES  40 A  518  ASP ASP TRP ASN ALA LYS LEU ALA ILE CYS ASN                  
HET     ZN  A 801       1                                                       
HET     ZN  A 802       1                                                       
HET     ZN  A 803       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  HOH   *211(H2 O)                                                    
HELIX    1   1 GLU A  139  LYS A  168  1                                  30    
HELIX    2   2 ALA A  177  CYS A  193  1                                  17    
HELIX    3   3 PHE A  218  MET A  225  1                                   8    
HELIX    4   4 GLU A  290  TYR A  302  1                                  13    
HELIX    5   5 MET A  359  ASN A  373  1                                  15    
HELIX    6   6 PRO A  374  VAL A  377  5                                   4    
HELIX    7   7 GLN A  406  TYR A  411  5                                   6    
HELIX    8   8 CYS A  444  ASN A  450  1                                   7    
HELIX    9   9 VAL A  486  GLY A  490  5                                   5    
HELIX   10  10 THR A  528  ASN A  538  1                                  11    
HELIX   11  11 TYR A  544  PHE A  548  5                                   5    
HELIX   12  12 SER A  550  GLU A  554  5                                   5    
HELIX   13  13 ASN A  588  ILE A  593  5                                   6    
SHEET    1   A 5 ILE A 215  PHE A 216  0                                        
SHEET    2   A 5 VAL A 322  VAL A 338 -1  O  TYR A 323   N  PHE A 216           
SHEET    3   A 5 VAL A 306  LEU A 312 -1  N  VAL A 306   O  PHE A 329           
SHEET    4   A 5 ILE A 249  SER A 256  1  N  VAL A 253   O  ILE A 309           
SHEET    5   A 5 ILE A 235  LEU A 238 -1  N  ASP A 236   O  SER A 252           
SHEET    1   B 4 ILE A 215  PHE A 216  0                                        
SHEET    2   B 4 VAL A 322  VAL A 338 -1  O  TYR A 323   N  PHE A 216           
SHEET    3   B 4 GLY A 344  ARG A 352 -1  O  GLU A 351   N  ARG A 330           
SHEET    4   B 4 VAL A 268  THR A 272 -1  N  ILE A 269   O  LEU A 350           
SHEET    1   C 4 TYR A 382  ASN A 384  0                                        
SHEET    2   C 4 VAL A 396  PHE A 399 -1  O  LEU A 398   N  ASN A 384           
SHEET    3   C 4 LEU A 495  ARG A 499  1  O  VAL A 497   N  TYR A 397           
SHEET    4   C 4 TRP A 505  SER A 509 -1  O  ARG A 508   N  GLU A 496           
SHEET    1   D 2 GLU A 412  TYR A 413  0                                        
SHEET    2   D 2 MET A 586  ARG A 587  1  O  ARG A 587   N  GLU A 412           
SHEET    1   E 4 ILE A 469  HIS A 470  0                                        
SHEET    2   E 4 VAL A 601  LEU A 607  1  O  PHE A 605   N  ILE A 469           
SHEET    3   E 4 ARG A 617  ALA A 622 -1  O  ARG A 617   N  VAL A 606           
SHEET    4   E 4 PHE A 518  GLU A 521 -1  N  CYS A 520   O  LEU A 620           
SHEET    1   F 2 VAL A 525  LEU A 527  0                                        
SHEET    2   F 2 ALA A 580  ASP A 582 -1  O  ASP A 582   N  VAL A 525           
SHEET    1   G 2 SER A 594  HIS A 595  0                                        
SHEET    2   G 2 SER A 633  LEU A 634  1  O  LEU A 634   N  SER A 594           
LINK         SG  CYS A 440                ZN    ZN A 802     1555   1555  2.30  
LINK         SG  CYS A 440                ZN    ZN A 803     1555   1555  2.30  
LINK         SG  CYS A 446                ZN    ZN A 801     1555   1555  2.30  
LINK         SG  CYS A 436                ZN    ZN A 803     1555   1555  2.31  
LINK         SG  CYS A 434                ZN    ZN A 801     1555   1555  2.32  
LINK         SG  CYS A 478                ZN    ZN A 802     1555   1555  2.34  
LINK         SG  CYS A 472                ZN    ZN A 801     1555   1555  2.37  
LINK         SG  CYS A 482                ZN    ZN A 802     1555   1555  2.37  
LINK         SG  CYS A 472                ZN    ZN A 802     1555   1555  2.40  
LINK         SG  CYS A 476                ZN    ZN A 801     1555   1555  2.43  
LINK         SG  CYS A 444                ZN    ZN A 803     1555   1555  2.43  
LINK         SG  CYS A 434                ZN    ZN A 803     1555   1555  2.56  
SITE     1 AC1  4 CYS A 434  CYS A 446  CYS A 472  CYS A 476                    
SITE     1 AC2  4 CYS A 440  CYS A 472  CYS A 478  CYS A 482                    
SITE     1 AC3  4 CYS A 434  CYS A 436  CYS A 440  CYS A 444                    
CRYST1   63.679   84.197   99.359  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      0.015704  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011877  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010065        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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