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Database: PDB
Entry: 4QEP
LinkDB: 4QEP
Original site: 4QEP 
HEADER    TRANSCRIPTION/DNA                       17-MAY-14   4QEP              
TITLE     CRYSTAL STRUCTURE OF KRYPTONITE IN COMPLEX WITH MCHG DNA AND SAH      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC   
COMPND   3 SUVH4;                                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: FUNCTIONAL FRAGMENT;                                       
COMPND   6 SYNONYM: HISTONE H3-K9 METHYLTRANSFERASE 4, H3-K9-HMTASE 4, PROTEIN  
COMPND   7 KRYPTONITE, PROTEIN SET DOMAIN GROUP 33, SUPPRESSOR OF VARIEGATION 3-
COMPND   8 9 HOMOLOG PROTEIN 4, SU(VAR)3-9 HOMOLOG PROTEIN 4;                   
COMPND   9 EC: 2.1.1.43;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: DNA (5'-D(*GP*GP*TP*AP*CP*TP*(5CM)                         
COMPND  13 P*AP*GP*CP*AP*GP*TP*AP*T)-3');                                       
COMPND  14 CHAIN: C;                                                            
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: DNA (5'-D(*AP*CP*TP*GP*CP*TP*GP*AP*GP*TP*AP*CP*CP*AP*T)-   
COMPND  18 3');                                                                 
COMPND  19 CHAIN: D;                                                            
COMPND  20 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 GENE: SUVH4, KYP, SDG33, SET33, AT5G13960, MAC12.7;                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-SUMO;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES                                                       
KEYWDS    SRA, SET, HISTONE METHYLATION, METHYLATED DNA, METHYLATION,           
KEYWDS   2 TRANSCRIPTION-DNA COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.DU,S.LI,D.J.PATEL                                                   
REVDAT   2   20-AUG-14 4QEP    1       JRNL                                     
REVDAT   1   30-JUL-14 4QEP    0                                                
JRNL        AUTH   J.DU,L.M.JOHNSON,M.GROTH,S.FENG,C.J.HALE,S.LI,A.A.VASHISHT,  
JRNL        AUTH 2 J.GALLEGO-BARTOLOME,J.A.WOHLSCHLEGEL,D.J.PATEL,S.E.JACOBSEN  
JRNL        TITL   MECHANISM OF DNA METHYLATION-DIRECTED HISTONE METHYLATION BY 
JRNL        TITL 2 KRYPTONITE.                                                  
JRNL        REF    MOL.CELL                      V.  55   495 2014              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   25018018                                                     
JRNL        DOI    10.1016/J.MOLCEL.2014.06.009                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 10811                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.770                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 516                             
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 49.6330 -  4.9198    0.85     2558   120  0.2192 0.2599        
REMARK   3     2  4.9198 -  3.9055    0.90     2564   118  0.1801 0.1964        
REMARK   3     3  3.9055 -  3.4119    0.92     2585   143  0.2047 0.2441        
REMARK   3     4  3.4119 -  3.1000    0.92     2588   135  0.2556 0.3464        
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)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.010           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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      :  0.016           4344                                  
REMARK   3   ANGLE     :  1.601           5964                                  
REMARK   3   CHIRALITY :  0.091            650                                  
REMARK   3   PLANARITY :  0.007            681                                  
REMARK   3   DIHEDRAL  : 22.092           1653                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 99 through 302 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.2863  19.1529 -14.4850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2097 T22:   0.2108                                     
REMARK   3      T33:   0.2033 T12:  -0.0264                                     
REMARK   3      T13:   0.0009 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8672 L22:   0.9419                                     
REMARK   3      L33:   3.4195 L12:   0.5361                                     
REMARK   3      L13:   0.6981 L23:   0.6392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0449 S12:   0.1410 S13:  -0.0752                       
REMARK   3      S21:  -0.1425 S22:   0.0426 S23:  -0.0105                       
REMARK   3      S31:  -0.0783 S32:  -0.0570 S33:   0.0022                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 303 through 564 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.5479   4.0560 -43.6655              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2198 T22:   0.2263                                     
REMARK   3      T33:   0.3250 T12:   0.0209                                     
REMARK   3      T13:   0.0207 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2833 L22:   1.7182                                     
REMARK   3      L33:   2.8504 L12:   0.2024                                     
REMARK   3      L13:   0.9034 L23:   1.6066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0309 S12:  -0.0068 S13:  -0.0331                       
REMARK   3      S21:  -0.0770 S22:  -0.1663 S23:   0.2170                       
REMARK   3      S31:   0.1199 S32:  -0.2627 S33:   0.1256                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 565 through 624 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -32.4605  14.9148 -42.3902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3255 T22:   0.4439                                     
REMARK   3      T33:   0.5255 T12:   0.1288                                     
REMARK   3      T13:  -0.0200 T23:  -0.1726                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5390 L22:   2.0497                                     
REMARK   3      L33:   1.8662 L12:   0.0516                                     
REMARK   3      L13:   0.2054 L23:  -0.1728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1382 S12:  -0.1779 S13:   0.6132                       
REMARK   3      S21:   0.0203 S22:  -0.1024 S23:   0.6473                       
REMARK   3      S31:  -0.3073 S32:  -0.7849 S33:   0.1245                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'C' and (resid 1 through 11 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   4.5498  18.3570 -18.4039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3773 T22:   0.4380                                     
REMARK   3      T33:   0.3069 T12:   0.0709                                     
REMARK   3      T13:   0.1431 T23:  -0.1800                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4053 L22:   5.9688                                     
REMARK   3      L33:   5.0301 L12:   1.8279                                     
REMARK   3      L13:   1.2428 L23:  -0.6426                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0755 S12:   1.0331 S13:  -0.3338                       
REMARK   3      S21:  -0.4452 S22:   0.4045 S23:  -1.1458                       
REMARK   3      S31:  -0.0463 S32:  -0.0504 S33:  -0.2569                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'D' and (resid 3 through 7 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7064   7.4389 -20.8996              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4959 T22:   0.6358                                     
REMARK   3      T33:   0.4261 T12:   0.3158                                     
REMARK   3      T13:   0.0313 T23:   0.0530                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2947 L22:   3.5766                                     
REMARK   3      L33:   4.9483 L12:  -0.5283                                     
REMARK   3      L13:   0.4649 L23:  -4.2020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1271 S12:   0.0896 S13:  -0.2150                       
REMARK   3      S21:  -0.2895 S22:  -0.3269 S23:  -0.5347                       
REMARK   3      S31:   0.7010 S32:   0.7020 S33:   0.2982                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'D' and (resid 8 through 15 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3460  30.1320 -15.5234              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6164 T22:   0.3539                                     
REMARK   3      T33:   0.3731 T12:  -0.1512                                     
REMARK   3      T13:  -0.1276 T23:   0.0751                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4582 L22:   3.3312                                     
REMARK   3      L33:   2.0085 L12:  -1.6502                                     
REMARK   3      L13:  -0.1230 L23:  -0.1022                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7376 S12:  -0.2374 S13:   0.3302                       
REMARK   3      S21:  -0.1373 S22:  -0.0657 S23:  -0.8008                       
REMARK   3      S31:  -0.6480 S32:   0.1672 S33:   0.3810                       
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 4QEP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085960.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMETER       
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   : 10851                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
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     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.15500                            
REMARK 200  R SYM                      (I) : 0.15500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.61500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4QEN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG200, 5% PEG3000, AND 0.1 M MES,   
REMARK 280  PH 6.0, VAPOR 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       27.17300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.87700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.78450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.87700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.17300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.78450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE ASYMMETRIC UNIT.              
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D                               
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    92                                                      
REMARK 465     ASN A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     LYS A    95                                                      
REMARK 465     ASP A    96                                                      
REMARK 465     VAL A    97                                                      
REMARK 465     ASN A    98                                                      
REMARK 465     GLN A   313                                                      
REMARK 465     VAL A   314                                                      
REMARK 465     ASN A   315                                                      
REMARK 465     PHE A   316                                                      
REMARK 465     VAL A   317                                                      
REMARK 465     ALA A   318                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     ARG A   320                                                      
REMARK 465     ILE A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     THR A   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     THR A   325                                                      
REMARK 465     SER A   326                                                      
REMARK 465     GLU A   327                                                      
REMARK 465     ILE A   328                                                      
REMARK 465     ASP A   486                                                      
REMARK 465     THR A   487                                                      
REMARK 465     ILE A   488                                                      
REMARK 465     SER A   489                                                      
REMARK 465     ASP A   490                                                      
REMARK 465     GLN A   500                                                      
REMARK 465     GLN A   501                                                      
REMARK 465     THR A   502                                                      
REMARK 465     MET A   503                                                      
REMARK 465     GLN A   504                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     LEU A   506                                                      
REMARK 465     GLY A   507                                                      
REMARK 465     GLY A   508                                                      
REMARK 465     ARG A   509                                                      
REMARK 465     GLN A   510                                                      
REMARK 465     ARG A   511                                                      
REMARK 465     ARG A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     ARG A   514                                                      
REMARK 465     ASP A   515                                                      
REMARK 465     VAL A   516                                                      
REMARK 465     ALA A   517                                                      
REMARK 465     VAL A   518                                                      
REMARK 465     PRO A   519                                                      
REMARK 465     MET A   520                                                      
REMARK 465     ASN A   521                                                      
REMARK 465     ASN A   522                                                      
REMARK 465     GLY A   523                                                      
REMARK 465     VAL A   524                                                      
REMARK 465     SER A   525                                                      
REMARK 465     GLN A   526                                                      
REMARK 465     SER A   527                                                      
REMARK 465     SER A   528                                                      
REMARK 465     GLU A   529                                                      
REMARK 465     ASP A   530                                                      
REMARK 465     GLU A   531                                                      
REMARK 465     ASN A   532                                                      
REMARK 465     ALA A   533                                                      
REMARK 465     GLY A   602                                                      
REMARK 465     PRO A   603                                                      
REMARK 465     ASP A   604                                                      
REMARK 465     GLY A   605                                                      
REMARK 465      DG C    12                                                      
REMARK 465      DT C    13                                                      
REMARK 465      DA C    14                                                      
REMARK 465      DT C    15                                                      
REMARK 465      DA D     1                                                      
REMARK 465      DC D     2                                                      
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 397   CB    CYS A 397   SG      0.107                       
REMARK 500     DA C   4   O3'    DC C   5   P      -0.096                       
REMARK 500     DC C   5   O3'    DT C   6   P      -0.092                       
REMARK 500     DC D   5   O3'    DT D   6   P      -0.131                       
REMARK 500     DT D   6   O3'    DG D   7   P      -0.081                       
REMARK 500     DG D   7   O3'    DA D   8   P      -0.087                       
REMARK 500     DA D   8   O3'    DG D   9   P      -0.080                       
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    ASP A 312   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    CYS A 397   CA  -  CB  -  SG  ANGL. DEV. =  13.6 DEGREES          
REMARK 500    CYS A 612   CA  -  CB  -  SG  ANGL. DEV. =   9.2 DEGREES          
REMARK 500     DT C   3   O3' -  P   -  O5' ANGL. DEV. = -12.3 DEGREES          
REMARK 500     DT C   6   O3' -  P   -  O5' ANGL. DEV. = -13.2 DEGREES          
REMARK 500     DA C   8   O4' -  C4' -  C3' ANGL. DEV. =  -2.9 DEGREES          
REMARK 500     DC C  10   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT D   6   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DG D   7   O5' -  P   -  OP1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DC D  12   O4' -  C1' -  N1  ANGL. DEV. =   2.2 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    ALA A 214      -71.30     78.35                                   
REMARK 500    THR A 228     -155.24   -104.76                                   
REMARK 500    ARG A 241      -93.58   -148.82                                   
REMARK 500    SER A 266      103.24    -55.21                                   
REMARK 500    SER A 267      -54.72    -22.46                                   
REMARK 500    PRO A 355       42.06    -76.96                                   
REMARK 500    CYS A 435      124.62    -36.47                                   
REMARK 500    LYS A 455       16.92   -144.52                                   
REMARK 500    ASN A 545     -156.03   -104.29                                   
REMARK 500    SER A 565      -49.66   -141.18                                   
REMARK 500    VAL A 607     -163.27     56.09                                   
REMARK 500    LYS A 608      150.56    177.80                                   
REMARK 500    CYS A 614      -68.66    -29.84                                   
REMARK 500    LYS A 621       -0.82     70.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    5CM C   7       -55.3      D          D   OUTSIDE RANGE           
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 804  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 395   SG                                                     
REMARK 620 2 CYS A 383   SG  114.5                                              
REMARK 620 3 CYS A 389   SG  108.9 118.5                                        
REMARK 620 4 CYS A 385   SG   94.5 101.2 116.7                                  
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 425   SG                                                     
REMARK 620 2 CYS A 431   SG  128.5                                              
REMARK 620 3 CYS A 435   SG  116.8 105.4                                        
REMARK 620 4 CYS A 389   SG   99.5 110.4  88.2                                  
REMARK 620 N                    1     2     3                                   
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 429   SG                                                     
REMARK 620 2 CYS A 383   SG  102.8                                              
REMARK 620 3 CYS A 425   SG  115.7 118.7                                        
REMARK 620 4 CYS A 397   SG   93.1 143.5  81.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 805  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 612   SG                                                     
REMARK 620 2 CYS A 619   SG  109.7                                              
REMARK 620 3 CYS A 614   SG   96.8 134.1                                        
REMARK 620 4 CYS A 554   SG  110.9 117.2  84.9                                  
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 SAH 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                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 805                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QEN   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX MCHH DNA AND SAH.                        
REMARK 900 RELATED ID: 4QEO   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX MCHH DNA, H3(1-15) PEPTIDE AND           
REMARK 900 SAH.                                                                 
DBREF  4QEP A   93   624  UNP    Q8GZB6   SUVH4_ARATH     93    624             
DBREF  4QEP C    1    15  PDB    4QEP     4QEP             1     15             
DBREF  4QEP D    1    15  PDB    4QEP     4QEP             1     15             
SEQADV 4QEP SER A   92  UNP  Q8GZB6              EXPRESSION TAG                 
SEQRES   1 A  533  SER ASN GLY LYS ASP VAL ASN LEU GLU PRO HIS LEU LYS          
SEQRES   2 A  533  VAL THR LYS CYS LEU ARG LEU PHE ASN LYS GLN TYR LEU          
SEQRES   3 A  533  LEU CYS VAL GLN ALA LYS LEU SER ARG PRO ASP LEU LYS          
SEQRES   4 A  533  GLY VAL THR GLU MET ILE LYS ALA LYS ALA ILE LEU TYR          
SEQRES   5 A  533  PRO ARG LYS ILE ILE GLY ASP LEU PRO GLY ILE ASP VAL          
SEQRES   6 A  533  GLY HIS ARG PHE PHE SER ARG ALA GLU MET CYS ALA VAL          
SEQRES   7 A  533  GLY PHE HIS ASN HIS TRP LEU ASN GLY ILE ASP TYR MET          
SEQRES   8 A  533  SER MET GLU TYR GLU LYS GLU TYR SER ASN TYR LYS LEU          
SEQRES   9 A  533  PRO LEU ALA VAL SER ILE VAL MET SER GLY GLN TYR GLU          
SEQRES  10 A  533  ASP ASP LEU ASP ASN ALA ASP THR VAL THR TYR THR GLY          
SEQRES  11 A  533  GLN GLY GLY HIS ASN LEU THR GLY ASN LYS ARG GLN ILE          
SEQRES  12 A  533  LYS ASP GLN LEU LEU GLU ARG GLY ASN LEU ALA LEU LYS          
SEQRES  13 A  533  HIS CYS CYS GLU TYR ASN VAL PRO VAL ARG VAL THR ARG          
SEQRES  14 A  533  GLY HIS ASN CYS LYS SER SER TYR THR LYS ARG VAL TYR          
SEQRES  15 A  533  THR TYR ASP GLY LEU TYR LYS VAL GLU LYS PHE TRP ALA          
SEQRES  16 A  533  GLN LYS GLY VAL SER GLY PHE THR VAL TYR LYS TYR ARG          
SEQRES  17 A  533  LEU LYS ARG LEU GLU GLY GLN PRO GLU LEU THR THR ASP          
SEQRES  18 A  533  GLN VAL ASN PHE VAL ALA GLY ARG ILE PRO THR SER THR          
SEQRES  19 A  533  SER GLU ILE GLU GLY LEU VAL CYS GLU ASP ILE SER GLY          
SEQRES  20 A  533  GLY LEU GLU PHE LYS GLY ILE PRO ALA THR ASN ARG VAL          
SEQRES  21 A  533  ASP ASP SER PRO VAL SER PRO THR SER GLY PHE THR TYR          
SEQRES  22 A  533  ILE LYS SER LEU ILE ILE GLU PRO ASN VAL ILE ILE PRO          
SEQRES  23 A  533  LYS SER SER THR GLY CYS ASN CYS ARG GLY SER CYS THR          
SEQRES  24 A  533  ASP SER LYS LYS CYS ALA CYS ALA LYS LEU ASN GLY GLY          
SEQRES  25 A  533  ASN PHE PRO TYR VAL ASP LEU ASN ASP GLY ARG LEU ILE          
SEQRES  26 A  533  GLU SER ARG ASP VAL VAL PHE GLU CYS GLY PRO HIS CYS          
SEQRES  27 A  533  GLY CYS GLY PRO LYS CYS VAL ASN ARG THR SER GLN LYS          
SEQRES  28 A  533  ARG LEU ARG PHE ASN LEU GLU VAL PHE ARG SER ALA LYS          
SEQRES  29 A  533  LYS GLY TRP ALA VAL ARG SER TRP GLU TYR ILE PRO ALA          
SEQRES  30 A  533  GLY SER PRO VAL CYS GLU TYR ILE GLY VAL VAL ARG ARG          
SEQRES  31 A  533  THR ALA ASP VAL ASP THR ILE SER ASP ASN GLU TYR ILE          
SEQRES  32 A  533  PHE GLU ILE ASP CYS GLN GLN THR MET GLN GLY LEU GLY          
SEQRES  33 A  533  GLY ARG GLN ARG ARG LEU ARG ASP VAL ALA VAL PRO MET          
SEQRES  34 A  533  ASN ASN GLY VAL SER GLN SER SER GLU ASP GLU ASN ALA          
SEQRES  35 A  533  PRO GLU PHE CYS ILE ASP ALA GLY SER THR GLY ASN PHE          
SEQRES  36 A  533  ALA ARG PHE ILE ASN HIS SER CYS GLU PRO ASN LEU PHE          
SEQRES  37 A  533  VAL GLN CYS VAL LEU SER SER HIS GLN ASP ILE ARG LEU          
SEQRES  38 A  533  ALA ARG VAL VAL LEU PHE ALA ALA ASP ASN ILE SER PRO          
SEQRES  39 A  533  MET GLN GLU LEU THR TYR ASP TYR GLY TYR ALA LEU ASP          
SEQRES  40 A  533  SER VAL HIS GLY PRO ASP GLY LYS VAL LYS GLN LEU ALA          
SEQRES  41 A  533  CYS TYR CYS GLY ALA LEU ASN CYS ARG LYS ARG LEU TYR          
SEQRES   1 C   15   DG  DG  DT  DA  DC  DT 5CM  DA  DG  DC  DA  DG  DT          
SEQRES   2 C   15   DA  DT                                                      
SEQRES   1 D   15   DA  DC  DT  DG  DC  DT  DG  DA  DG  DT  DA  DC  DC          
SEQRES   2 D   15   DA  DT                                                      
MODRES 4QEP 5CM C    7   DC                                                     
HET    5CM  C   7      20                                                       
HET    SAH  A 801      26                                                       
HET     ZN  A 802       1                                                       
HET     ZN  A 803       1                                                       
HET     ZN  A 804       1                                                       
HET     ZN  A 805       1                                                       
HETNAM     5CM 5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE                      
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM      ZN ZINC ION                                                         
FORMUL   2  5CM    C10 H16 N3 O7 P                                              
FORMUL   4  SAH    C14 H20 N6 O5 S                                              
FORMUL   5   ZN    4(ZN 2+)                                                     
HELIX    1   1 GLU A  100  ALA A  122  1                                  23    
HELIX    2   2 ARG A  126  ALA A  138  1                                  13    
HELIX    3   3 SER A  162  VAL A  169  1                                   8    
HELIX    4   4 SER A  183  GLU A  187  5                                   5    
HELIX    5   5 ARG A  241  ASN A  253  1                                  13    
HELIX    6   6 CYS A  395  ASN A  401  1                                   7    
HELIX    7   7 CYS A  435  LYS A  442  5                                   8    
HELIX    8   8 ALA A  483  VAL A  485  5                                   3    
HELIX    9   9 ASN A  545  ILE A  550  5                                   6    
HELIX   10  10 ASP A  569  ALA A  573  5                                   5    
SHEET    1   A 5 ARG A 159  PHE A 160  0                                        
SHEET    2   A 5 ARG A 271  LYS A 288 -1  O  TYR A 273   N  PHE A 160           
SHEET    3   A 5 VAL A 256  ASN A 263 -1  N  VAL A 256   O  TYR A 279           
SHEET    4   A 5 LEU A 197  MET A 203  1  N  VAL A 199   O  ARG A 257           
SHEET    5   A 5 ILE A 179  MET A 182 -1  N  ASP A 180   O  SER A 200           
SHEET    1   B 5 ARG A 159  PHE A 160  0                                        
SHEET    2   B 5 ARG A 271  LYS A 288 -1  O  TYR A 273   N  PHE A 160           
SHEET    3   B 5 THR A 294  ARG A 302 -1  O  VAL A 295   N  GLN A 287           
SHEET    4   B 5 THR A 216  THR A 220 -1  N  TYR A 219   O  TYR A 298           
SHEET    5   B 5 LEU A 211  ASP A 212 -1  N  LEU A 211   O  THR A 218           
SHEET    1   C 4 LEU A 331  CYS A 333  0                                        
SHEET    2   C 4 ALA A 347  THR A 348 -1  O  ALA A 347   N  VAL A 332           
SHEET    3   C 4 LEU A 448  ARG A 452  1  O  ARG A 452   N  THR A 348           
SHEET    4   C 4 TRP A 458  SER A 462 -1  O  ARG A 461   N  GLU A 449           
SHEET    1   D 2 THR A 363  TYR A 364  0                                        
SHEET    2   D 2 THR A 543  GLY A 544  1  O  GLY A 544   N  THR A 363           
SHEET    1   E 4 ILE A 369  ILE A 370  0                                        
SHEET    2   E 4 VAL A 478  ARG A 481  1  O  VAL A 479   N  ILE A 369           
SHEET    3   E 4 PHE A 536  ASP A 539 -1  O  ASP A 539   N  VAL A 478           
SHEET    4   E 4 ILE A 494  GLU A 496 -1  N  PHE A 495   O  ILE A 538           
SHEET    1   F 2 TYR A 407  VAL A 408  0                                        
SHEET    2   F 2 ARG A 414  LEU A 415 -1  O  ARG A 414   N  VAL A 408           
SHEET    1   G 4 VAL A 421  PHE A 423  0                                        
SHEET    2   G 4 LEU A 558  LEU A 564  1  O  LEU A 564   N  VAL A 422           
SHEET    3   G 4 ARG A 574  ALA A 579 -1  O  VAL A 576   N  GLN A 561           
SHEET    4   G 4 PRO A 471  GLU A 474 -1  N  CYS A 473   O  LEU A 577           
SHEET    1   H 2 ASN A 551  HIS A 552  0                                        
SHEET    2   H 2 THR A 590  TYR A 591  1  O  TYR A 591   N  ASN A 551           
LINK         O3'  DT C   6                 P   5CM C   7     1555   1555  1.52  
LINK         O3' 5CM C   7                 P    DA C   8     1555   1555  1.61  
LINK         SG  CYS A 395                ZN    ZN A 804     1555   1555  2.11  
LINK         SG  CYS A 425                ZN    ZN A 803     1555   1555  2.17  
LINK         SG  CYS A 431                ZN    ZN A 803     1555   1555  2.22  
LINK         SG  CYS A 435                ZN    ZN A 803     1555   1555  2.28  
LINK         SG  CYS A 429                ZN    ZN A 802     1555   1555  2.32  
LINK         SG  CYS A 383                ZN    ZN A 804     1555   1555  2.36  
LINK         SG  CYS A 612                ZN    ZN A 805     1555   1555  2.37  
LINK         SG  CYS A 389                ZN    ZN A 804     1555   1555  2.37  
LINK         SG  CYS A 389                ZN    ZN A 803     1555   1555  2.38  
LINK         SG  CYS A 383                ZN    ZN A 802     1555   1555  2.40  
LINK         SG  CYS A 619                ZN    ZN A 805     1555   1555  2.41  
LINK         SG  CYS A 385                ZN    ZN A 804     1555   1555  2.46  
LINK         SG  CYS A 425                ZN    ZN A 802     1555   1555  2.57  
LINK         SG  CYS A 397                ZN    ZN A 802     1555   1555  2.60  
LINK         SG  CYS A 614                ZN    ZN A 805     1555   1555  2.73  
LINK         SG  CYS A 554                ZN    ZN A 805     1555   1555  2.75  
CISPEP   1 LEU A  195    PRO A  196          0         3.20                     
SITE     1 AC1 10 LYS A 456  GLY A 457  TRP A 458  TYR A 493                    
SITE     2 AC1 10 ARG A 548  ASN A 551  HIS A 552  TYR A 593                    
SITE     3 AC1 10 CYS A 612  TYR A 613                                          
SITE     1 AC2  5 CYS A 383  CYS A 397  CYS A 425  CYS A 429                    
SITE     2 AC2  5  ZN A 804                                                     
SITE     1 AC3  4 CYS A 389  CYS A 425  CYS A 431  CYS A 435                    
SITE     1 AC4  5 CYS A 383  CYS A 385  CYS A 389  CYS A 395                    
SITE     2 AC4  5  ZN A 802                                                     
SITE     1 AC5  4 CYS A 554  CYS A 612  CYS A 614  CYS A 619                    
CRYST1   54.346   95.569  121.754  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      0.018401  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010464  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008213        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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