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Database: PDB
Entry: 5CIU
LinkDB: 5CIU
Original site: 5CIU 
HEADER    TRANSFERASE                             13-JUL-15   5CIU              
TITLE     STRUCTURAL BASIS OF THE RECOGNITION OF H3K36ME3 BY DNMT3B PWWP DOMAIN 
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;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HISTONE H3.2;                                              
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 SYNONYM: HISTONE H3/M,HISTONE H3/O;                                  
COMPND  11 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;                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    PROTEIN-PEPTIDE COMPLEX, DNMT3B, PWWP DOMAIN, HISTONE BINDING,        
KEYWDS   2 H3K36ME3, METHYLTRANSFERASE 3 BETA, S-ADENOSYL-L-METHIONINE,         
KEYWDS   3 TRANSFERASE, ZINC-FINGER                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.RONDELET,T.DAL MASO,L.WILLEMS,J.WOUTERS                             
REVDAT   3   12-JUN-19 5CIU    1       AUTHOR REMARK ATOM                       
REVDAT   2   04-MAY-16 5CIU    1       JRNL                                     
REVDAT   1   30-MAR-16 5CIU    0                                                
JRNL        AUTH   G.RONDELET,T.DAL MASO,L.WILLEMS,J.WOUTERS                    
JRNL        TITL   STRUCTURAL BASIS FOR RECOGNITION OF HISTONE H3K36ME3         
JRNL        TITL 2 NUCLEOSOME BY HUMAN DE NOVO DNA METHYLTRANSFERASES 3A AND    
JRNL        TITL 3 3B.                                                          
JRNL        REF    J.STRUCT.BIOL.                V. 194   357 2016              
JRNL        REFN                   ESSN 1095-8657                               
JRNL        PMID   26993463                                                     
JRNL        DOI    10.1016/J.JSB.2016.03.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 2.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24436                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1905                            
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 36.7234 -  5.3935    0.97     1694   148  0.2347 0.2472        
REMARK   3     2  5.3935 -  4.2831    1.00     1653   141  0.1836 0.2014        
REMARK   3     3  4.2831 -  3.7423    1.00     1632   133  0.1904 0.1851        
REMARK   3     4  3.7423 -  3.4004    1.00     1633   136  0.1978 0.2501        
REMARK   3     5  3.4004 -  3.1568    1.00     1616   132  0.2253 0.2806        
REMARK   3     6  3.1568 -  2.9708    1.00     1606   132  0.2465 0.3166        
REMARK   3     7  2.9708 -  2.8220    1.00     1571   135  0.2481 0.3184        
REMARK   3     8  2.8220 -  2.6992    1.00     1612   140  0.2564 0.3434        
REMARK   3     9  2.6992 -  2.5954    1.00     1596   135  0.2609 0.3185        
REMARK   3    10  2.5954 -  2.5058    1.00     1584   134  0.2736 0.3266        
REMARK   3    11  2.5058 -  2.4275    1.00     1582   136  0.2885 0.3455        
REMARK   3    12  2.4275 -  2.3581    1.00     1580   134  0.2788 0.3145        
REMARK   3    13  2.3581 -  2.2960    1.00     1568   133  0.2992 0.3533        
REMARK   3    14  2.2960 -  2.2400    1.00     1604   136  0.3168 0.3815        
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)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.700           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.45                          
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      :  0.009           2162                                  
REMARK   3   ANGLE     :  1.204           2898                                  
REMARK   3   CHIRALITY :  0.087            282                                  
REMARK   3   PLANARITY :  0.005            354                                  
REMARK   3   DIHEDRAL  : 13.937            774                                  
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 5CIU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211709.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 2                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9801                             
REMARK 200  MONOCHROMATOR                  : CRYOGENICALLY COOLED CHANNEL-CUT   
REMARK 200                                   SI[111]                            
REMARK 200  OPTICS                         : X-RAY FLUORESCCENCE DETECTOR       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24436                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.240                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.4400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.950                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.2                                          
REMARK 200 STARTING MODEL: 3QKJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM CITRATE TRIBASIC, PH 6.5,    
REMARK 280  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      105.46667            
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       52.73333            
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       52.73333            
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      105.46667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 950 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 7750 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 910 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 7380 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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      HOH A 416  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   215                                                      
REMARK 465     PRO A   318                                                      
REMARK 465     SER A   319                                                      
REMARK 465     SER A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     GLY A   322                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     LEU A   325                                                      
REMARK 465     GLU A   326                                                      
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   215                                                      
REMARK 465     ALA B   290                                                      
REMARK 465     THR B   291                                                      
REMARK 465     THR B   316                                                      
REMARK 465     PHE B   317                                                      
REMARK 465     PRO B   318                                                      
REMARK 465     SER B   319                                                      
REMARK 465     SER B   320                                                      
REMARK 465     PRO B   321                                                      
REMARK 465     GLY B   322                                                      
REMARK 465     ASP B   323                                                      
REMARK 465     SER B   324                                                      
REMARK 465     LEU B   325                                                      
REMARK 465     GLU B   326                                                      
REMARK 465     ASP B   327                                                      
REMARK 465     GLN B   328                                                      
REMARK 465     ASN B   352                                                      
REMARK 465     THR B   353                                                      
REMARK 465     GLN B   354                                                      
REMARK 465     PRO B   355                                                      
REMARK 465     SER C    28                                                      
REMARK 465     ALA C    29                                                      
REMARK 465     PRO C    30                                                      
REMARK 465     ALA C    31                                                      
REMARK 465     HIS C    39                                                      
REMARK 465     ARG C    40                                                      
REMARK 465     TYR C    41                                                      
REMARK 465     ARG C    42                                                      
REMARK 465     SER D    28                                                      
REMARK 465     ALA D    29                                                      
REMARK 465     PRO D    30                                                      
REMARK 465     ALA D    31                                                      
REMARK 465     HIS D    39                                                      
REMARK 465     ARG D    40                                                      
REMARK 465     TYR D    41                                                      
REMARK 465     ARG D    42                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  234   CG   CD   CE   NZ                                   
REMARK 480     LYS B  234   CB   CG   CD   CE   NZ                              
REMARK 480     LYS B  330   CB   CG   CD   CE   NZ                              
REMARK 480     GLU B  334   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS B  341   CB   CG   CD   CE   NZ                              
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   NZ   LYS A   232     O    PHE A   236              2.04            
REMARK 500   O    PRO A   342     O    HOH A   401              2.13            
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    PHE A 223      138.10     79.94                                   
REMARK 500    LYS A 251      -98.58   -117.30                                   
REMARK 500    THR A 316      -63.14   -109.18                                   
REMARK 500    TYR B 217       19.15     81.94                                   
REMARK 500    LYS B 251      -95.83   -108.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 496        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH A 497        DISTANCE =  7.83 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401                 
DBREF  5CIU A  206   355  UNP    Q9UBC3   DNM3B_HUMAN    206    355             
DBREF  5CIU B  206   355  UNP    Q9UBC3   DNM3B_HUMAN    206    355             
DBREF  5CIU C   28    42  PDB    5CIU     5CIU            28     42             
DBREF  5CIU D   28    42  PDB    5CIU     5CIU            28     42             
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                                  
SEQRES   1 C   15  SER ALA PRO ALA THR GLY GLY VAL M3L LYS PRO HIS ARG          
SEQRES   2 C   15  TYR ARG                                                      
SEQRES   1 D   15  SER ALA PRO ALA THR GLY GLY VAL M3L LYS PRO HIS ARG          
SEQRES   2 D   15  TYR ARG                                                      
MODRES 5CIU M3L C   36  LYS  MODIFIED RESIDUE                                   
MODRES 5CIU M3L D   36  LYS  MODIFIED RESIDUE                                   
HET    M3L  C  36      12                                                       
HET    M3L  D  36      12                                                       
HET    GOL  B 401       6                                                       
HETNAM     M3L N-TRIMETHYLLYSINE                                                
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  M3L    2(C9 H21 N2 O2 1+)                                           
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *163(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 GLN A  328  GLY A  338  1                                  11    
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 ASP B  275  LEU B  277  5                                   3    
HELIX    8 AA8 LEU B  282  PHE B  287  1                                   6    
HELIX    9 AA9 LEU B  295  GLY B  314  1                                  20    
HELIX   10 AB1 LYS B  330  GLY B  338  1                                   9    
HELIX   11 AB2 GLY B  344  LEU B  348  5                                   5    
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  MET A 242   O  GLN A 262           
SHEET    4 AA1 5 LEU A 228  GLY A 231 -1  N  VAL A 229   O  ALA A 241           
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 239  VAL B 244 -1  N  MET B 242   O  GLN B 262           
SHEET    4 AA2 5 LEU B 228  GLY B 231 -1  N  VAL B 229   O  ALA B 241           
SHEET    5 AA2 5 VAL B 278  ALA B 279 -1  O  VAL B 278   N  TRP B 230           
LINK         C   VAL C  35                 N   M3L C  36     1555   1555  1.33  
LINK         C   M3L C  36                 N   LYS C  37     1555   1555  1.33  
LINK         C   VAL D  35                 N   M3L D  36     1555   1555  1.34  
LINK         C   M3L D  36                 N   LYS D  37     1555   1555  1.33  
CISPEP   1 LYS A  341    PRO A  342          0         9.11                     
CISPEP   2 ASP B  219    GLY B  220          0        -3.61                     
CISPEP   3 LYS B  341    PRO B  342          0         5.53                     
SITE     1 AC1  2 ARG B 252  VAL C  35                                          
CRYST1   73.437   73.437  158.200  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      0.013617  0.007862  0.000000        0.00000                         
SCALE2      0.000000  0.015724  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006321        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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