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Database: PDB
Entry: 5NV2
LinkDB: 5NV2
Original site: 5NV2 
HEADER    TRANSFERASE                             03-MAY-17   5NV2              
TITLE     HUMAN DNMT3B PWWP DOMAIN IN COMPLEX WITH N-ISOPROPYL-1,5-             
TITLE    2 DIMETHYLHEXYLAMINE (METRON S)                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3B;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DNMT3B,DNA METHYLTRANSFERASE HSAIIIB,M.HSAIIIB;             
COMPND   5 EC: 2.1.1.37;                                                        
COMPND   6 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: DNMT3B;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28-MHL                                 
KEYWDS    DNMT3B PWWP DOMAIN, HISTONE BINDING, BETA BARREL, LIGAND, TRANSFERASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.RONDELET,J.WOUTERS                                                  
REVDAT   3   16-OCT-19 5NV2    1       REMARK                                   
REVDAT   2   27-MAR-19 5NV2    1       JRNL                                     
REVDAT   1   30-MAY-18 5NV2    0                                                
JRNL        AUTH   G.RONDELET,T.DAL MASO,A.MANIQUET,Q.THEMANS,J.WOUTERS         
JRNL        TITL   TARGETING PWWP DOMAIN OF DNA METHYLTRANSFERASE 3B FOR        
JRNL        TITL 2 EPIGENETIC CANCER THERAPY: IDENTIFICATION AND STRUCTURAL     
JRNL        TITL 3 CHARACTERIZATION OF NEW POTENTIAL PROTEIN-PROTEIN            
JRNL        TITL 4 INTERACTION INHIBITORS                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.03 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.1_1168                                    
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.62                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 33471                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1674                            
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 40.6284 -  4.6423    1.00     2832   150  0.1809 0.2164        
REMARK   3     2  4.6423 -  3.6855    1.00     2714   142  0.1651 0.1837        
REMARK   3     3  3.6855 -  3.2199    1.00     2660   140  0.1950 0.2583        
REMARK   3     4  3.2199 -  2.9256    1.00     2671   141  0.2284 0.2904        
REMARK   3     5  2.9256 -  2.7159    1.00     2636   139  0.2229 0.2683        
REMARK   3     6  2.7159 -  2.5558    1.00     2642   139  0.2198 0.2711        
REMARK   3     7  2.5558 -  2.4278    1.00     2619   138  0.2333 0.2466        
REMARK   3     8  2.4278 -  2.3222    1.00     2603   137  0.2343 0.2958        
REMARK   3     9  2.3222 -  2.2328    1.00     2628   138  0.2469 0.3018        
REMARK   3    10  2.2328 -  2.1557    1.00     2604   137  0.2804 0.3237        
REMARK   3    11  2.1557 -  2.0883    1.00     2607   137  0.3085 0.3305        
REMARK   3    12  2.0883 -  2.0286    0.99     2581   136  0.3705 0.3900        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.400           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.70                          
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      :  0.008           2263                                  
REMARK   3   ANGLE     :  1.102           3047                                  
REMARK   3   CHIRALITY :  0.081            297                                  
REMARK   3   PLANARITY :  0.005            370                                  
REMARK   3   DIHEDRAL  : 13.776            800                                  
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 5NV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004778.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.7-6.7                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978570                           
REMARK 200  MONOCHROMATOR                  : CHANNEL CUT MONOCHROMATOR          
REMARK 200                                   CRYSTAL (SI(111))                  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33473                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.029                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.620                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.800                              
REMARK 200  R MERGE                    (I) : 0.04200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.7600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.87000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.380                              
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: 3QKJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES,0.2 M LI2SO4, 23-33% PEG       
REMARK 280  3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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      104.44667            
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       52.22333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       52.22333            
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      104.44667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 S    SO4 B 404  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 548  LIES ON A SPECIAL POSITION.                          
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     GLU A   206                                                      
REMARK 465     ALA A   207                                                      
REMARK 465     ASP A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     GLY A   210                                                      
REMARK 465     ASP A   211                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     ASP A   213                                                      
REMARK 465     SER A   214                                                      
REMARK 465     SER A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     GLY A   322                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     ASN A   352                                                      
REMARK 465     THR A   353                                                      
REMARK 465     GLN A   354                                                      
REMARK 465     PRO A   355                                                      
REMARK 465     GLU B   206                                                      
REMARK 465     ALA B   207                                                      
REMARK 465     ASP B   208                                                      
REMARK 465     SER B   209                                                      
REMARK 465     GLY B   210                                                      
REMARK 465     ASP B   211                                                      
REMARK 465     GLY B   212                                                      
REMARK 465     ASP B   213                                                      
REMARK 465     SER B   214                                                      
REMARK 465     SER B   320                                                      
REMARK 465     PRO B   321                                                      
REMARK 465     GLY B   322                                                      
REMARK 465     ASP B   323                                                      
REMARK 465     ASN B   352                                                      
REMARK 465     THR B   353                                                      
REMARK 465     GLN B   354                                                      
REMARK 465     PRO B   355                                                      
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    GLN A 218       68.41   -106.53                                   
REMARK 500    PHE A 223      126.62     82.46                                   
REMARK 500    LYS A 251      -96.40   -125.46                                   
REMARK 500    GLN B 218       77.53   -100.48                                   
REMARK 500    PHE B 223      128.21     84.35                                   
REMARK 500    LEU B 325      -73.68    -60.06                                   
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 9AE A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9AE B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404                 
DBREF  5NV2 A  206   355  UNP    Q9UBC3   DNM3B_HUMAN    206    355             
DBREF  5NV2 B  206   355  UNP    Q9UBC3   DNM3B_HUMAN    206    355             
SEQRES   1 A  150  GLU ALA ASP SER GLY ASP GLY ASP SER SER GLU TYR GLN          
SEQRES   2 A  150  ASP GLY LYS GLU PHE GLY ILE GLY ASP LEU VAL TRP GLY          
SEQRES   3 A  150  LYS ILE LYS GLY PHE SER TRP TRP PRO ALA MET VAL VAL          
SEQRES   4 A  150  SER TRP LYS ALA THR SER LYS ARG GLN ALA MET SER GLY          
SEQRES   5 A  150  MET ARG TRP VAL GLN TRP PHE GLY ASP GLY LYS PHE SER          
SEQRES   6 A  150  GLU VAL SER ALA ASP LYS LEU VAL ALA LEU GLY LEU PHE          
SEQRES   7 A  150  SER GLN HIS PHE ASN LEU ALA THR PHE ASN LYS LEU VAL          
SEQRES   8 A  150  SER TYR ARG LYS ALA MET TYR HIS ALA LEU GLU LYS ALA          
SEQRES   9 A  150  ARG VAL ARG ALA GLY LYS THR PHE PRO SER SER PRO GLY          
SEQRES  10 A  150  ASP SER LEU GLU ASP GLN LEU LYS PRO MET LEU GLU TRP          
SEQRES  11 A  150  ALA HIS GLY GLY PHE LYS PRO THR GLY ILE GLU GLY LEU          
SEQRES  12 A  150  LYS PRO ASN ASN THR GLN PRO                                  
SEQRES   1 B  150  GLU ALA ASP SER GLY ASP GLY ASP SER SER GLU TYR GLN          
SEQRES   2 B  150  ASP GLY LYS GLU PHE GLY ILE GLY ASP LEU VAL TRP GLY          
SEQRES   3 B  150  LYS ILE LYS GLY PHE SER TRP TRP PRO ALA MET VAL VAL          
SEQRES   4 B  150  SER TRP LYS ALA THR SER LYS ARG GLN ALA MET SER GLY          
SEQRES   5 B  150  MET ARG TRP VAL GLN TRP PHE GLY ASP GLY LYS PHE SER          
SEQRES   6 B  150  GLU VAL SER ALA ASP LYS LEU VAL ALA LEU GLY LEU PHE          
SEQRES   7 B  150  SER GLN HIS PHE ASN LEU ALA THR PHE ASN LYS LEU VAL          
SEQRES   8 B  150  SER TYR ARG LYS ALA MET TYR HIS ALA LEU GLU LYS ALA          
SEQRES   9 B  150  ARG VAL ARG ALA GLY LYS THR PHE PRO SER SER PRO GLY          
SEQRES  10 B  150  ASP SER LEU GLU ASP GLN LEU LYS PRO MET LEU GLU TRP          
SEQRES  11 B  150  ALA HIS GLY GLY PHE LYS PRO THR GLY ILE GLU GLY LEU          
SEQRES  12 B  150  LYS PRO ASN ASN THR GLN PRO                                  
HET    9AE  A 401      12                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HET    9AE  B 401      12                                                       
HET    SO4  B 402       5                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 404       5                                                       
HETNAM     9AE (2~{S})-6-METHYL-~{N}-PROPAN-2-YL-HEPTAN-2-AMINE                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  9AE    2(C11 H25 N)                                                 
FORMUL   4  SO4    8(O4 S 2-)                                                   
FORMUL  13  HOH   *104(H2 O)                                                    
HELIX    1 AA1 SER A  245  THR A  249  5                                   5    
HELIX    2 AA2 ASN A  288  LEU A  295  1                                   8    
HELIX    3 AA3 LEU A  295  GLY A  314  1                                  20    
HELIX    4 AA4 LEU A  325  GLY A  338  1                                  14    
HELIX    5 AA5 GLY A  344  LYS A  349  5                                   6    
HELIX    6 AA6 SER B  245  THR B  249  5                                   5    
HELIX    7 AA7 LEU B  282  PHE B  287  1                                   6    
HELIX    8 AA8 ASN B  288  LEU B  295  1                                   8    
HELIX    9 AA9 LEU B  295  GLY B  314  1                                  20    
HELIX   10 AB1 LEU B  325  GLY B  338  1                                  14    
HELIX   11 AB2 THR B  343  LYS B  349  5                                   7    
SHEET    1 AA1 5 PHE A 269  SER A 273  0                                        
SHEET    2 AA1 5 MET A 258  TRP A 263 -1  N  ARG A 259   O  VAL A 272           
SHEET    3 AA1 5 TRP A 239  VAL A 244 -1  N  VAL A 244   O  TRP A 260           
SHEET    4 AA1 5 LEU A 228  GLY A 231 -1  N  GLY A 231   O  TRP A 239           
SHEET    5 AA1 5 LEU A 277  ALA A 279 -1  O  VAL A 278   N  TRP A 230           
SHEET    1 AA2 5 PHE B 269  SER B 273  0                                        
SHEET    2 AA2 5 MET B 258  TRP B 263 -1  N  ARG B 259   O  VAL B 272           
SHEET    3 AA2 5 TRP B 238  VAL B 244 -1  N  MET B 242   O  GLN B 262           
SHEET    4 AA2 5 LEU B 228  LYS B 232 -1  N  GLY B 231   O  TRP B 239           
SHEET    5 AA2 5 LEU B 277  ALA B 279 -1  O  VAL B 278   N  TRP B 230           
CISPEP   1 LYS A  341    PRO A  342          0         4.98                     
CISPEP   2 LYS B  341    PRO B  342          0         6.04                     
SITE     1 AC1  4 ILE A 233  TRP A 239  ASP A 266  HOH A 508                    
SITE     1 AC2  3 LYS A 308  ARG A 312  ASN A 351                               
SITE     1 AC3  2 ARG A 310  LYS B 234                                          
SITE     1 AC4  5 LYS A 251  ARG A 252  HOH A 524  HOH A 529                    
SITE     2 AC4  5 HIS B 304                                                     
SITE     1 AC5  3 LYS A 232  LYS A 234  GLY A 235                               
SITE     1 AC6  3 LYS A 251  ARG A 252  GLY B 265                               
SITE     1 AC7  6 ILE B 233  PHE B 236  TRP B 239  TRP B 263                    
SITE     2 AC7  6 ASP B 266  SER B 297                                          
SITE     1 AC8  4 ASP A 275  LYS B 308  ARG B 312  ASN B 351                    
SITE     1 AC9  3 LYS B 251  ARG B 252  HOH B 502                               
SITE     1 AD1  2 LYS B 232  TRP B 238                                          
CRYST1   74.630   74.630  156.670  90.00  90.00 120.00 P 32 2 1     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      0.013399  0.007736  0.000000        0.00000                         
SCALE2      0.000000  0.015472  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006383        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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