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Database: PDB
Entry: 4U7P
LinkDB: 4U7P
Original site: 4U7P 
HEADER    TRANSFERASE/TRANSFERASE REGULATOR       31-JUL-14   4U7P              
TITLE     CRYSTAL STRUCTURE OF DNMT3A-DNMT3L COMPLEX                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3A;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 455-912;                                      
COMPND   5 SYNONYM: DNA METHYLTRANSFERASES DNMT3A;                              
COMPND   6 EC: 2.1.1.37;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3-LIKE;                 
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 178-379;                                      
COMPND  12 SYNONYM: DNA METHYLTRANSFERASES DNMT3L;                              
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DNMT3A;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: DNMT3L;                                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DNA METHYLTRANSFERASE, AUTOINHIBITORY FORM, TRANSFERASE-TRANSFERASE   
KEYWDS   2 REGULATOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.WANG,X.GUO,J.LI,J.XIAO,X.YIN,S.HE,J.WANG,Y.XU                       
REVDAT   3   04-FEB-15 4U7P    1       JRNL                                     
REVDAT   2   17-DEC-14 4U7P    1       JRNL                                     
REVDAT   1   12-NOV-14 4U7P    0                                                
JRNL        AUTH   X.GUO,L.WANG,J.LI,Z.DING,J.XIAO,X.YIN,S.HE,P.SHI,L.DONG,     
JRNL        AUTH 2 G.LI,C.TIAN,J.WANG,Y.CONG,Y.XU                               
JRNL        TITL   STRUCTURAL INSIGHT INTO AUTOINHIBITION AND HISTONE           
JRNL        TITL 2 H3-INDUCED ACTIVATION OF DNMT3A                              
JRNL        REF    NATURE                        V. 517   640 2015              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   25383530                                                     
JRNL        DOI    10.1038/NATURE13899                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.01                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 13977                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1392                            
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 42.0077 -  9.3907    0.99     1540   171  0.2032 0.2412        
REMARK   3     2  9.3907 -  7.4674    1.00     1567   177  0.2051 0.2253        
REMARK   3     3  7.4674 -  6.5274    1.00     1597   136  0.2169 0.2477        
REMARK   3     4  6.5274 -  5.9324    1.00     1562   168  0.2082 0.2411        
REMARK   3     5  5.9324 -  5.5082    1.00     1551   185  0.1918 0.2509        
REMARK   3     6  5.5082 -  5.1841    1.00     1561   169  0.1960 0.2697        
REMARK   3     7  5.1841 -  4.9249    0.99     1554   151  0.1939 0.2431        
REMARK   3     8  4.9249 -  4.7108    0.97     1498   167  0.2001 0.2229        
REMARK   3     9  4.7108 -  4.5296    0.80     1224   160  0.2253 0.2927        
REMARK   3    10  4.5296 -  4.3735    0.56      885    98  0.2471 0.3362        
REMARK   3    11  4.3735 -  4.2369    0.54      817    99  0.2589 0.2981        
REMARK   3    12  4.2369 -  4.1159    0.53      829    96  0.2748 0.3589        
REMARK   3    13  4.1159 -  4.0076    0.53      817    92  0.3009 0.3499        
REMARK   3    14  4.0076 -  3.9099    0.52      802   102  0.3167 0.3183        
REMARK   3    15  3.9099 -  3.8211    0.45      720    65  0.3248 0.3406        
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)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.850           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.31                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.33                          
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      :  0.006           5218                                  
REMARK   3   ANGLE     :  0.977           7072                                  
REMARK   3   CHIRALITY :  0.036            744                                  
REMARK   3   PLANARITY :  0.005            916                                  
REMARK   3   DIHEDRAL  : 14.243           1944                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4U7P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202950.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6-6.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2816                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
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   : 14153                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.87000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2QRV, 3A1A                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M BIS-TRIS, 0.1M SODIUM MALONATE,    
REMARK 280  8% PEG3350, PH 5.6, VAPOR DIFFUSION, TEMPERATURE 291K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       37.66800            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       37.66800            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       37.66800            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       37.66800            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       37.66800            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       37.66800            
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: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   447                                                      
REMARK 465     PRO A   448                                                      
REMARK 465     LEU A   449                                                      
REMARK 465     GLY A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     PRO A   452                                                      
REMARK 465     GLU A   453                                                      
REMARK 465     PHE A   454                                                      
REMARK 465     LYS A   455                                                      
REMARK 465     LYS A   456                                                      
REMARK 465     PRO A   457                                                      
REMARK 465     ARG A   458                                                      
REMARK 465     LYS A   459                                                      
REMARK 465     SER A   460                                                      
REMARK 465     THR A   461                                                      
REMARK 465     ALA A   462                                                      
REMARK 465     GLU A   463                                                      
REMARK 465     LYS A   464                                                      
REMARK 465     PRO A   465                                                      
REMARK 465     LYS A   466                                                      
REMARK 465     VAL A   467                                                      
REMARK 465     LYS A   468                                                      
REMARK 465     GLU A   469                                                      
REMARK 465     ILE A   470                                                      
REMARK 465     ILE A   471                                                      
REMARK 465     ASP A   472                                                      
REMARK 465     GLU A   473                                                      
REMARK 465     ILE A   833                                                      
REMARK 465     THR A   834                                                      
REMARK 465     THR A   835                                                      
REMARK 465     ARG A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     ASN A   838                                                      
REMARK 465     SER A   839                                                      
REMARK 465     ILE A   840                                                      
REMARK 465     LYS A   841                                                      
REMARK 465     GLN A   842                                                      
REMARK 465     GLY A   843                                                      
REMARK 465     LYS A   844                                                      
REMARK 465     ASP A   845                                                      
REMARK 465     GLY B   171                                                      
REMARK 465     PRO B   172                                                      
REMARK 465     LEU B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     SER B   175                                                      
REMARK 465     GLU B   176                                                      
REMARK 465     PHE B   177                                                      
REMARK 465     MET B   178                                                      
REMARK 465     LYS B   354                                                      
REMARK 465     LEU B   355                                                      
REMARK 465     ALA B   356                                                      
REMARK 465     SER B   379                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    TYR A   528     OG   SER A   535              2.04            
REMARK 500   NZ   LYS B   376     O    PHE B   378              2.13            
REMARK 500   OE2  GLU A   733     NH1  ARG A   736              2.19            
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    SER A 496      -72.90    -84.64                                   
REMARK 500    SER A 535      -23.65     64.03                                   
REMARK 500    TYR A 536     -134.56     40.54                                   
REMARK 500    CYS A 541       19.43     58.90                                   
REMARK 500    ARG A 544      -72.52   -110.85                                   
REMARK 500    CYS A 554      -71.20   -119.71                                   
REMARK 500    LYS A 577       -4.58     82.09                                   
REMARK 500    ASP A 618       79.76     52.26                                   
REMARK 500    PHE A 640       71.89     53.42                                   
REMARK 500    ALA A 644       59.80    -63.12                                   
REMARK 500    VAL A 665      -62.04   -105.14                                   
REMARK 500    CYS A 666      105.93    -45.01                                   
REMARK 500    HIS A 677       10.76   -142.38                                   
REMARK 500    CYS A 710      -76.93    -88.54                                   
REMARK 500    ASN A 711     -108.93     50.11                                   
REMARK 500    ASP A 712       -6.41    -57.63                                   
REMARK 500    ARG A 729      -38.38    -35.20                                   
REMARK 500    VAL A 785      -14.12   -144.26                                   
REMARK 500    ARG A 831      -66.22   -130.79                                   
REMARK 500    HIS A 847      -73.72    -76.74                                   
REMARK 500    SER A 878     -150.62     57.13                                   
REMARK 500    PRO B 183      153.18    -49.72                                   
REMARK 500    ARG B 186       -6.54   -146.23                                   
REMARK 500    PHE B 196      -31.65     63.90                                   
REMARK 500    GLU B 210      -77.90    -82.26                                   
REMARK 500    SER B 211      176.47    174.10                                   
REMARK 500    SER B 213      -62.57   -139.28                                   
REMARK 500    PRO B 215       63.86   -100.46                                   
REMARK 500    VAL B 224       31.44    -95.43                                   
REMARK 500    ASP B 226       63.36   -114.62                                   
REMARK 500    TRP B 235       23.86    -75.13                                   
REMARK 500    THR B 251     -141.30     48.02                                   
REMARK 500    CYS B 252      -64.25   -132.63                                   
REMARK 500    ASP B 253     -114.87     57.10                                   
REMARK 500    ASN B 287       55.09   -101.93                                   
REMARK 500    LEU B 317       87.62    -64.75                                   
REMARK 500    ILE B 330      -55.59   -135.07                                   
REMARK 500    ARG B 333      -88.60   -121.08                                   
REMARK 500    HIS B 334      -21.58     57.74                                   
REMARK 500    TRP B 335     -156.89     43.71                                   
REMARK 500    ALA B 336      -63.17   -145.96                                   
REMARK 500    GLN B 351      -74.47   -121.34                                   
REMARK 500    PRO B 370        9.25    -69.14                                   
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 A1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 494   SG                                                     
REMARK 620 2 CYS A 497   SG  119.6                                              
REMARK 620 3 CYS A 514   SG  116.3 118.8                                        
REMARK 620 4 CYS A 517   SG  101.3  98.2  93.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 537   SG                                                     
REMARK 620 2 CYS A 540   SG  106.1                                              
REMARK 620 3 CYS A 559   SG   96.8 135.2                                        
REMARK 620 4 CYS A 562   SG  118.5 109.7  91.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 549   SG                                                     
REMARK 620 2 CYS A 554   SG  115.7                                              
REMARK 620 3 CYS A 583   SG  111.0 112.6                                        
REMARK 620 4 CYS A 586   SG  107.0  86.4 122.4                                  
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 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 1004                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4U7T   RELATED DB: PDB                                   
DBREF  4U7P A  455   912  UNP    Q9Y6K1   DNM3A_HUMAN    455    912             
DBREF  4U7P B  178   379  UNP    Q9UJW3   DNM3L_HUMAN    178    379             
SEQADV 4U7P GLY A  447  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7P PRO A  448  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7P LEU A  449  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7P GLY A  450  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7P SER A  451  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7P PRO A  452  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7P GLU A  453  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7P PHE A  454  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7P GLY B  171  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7P PRO B  172  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7P LEU B  173  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7P GLY B  174  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7P SER B  175  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7P GLU B  176  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7P PHE B  177  UNP  Q9UJW3              EXPRESSION TAG                 
SEQRES   1 A  466  GLY PRO LEU GLY SER PRO GLU PHE LYS LYS PRO ARG LYS          
SEQRES   2 A  466  SER THR ALA GLU LYS PRO LYS VAL LYS GLU ILE ILE ASP          
SEQRES   3 A  466  GLU ARG THR ARG GLU ARG LEU VAL TYR GLU VAL ARG GLN          
SEQRES   4 A  466  LYS CYS ARG ASN ILE GLU ASP ILE CYS ILE SER CYS GLY          
SEQRES   5 A  466  SER LEU ASN VAL THR LEU GLU HIS PRO LEU PHE VAL GLY          
SEQRES   6 A  466  GLY MET CYS GLN ASN CYS LYS ASN CYS PHE LEU GLU CYS          
SEQRES   7 A  466  ALA TYR GLN TYR ASP ASP ASP GLY TYR GLN SER TYR CYS          
SEQRES   8 A  466  THR ILE CYS CYS GLY GLY ARG GLU VAL LEU MET CYS GLY          
SEQRES   9 A  466  ASN ASN ASN CYS CYS ARG CYS PHE CYS VAL GLU CYS VAL          
SEQRES  10 A  466  ASP LEU LEU VAL GLY PRO GLY ALA ALA GLN ALA ALA ILE          
SEQRES  11 A  466  LYS GLU ASP PRO TRP ASN CYS TYR MET CYS GLY HIS LYS          
SEQRES  12 A  466  GLY THR TYR GLY LEU LEU ARG ARG ARG GLU ASP TRP PRO          
SEQRES  13 A  466  SER ARG LEU GLN MET PHE PHE ALA ASN ASN HIS ASP GLN          
SEQRES  14 A  466  GLU PHE ASP PRO PRO LYS VAL TYR PRO PRO VAL PRO ALA          
SEQRES  15 A  466  GLU LYS ARG LYS PRO ILE ARG VAL LEU SER LEU PHE ASP          
SEQRES  16 A  466  GLY ILE ALA THR GLY LEU LEU VAL LEU LYS ASP LEU GLY          
SEQRES  17 A  466  ILE GLN VAL ASP ARG TYR ILE ALA SER GLU VAL CYS GLU          
SEQRES  18 A  466  ASP SER ILE THR VAL GLY MET VAL ARG HIS GLN GLY LYS          
SEQRES  19 A  466  ILE MET TYR VAL GLY ASP VAL ARG SER VAL THR GLN LYS          
SEQRES  20 A  466  HIS ILE GLN GLU TRP GLY PRO PHE ASP LEU VAL ILE GLY          
SEQRES  21 A  466  GLY SER PRO CYS ASN ASP LEU SER ILE VAL ASN PRO ALA          
SEQRES  22 A  466  ARG LYS GLY LEU TYR GLU GLY THR GLY ARG LEU PHE PHE          
SEQRES  23 A  466  GLU PHE TYR ARG LEU LEU HIS ASP ALA ARG PRO LYS GLU          
SEQRES  24 A  466  GLY ASP ASP ARG PRO PHE PHE TRP LEU PHE GLU ASN VAL          
SEQRES  25 A  466  VAL ALA MET GLY VAL SER ASP LYS ARG ASP ILE SER ARG          
SEQRES  26 A  466  PHE LEU GLU SER ASN PRO VAL MET ILE ASP ALA LYS GLU          
SEQRES  27 A  466  VAL SER ALA ALA HIS ARG ALA ARG TYR PHE TRP GLY ASN          
SEQRES  28 A  466  LEU PRO GLY MET ASN ARG PRO LEU ALA SER THR VAL ASN          
SEQRES  29 A  466  ASP LYS LEU GLU LEU GLN GLU CYS LEU GLU HIS GLY ARG          
SEQRES  30 A  466  ILE ALA LYS PHE SER LYS VAL ARG THR ILE THR THR ARG          
SEQRES  31 A  466  SER ASN SER ILE LYS GLN GLY LYS ASP GLN HIS PHE PRO          
SEQRES  32 A  466  VAL PHE MET ASN GLU LYS GLU ASP ILE LEU TRP CYS THR          
SEQRES  33 A  466  GLU MET GLU ARG VAL PHE GLY PHE PRO VAL HIS TYR THR          
SEQRES  34 A  466  ASP VAL SER ASN MET SER ARG LEU ALA ARG GLN ARG LEU          
SEQRES  35 A  466  LEU GLY ARG SER TRP SER VAL PRO VAL ILE ARG HIS LEU          
SEQRES  36 A  466  PHE ALA PRO LEU LYS GLU TYR PHE ALA CYS VAL                  
SEQRES   1 B  209  GLY PRO LEU GLY SER GLU PHE MET PHE GLU THR VAL PRO          
SEQRES   2 B  209  VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU PHE          
SEQRES   3 B  209  GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE LEU          
SEQRES   4 B  209  GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL VAL          
SEQRES   5 B  209  ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU TRP          
SEQRES   6 B  209  GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO LEU          
SEQRES   7 B  209  GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU PHE          
SEQRES   8 B  209  GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS PRO          
SEQRES   9 B  209  GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP ASN          
SEQRES  10 B  209  LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER ARG          
SEQRES  11 B  209  PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL HIS          
SEQRES  12 B  209  GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER ASN          
SEQRES  13 B  209  ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL SER          
SEQRES  14 B  209  GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN SER          
SEQRES  15 B  209  SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL LYS          
SEQRES  16 B  209  ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR PHE          
SEQRES  17 B  209  SER                                                          
HET     ZN  A1001       1                                                       
HET     ZN  A1002       1                                                       
HET     ZN  A1003       1                                                       
HET    SAH  A1004      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   3   ZN    3(ZN 2+)                                                     
FORMUL   6  SAH    C14 H20 N6 O5 S                                              
HELIX    1 AA1 ARG A  474  GLN A  485  1                                  12    
HELIX    2 AA2 ASN A  489  ILE A  493  5                                   5    
HELIX    3 AA3 CYS A  514  TYR A  528  1                                  15    
HELIX    4 AA4 VAL A  560  VAL A  567  1                                   8    
HELIX    5 AA5 GLY A  570  ILE A  576  1                                   7    
HELIX    6 AA6 ASP A  600  PHE A  609  1                                  10    
HELIX    7 AA7 ALA A  644  GLY A  654  1                                  11    
HELIX    8 AA8 CYS A  666  HIS A  677  1                                  12    
HELIX    9 AA9 THR A  691  TRP A  698  1                                   8    
HELIX   10 AB1 CYS A  710  SER A  714  5                                   5    
HELIX   11 AB2 ARG A  729  ASP A  740  1                                  12    
HELIX   12 AB3 GLY A  762  GLU A  774  1                                  13    
HELIX   13 AB4 LYS A  783  VAL A  785  5                                   3    
HELIX   14 AB5 GLU A  814  CYS A  818  5                                   5    
HELIX   15 AB6 TRP A  860  GLY A  869  1                                  10    
HELIX   16 AB7 SER A  881  ARG A  891  1                                  11    
HELIX   17 AB8 SER A  894  PHE A  902  1                                   9    
HELIX   18 AB9 ALA A  903  LYS A  906  5                                   4    
HELIX   19 AC1 PRO B  183  ARG B  187  5                                   5    
HELIX   20 AC2 ILE B  199  LEU B  206  1                                   8    
HELIX   21 AC3 ASP B  223  THR B  227  5                                   5    
HELIX   22 AC4 VAL B  228  TRP B  235  1                                   8    
HELIX   23 AC5 PRO B  255  ARG B  271  1                                  17    
HELIX   24 AC6 ASN B  291  LEU B  302  1                                  12    
HELIX   25 AC7 SER B  339  LYS B  350  1                                  12    
HELIX   26 AC8 THR B  361  ASN B  366  1                                   6    
HELIX   27 AC9 CYS B  367  TYR B  374  5                                   8    
SHEET    1 AA1 2 LEU A 504  GLU A 505  0                                        
SHEET    2 AA1 2 GLY A 512  MET A 513 -1  O  MET A 513   N  LEU A 504           
SHEET    1 AA2 2 VAL A 546  MET A 548  0                                        
SHEET    2 AA2 2 CYS A 557  CYS A 559 -1  O  PHE A 558   N  LEU A 547           
SHEET    1 AA3 2 THR A 591  TYR A 592  0                                        
SHEET    2 AA3 2 LEU A 595  ARG A 596 -1  O  LEU A 595   N  TYR A 592           
SHEET    1 AA4 7 ILE A 681  VAL A 684  0                                        
SHEET    2 AA4 7 VAL A 657  SER A 663  1  N  TYR A 660   O  MET A 682           
SHEET    3 AA4 7 ILE A 634  LEU A 639  1  N  SER A 638   O  SER A 663           
SHEET    4 AA4 7 LEU A 703  GLY A 707  1  O  LEU A 703   N  LEU A 637           
SHEET    5 AA4 7 PHE A 752  VAL A 758  1  O  PHE A 752   N  VAL A 704           
SHEET    6 AA4 7 ALA A 791  GLY A 796 -1  O  TRP A 795   N  PHE A 755           
SHEET    7 AA4 7 VAL A 778  ASP A 781 -1  N  ILE A 780   O  ARG A 792           
SHEET    1 AA5 3 ILE A 824  ALA A 825  0                                        
SHEET    2 AA5 3 VAL A 850  PHE A 851 -1  O  PHE A 851   N  ILE A 824           
SHEET    3 AA5 3 GLU A 856  ASP A 857 -1  O  ASP A 857   N  VAL A 850           
SHEET    1 AA6 6 LEU B 218  VAL B 221  0                                        
SHEET    2 AA6 6 VAL B 192  LEU B 195  1  N  VAL B 192   O  LYS B 219           
SHEET    3 AA6 6 LEU B 240  ALA B 244  1  O  TYR B 242   N  LEU B 195           
SHEET    4 AA6 6 PHE B 281  ASP B 286  1  O  MET B 283   N  VAL B 241           
SHEET    5 AA6 6 LEU B 317  SER B 325 -1  O  TRP B 324   N  PHE B 284           
SHEET    6 AA6 6 VAL B 307  VAL B 312 -1  N  VAL B 307   O  VAL B 323           
LINK         SG  CYS A 494                ZN    ZN A1002     1555   1555  2.37  
LINK         SG  CYS A 497                ZN    ZN A1002     1555   1555  2.35  
LINK         SG  CYS A 514                ZN    ZN A1002     1555   1555  2.26  
LINK         SG  CYS A 517                ZN    ZN A1002     1555   1555  2.17  
LINK         SG  CYS A 537                ZN    ZN A1001     1555   1555  2.39  
LINK         SG  CYS A 540                ZN    ZN A1001     1555   1555  2.22  
LINK         SG  CYS A 549                ZN    ZN A1003     1555   1555  2.44  
LINK         SG  CYS A 554                ZN    ZN A1003     1555   1555  2.36  
LINK         SG  CYS A 559                ZN    ZN A1001     1555   1555  2.32  
LINK         SG  CYS A 562                ZN    ZN A1001     1555   1555  2.38  
LINK         SG  CYS A 583                ZN    ZN A1003     1555   1555  2.27  
LINK         SG  CYS A 586                ZN    ZN A1003     1555   1555  2.28  
CISPEP   1 TYR A  536    CYS A  537          0        -3.92                     
CISPEP   2 GLU A  629    LYS A  630          0        -0.50                     
CISPEP   3 SER B  213    ASP B  214          0        11.08                     
CISPEP   4 PRO B  215    GLY B  216          0        -7.18                     
SITE     1 AC1  4 CYS A 537  CYS A 540  CYS A 559  CYS A 562                    
SITE     1 AC2  4 CYS A 494  CYS A 497  CYS A 514  CYS A 517                    
SITE     1 AC3  4 CYS A 549  CYS A 554  CYS A 583  CYS A 586                    
SITE     1 AC4 15 PHE A 640  ASP A 641  ILE A 643  THR A 645                    
SITE     2 AC4 15 GLU A 664  VAL A 665  CYS A 666  ASP A 686                    
SITE     3 AC4 15 VAL A 687  GLY A 707  PRO A 709  LEU A 730                    
SITE     4 AC4 15 ARG A 891  SER A 892  TRP A 893                               
CRYST1  252.031  252.031   75.336  90.00  90.00 120.00 P 63 2 2     12          
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      0.003968  0.002291  0.000000        0.00000                         
SCALE2      0.000000  0.004582  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013274        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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