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Database: PDB
Entry: 4QTU
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Original site: 4QTU 
HEADER    TRANSFERASE                             09-JUL-14   4QTU              
TITLE     STRUCTURE OF S. CEREVISIAE BUD23-TRM112 COMPLEX INVOLVED IN FORMATION 
TITLE    2 OF M7G1575 ON 18S RRNA (SAM BOUND FORM)                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MULTIFUNCTIONAL METHYLTRANSFERASE SUBUNIT TRM112;          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: RRNA MTASE ACTIVATOR SUBUNIT, ERF1 METHYLTRANSFERASE SUBUNIT
COMPND   5 TRM112, ERF1 MTASE SUBUNIT TRM112, TRNA METHYLTRANSFERASE 112;       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PUTATIVE METHYLTRANSFERASE BUD23;                          
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: FRAGMENT RESIDUES 1-202;                                   
COMPND  11 SYNONYM: RRNA MTASE CATALYTIC SUBUNIT, BUD SITE SELECTION PROTEIN 23;
COMPND  12 EC: 2.1.1.-;                                                         
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;                 
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 GENE: N3445, TRM112, YNR046W;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;                 
SOURCE  10 ORGANISM_COMMON: YEAST;                                              
SOURCE  11 ORGANISM_TAXID: 559292;                                              
SOURCE  12 GENE: BUD23, YCR047C, YCR47C;                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CLASS I, METHYLTRANSFERASE, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LETOQUART,E.HUVELLE,L.WACHEUL,G.BOURGEOIS,C.ZORBAS,M.GRAILLE,       
AUTHOR   2 V.HEURGUE-HAMARD,D.L.J.LAFONTAINE                                    
REVDAT   5   06-DEC-23 4QTU    1       REMARK                                   
REVDAT   4   08-NOV-23 4QTU    1       REMARK                                   
REVDAT   3   24-AUG-22 4QTU    1       JRNL   REMARK SEQADV LINK                
REVDAT   2   03-JAN-18 4QTU    1       TITLE                                    
REVDAT   1   24-DEC-14 4QTU    0                                                
JRNL        AUTH   J.LETOQUART,E.HUVELLE,L.WACHEUL,G.BOURGEOIS,C.ZORBAS,        
JRNL        AUTH 2 M.GRAILLE,V.HEURGUE-HAMARD,D.L.LAFONTAINE                    
JRNL        TITL   STRUCTURAL AND FUNCTIONAL STUDIES OF BUD23-TRM112 REVEAL 18S 
JRNL        TITL 2 RRNA N7-G1575 METHYLATION OCCURS ON LATE 40S PRECURSOR       
JRNL        TITL 3 RIBOSOMES.                                                   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111 E5518 2014              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   25489090                                                     
JRNL        DOI    10.1073/PNAS.1413089111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 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-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) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.31                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 38373                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1917                            
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 38.3136 -  5.1142    0.99     2712   142  0.1578 0.1971        
REMARK   3     2  5.1142 -  4.0608    1.00     2658   140  0.1415 0.1990        
REMARK   3     3  4.0608 -  3.5479    0.99     2624   139  0.1577 0.2019        
REMARK   3     4  3.5479 -  3.2237    0.99     2640   138  0.1818 0.1954        
REMARK   3     5  3.2237 -  2.9927    1.00     2613   138  0.1954 0.2225        
REMARK   3     6  2.9927 -  2.8163    1.00     2612   137  0.1907 0.2906        
REMARK   3     7  2.8163 -  2.6753    1.00     2646   140  0.1938 0.2714        
REMARK   3     8  2.6753 -  2.5589    1.00     2594   136  0.1935 0.2300        
REMARK   3     9  2.5589 -  2.4604    1.00     2624   138  0.1986 0.2623        
REMARK   3    10  2.4604 -  2.3755    1.00     2597   137  0.1977 0.2915        
REMARK   3    11  2.3755 -  2.3012    1.00     2637   139  0.2123 0.2764        
REMARK   3    12  2.3012 -  2.2355    0.98     2526   131  0.2613 0.3125        
REMARK   3    13  2.2355 -  2.1766    1.00     2635   139  0.2518 0.3302        
REMARK   3    14  2.1766 -  2.1235    0.90     2338   123  0.2606 0.3334        
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)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.880           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.88                          
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      :  0.008           5165                                  
REMARK   3   ANGLE     :  1.110           6963                                  
REMARK   3   CHIRALITY :  0.046            783                                  
REMARK   3   PLANARITY :  0.005            893                                  
REMARK   3   DIHEDRAL  : 15.530           1913                                  
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 4QTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000086505.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-12                          
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               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9801                             
REMARK 200  MONOCHROMATOR                  : CHANNEL CUT CRYOGENICALLY COOLED   
REMARK 200                                   MONOCHROMATOR CRYSTAL              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, XSCALE                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38373                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.124                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.7                               
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: SHARP                                                 
REMARK 200 STARTING MODEL: 4QTT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       26.86650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 2450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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     VAL A   135                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     PRO B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     HIS B   203                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     HIS B   208                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 465     PRO D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     LEU D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     PRO D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     ILE D    12                                                      
REMARK 465     PHE D    13                                                      
REMARK 465     TYR D    14                                                      
REMARK 465     ASN D    15                                                      
REMARK 465     ASP D    16                                                      
REMARK 465     SER D    17                                                      
REMARK 465     ALA D   126                                                      
REMARK 465     ASP D   127                                                      
REMARK 465     THR D   128                                                      
REMARK 465     SER D   129                                                      
REMARK 465     TYR D   130                                                      
REMARK 465     ASN D   131                                                      
REMARK 465     HIS D   203                                                      
REMARK 465     HIS D   204                                                      
REMARK 465     HIS D   205                                                      
REMARK 465     HIS D   206                                                      
REMARK 465     HIS D   207                                                      
REMARK 465     HIS D   208                                                      
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   OD2  ASP C    37     OG   SER C    39              2.15            
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    PRO A 132      -38.57    -37.38                                   
REMARK 500    PHE B  13      -46.74   -134.00                                   
REMARK 500    CSO D 124       63.77   -111.62                                   
REMARK 500    LYS D 161      -76.49    -94.59                                   
REMARK 500    ASP D 186       53.27     35.67                                   
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 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  11   SG                                                     
REMARK 620 2 CYS A  16   SG  111.4                                              
REMARK 620 3 CYS A 112   SG  105.0 116.6                                        
REMARK 620 4 CYS A 115   SG  111.8 105.0 107.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  11   SG                                                     
REMARK 620 2 CYS C  16   SG  115.8                                              
REMARK 620 3 CYS C 112   SG  104.4 119.0                                        
REMARK 620 4 CYS C 115   SG  104.9 102.9 109.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QTM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QTT   RELATED DB: PDB                                   
DBREF  4QTU A    1   135  UNP    P53738   TR112_YEAST      1    135             
DBREF  4QTU B    1   202  UNP    P25627   BUD23_YEAST      1    202             
DBREF  4QTU C    1   135  UNP    P53738   TR112_YEAST      1    135             
DBREF  4QTU D    1   202  UNP    P25627   BUD23_YEAST      1    202             
SEQADV 4QTU HIS B  203  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS B  204  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS B  205  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS B  206  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS B  207  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS B  208  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS D  203  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS D  204  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS D  205  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS D  206  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS D  207  UNP  P25627              EXPRESSION TAG                 
SEQADV 4QTU HIS D  208  UNP  P25627              EXPRESSION TAG                 
SEQRES   1 A  135  MET LYS PHE LEU THR THR ASN PHE LEU LYS CYS SER VAL          
SEQRES   2 A  135  LYS ALA CYS ASP THR SER ASN ASP ASN PHE PRO LEU GLN          
SEQRES   3 A  135  TYR ASP GLY SER LYS CYS GLN LEU VAL GLN ASP GLU SER          
SEQRES   4 A  135  ILE GLU PHE ASN PRO GLU PHE LEU LEU ASN ILE VAL ASP          
SEQRES   5 A  135  ARG VAL ASP TRP PRO ALA VAL LEU THR VAL ALA ALA GLU          
SEQRES   6 A  135  LEU GLY ASN ASN ALA LEU PRO PRO THR LYS PRO SER PHE          
SEQRES   7 A  135  PRO SER SER ILE GLN GLU LEU THR ASP ASP ASP MET ALA          
SEQRES   8 A  135  ILE LEU ASN ASP LEU HIS THR LEU LEU LEU GLN THR SER          
SEQRES   9 A  135  ILE ALA GLU GLY GLU MET LYS CYS ARG ASN CYS GLY HIS          
SEQRES  10 A  135  ILE TYR TYR ILE LYS ASN GLY ILE PRO ASN LEU LEU LEU          
SEQRES  11 A  135  PRO PRO HIS LEU VAL                                          
SEQRES   1 B  208  MET SER ARG PRO GLU GLU LEU ALA PRO PRO GLU ILE PHE          
SEQRES   2 B  208  TYR ASN ASP SER GLU ALA HIS LYS TYR THR GLY SER THR          
SEQRES   3 B  208  ARG VAL GLN HIS ILE GLN ALA LYS MET THR LEU ARG ALA          
SEQRES   4 B  208  LEU GLU LEU LEU ASN LEU GLN PRO CYS SER PHE ILE LEU          
SEQRES   5 B  208  ASP ILE GLY CYS GLY SER GLY LEU SER GLY GLU ILE LEU          
SEQRES   6 B  208  THR GLN GLU GLY ASP HIS VAL TRP CYS GLY LEU ASP ILE          
SEQRES   7 B  208  SER PRO SER MET LEU ALA THR GLY LEU SER ARG GLU LEU          
SEQRES   8 B  208  GLU GLY ASP LEU MET LEU GLN ASP MET GLY THR GLY ILE          
SEQRES   9 B  208  PRO PHE ARG ALA GLY SER PHE ASP ALA ALA ILE SER ILE          
SEQRES  10 B  208  SER ALA ILE GLN TRP LEU CSO ASN ALA ASP THR SER TYR          
SEQRES  11 B  208  ASN ASP PRO LYS GLN ARG LEU MET ARG PHE PHE ASN THR          
SEQRES  12 B  208  LEU TYR ALA ALA LEU LYS LYS GLY GLY LYS PHE VAL ALA          
SEQRES  13 B  208  GLN PHE TYR PRO LYS ASN ASP ASP GLN VAL ASP ASP ILE          
SEQRES  14 B  208  LEU GLN SER ALA LYS VAL ALA GLY PHE SER GLY GLY LEU          
SEQRES  15 B  208  VAL VAL ASP ASP PRO GLU SER LYS LYS ASN LYS LYS TYR          
SEQRES  16 B  208  TYR LEU VAL LEU SER SER GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 C  135  MET LYS PHE LEU THR THR ASN PHE LEU LYS CYS SER VAL          
SEQRES   2 C  135  LYS ALA CYS ASP THR SER ASN ASP ASN PHE PRO LEU GLN          
SEQRES   3 C  135  TYR ASP GLY SER LYS CYS GLN LEU VAL GLN ASP GLU SER          
SEQRES   4 C  135  ILE GLU PHE ASN PRO GLU PHE LEU LEU ASN ILE VAL ASP          
SEQRES   5 C  135  ARG VAL ASP TRP PRO ALA VAL LEU THR VAL ALA ALA GLU          
SEQRES   6 C  135  LEU GLY ASN ASN ALA LEU PRO PRO THR LYS PRO SER PHE          
SEQRES   7 C  135  PRO SER SER ILE GLN GLU LEU THR ASP ASP ASP MET ALA          
SEQRES   8 C  135  ILE LEU ASN ASP LEU HIS THR LEU LEU LEU GLN THR SER          
SEQRES   9 C  135  ILE ALA GLU GLY GLU MET LYS CYS ARG ASN CYS GLY HIS          
SEQRES  10 C  135  ILE TYR TYR ILE LYS ASN GLY ILE PRO ASN LEU LEU LEU          
SEQRES  11 C  135  PRO PRO HIS LEU VAL                                          
SEQRES   1 D  208  MET SER ARG PRO GLU GLU LEU ALA PRO PRO GLU ILE PHE          
SEQRES   2 D  208  TYR ASN ASP SER GLU ALA HIS LYS TYR THR GLY SER THR          
SEQRES   3 D  208  ARG VAL GLN HIS ILE GLN ALA LYS MET THR LEU ARG ALA          
SEQRES   4 D  208  LEU GLU LEU LEU ASN LEU GLN PRO CYS SER PHE ILE LEU          
SEQRES   5 D  208  ASP ILE GLY CYS GLY SER GLY LEU SER GLY GLU ILE LEU          
SEQRES   6 D  208  THR GLN GLU GLY ASP HIS VAL TRP CYS GLY LEU ASP ILE          
SEQRES   7 D  208  SER PRO SER MET LEU ALA THR GLY LEU SER ARG GLU LEU          
SEQRES   8 D  208  GLU GLY ASP LEU MET LEU GLN ASP MET GLY THR GLY ILE          
SEQRES   9 D  208  PRO PHE ARG ALA GLY SER PHE ASP ALA ALA ILE SER ILE          
SEQRES  10 D  208  SER ALA ILE GLN TRP LEU CSO ASN ALA ASP THR SER TYR          
SEQRES  11 D  208  ASN ASP PRO LYS GLN ARG LEU MET ARG PHE PHE ASN THR          
SEQRES  12 D  208  LEU TYR ALA ALA LEU LYS LYS GLY GLY LYS PHE VAL ALA          
SEQRES  13 D  208  GLN PHE TYR PRO LYS ASN ASP ASP GLN VAL ASP ASP ILE          
SEQRES  14 D  208  LEU GLN SER ALA LYS VAL ALA GLY PHE SER GLY GLY LEU          
SEQRES  15 D  208  VAL VAL ASP ASP PRO GLU SER LYS LYS ASN LYS LYS TYR          
SEQRES  16 D  208  TYR LEU VAL LEU SER SER GLY HIS HIS HIS HIS HIS HIS          
MODRES 4QTU CSO B  124  CYS  S-HYDROXYCYSTEINE                                  
MODRES 4QTU CSO D  124  CYS  S-HYDROXYCYSTEINE                                  
HET    CSO  B 124       7                                                       
HET    CSO  D 124       7                                                       
HET     ZN  A 201       1                                                       
HET    EDO  A 202       4                                                       
HET    EDO  A 203       4                                                       
HET    EDO  A 204       4                                                       
HET    EDO  A 205       4                                                       
HET    EDO  A 206       4                                                       
HET    EDO  A 207       4                                                       
HET    SAM  B 301      27                                                       
HET    EDO  B 302       4                                                       
HET    EDO  B 303       4                                                       
HET    EDO  B 304       4                                                       
HET    EDO  B 305       4                                                       
HET    EDO  B 306       4                                                       
HET    EDO  B 307       4                                                       
HET    EDO  B 308       4                                                       
HET    EDO  B 309       4                                                       
HET    EDO  B 310       4                                                       
HET    EDO  B 311       4                                                       
HET     ZN  C 201       1                                                       
HET    EDO  C 202       4                                                       
HET    EDO  C 203       4                                                       
HET    SAM  D 301      27                                                       
HET    EDO  D 302       4                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM      ZN ZINC ION                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  CSO    2(C3 H7 N O3 S)                                              
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   6  EDO    19(C2 H6 O2)                                                 
FORMUL  12  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL  28  HOH   *173(H2 O)                                                    
HELIX    1   1 LYS A    2  ASN A    7  1                                   6    
HELIX    2   2 VAL A   13  SER A   19  5                                   7    
HELIX    3   3 ASN A   43  VAL A   51  1                                   9    
HELIX    4   4 ASP A   52  VAL A   54  5                                   3    
HELIX    5   5 ASP A   55  LEU A   66  1                                  12    
HELIX    6   6 SER A   81  LEU A   85  5                                   5    
HELIX    7   7 THR A   86  LEU A  101  1                                  16    
HELIX    8   8 ASN B   15  SER B   25  1                                  11    
HELIX    9   9 SER B   25  ASN B   44  1                                  20    
HELIX   10  10 GLY B   59  ASP B   70  1                                  12    
HELIX   11  11 SER B   79  LEU B   87  1                                   9    
HELIX   12  12 ASP B   99  GLY B  103  5                                   5    
HELIX   13  13 ALA B  119  ASN B  125  5                                   7    
HELIX   14  14 ASP B  132  ALA B  147  1                                  16    
HELIX   15  15 ASN B  162  GLY B  177  1                                  16    
HELIX   16  16 LYS C    2  ASN C    7  1                                   6    
HELIX   17  17 VAL C   13  ASP C   17  5                                   5    
HELIX   18  18 ASN C   43  VAL C   51  1                                   9    
HELIX   19  19 ASP C   55  LEU C   66  1                                  12    
HELIX   20  20 SER C   81  LEU C   85  5                                   5    
HELIX   21  21 THR C   86  LEU C  101  1                                  16    
HELIX   22  22 ALA D   19  GLY D   24  1                                   6    
HELIX   23  23 SER D   25  ASN D   44  1                                  20    
HELIX   24  24 GLY D   59  ASP D   70  1                                  12    
HELIX   25  25 SER D   79  SER D   88  1                                  10    
HELIX   26  26 ASP D   99  GLY D  103  5                                   5    
HELIX   27  27 ALA D  119  CSO D  124  5                                   6    
HELIX   28  28 PRO D  133  ALA D  147  1                                  15    
HELIX   29  29 ASN D  162  GLY D  177  1                                  16    
SHEET    1   A 3 GLN A  26  TYR A  27  0                                        
SHEET    2   A 3 THR A 103  LYS A 111 -1  O  LYS A 111   N  GLN A  26           
SHEET    3   A 3 GLN A  33  GLN A  36 -1  N  GLN A  33   O  GLU A 107           
SHEET    1   B 4 GLN A  26  TYR A  27  0                                        
SHEET    2   B 4 THR A 103  LYS A 111 -1  O  LYS A 111   N  GLN A  26           
SHEET    3   B 4 ILE A 118  LYS A 122 -1  O  TYR A 119   N  MET A 110           
SHEET    4   B 4 ILE A 125  PRO A 126 -1  O  ILE A 125   N  LYS A 122           
SHEET    1   C14 ASP B  94  LEU B  97  0                                        
SHEET    2   C14 VAL B  72  ASP B  77  1  N  GLY B  75   O  ASP B  94           
SHEET    3   C14 PHE B  50  ILE B  54  1  N  ASP B  53   O  CYS B  74           
SHEET    4   C14 PHE B 111  ILE B 117  1  O  ILE B 115   N  ILE B  54           
SHEET    5   C14 LEU B 148  PHE B 158  1  O  LYS B 149   N  PHE B 111           
SHEET    6   C14 LYS B 194  SER B 200 -1  O  LEU B 197   N  ALA B 156           
SHEET    7   C14 SER B 179  ASP B 185 -1  N  VAL B 183   O  TYR B 196           
SHEET    8   C14 SER D 179  ASP D 185 -1  O  LEU D 182   N  VAL B 184           
SHEET    9   C14 LYS D 194  SER D 200 -1  O  VAL D 198   N  GLY D 181           
SHEET   10   C14 LEU D 148  PHE D 158 -1  N  ALA D 156   O  LEU D 197           
SHEET   11   C14 PHE D 111  ILE D 117  1  N  PHE D 111   O  LYS D 149           
SHEET   12   C14 PHE D  50  ILE D  54  1  N  LEU D  52   O  ILE D 115           
SHEET   13   C14 VAL D  72  ASP D  77  1  O  CYS D  74   N  ASP D  53           
SHEET   14   C14 ASP D  94  LEU D  97  1  O  ASP D  94   N  GLY D  75           
SHEET    1   D 3 GLN C  26  TYR C  27  0                                        
SHEET    2   D 3 THR C 103  LYS C 111 -1  O  LYS C 111   N  GLN C  26           
SHEET    3   D 3 GLN C  33  GLN C  36 -1  N  GLN C  33   O  GLU C 107           
SHEET    1   E 4 GLN C  26  TYR C  27  0                                        
SHEET    2   E 4 THR C 103  LYS C 111 -1  O  LYS C 111   N  GLN C  26           
SHEET    3   E 4 ILE C 118  LYS C 122 -1  O  TYR C 119   N  MET C 110           
SHEET    4   E 4 ILE C 125  ASN C 127 -1  O  ASN C 127   N  TYR C 120           
LINK         C   LEU B 123                 N   CSO B 124     1555   1555  1.33  
LINK         C   CSO B 124                 N   ASN B 125     1555   1555  1.33  
LINK         C   LEU D 123                 N   CSO D 124     1555   1555  1.33  
LINK         C   CSO D 124                 N   ASN D 125     1555   1555  1.33  
LINK         SG  CYS A  11                ZN    ZN A 201     1555   1555  2.43  
LINK         SG  CYS A  16                ZN    ZN A 201     1555   1555  2.27  
LINK         SG  CYS A 112                ZN    ZN A 201     1555   1555  2.26  
LINK         SG  CYS A 115                ZN    ZN A 201     1555   1555  2.35  
LINK         SG  CYS C  11                ZN    ZN C 201     1555   1555  2.35  
LINK         SG  CYS C  16                ZN    ZN C 201     1555   1555  2.28  
LINK         SG  CYS C 112                ZN    ZN C 201     1555   1555  2.41  
LINK         SG  CYS C 115                ZN    ZN C 201     1555   1555  2.42  
CISPEP   1 PHE A   23    PRO A   24          0        -4.37                     
CISPEP   2 PHE C   23    PRO C   24          0        -6.30                     
SITE     1 AC1  4 CYS A  11  CYS A  16  CYS A 112  CYS A 115                    
SITE     1 AC2  4 LYS A  14  LEU A 134  HOH A 309  ARG B 139                    
SITE     1 AC3  1 GLN A  36                                                     
SITE     1 AC4  6 HIS A 117  ILE A 118  TYR A 119  TYR A 120                    
SITE     2 AC4  6 ASN A 127  LEU A 129                                          
SITE     1 AC5  4 LEU A  48  ASP A  52  PHE A  78  PRO A  79                    
SITE     1 AC6  2 ASP A  87  TYR B 159                                          
SITE     1 AC7  6 HOH A 315  HOH A 317  HOH A 338  GLN B 121                    
SITE     2 AC7  6 TRP B 122  LYS B 161                                          
SITE     1 AC8 22 TYR B  22  GLN B  32  GLY B  55  CYS B  56                    
SITE     2 AC8 22 GLY B  57  LEU B  60  SER B  61  ASP B  77                    
SITE     3 AC8 22 ILE B  78  SER B  79  MET B  82  GLN B  98                    
SITE     4 AC8 22 ASP B  99  MET B 100  ILE B 117  SER B 118                    
SITE     5 AC8 22 ALA B 119  TRP B 122  EDO B 302  HOH B 401                    
SITE     6 AC8 22 HOH B 406  HOH B 438                                          
SITE     1 AC9  4 THR A  86  ASP A  87  ASP A  88  SAM B 301                    
SITE     1 BC1  2 ARG B 139  ASN B 142                                          
SITE     1 BC2  7 LEU B 170  LYS B 174  PHE B 178  SER B 179                    
SITE     2 BC2  7 GLY B 180  ASP D 186  GLU D 188                               
SITE     1 BC3  3 GLU B 188  LEU D 170  GLY D 180                               
SITE     1 BC4  3 SER B  25  THR B  26  ARG B  27                               
SITE     1 BC5  2 GLN B  67  GLU B  68                                          
SITE     1 BC6  6 ASN A  43  ASP B  70  HIS B  71  VAL B  72                    
SITE     2 BC6  6 GLU B  92  HOH B 422                                          
SITE     1 BC7  4 LEU B  45  GLU B  68  HIS B  71  HOH B 408                    
SITE     1 BC8  6 ILE B  12  TYR B  14  SER B  79  PRO B  80                    
SITE     2 BC8  6 SER B  81  HOH B 458                                          
SITE     1 BC9  3 ARG B  38  VAL D 198  EDO D 302                               
SITE     1 CC1  4 CYS C  11  CYS C  16  CYS C 112  CYS C 115                    
SITE     1 CC2  7 THR A  18  SER A  19  ASN A  20  ASP A  21                    
SITE     2 CC2  7 HOH A 332  LYS C  75  SER C  77                               
SITE     1 CC3  4 ILE C 118  TYR C 119  TYR C 120  ASN C 127                    
SITE     1 CC4 18 TYR D  22  GLN D  32  GLY D  55  CYS D  56                    
SITE     2 CC4 18 GLY D  57  LEU D  60  SER D  61  ASP D  77                    
SITE     3 CC4 18 ILE D  78  SER D  79  MET D  82  GLN D  98                    
SITE     4 CC4 18 ASP D  99  MET D 100  ILE D 117  SER D 118                    
SITE     5 CC4 18 TRP D 122  HOH D 401                                          
SITE     1 CC5  4 VAL B 183  VAL B 198  EDO B 311  ARG D  38                    
CRYST1   75.472   53.733   85.205  90.00  94.55  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013250  0.000000  0.001055        0.00000                         
SCALE2      0.000000  0.018611  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011774        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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