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Database: PDB
Entry: 4QBQ
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HEADER    TRANSFERASE                             08-MAY-14   4QBQ              
TITLE     CRYSTAL STRUCTURE OF DNMT3A ADD DOMAIN BOUND TO H3 PEPTIDE            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3A;                     
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: ADD DOMAIN, UNP RESIDUES 476-611;                          
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;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: HISTONE H3;                                                
COMPND  11 CHAIN: P;                                                            
COMPND  12 FRAGMENT: H3 N-TERMINAL 1-15;                                        
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DNMT3A;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.             
KEYWDS    ZINC FINGER, HISTONE BINDING, TRANSFERASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,D.J.PATEL                                                        
REVDAT   1   13-MAY-15 4QBQ    0                                                
JRNL        AUTH   K.NOH,H.WANG,H.KIM,W.WENDERSKI,F.FANG,C.LI,S.DEWELL,X.WU,    
JRNL        AUTH 2 A.FERRIS,S.H.HUGHES,D.ZHENG,A.M.MELNICK,D.J.PATEL,H.LI,      
JRNL        AUTH 3 C.D.ALLIS                                                    
JRNL        TITL   ENGINEERING OF A HISTONE-RECOGNITION DOMAIN IN A DE NOVO DNA 
JRNL        TITL 2 METHYLTRANSFERASE ALTERS THE EPIGENETIC LANDSCAPE OF ESCS    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.56                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 10329                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.810                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 497                             
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 41.5627 -  3.8191    1.00     2520   123  0.1556 0.2031        
REMARK   3     2  3.8191 -  3.0316    1.00     2465   129  0.1687 0.2172        
REMARK   3     3  3.0316 -  2.6485    1.00     2479   124  0.1982 0.2693        
REMARK   3     4  2.6485 -  2.4064    0.97     2368   121  0.2096 0.2954        
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)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           2235                                  
REMARK   3   ANGLE     :  1.262           3012                                  
REMARK   3   CHIRALITY :  0.082            312                                  
REMARK   3   PLANARITY :  0.004            401                                  
REMARK   3   DIHEDRAL  : 18.089            827                                  
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 4QBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-MAY-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085853.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-10                          
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               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10349                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 29% PEGMME5000, 0.1M BIS-TRIS PROPANE-   
REMARK 280  HCL, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K        
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       28.21200            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, P                               
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   848     O    HOH A   849              1.93            
REMARK 500   O    HOH A   806     O    HOH A   843              1.95            
REMARK 500   O    HOH A   821     O    HOH A   836              2.02            
REMARK 500   NH2  ARG A   596     O    HOH A   838              2.14            
REMARK 500   OE1  GLU A   505     NH2  ARG A   604              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 544     -101.44    -95.19                                   
REMARK 500    CYS A 554      -71.21   -121.68                                   
REMARK 500    LYS A 577       48.71    -93.54                                   
REMARK 500    CYS C 497      -16.27   -143.16                                   
REMARK 500    ARG C 544      -73.02    -96.38                                   
REMARK 500    ASN C 552      -93.34     54.43                                   
REMARK 500    ASN C 553        9.69    -67.94                                   
REMARK 500    CYS C 554      -69.40   -103.20                                   
REMARK 500    PRO C 580     -155.63    -74.89                                   
REMARK 500    PHE C 609       45.85    -91.78                                   
REMARK 500    ALA P   7       74.17   -112.58                                   
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 C 835        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH C 840        DISTANCE =  7.71 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 703  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 517   SG                                                     
REMARK 620 2 CYS C 494   SG  109.5                                              
REMARK 620 3 CYS C 497   SG  102.6 113.9                                        
REMARK 620 4 CYS C 514   SG  109.5 115.9 104.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 703  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 517   SG                                                     
REMARK 620 2 CYS A 494   SG  111.9                                              
REMARK 620 3 CYS A 514   SG  101.8 113.7                                        
REMARK 620 4 CYS A 497   SG  108.8 114.0 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 554   SG                                                     
REMARK 620 2 CYS C 549   SG  112.0                                              
REMARK 620 3 CYS C 583   SG  106.0 108.2                                        
REMARK 620 4 CYS C 586   SG   98.6 119.9 111.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 562   SG                                                     
REMARK 620 2 CYS A 540   SG  110.7                                              
REMARK 620 3 CYS A 537   SG  113.4 106.3                                        
REMARK 620 4 CYS A 559   SG  103.0 110.4 113.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 562   SG                                                     
REMARK 620 2 CYS C 559   SG  110.2                                              
REMARK 620 3 CYS C 537   SG  111.2 112.5                                        
REMARK 620 4 CYS C 540   SG  106.1 112.2 104.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 549   SG                                                     
REMARK 620 2 CYS A 586   SG  110.0                                              
REMARK 620 3 CYS A 554   SG  115.5 103.9                                        
REMARK 620 4 CYS A 583   SG  110.6 113.7 103.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 703                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QBR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QBS   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF THE ENTITY2 OF THIS PROTEIN WAS NOT AVAILABLE AT     
REMARK 999 THE UNIPROT KNOWLEDGEBASE DATABASE (UNIPROTKB) AT THE TIME OF        
REMARK 999 DEPOSITION. AUTHORS STATE THAT THE ENTITY2 HAS THE GENEBANK          
REMARK 999 ACCESSION NUMBER AAH43617.1.                                         
DBREF  4QBQ A  479   610  UNP    Q9Y6K1   DNM3A_HUMAN    479    610             
DBREF  4QBQ C  479   610  UNP    Q9Y6K1   DNM3A_HUMAN    479    610             
DBREF  4QBQ P    1     8  PDB    4QBQ     4QBQ             1      8             
SEQADV 4QBQ GLY A  474  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBQ PRO A  475  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBQ LEU A  476  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBQ GLY A  477  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBQ SER A  478  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBQ GLY C  474  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBQ PRO C  475  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBQ LEU C  476  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBQ GLY C  477  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBQ SER C  478  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQRES   1 A  137  GLY PRO LEU GLY SER LEU VAL TYR GLU VAL ARG GLN LYS          
SEQRES   2 A  137  CYS ARG ASN ILE GLU ASP ILE CYS ILE SER CYS GLY SER          
SEQRES   3 A  137  LEU ASN VAL THR LEU GLU HIS PRO LEU PHE VAL GLY GLY          
SEQRES   4 A  137  MET CYS GLN ASN CYS LYS ASN CYS PHE LEU GLU CYS ALA          
SEQRES   5 A  137  TYR GLN TYR ASP ASP ASP GLY TYR GLN SER TYR CYS THR          
SEQRES   6 A  137  ILE CYS CYS GLY GLY ARG GLU VAL LEU MET CYS GLY ASN          
SEQRES   7 A  137  ASN ASN CYS CYS ARG CYS PHE CYS VAL GLU CYS VAL ASP          
SEQRES   8 A  137  LEU LEU VAL GLY PRO GLY ALA ALA GLN ALA ALA ILE LYS          
SEQRES   9 A  137  GLU ASP PRO TRP ASN CYS TYR MET CYS GLY HIS LYS GLY          
SEQRES  10 A  137  THR TYR GLY LEU LEU ARG ARG ARG GLU ASP TRP PRO SER          
SEQRES  11 A  137  ARG LEU GLN MET PHE PHE ALA                                  
SEQRES   1 C  137  GLY PRO LEU GLY SER LEU VAL TYR GLU VAL ARG GLN LYS          
SEQRES   2 C  137  CYS ARG ASN ILE GLU ASP ILE CYS ILE SER CYS GLY SER          
SEQRES   3 C  137  LEU ASN VAL THR LEU GLU HIS PRO LEU PHE VAL GLY GLY          
SEQRES   4 C  137  MET CYS GLN ASN CYS LYS ASN CYS PHE LEU GLU CYS ALA          
SEQRES   5 C  137  TYR GLN TYR ASP ASP ASP GLY TYR GLN SER TYR CYS THR          
SEQRES   6 C  137  ILE CYS CYS GLY GLY ARG GLU VAL LEU MET CYS GLY ASN          
SEQRES   7 C  137  ASN ASN CYS CYS ARG CYS PHE CYS VAL GLU CYS VAL ASP          
SEQRES   8 C  137  LEU LEU VAL GLY PRO GLY ALA ALA GLN ALA ALA ILE LYS          
SEQRES   9 C  137  GLU ASP PRO TRP ASN CYS TYR MET CYS GLY HIS LYS GLY          
SEQRES  10 C  137  THR TYR GLY LEU LEU ARG ARG ARG GLU ASP TRP PRO SER          
SEQRES  11 C  137  ARG LEU GLN MET PHE PHE ALA                                  
SEQRES   1 P    8  ALA ARG THR LYS GLN THR ALA ARG                              
HET     ZN  A 701       1                                                       
HET     ZN  A 702       1                                                       
HET     ZN  A 703       1                                                       
HET     ZN  C 701       1                                                       
HET     ZN  C 702       1                                                       
HET     ZN  C 703       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   4   ZN    6(ZN 2+)                                                     
FORMUL  10  HOH   *104(H2 O)                                                    
HELIX    1   1 GLY A  474  GLN A  485  1                                  12    
HELIX    2   2 ASN A  489  ILE A  493  5                                   5    
HELIX    3   3 CYS A  514  ALA A  525  1                                  12    
HELIX    4   4 VAL A  560  VAL A  567  1                                   8    
HELIX    5   5 GLY A  570  LYS A  577  1                                   8    
HELIX    6   6 ASP A  600  PHE A  609  1                                  10    
HELIX    7   7 PRO C  475  GLN C  485  1                                  11    
HELIX    8   8 ASN C  489  ILE C  493  5                                   5    
HELIX    9   9 CYS C  514  CYS C  524  1                                  11    
HELIX   10  10 VAL C  560  VAL C  567  1                                   8    
HELIX   11  11 GLY C  570  GLU C  578  1                                   9    
HELIX   12  12 ASP C  600  PHE C  609  1                                  10    
SHEET    1   A 2 LEU A 504  GLU A 505  0                                        
SHEET    2   A 2 GLY A 512  MET A 513 -1  O  MET A 513   N  LEU A 504           
SHEET    1   B 2 VAL A 546  MET A 548  0                                        
SHEET    2   B 2 CYS A 557  CYS A 559 -1  O  PHE A 558   N  LEU A 547           
SHEET    1   C 2 THR A 591  TYR A 592  0                                        
SHEET    2   C 2 LEU A 595  ARG A 596 -1  O  LEU A 595   N  TYR A 592           
SHEET    1   D 2 LEU C 504  GLU C 505  0                                        
SHEET    2   D 2 GLY C 512  MET C 513 -1  O  MET C 513   N  LEU C 504           
SHEET    1   E 3 CYS C 557  CYS C 559  0                                        
SHEET    2   E 3 GLU C 545  MET C 548 -1  N  LEU C 547   O  PHE C 558           
SHEET    3   E 3 THR P   3  GLN P   5 -1  O  LYS P   4   N  VAL C 546           
SHEET    1   F 2 THR C 591  TYR C 592  0                                        
SHEET    2   F 2 LEU C 595  ARG C 596 -1  O  LEU C 595   N  TYR C 592           
SSBOND   1 CYS C  524    CYS C  541                          1555   1555  2.03  
LINK         SG  CYS C 517                ZN    ZN C 703     1555   1555  2.38  
LINK         SG  CYS C 494                ZN    ZN C 703     1555   1555  2.39  
LINK         SG  CYS A 517                ZN    ZN A 703     1555   1555  2.40  
LINK         SG  CYS C 554                ZN    ZN C 701     1555   1555  2.42  
LINK         SG  CYS A 562                ZN    ZN A 702     1555   1555  2.42  
LINK         SG  CYS C 549                ZN    ZN C 701     1555   1555  2.44  
LINK         SG  CYS C 562                ZN    ZN C 702     1555   1555  2.46  
LINK         SG  CYS A 540                ZN    ZN A 702     1555   1555  2.47  
LINK         SG  CYS C 559                ZN    ZN C 702     1555   1555  2.47  
LINK         SG  CYS A 549                ZN    ZN A 701     1555   1555  2.47  
LINK         SG  CYS A 586                ZN    ZN A 701     1555   1555  2.48  
LINK         SG  CYS A 537                ZN    ZN A 702     1555   1555  2.49  
LINK         SG  CYS A 559                ZN    ZN A 702     1555   1555  2.49  
LINK         SG  CYS A 494                ZN    ZN A 703     1555   1555  2.49  
LINK         SG  CYS C 537                ZN    ZN C 702     1555   1555  2.52  
LINK         SG  CYS A 514                ZN    ZN A 703     1555   1555  2.52  
LINK         SG  CYS A 554                ZN    ZN A 701     1555   1555  2.52  
LINK         SG  CYS A 583                ZN    ZN A 701     1555   1555  2.53  
LINK         SG  CYS C 497                ZN    ZN C 703     1555   1555  2.53  
LINK         SG  CYS A 497                ZN    ZN A 703     1555   1555  2.54  
LINK         SG  CYS C 540                ZN    ZN C 702     1555   1555  2.55  
LINK         SG  CYS C 514                ZN    ZN C 703     1555   1555  2.56  
LINK         SG  CYS C 583                ZN    ZN C 701     1555   1555  2.57  
LINK         SG  CYS C 586                ZN    ZN C 701     1555   1555  2.59  
CISPEP   1 ASP A  579    PRO A  580          0        -4.83                     
CISPEP   2 ASP C  579    PRO C  580          0        -4.19                     
SITE     1 AC1  4 CYS A 549  CYS A 554  CYS A 583  CYS A 586                    
SITE     1 AC2  4 CYS A 537  CYS A 540  CYS A 559  CYS A 562                    
SITE     1 AC3  4 CYS A 494  CYS A 497  CYS A 514  CYS A 517                    
SITE     1 AC4  4 CYS C 549  CYS C 554  CYS C 583  CYS C 586                    
SITE     1 AC5  4 CYS C 537  CYS C 540  CYS C 559  CYS C 562                    
SITE     1 AC6  4 CYS C 494  CYS C 497  CYS C 514  CYS C 517                    
CRYST1   41.557   56.424   57.301  90.00  90.27  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024063  0.000000  0.000114        0.00000                         
SCALE2      0.000000  0.017723  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017452        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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