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Database: PDB
Entry: 5EX0
LinkDB: 5EX0
Original site: 5EX0 
HEADER    TRANSFERASE                             23-NOV-15   5EX0              
TITLE     CRYSTAL STRUCTURE OF HUMAN SMYD3 IN COMPLEX WITH A MAP3K2 PEPTIDE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SMYD3;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SET AND MYND DOMAIN-CONTAINING PROTEIN 3,ZINC FINGER MYND   
COMPND   5 DOMAIN-CONTAINING PROTEIN 1;                                         
COMPND   6 EC: 2.1.1.43;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: MAP3K2 PEPTIDE;                                            
COMPND  11 CHAIN: D;                                                            
COMPND  12 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: SMYD3, ZMYND1, ZNFN3A1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIL;                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-SMT;                               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    SET DOMAIN, METHYLATION, CHROMATIN, CANCER, TRANSFERASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.FU,N.LIU,Q.QIAO,M.WANG,J.MIN,B.ZHU,R.M.XU,N.YANG                    
REVDAT   3   18-OCT-17 5EX0    1       JRNL   REMARK                            
REVDAT   2   25-MAY-16 5EX0    1       JRNL                                     
REVDAT   1   09-MAR-16 5EX0    0                                                
JRNL        AUTH   W.FU,N.LIU,Q.QIAO,M.WANG,J.MIN,B.ZHU,R.M.XU,N.YANG           
JRNL        TITL   STRUCTURAL BASIS FOR SUBSTRATE PREFERENCE OF SMYD3, A SET    
JRNL        TITL 2 DOMAIN-CONTAINING PROTEIN LYSINE METHYLTRANSFERASE           
JRNL        REF    J.BIOL.CHEM.                  V. 291  9173 2016              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   26929412                                                     
JRNL        DOI    10.1074/JBC.M115.709832                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.66                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 18261                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.140                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 938                             
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 47.6679 -  5.1392    0.99     2709   129  0.1767 0.2038        
REMARK   3     2  5.1392 -  4.0798    1.00     2582   141  0.1433 0.1816        
REMARK   3     3  4.0798 -  3.5643    1.00     2552   135  0.1590 0.2051        
REMARK   3     4  3.5643 -  3.2385    1.00     2554   143  0.1790 0.2335        
REMARK   3     5  3.2385 -  3.0064    1.00     2496   153  0.2085 0.2695        
REMARK   3     6  3.0064 -  2.8292    0.99     2506   125  0.2247 0.2924        
REMARK   3     7  2.8292 -  2.7000    0.77     1924   112  0.2582 0.3433        
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)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.550           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.89                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.40                          
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      :  0.004           3627                                  
REMARK   3   ANGLE     :  0.798           4886                                  
REMARK   3   CHIRALITY :  0.032            532                                  
REMARK   3   PLANARITY :  0.003            633                                  
REMARK   3   DIHEDRAL  : 13.438           1410                                  
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: SF FILE CONTAINS FRIEDEL PAIRS UNDER      
REMARK   3  I/F_MINUS AND I/F_PLUS COLUMNS.                                     
REMARK   4                                                                      
REMARK   4 5EX0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000215634.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
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   : 18908                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73200                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 3MEK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.4M NAAC, PH 7.5, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       26.79900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.60750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.09050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.60750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.79900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.09050            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 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     SER A    -2                                                      
REMARK 465     GLU A    -1                                                      
REMARK 465     GLU D   256                                                      
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   678     O    HOH A   711              2.16            
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    ASN A 187     -154.61    -88.47                                   
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 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  49   SG                                                     
REMARK 620 2 CYS A  52   SG  106.9                                              
REMARK 620 3 CYS A  71   SG  118.2 108.9                                        
REMARK 620 4 CYS A  75   SG  109.3 114.3  99.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  62   SG                                                     
REMARK 620 2 CYS A  65   SG  109.6                                              
REMARK 620 3 HIS A  83   NE2 113.5 105.2                                        
REMARK 620 4 CYS A  87   SG  113.9 110.7 103.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 208   SG                                                     
REMARK 620 2 CYS A 261   SG  116.7                                              
REMARK 620 3 CYS A 263   SG  108.5 103.4                                        
REMARK 620 4 CYS A 266   SG   96.7 114.5 117.6                                  
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 506                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EX3   RELATED DB: PDB                                   
DBREF  5EX0 A    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
DBREF  5EX0 D  256   265  PDB    5EX0     5EX0           256    265             
SEQADV 5EX0 SER A   -2  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5EX0 GLU A   -1  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5EX0 PHE A    0  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 5EX0 ASN A   13  UNP  Q9H7B4    LYS    13 ENGINEERED MUTATION            
SEQADV 5EX0 ARG A  140  UNP  Q9H7B4    LYS   140 ENGINEERED MUTATION            
SEQRES   1 A  431  SER GLU PHE MET GLU PRO LEU LYS VAL GLU LYS PHE ALA          
SEQRES   2 A  431  THR ALA ASN ARG GLY ASN GLY LEU ARG ALA VAL THR PRO          
SEQRES   3 A  431  LEU ARG PRO GLY GLU LEU LEU PHE ARG SER ASP PRO LEU          
SEQRES   4 A  431  ALA TYR THR VAL CYS LYS GLY SER ARG GLY VAL VAL CYS          
SEQRES   5 A  431  ASP ARG CYS LEU LEU GLY LYS GLU LYS LEU MET ARG CYS          
SEQRES   6 A  431  SER GLN CYS ARG VAL ALA LYS TYR CYS SER ALA LYS CYS          
SEQRES   7 A  431  GLN LYS LYS ALA TRP PRO ASP HIS LYS ARG GLU CYS LYS          
SEQRES   8 A  431  CYS LEU LYS SER CYS LYS PRO ARG TYR PRO PRO ASP SER          
SEQRES   9 A  431  VAL ARG LEU LEU GLY ARG VAL VAL PHE LYS LEU MET ASP          
SEQRES  10 A  431  GLY ALA PRO SER GLU SER GLU LYS LEU TYR SER PHE TYR          
SEQRES  11 A  431  ASP LEU GLU SER ASN ILE ASN LYS LEU THR GLU ASP ARG          
SEQRES  12 A  431  LYS GLU GLY LEU ARG GLN LEU VAL MET THR PHE GLN HIS          
SEQRES  13 A  431  PHE MET ARG GLU GLU ILE GLN ASP ALA SER GLN LEU PRO          
SEQRES  14 A  431  PRO ALA PHE ASP LEU PHE GLU ALA PHE ALA LYS VAL ILE          
SEQRES  15 A  431  CYS ASN SER PHE THR ILE CYS ASN ALA GLU MET GLN GLU          
SEQRES  16 A  431  VAL GLY VAL GLY LEU TYR PRO SER ILE SER LEU LEU ASN          
SEQRES  17 A  431  HIS SER CYS ASP PRO ASN CYS SER ILE VAL PHE ASN GLY          
SEQRES  18 A  431  PRO HIS LEU LEU LEU ARG ALA VAL ARG ASP ILE GLU VAL          
SEQRES  19 A  431  GLY GLU GLU LEU THR ILE CYS TYR LEU ASP MET LEU MET          
SEQRES  20 A  431  THR SER GLU GLU ARG ARG LYS GLN LEU ARG ASP GLN TYR          
SEQRES  21 A  431  CYS PHE GLU CYS ASP CYS PHE ARG CYS GLN THR GLN ASP          
SEQRES  22 A  431  LYS ASP ALA ASP MET LEU THR GLY ASP GLU GLN VAL TRP          
SEQRES  23 A  431  LYS GLU VAL GLN GLU SER LEU LYS LYS ILE GLU GLU LEU          
SEQRES  24 A  431  LYS ALA HIS TRP LYS TRP GLU GLN VAL LEU ALA MET CYS          
SEQRES  25 A  431  GLN ALA ILE ILE SER SER ASN SER GLU ARG LEU PRO ASP          
SEQRES  26 A  431  ILE ASN ILE TYR GLN LEU LYS VAL LEU ASP CYS ALA MET          
SEQRES  27 A  431  ASP ALA CYS ILE ASN LEU GLY LEU LEU GLU GLU ALA LEU          
SEQRES  28 A  431  PHE TYR GLY THR ARG THR MET GLU PRO TYR ARG ILE PHE          
SEQRES  29 A  431  PHE PRO GLY SER HIS PRO VAL ARG GLY VAL GLN VAL MET          
SEQRES  30 A  431  LYS VAL GLY LYS LEU GLN LEU HIS GLN GLY MET PHE PRO          
SEQRES  31 A  431  GLN ALA MET LYS ASN LEU ARG LEU ALA PHE ASP ILE MET          
SEQRES  32 A  431  ARG VAL THR HIS GLY ARG GLU HIS SER LEU ILE GLU ASP          
SEQRES  33 A  431  LEU ILE LEU LEU LEU GLU GLU CYS ASP ALA ASN ILE ARG          
SEQRES  34 A  431  ALA SER                                                      
SEQRES   1 D   10  GLU LYS PHE GLY LYS GLY GLY THR TYR PRO                      
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET    SAH  A 504      26                                                       
HET    ACY  A 505       4                                                       
HET    ACY  A 506       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     ACY ACETIC ACID                                                      
FORMUL   3   ZN    3(ZN 2+)                                                     
FORMUL   6  SAH    C14 H20 N6 O5 S                                              
FORMUL   7  ACY    2(C2 H4 O2)                                                  
FORMUL   9  HOH   *117(H2 O)                                                    
HELIX    1 AA1 LYS A   42  ARG A   45  5                                   4    
HELIX    2 AA2 SER A   72  ALA A   79  1                                   8    
HELIX    3 AA3 ALA A   79  LYS A   94  1                                  16    
HELIX    4 AA4 PRO A   99  LEU A  112  1                                  14    
HELIX    5 AA5 SER A  118  LYS A  122  5                                   5    
HELIX    6 AA6 SER A  125  LEU A  129  5                                   5    
HELIX    7 AA7 ASN A  132  LEU A  136  5                                   5    
HELIX    8 AA8 THR A  137  MET A  155  1                                  19    
HELIX    9 AA9 ASP A  161  LEU A  165  5                                   5    
HELIX   10 AB1 ASP A  170  ASN A  181  1                                  12    
HELIX   11 AB2 SER A  200  LEU A  204  5                                   5    
HELIX   12 AB3 THR A  245  CYS A  258  1                                  14    
HELIX   13 AB4 CYS A  263  THR A  268  1                                   6    
HELIX   14 AB5 LYS A  271  LEU A  276  1                                   6    
HELIX   15 AB6 ASP A  279  HIS A  299  1                                  21    
HELIX   16 AB7 LYS A  301  SER A  317  1                                  17    
HELIX   17 AB8 ASN A  324  ASN A  340  1                                  17    
HELIX   18 AB9 LEU A  343  ARG A  353  1                                  11    
HELIX   19 AC1 THR A  354  PHE A  362  1                                   9    
HELIX   20 AC2 HIS A  366  HIS A  382  1                                  17    
HELIX   21 AC3 MET A  385  HIS A  404  1                                  20    
HELIX   22 AC4 HIS A  408  SER A  428  1                                  21    
SHEET    1 AA1 2 VAL A   6  ALA A  10  0                                        
SHEET    2 AA1 2 ASN A  16  ALA A  20 -1  O  GLY A  17   N  PHE A   9           
SHEET    1 AA2 3 LEU A  29  SER A  33  0                                        
SHEET    2 AA2 3 HIS A 220  ALA A 225 -1  O  LEU A 223   N  LEU A  30           
SHEET    3 AA2 3 CYS A 212  ASN A 217 -1  N  ASN A 217   O  HIS A 220           
SHEET    1 AA3 3 ALA A  37  VAL A  40  0                                        
SHEET    2 AA3 3 GLU A 192  LEU A 197 -1  O  LEU A 197   N  ALA A  37           
SHEET    3 AA3 3 SER A 182  CYS A 186 -1  N  PHE A 183   O  GLY A 196           
SHEET    1 AA4 2 MET A  60  ARG A  61  0                                        
SHEET    2 AA4 2 LYS A  69  TYR A  70 -1  O  TYR A  70   N  MET A  60           
SHEET    1 AA5 2 ASN A 205  HIS A 206  0                                        
SHEET    2 AA5 2 THR A 236  ILE A 237  1  O  ILE A 237   N  ASN A 205           
LINK         SG  CYS A  49                ZN    ZN A 501     1555   1555  2.30  
LINK         SG  CYS A  52                ZN    ZN A 501     1555   1555  2.40  
LINK         SG  CYS A  62                ZN    ZN A 502     1555   1555  2.32  
LINK         SG  CYS A  65                ZN    ZN A 502     1555   1555  2.31  
LINK         SG  CYS A  71                ZN    ZN A 501     1555   1555  2.38  
LINK         SG  CYS A  75                ZN    ZN A 501     1555   1555  2.16  
LINK         NE2 HIS A  83                ZN    ZN A 502     1555   1555  2.01  
LINK         SG  CYS A  87                ZN    ZN A 502     1555   1555  2.17  
LINK         SG  CYS A 208                ZN    ZN A 503     1555   1555  2.36  
LINK         SG  CYS A 261                ZN    ZN A 503     1555   1555  2.28  
LINK         SG  CYS A 263                ZN    ZN A 503     1555   1555  2.23  
LINK         SG  CYS A 266                ZN    ZN A 503     1555   1555  2.32  
CISPEP   1 LYS A   94    PRO A   95          0         1.97                     
SITE     1 AC1  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 AC2  4 CYS A  62  CYS A  65  HIS A  83  CYS A  87                    
SITE     1 AC3  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 AC4 17 ARG A  14  GLY A  15  ASN A  16  TYR A 124                    
SITE     2 AC4 17 ASN A 132  CYS A 180  ASN A 181  SER A 202                    
SITE     3 AC4 17 LEU A 203  LEU A 204  ASN A 205  HIS A 206                    
SITE     4 AC4 17 TYR A 239  TYR A 257  PHE A 259  HOH A 618                    
SITE     5 AC4 17 LYS D 260                                                     
SITE     1 AC5  3 ARG A 359  ARG A 369  HOH A 679                               
SITE     1 AC6  3 GLN A 152  ILE A 159  LEU A 165                               
CRYST1   53.598  104.181  117.215  90.00  90.00  90.00 P 21 21 21    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      0.018657  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009599  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008531        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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