GenomeNet

Database: PDB
Entry: 4QBS
LinkDB: 4QBS
Original site: 4QBS 
HEADER    TRANSFERASE                             08-MAY-14   4QBS              
TITLE     CRYSTAL STRUCTURE OF DNMT3A ADD DOMAIN E545R MUTANT BOUND TO H3T3PH   
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3A;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ADD DOMAIN, UNP RESIDUES 456-661;                          
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 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: HISTONE H3;                                                
COMPND  12 CHAIN: P;                                                            
COMPND  13 FRAGMENT: H3 N-TERMINAL 1-10;                                        
COMPND  14 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.WANG,H.LI                                                           
REVDAT   1   13-MAY-15 4QBS    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.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 13009                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.890                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 636                             
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 40.8486 -  3.0775    0.98     2567   123  0.1545 0.1727        
REMARK   3     2  3.0775 -  2.4428    1.00     2489   130  0.1789 0.2054        
REMARK   3     3  2.4428 -  2.1340    1.00     2473   106  0.1706 0.2535        
REMARK   3     4  2.1340 -  1.9389    1.00     2448   138  0.1741 0.2287        
REMARK   3     5  1.9389 -  1.8000    1.00     2396   139  0.1843 0.2338        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.480           
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      :  0.010           1182                                  
REMARK   3   ANGLE     :  1.308           1599                                  
REMARK   3   CHIRALITY :  0.053            166                                  
REMARK   3   PLANARITY :  0.006            211                                  
REMARK   3   DIHEDRAL  : 14.456            446                                  
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 4QBS 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 RCSB085855.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-13                          
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               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 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 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13016                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
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     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09100                            
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
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   (%): 40.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1M BIS-TRIS, 0.2M         
REMARK 280  AMMONIUM SULFATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       23.97433            
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       47.94867            
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       47.94867            
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       23.97433            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7950 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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   O3   SO4 A   704     O    HOH A   898              1.67            
REMARK 500   O    HOH A   833     O    HOH A   861              2.14            
REMARK 500   O    ASN A   553     O    HOH A   899              2.15            
REMARK 500   OG   SER A   603     O    HOH A   862              2.17            
REMARK 500   O    ILE A   539     O    HOH A   879              2.19            
REMARK 500   O    HOH A   878     O    HOH A   901              2.19            
REMARK 500   OD1  ASN A   553     O    HOH A   901              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   837     O    HOH A   890     4655     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 586   CB    CYS A 586   SG     -0.097                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 559   SG                                                     
REMARK 620 2 CYS A 562   SG  103.9                                              
REMARK 620 3 CYS A 540   SG  112.7 107.5                                        
REMARK 620 4 CYS A 537   SG  112.7 113.3 106.7                                  
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 497   SG                                                     
REMARK 620 2 CYS A 494   SG  115.3                                              
REMARK 620 3 CYS A 517   SG  109.5 103.7                                        
REMARK 620 4 CYS A 514   SG  106.1 115.1 106.7                                  
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 554   SG  106.4                                              
REMARK 620 3 CYS A 586   SG  113.2  98.4                                        
REMARK 620 4 CYS A 583   SG  108.5 111.0 118.5                                  
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 SO4 A 704                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QBR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QBQ   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.                                                          
DBREF  4QBS A  476   611  UNP    Q9Y6K1   DNM3A_HUMAN    476    611             
DBREF  4QBS P    1     7  PDB    4QBS     4QBS             1      7             
SEQADV 4QBS GLY A  474  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBS SER A  475  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4QBS ARG A  545  UNP  Q9Y6K1    GLU   545 ENGINEERED MUTATION            
SEQRES   1 A  138  GLY SER ARG GLU ARG LEU VAL TYR GLU VAL ARG GLN LYS          
SEQRES   2 A  138  CYS ARG ASN ILE GLU ASP ILE CYS ILE SER CYS GLY SER          
SEQRES   3 A  138  LEU ASN VAL THR LEU GLU HIS PRO LEU PHE VAL GLY GLY          
SEQRES   4 A  138  MET CYS GLN ASN CYS LYS ASN CYS PHE LEU GLU CYS ALA          
SEQRES   5 A  138  TYR GLN TYR ASP ASP ASP GLY TYR GLN SER TYR CYS THR          
SEQRES   6 A  138  ILE CYS CYS GLY GLY ARG ARG VAL LEU MET CYS GLY ASN          
SEQRES   7 A  138  ASN ASN CYS CYS ARG CYS PHE CYS VAL GLU CYS VAL ASP          
SEQRES   8 A  138  LEU LEU VAL GLY PRO GLY ALA ALA GLN ALA ALA ILE LYS          
SEQRES   9 A  138  GLU ASP PRO TRP ASN CYS TYR MET CYS GLY HIS LYS GLY          
SEQRES  10 A  138  THR TYR GLY LEU LEU ARG ARG ARG GLU ASP TRP PRO SER          
SEQRES  11 A  138  ARG LEU GLN MET PHE PHE ALA ASN                              
SEQRES   1 P    7  ALA ARG TPO LYS GLN THR ALA                                  
MODRES 4QBS TPO P    3  THR  PHOSPHOTHREONINE                                   
HET    TPO  P   3      11                                                       
HET     ZN  A 701       1                                                       
HET     ZN  A 702       1                                                       
HET     ZN  A 703       1                                                       
HET    SO4  A 704       5                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   2  TPO    C4 H10 N O6 P                                                
FORMUL   3   ZN    3(ZN 2+)                                                     
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  HOH   *125(H2 O)                                                    
HELIX    1   1 SER A  475  GLN A  485  1                                  11    
HELIX    2   2 ASN A  489  ILE A  493  5                                   5    
HELIX    3   3 GLN A  515  ALA A  525  1                                  11    
HELIX    4   4 VAL A  560  VAL A  567  1                                   8    
HELIX    5   5 GLY A  570  GLU A  578  1                                   9    
HELIX    6   6 ASP A  600  PHE A  609  1                                  10    
SHEET    1   A 2 VAL A 502  GLU A 505  0                                        
SHEET    2   A 2 GLY A 512  CYS A 514 -1  O  MET A 513   N  THR A 503           
SHEET    1   B 3 CYS A 557  CYS A 559  0                                        
SHEET    2   B 3 ARG A 545  MET A 548 -1  N  LEU A 547   O  PHE A 558           
SHEET    3   B 3 TPO P   3  GLN P   5 -1  O  LYS P   4   N  VAL A 546           
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           
LINK         C   ARG P   2                 N   TPO P   3     1555   1555  1.33  
LINK         C   TPO P   3                 N   LYS P   4     1555   1555  1.33  
LINK         SG  CYS A 559                ZN    ZN A 702     1555   1555  2.26  
LINK         SG  CYS A 562                ZN    ZN A 702     1555   1555  2.28  
LINK         SG  CYS A 497                ZN    ZN A 703     1555   1555  2.29  
LINK         SG  CYS A 549                ZN    ZN A 701     1555   1555  2.29  
LINK         SG  CYS A 554                ZN    ZN A 701     1555   1555  2.31  
LINK         SG  CYS A 586                ZN    ZN A 701     1555   1555  2.33  
LINK         SG  CYS A 494                ZN    ZN A 703     1555   1555  2.33  
LINK         SG  CYS A 583                ZN    ZN A 701     1555   1555  2.33  
LINK         SG  CYS A 540                ZN    ZN A 702     1555   1555  2.34  
LINK         SG  CYS A 517                ZN    ZN A 703     1555   1555  2.36  
LINK         SG  CYS A 537                ZN    ZN A 702     1555   1555  2.37  
LINK         SG  CYS A 514                ZN    ZN A 703     1555   1555  2.38  
CISPEP   1 ASP A  579    PRO A  580          0        -1.00                     
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  5 GLY A 587  HIS A 588  LYS A 589  TYR A 592                    
SITE     2 AC4  5 HOH A 898                                                     
CRYST1   57.286   57.286   71.923  90.00  90.00 120.00 P 31 2 1      6          
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      0.017456  0.010078  0.000000        0.00000                         
SCALE2      0.000000  0.020157  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013904        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system