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Database: PDB
Entry: 3LLR
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Original site: 3LLR 
HEADER    TRANSFERASE                             29-JAN-10   3LLR              
TITLE     CRYSTAL STRUCTURE OF THE PWWP DOMAIN OF HUMAN DNA (CYTOSINE-5-)-      
TITLE    2 METHYLTRANSFERASE 3 ALPHA                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3A;                     
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 FRAGMENT: PWWP DOMAIN (UNP RESIDUES 275-427);                        
COMPND   5 SYNONYM: DNMT3A, DNA METHYLTRANSFERASE HSAIIIA, DNA MTASE HSAIIIA,   
COMPND   6 M.HSAIIIA;                                                           
COMPND   7 EC: 2.1.1.37;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DNMT3A;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, DNA METHYLTRANSFERASE, METHYLYSINE BINDING, STRUCTURAL   
KEYWDS   2 GENOMICS CONSORTIUM, SGC, ALTERNATIVE PROMOTER USAGE, CHROMATIN      
KEYWDS   3 REGULATOR, DNA-BINDING, METAL-BINDING, METHYLTRANSFERASE, NUCLEUS,   
KEYWDS   4 PHOSPHOPROTEIN, REPRESSOR, S-ADENOSYL-L-METHIONINE, ZINC-FINGER      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.QIU,L.DOMBROVSKI,S.NI,J.WEIGELT,C.BOUTRA,C.H.ARROWSMITH,            
AUTHOR   2 A.M.EDWARDS,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)          
REVDAT   4   01-NOV-17 3LLR    1       REMARK                                   
REVDAT   3   28-MAR-12 3LLR    1       JRNL   VERSN                             
REVDAT   2   29-JUN-11 3LLR    1       JRNL                                     
REVDAT   1   23-MAR-10 3LLR    0                                                
JRNL        AUTH   H.WU,H.ZENG,R.LAM,W.TEMPEL,M.F.AMAYA,C.XU,L.DOMBROVSKI,      
JRNL        AUTH 2 W.QIU,Y.WANG,J.MIN                                           
JRNL        TITL   STRUCTURAL AND HISTONE BINDING ABILITY CHARACTERIZATIONS OF  
JRNL        TITL 2 HUMAN PWWP DOMAINS.                                          
JRNL        REF    PLOS ONE                      V.   6 18919 2011              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   21720545                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0018919                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 34711                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1819                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2523                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 121                          
REMARK   3   BIN FREE R VALUE                    : 0.3480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5340                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 75                                      
REMARK   3   SOLVENT ATOMS            : 362                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.360         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.245         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.160         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.372         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.908                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.883                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5632 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7617 ; 0.954 ; 1.939       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   675 ; 4.897 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   241 ;23.738 ;22.241       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   895 ;13.224 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;12.239 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   733 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4310 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3340 ; 0.379 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5328 ; 0.706 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2292 ; 0.681 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2282 ; 1.169 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3LLR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000057433.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36565                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.760                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07470                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.77                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.25590                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.160                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: 1KHC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 3,350, 0.1 M AMMONIUM SULFATE,   
REMARK 280  0.1M BISTRIS, PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       41.99500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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     0                                                      
REMARK 465     THR A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     VAL A   112                                                      
REMARK 465     CYS A   113                                                      
REMARK 465     HIS A   114                                                      
REMARK 465     ASP A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     ASP A   117                                                      
REMARK 465     GLU A   118                                                      
REMARK 465     SER A   119                                                      
REMARK 465     ASP A   120                                                      
REMARK 465     THR A   121                                                      
REMARK 465     ALA A   122                                                      
REMARK 465     LYS A   123                                                      
REMARK 465     GLU A   152                                                      
REMARK 465     GLU A   153                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     THR B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     VAL B   112                                                      
REMARK 465     CYS B   113                                                      
REMARK 465     HIS B   114                                                      
REMARK 465     ASP B   115                                                      
REMARK 465     SER B   116                                                      
REMARK 465     ASP B   117                                                      
REMARK 465     GLU B   118                                                      
REMARK 465     SER B   119                                                      
REMARK 465     ASP B   120                                                      
REMARK 465     THR B   121                                                      
REMARK 465     ALA B   122                                                      
REMARK 465     LYS B   123                                                      
REMARK 465     GLU B   152                                                      
REMARK 465     GLU B   153                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     THR C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     ASP C     5                                                      
REMARK 465     ASP C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     PRO C     8                                                      
REMARK 465     PRO C   111                                                      
REMARK 465     VAL C   112                                                      
REMARK 465     CYS C   113                                                      
REMARK 465     HIS C   114                                                      
REMARK 465     ASP C   115                                                      
REMARK 465     SER C   116                                                      
REMARK 465     ASP C   117                                                      
REMARK 465     GLU C   118                                                      
REMARK 465     SER C   119                                                      
REMARK 465     ASP C   120                                                      
REMARK 465     THR C   121                                                      
REMARK 465     ALA C   122                                                      
REMARK 465     GLU C   152                                                      
REMARK 465     GLU C   153                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     THR D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     GLY D     4                                                      
REMARK 465     ASP D     5                                                      
REMARK 465     ASP D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     GLU D   152                                                      
REMARK 465     GLU D   153                                                      
REMARK 465     GLY E     0                                                      
REMARK 465     THR E     1                                                      
REMARK 465     LYS E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     GLY E     4                                                      
REMARK 465     ASP E     5                                                      
REMARK 465     ASP E     6                                                      
REMARK 465     GLU E     7                                                      
REMARK 465     PRO E     8                                                      
REMARK 465     VAL E   112                                                      
REMARK 465     CYS E   113                                                      
REMARK 465     HIS E   114                                                      
REMARK 465     ASP E   115                                                      
REMARK 465     SER E   116                                                      
REMARK 465     ASP E   117                                                      
REMARK 465     GLU E   118                                                      
REMARK 465     SER E   119                                                      
REMARK 465     ASP E   120                                                      
REMARK 465     THR E   121                                                      
REMARK 465     GLU E   152                                                      
REMARK 465     GLU E   153                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO B   8    CB   CG   CD                                        
REMARK 470     LYS C 123    CG   CD   CE   NZ                                   
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    GLU A  11       59.12    -93.18                                   
REMARK 500    ARG A  44     -146.67   -133.22                                   
REMARK 500    SER A  75       31.83    -80.29                                   
REMARK 500    GLU B  11       64.88   -101.42                                   
REMARK 500    ARG B  44     -134.03   -118.72                                   
REMARK 500    SER B  75       34.83    -78.45                                   
REMARK 500    ARG C  44     -132.17   -115.07                                   
REMARK 500    SER C  75       44.70    -82.82                                   
REMARK 500    ARG D  44     -151.81   -111.82                                   
REMARK 500    SER D  75       37.73    -81.42                                   
REMARK 500    ARG E  27     -122.64     49.55                                   
REMARK 500    ARG E  44     -151.45   -103.31                                   
REMARK 500    SER E  75       35.85    -80.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB A 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB B 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB C 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB D 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB E 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 155                 
DBREF  3LLR A    1   153  UNP    Q9Y6K1   DNM3A_HUMAN    275    427             
DBREF  3LLR B    1   153  UNP    Q9Y6K1   DNM3A_HUMAN    275    427             
DBREF  3LLR C    1   153  UNP    Q9Y6K1   DNM3A_HUMAN    275    427             
DBREF  3LLR D    1   153  UNP    Q9Y6K1   DNM3A_HUMAN    275    427             
DBREF  3LLR E    1   153  UNP    Q9Y6K1   DNM3A_HUMAN    275    427             
SEQADV 3LLR GLY A    0  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 3LLR GLY B    0  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 3LLR GLY C    0  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 3LLR GLY D    0  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 3LLR GLY E    0  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQRES   1 A  154  GLY THR LYS ALA GLY ASP ASP GLU PRO GLU TYR GLU ASP          
SEQRES   2 A  154  GLY ARG GLY PHE GLY ILE GLY GLU LEU VAL TRP GLY LYS          
SEQRES   3 A  154  LEU ARG GLY PHE SER TRP TRP PRO GLY ARG ILE VAL SER          
SEQRES   4 A  154  TRP TRP MET THR GLY ARG SER ARG ALA ALA GLU GLY THR          
SEQRES   5 A  154  ARG TRP VAL MET TRP PHE GLY ASP GLY LYS PHE SER VAL          
SEQRES   6 A  154  VAL CYS VAL GLU LYS LEU MET PRO LEU SER SER PHE CYS          
SEQRES   7 A  154  SER ALA PHE HIS GLN ALA THR TYR ASN LYS GLN PRO MET          
SEQRES   8 A  154  TYR ARG LYS ALA ILE TYR GLU VAL LEU GLN VAL ALA SER          
SEQRES   9 A  154  SER ARG ALA GLY LYS LEU PHE PRO VAL CYS HIS ASP SER          
SEQRES  10 A  154  ASP GLU SER ASP THR ALA LYS ALA VAL GLU VAL GLN ASN          
SEQRES  11 A  154  LYS PRO MET ILE GLU TRP ALA LEU GLY GLY PHE GLN PRO          
SEQRES  12 A  154  SER GLY PRO LYS GLY LEU GLU PRO PRO GLU GLU                  
SEQRES   1 B  154  GLY THR LYS ALA GLY ASP ASP GLU PRO GLU TYR GLU ASP          
SEQRES   2 B  154  GLY ARG GLY PHE GLY ILE GLY GLU LEU VAL TRP GLY LYS          
SEQRES   3 B  154  LEU ARG GLY PHE SER TRP TRP PRO GLY ARG ILE VAL SER          
SEQRES   4 B  154  TRP TRP MET THR GLY ARG SER ARG ALA ALA GLU GLY THR          
SEQRES   5 B  154  ARG TRP VAL MET TRP PHE GLY ASP GLY LYS PHE SER VAL          
SEQRES   6 B  154  VAL CYS VAL GLU LYS LEU MET PRO LEU SER SER PHE CYS          
SEQRES   7 B  154  SER ALA PHE HIS GLN ALA THR TYR ASN LYS GLN PRO MET          
SEQRES   8 B  154  TYR ARG LYS ALA ILE TYR GLU VAL LEU GLN VAL ALA SER          
SEQRES   9 B  154  SER ARG ALA GLY LYS LEU PHE PRO VAL CYS HIS ASP SER          
SEQRES  10 B  154  ASP GLU SER ASP THR ALA LYS ALA VAL GLU VAL GLN ASN          
SEQRES  11 B  154  LYS PRO MET ILE GLU TRP ALA LEU GLY GLY PHE GLN PRO          
SEQRES  12 B  154  SER GLY PRO LYS GLY LEU GLU PRO PRO GLU GLU                  
SEQRES   1 C  154  GLY THR LYS ALA GLY ASP ASP GLU PRO GLU TYR GLU ASP          
SEQRES   2 C  154  GLY ARG GLY PHE GLY ILE GLY GLU LEU VAL TRP GLY LYS          
SEQRES   3 C  154  LEU ARG GLY PHE SER TRP TRP PRO GLY ARG ILE VAL SER          
SEQRES   4 C  154  TRP TRP MET THR GLY ARG SER ARG ALA ALA GLU GLY THR          
SEQRES   5 C  154  ARG TRP VAL MET TRP PHE GLY ASP GLY LYS PHE SER VAL          
SEQRES   6 C  154  VAL CYS VAL GLU LYS LEU MET PRO LEU SER SER PHE CYS          
SEQRES   7 C  154  SER ALA PHE HIS GLN ALA THR TYR ASN LYS GLN PRO MET          
SEQRES   8 C  154  TYR ARG LYS ALA ILE TYR GLU VAL LEU GLN VAL ALA SER          
SEQRES   9 C  154  SER ARG ALA GLY LYS LEU PHE PRO VAL CYS HIS ASP SER          
SEQRES  10 C  154  ASP GLU SER ASP THR ALA LYS ALA VAL GLU VAL GLN ASN          
SEQRES  11 C  154  LYS PRO MET ILE GLU TRP ALA LEU GLY GLY PHE GLN PRO          
SEQRES  12 C  154  SER GLY PRO LYS GLY LEU GLU PRO PRO GLU GLU                  
SEQRES   1 D  154  GLY THR LYS ALA GLY ASP ASP GLU PRO GLU TYR GLU ASP          
SEQRES   2 D  154  GLY ARG GLY PHE GLY ILE GLY GLU LEU VAL TRP GLY LYS          
SEQRES   3 D  154  LEU ARG GLY PHE SER TRP TRP PRO GLY ARG ILE VAL SER          
SEQRES   4 D  154  TRP TRP MET THR GLY ARG SER ARG ALA ALA GLU GLY THR          
SEQRES   5 D  154  ARG TRP VAL MET TRP PHE GLY ASP GLY LYS PHE SER VAL          
SEQRES   6 D  154  VAL CYS VAL GLU LYS LEU MET PRO LEU SER SER PHE CYS          
SEQRES   7 D  154  SER ALA PHE HIS GLN ALA THR TYR ASN LYS GLN PRO MET          
SEQRES   8 D  154  TYR ARG LYS ALA ILE TYR GLU VAL LEU GLN VAL ALA SER          
SEQRES   9 D  154  SER ARG ALA GLY LYS LEU PHE PRO VAL CYS HIS ASP SER          
SEQRES  10 D  154  ASP GLU SER ASP THR ALA LYS ALA VAL GLU VAL GLN ASN          
SEQRES  11 D  154  LYS PRO MET ILE GLU TRP ALA LEU GLY GLY PHE GLN PRO          
SEQRES  12 D  154  SER GLY PRO LYS GLY LEU GLU PRO PRO GLU GLU                  
SEQRES   1 E  154  GLY THR LYS ALA GLY ASP ASP GLU PRO GLU TYR GLU ASP          
SEQRES   2 E  154  GLY ARG GLY PHE GLY ILE GLY GLU LEU VAL TRP GLY LYS          
SEQRES   3 E  154  LEU ARG GLY PHE SER TRP TRP PRO GLY ARG ILE VAL SER          
SEQRES   4 E  154  TRP TRP MET THR GLY ARG SER ARG ALA ALA GLU GLY THR          
SEQRES   5 E  154  ARG TRP VAL MET TRP PHE GLY ASP GLY LYS PHE SER VAL          
SEQRES   6 E  154  VAL CYS VAL GLU LYS LEU MET PRO LEU SER SER PHE CYS          
SEQRES   7 E  154  SER ALA PHE HIS GLN ALA THR TYR ASN LYS GLN PRO MET          
SEQRES   8 E  154  TYR ARG LYS ALA ILE TYR GLU VAL LEU GLN VAL ALA SER          
SEQRES   9 E  154  SER ARG ALA GLY LYS LEU PHE PRO VAL CYS HIS ASP SER          
SEQRES  10 E  154  ASP GLU SER ASP THR ALA LYS ALA VAL GLU VAL GLN ASN          
SEQRES  11 E  154  LYS PRO MET ILE GLU TRP ALA LEU GLY GLY PHE GLN PRO          
SEQRES  12 E  154  SER GLY PRO LYS GLY LEU GLU PRO PRO GLU GLU                  
HET    BTB  A 154      14                                                       
HET    BTB  B 154      14                                                       
HET    SO4  B 155       5                                                       
HET    BTB  C 154      14                                                       
HET    BTB  D 154      14                                                       
HET    BTB  E 154      14                                                       
HETNAM     BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-                 
HETNAM   2 BTB  PROPANE-1,3-DIOL                                                
HETNAM     SO4 SULFATE ION                                                      
HETSYN     BTB BIS-TRIS BUFFER                                                  
FORMUL   6  BTB    5(C8 H19 N O5)                                               
FORMUL   8  SO4    O4 S 2-                                                      
FORMUL  12  HOH   *362(H2 O)                                                    
HELIX    1   1 SER A   38  THR A   42  5                                   5    
HELIX    2   2 SER A   75  PHE A   80  1                                   6    
HELIX    3   3 HIS A   81  GLN A   88  1                                   8    
HELIX    4   4 GLN A   88  GLY A  107  1                                  20    
HELIX    5   5 ALA A  124  GLY A  138  1                                  15    
HELIX    6   6 GLY A  144  GLU A  149  5                                   6    
HELIX    7   7 SER B   38  THR B   42  5                                   5    
HELIX    8   8 SER B   75  PHE B   80  1                                   6    
HELIX    9   9 HIS B   81  GLN B   88  1                                   8    
HELIX   10  10 GLN B   88  GLY B  107  1                                  20    
HELIX   11  11 ALA B  124  GLY B  138  1                                  15    
HELIX   12  12 GLY B  144  GLU B  149  5                                   6    
HELIX   13  13 SER C   38  THR C   42  5                                   5    
HELIX   14  14 SER C   75  PHE C   80  1                                   6    
HELIX   15  15 HIS C   81  GLN C   88  1                                   8    
HELIX   16  16 GLN C   88  GLY C  107  1                                  20    
HELIX   17  17 LYS C  123  GLY C  138  1                                  16    
HELIX   18  18 GLY C  144  GLU C  149  5                                   6    
HELIX   19  19 SER D   38  THR D   42  5                                   5    
HELIX   20  20 SER D   75  PHE D   80  1                                   6    
HELIX   21  21 HIS D   81  GLN D   88  1                                   8    
HELIX   22  22 GLN D   88  GLY D  107  1                                  20    
HELIX   23  23 GLU D  118  ALA D  122  5                                   5    
HELIX   24  24 LYS D  123  GLY D  138  1                                  16    
HELIX   25  25 SER D  143  GLU D  149  5                                   7    
HELIX   26  26 SER E   38  THR E   42  5                                   5    
HELIX   27  27 SER E   75  PHE E   80  1                                   6    
HELIX   28  28 HIS E   81  GLN E   88  1                                   8    
HELIX   29  29 GLN E   88  GLY E  107  1                                  20    
HELIX   30  30 ALA E  122  GLY E  138  1                                  17    
HELIX   31  31 GLY E  144  GLU E  149  5                                   6    
SHEET    1   A 5 PHE A  62  CYS A  66  0                                        
SHEET    2   A 5 THR A  51  TRP A  56 -1  N  ARG A  52   O  VAL A  65           
SHEET    3   A 5 TRP A  32  VAL A  37 -1  N  ARG A  35   O  MET A  55           
SHEET    4   A 5 LEU A  21  GLY A  24 -1  N  VAL A  22   O  GLY A  34           
SHEET    5   A 5 LEU A  70  PRO A  72 -1  O  MET A  71   N  TRP A  23           
SHEET    1   B 5 PHE B  62  CYS B  66  0                                        
SHEET    2   B 5 THR B  51  TRP B  56 -1  N  VAL B  54   O  SER B  63           
SHEET    3   B 5 TRP B  32  VAL B  37 -1  N  ARG B  35   O  MET B  55           
SHEET    4   B 5 LEU B  21  GLY B  24 -1  N  VAL B  22   O  GLY B  34           
SHEET    5   B 5 LEU B  70  PRO B  72 -1  O  MET B  71   N  TRP B  23           
SHEET    1   C 5 PHE C  62  CYS C  66  0                                        
SHEET    2   C 5 THR C  51  TRP C  56 -1  N  ARG C  52   O  VAL C  65           
SHEET    3   C 5 TRP C  32  VAL C  37 -1  N  ARG C  35   O  MET C  55           
SHEET    4   C 5 LEU C  21  GLY C  24 -1  N  VAL C  22   O  GLY C  34           
SHEET    5   C 5 LEU C  70  PRO C  72 -1  O  MET C  71   N  TRP C  23           
SHEET    1   D 5 PHE D  62  CYS D  66  0                                        
SHEET    2   D 5 THR D  51  TRP D  56 -1  N  VAL D  54   O  SER D  63           
SHEET    3   D 5 TRP D  32  VAL D  37 -1  N  ARG D  35   O  MET D  55           
SHEET    4   D 5 LEU D  21  GLY D  24 -1  N  VAL D  22   O  GLY D  34           
SHEET    5   D 5 LEU D  70  PRO D  72 -1  O  MET D  71   N  TRP D  23           
SHEET    1   E 5 PHE E  62  CYS E  66  0                                        
SHEET    2   E 5 THR E  51  TRP E  56 -1  N  ARG E  52   O  VAL E  65           
SHEET    3   E 5 TRP E  31  VAL E  37 -1  N  ARG E  35   O  MET E  55           
SHEET    4   E 5 LEU E  21  LYS E  25 -1  N  VAL E  22   O  GLY E  34           
SHEET    5   E 5 LEU E  70  PRO E  72 -1  O  MET E  71   N  TRP E  23           
CISPEP   1 GLN A  141    PRO A  142          0         5.22                     
CISPEP   2 GLN B  141    PRO B  142          0         3.02                     
CISPEP   3 GLN C  141    PRO C  142          0         4.04                     
CISPEP   4 GLN D  141    PRO D  142          0         3.14                     
CISPEP   5 GLN E  141    PRO E  142          0         5.03                     
SITE     1 AC1  7 PHE A  29  TRP A  32  TRP A  56  ASP A  59                    
SITE     2 AC1  7 LYS A  61  MET A  90  HOH A 184                               
SITE     1 AC2  7 LEU B  26  PHE B  29  TRP B  32  TRP B  56                    
SITE     2 AC2  7 ASP B  59  HOH B 171  HOH B 214                               
SITE     1 AC3  9 LEU C  26  PHE C  29  TRP C  32  TRP C  56                    
SITE     2 AC3  9 ASP C  59  LYS C  61  MET C  90  HOH C 160                    
SITE     3 AC3  9 HOH C 354                                                     
SITE     1 AC4  7 LEU D  26  PHE D  29  TRP D  32  TRP D  56                    
SITE     2 AC4  7 ASP D  59  MET D  90  HOH D 339                               
SITE     1 AC5  7 LEU E  26  PHE E  29  TRP E  32  TRP E  56                    
SITE     2 AC5  7 ASP E  59  MET E  90  HOH E 166                               
SITE     1 AC6  4 LEU B  26  ARG B  27  HOH B 216  HOH B 362                    
CRYST1   67.110   83.990   74.590  90.00  90.48  90.00 P 1 21 1     10          
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      0.014901  0.000000  0.000125        0.00000                         
SCALE2      0.000000  0.011906  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013407        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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