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Database: PDB
Entry: 6J46
LinkDB: 6J46
Original site: 6J46 
HEADER    TRANSFERASE                             08-JAN-19   6J46              
TITLE     LEPI-SAH COMPLEX STRUCTURE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: O-METHYLTRANSFERASE LEPI;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: LEPORINS BIOSYNTHESIS PROTEIN I;                            
COMPND   5 EC: 2.1.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS FLAVUS (STRAIN ATCC 200026 / FGSC   
SOURCE   3 A1120 / NRRL 3357 / JCM 12722 / SRRC 167);                           
SOURCE   4 ORGANISM_TAXID: 332952;                                              
SOURCE   5 STRAIN: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167; 
SOURCE   6 GENE: LEPI, AFLA_066940;                                             
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    COMPLEX, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.QIU,C.WEI                                                           
REVDAT   4   20-MAR-24 6J46    1       SOURCE                                   
REVDAT   3   22-NOV-23 6J46    1       REMARK                                   
REVDAT   2   13-NOV-19 6J46    1       JRNL                                     
REVDAT   1   01-MAY-19 6J46    0                                                
JRNL        AUTH   Q.SUN,Y.HU,Y.GU,J.HUANG,J.HE,L.LUO,Y.YANG,S.YIN,C.DOU,       
JRNL        AUTH 2 T.WANG,X.FU,L.HE,S.QI,X.ZHU,S.YANG,X.WEI,W.CHENG             
JRNL        TITL   DECIPHERING THE REGULATORY AND CATALYTIC MECHANISMS OF AN    
JRNL        TITL 2 UNUSUAL SAM-DEPENDENT ENZYME.                                
JRNL        REF    SIGNAL TRANSDUCT TARGET THER  V.   4    17 2019              
JRNL        REFN                   ESSN 2059-3635                               
JRNL        PMID   31149354                                                     
JRNL        DOI    10.1038/S41392-019-0052-Y                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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) : 2.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.20                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 28554                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1413                            
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 53.2130 -  5.6441    0.97     2973   138  0.1735 0.2027        
REMARK   3     2  5.6441 -  4.4806    0.99     2965   157  0.1875 0.2475        
REMARK   3     3  4.4806 -  3.9145    1.00     2947   155  0.1868 0.1962        
REMARK   3     4  3.9145 -  3.5566    1.00     2928   179  0.2083 0.2438        
REMARK   3     5  3.5566 -  3.3018    0.95     2821   123  0.2492 0.2641        
REMARK   3     6  3.3018 -  3.1071    0.99     2931   146  0.2543 0.2931        
REMARK   3     7  3.1071 -  2.9515    0.99     2911   136  0.2605 0.3193        
REMARK   3     8  2.9515 -  2.8230    0.99     2926   145  0.2757 0.2990        
REMARK   3     9  2.8230 -  2.7144    0.99     2889   173  0.2873 0.3510        
REMARK   3    10  2.7144 -  2.6207    0.30      850    61  0.3941 0.4360        
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.600           
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      :  0.003           6339                                  
REMARK   3   ANGLE     :  0.583           8623                                  
REMARK   3   CHIRALITY :  0.041            965                                  
REMARK   3   PLANARITY :  0.004           1126                                  
REMARK   3   DIHEDRAL  : 17.580           3885                                  
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 6J46 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300010339.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 X CDTE 1M         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28684                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.621                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.202                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.7                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.82700                            
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: PHENIX                                                
REMARK 200 STARTING MODEL: 6J1O                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.10M BIS-TRIS PH 7.0, 35% PEG 400,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       79.90850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.16650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.90850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.16650            
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: 9900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 103       19.99     59.50                                   
REMARK 500    TYR A 154       70.15     58.27                                   
REMARK 500    GLU A 219       56.60   -148.33                                   
REMARK 500    ASP A 252     -165.89   -165.31                                   
REMARK 500    ARG B 103       19.66     59.22                                   
REMARK 500    ASN B 137      -70.41   -108.39                                   
REMARK 500    GLU B 219       57.87   -147.05                                   
REMARK 500    ASP B 252     -165.22   -165.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 401                 
DBREF  6J46 A    1   387  UNP    B8NJH3   LEPI_ASPFN       1    387             
DBREF  6J46 B    1   387  UNP    B8NJH3   LEPI_ASPFN       1    387             
SEQRES   1 A  387  MET GLU THR VAL ALA ALA ILE LYS THR LEU ILE GLN GLN          
SEQRES   2 A  387  LEU ALA GLN SER THR ASP GLN PHE GLY ARG ALA GLU ILE          
SEQRES   3 A  387  ASN ASP ALA LEU ARG GLU LEU GLN TYR SER LEU GLU THR          
SEQRES   4 A  387  PRO PHE ASP THR VAL MET ARG MET SER LEU ASP THR CYS          
SEQRES   5 A  387  GLN VAL ALA VAL ALA ARG ILE GLY SER ASP LEU GLY LEU          
SEQRES   6 A  387  PHE LYS HIS LEU SER GLN CYS ALA SER PRO GLN SER ALA          
SEQRES   7 A  387  GLU GLU LEU ALA ASP HIS LEU GLY CYS GLY ARG GLU LEU          
SEQRES   8 A  387  MET SER ARG LEU LEU ARG TYR MET ALA SER VAL ARG MET          
SEQRES   9 A  387  VAL GLN GLN THR ASP ASP ILE LYS TYR ILE SER SER ASN          
SEQRES  10 A  387  ILE THR GLN THR LEU ALA VAL PRO GLY LEU GLU ALA GLY          
SEQRES  11 A  387  MET ARG HIS ALA PHE GLU ASN LEU TRP PRO VAL LEU MET          
SEQRES  12 A  387  ALA LEU PRO ASP PHE LEU ALA GLU ARG LYS TYR PRO ASP          
SEQRES  13 A  387  ILE VAL ASP ALA LYS ASP THR ALA PHE GLN LYS ALA PHE          
SEQRES  14 A  387  ASN THR ASP GLN ASP CYS PHE HIS TRP LEU ALA THR GLN          
SEQRES  15 A  387  PRO THR ARG ILE ALA ASN PHE LYS VAL LEU LEU THR ASP          
SEQRES  16 A  387  GLU ARG THR PRO ASN PHE LEU SER THR PHE PRO LEU GLU          
SEQRES  17 A  387  LYS GLU LEU GLY SER TRP SER ALA GLU PRO GLU LYS ALA          
SEQRES  18 A  387  LEU PHE VAL ASP ILE GLY GLY GLY MET GLY HIS ALA CYS          
SEQRES  19 A  387  ILE ARG LEU ARG GLU LYS TYR PRO ASN GLN PRO GLY ARG          
SEQRES  20 A  387  VAL ILE LEU GLN ASP LEU PRO PRO VAL LEU GLN ALA ALA          
SEQRES  21 A  387  GLN ALA THR LEU PRO LEU SER GLY ILE GLU SER MET PRO          
SEQRES  22 A  387  HIS ASN PHE HIS THR PRO GLN PRO VAL GLN GLY ALA LYS          
SEQRES  23 A  387  PHE TYR PHE LEU ARG LEU ILE LEU ARG ASP PHE PRO ASP          
SEQRES  24 A  387  HIS GLN ALA LEU GLU ILE LEU GLN ASN ILE VAL PRO ALA          
SEQRES  25 A  387  MET ASP ALA GLU SER ARG ILE VAL ILE ASP ASP GLY VAL          
SEQRES  26 A  387  PRO PRO GLU LYS GLY ALA ARG TRP ALA GLU THR GLY THR          
SEQRES  27 A  387  ASP ILE CYS ILE MET SER ALA LEU GLY SER LYS GLU ARG          
SEQRES  28 A  387  THR GLN ARG GLN TRP GLU GLU LEU ALA ALA LYS ALA GLY          
SEQRES  29 A  387  LEU GLN LEU GLN ALA LEU TYR GLN TYR THR TRP PRO VAL          
SEQRES  30 A  387  VAL ASN ALA ALA MET VAL PHE SER LEU GLN                      
SEQRES   1 B  387  MET GLU THR VAL ALA ALA ILE LYS THR LEU ILE GLN GLN          
SEQRES   2 B  387  LEU ALA GLN SER THR ASP GLN PHE GLY ARG ALA GLU ILE          
SEQRES   3 B  387  ASN ASP ALA LEU ARG GLU LEU GLN TYR SER LEU GLU THR          
SEQRES   4 B  387  PRO PHE ASP THR VAL MET ARG MET SER LEU ASP THR CYS          
SEQRES   5 B  387  GLN VAL ALA VAL ALA ARG ILE GLY SER ASP LEU GLY LEU          
SEQRES   6 B  387  PHE LYS HIS LEU SER GLN CYS ALA SER PRO GLN SER ALA          
SEQRES   7 B  387  GLU GLU LEU ALA ASP HIS LEU GLY CYS GLY ARG GLU LEU          
SEQRES   8 B  387  MET SER ARG LEU LEU ARG TYR MET ALA SER VAL ARG MET          
SEQRES   9 B  387  VAL GLN GLN THR ASP ASP ILE LYS TYR ILE SER SER ASN          
SEQRES  10 B  387  ILE THR GLN THR LEU ALA VAL PRO GLY LEU GLU ALA GLY          
SEQRES  11 B  387  MET ARG HIS ALA PHE GLU ASN LEU TRP PRO VAL LEU MET          
SEQRES  12 B  387  ALA LEU PRO ASP PHE LEU ALA GLU ARG LYS TYR PRO ASP          
SEQRES  13 B  387  ILE VAL ASP ALA LYS ASP THR ALA PHE GLN LYS ALA PHE          
SEQRES  14 B  387  ASN THR ASP GLN ASP CYS PHE HIS TRP LEU ALA THR GLN          
SEQRES  15 B  387  PRO THR ARG ILE ALA ASN PHE LYS VAL LEU LEU THR ASP          
SEQRES  16 B  387  GLU ARG THR PRO ASN PHE LEU SER THR PHE PRO LEU GLU          
SEQRES  17 B  387  LYS GLU LEU GLY SER TRP SER ALA GLU PRO GLU LYS ALA          
SEQRES  18 B  387  LEU PHE VAL ASP ILE GLY GLY GLY MET GLY HIS ALA CYS          
SEQRES  19 B  387  ILE ARG LEU ARG GLU LYS TYR PRO ASN GLN PRO GLY ARG          
SEQRES  20 B  387  VAL ILE LEU GLN ASP LEU PRO PRO VAL LEU GLN ALA ALA          
SEQRES  21 B  387  GLN ALA THR LEU PRO LEU SER GLY ILE GLU SER MET PRO          
SEQRES  22 B  387  HIS ASN PHE HIS THR PRO GLN PRO VAL GLN GLY ALA LYS          
SEQRES  23 B  387  PHE TYR PHE LEU ARG LEU ILE LEU ARG ASP PHE PRO ASP          
SEQRES  24 B  387  HIS GLN ALA LEU GLU ILE LEU GLN ASN ILE VAL PRO ALA          
SEQRES  25 B  387  MET ASP ALA GLU SER ARG ILE VAL ILE ASP ASP GLY VAL          
SEQRES  26 B  387  PRO PRO GLU LYS GLY ALA ARG TRP ALA GLU THR GLY THR          
SEQRES  27 B  387  ASP ILE CYS ILE MET SER ALA LEU GLY SER LYS GLU ARG          
SEQRES  28 B  387  THR GLN ARG GLN TRP GLU GLU LEU ALA ALA LYS ALA GLY          
SEQRES  29 B  387  LEU GLN LEU GLN ALA LEU TYR GLN TYR THR TRP PRO VAL          
SEQRES  30 B  387  VAL ASN ALA ALA MET VAL PHE SER LEU GLN                      
HET    SAH  A 401      26                                                       
HET    SAH  B 401      26                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   3  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   5  HOH   *20(H2 O)                                                     
HELIX    1 AA1 MET A    1  THR A   18  1                                  18    
HELIX    2 AA2 ASP A   19  LEU A   37  1                                  19    
HELIX    3 AA3 THR A   39  ASP A   50  1                                  12    
HELIX    4 AA4 THR A   51  GLY A   64  1                                  14    
HELIX    5 AA5 GLY A   64  GLN A   71  1                                   8    
HELIX    6 AA6 SER A   77  GLY A   86  1                                  10    
HELIX    7 AA7 GLY A   88  VAL A  102  1                                  15    
HELIX    8 AA8 SER A  116  VAL A  124  1                                   9    
HELIX    9 AA9 VAL A  124  ASN A  137  1                                  14    
HELIX   10 AB1 ASN A  137  ARG A  152  1                                  16    
HELIX   11 AB2 THR A  163  ASN A  170  1                                   8    
HELIX   12 AB3 ASP A  174  THR A  181  1                                   8    
HELIX   13 AB4 GLN A  182  LEU A  193  1                                  12    
HELIX   14 AB5 ASN A  200  THR A  204  5                                   5    
HELIX   15 AB6 PRO A  206  GLY A  212  1                                   7    
HELIX   16 AB7 GLY A  231  TYR A  241  1                                  11    
HELIX   17 AB8 LEU A  253  GLN A  261  1                                   9    
HELIX   18 AB9 ALA A  262  LEU A  264  5                                   3    
HELIX   19 AC1 ILE A  293  PHE A  297  5                                   5    
HELIX   20 AC2 PRO A  298  ASN A  308  1                                  11    
HELIX   21 AC3 ILE A  309  MET A  313  5                                   5    
HELIX   22 AC4 ARG A  332  GLY A  347  1                                  16    
HELIX   23 AC5 THR A  352  ALA A  363  1                                  12    
HELIX   24 AC6 GLU B    2  THR B   18  1                                  17    
HELIX   25 AC7 ASP B   19  GLU B   38  1                                  20    
HELIX   26 AC8 THR B   39  ASP B   50  1                                  12    
HELIX   27 AC9 THR B   51  GLY B   64  1                                  14    
HELIX   28 AD1 GLY B   64  GLN B   71  1                                   8    
HELIX   29 AD2 SER B   77  GLY B   86  1                                  10    
HELIX   30 AD3 GLY B   88  VAL B  102  1                                  15    
HELIX   31 AD4 SER B  116  VAL B  124  1                                   9    
HELIX   32 AD5 VAL B  124  ASN B  137  1                                  14    
HELIX   33 AD6 ASN B  137  ARG B  152  1                                  16    
HELIX   34 AD7 THR B  163  ASN B  170  1                                   8    
HELIX   35 AD8 ASP B  174  THR B  181  1                                   8    
HELIX   36 AD9 GLN B  182  THR B  194  1                                  13    
HELIX   37 AE1 ASN B  200  THR B  204  5                                   5    
HELIX   38 AE2 PRO B  206  GLY B  212  1                                   7    
HELIX   39 AE3 GLY B  231  TYR B  241  1                                  11    
HELIX   40 AE4 LEU B  253  GLN B  261  1                                   9    
HELIX   41 AE5 ILE B  293  PHE B  297  5                                   5    
HELIX   42 AE6 PRO B  298  ASN B  308  1                                  11    
HELIX   43 AE7 ILE B  309  MET B  313  5                                   5    
HELIX   44 AE8 ARG B  332  GLY B  347  1                                  16    
HELIX   45 AE9 THR B  352  ALA B  363  1                                  12    
SHEET    1 AA1 2 GLN A 106  GLN A 107  0                                        
SHEET    2 AA1 2 TYR A 113  ILE A 114 -1  O  ILE A 114   N  GLN A 106           
SHEET    1 AA2 7 ILE A 269  PRO A 273  0                                        
SHEET    2 AA2 7 ARG A 247  ASP A 252  1  N  LEU A 250   O  GLU A 270           
SHEET    3 AA2 7 ALA A 221  ILE A 226  1  N  ASP A 225   O  ILE A 249           
SHEET    4 AA2 7 PHE A 287  ARG A 291  1  O  PHE A 289   N  VAL A 224           
SHEET    5 AA2 7 ARG A 318  GLY A 324  1  O  VAL A 320   N  TYR A 288           
SHEET    6 AA2 7 ASN A 379  SER A 385 -1  O  PHE A 384   N  ILE A 319           
SHEET    7 AA2 7 GLN A 366  GLN A 372 -1  N  GLN A 368   O  VAL A 383           
SHEET    1 AA3 2 GLN B 106  GLN B 107  0                                        
SHEET    2 AA3 2 TYR B 113  ILE B 114 -1  O  ILE B 114   N  GLN B 106           
SHEET    1 AA4 7 ILE B 269  PRO B 273  0                                        
SHEET    2 AA4 7 ARG B 247  ASP B 252  1  N  LEU B 250   O  GLU B 270           
SHEET    3 AA4 7 ALA B 221  ILE B 226  1  N  PHE B 223   O  ILE B 249           
SHEET    4 AA4 7 PHE B 287  ARG B 291  1  O  PHE B 289   N  VAL B 224           
SHEET    5 AA4 7 ARG B 318  GLY B 324  1  O  VAL B 320   N  TYR B 288           
SHEET    6 AA4 7 ASN B 379  SER B 385 -1  O  PHE B 384   N  ILE B 319           
SHEET    7 AA4 7 GLN B 366  GLN B 372 -1  N  GLN B 368   O  VAL B 383           
CISPEP   1 THR A  198    PRO A  199          0        -0.76                     
CISPEP   2 GLU A  217    PRO A  218          0        -0.64                     
CISPEP   3 TRP A  375    PRO A  376          0        -1.69                     
CISPEP   4 THR B  198    PRO B  199          0         0.10                     
CISPEP   5 GLU B  217    PRO B  218          0        -0.93                     
CISPEP   6 TRP B  375    PRO B  376          0        -1.41                     
SITE     1 AC1 12 LEU A 193  GLY A 227  GLY A 228  GLY A 229                    
SITE     2 AC1 12 ASP A 252  LEU A 253  VAL A 256  HIS A 274                    
SITE     3 AC1 12 ASN A 275  PHE A 276  HIS A 277  ARG A 291                    
SITE     1 AC2 10 LEU B 193  GLY B 227  GLY B 229  ASP B 252                    
SITE     2 AC2 10 VAL B 256  HIS B 274  ASN B 275  PHE B 276                    
SITE     3 AC2 10 ARG B 291  HOH B 508                                          
CRYST1  159.817   62.333  112.735  90.00 112.45  90.00 C 1 2 1       8          
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      0.006257  0.000000  0.002585        0.00000                         
SCALE2      0.000000  0.016043  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009598        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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