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Database: PDB
Entry: 3F2K
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HEADER    TRANSFERASE                             29-OCT-08   3F2K              
TITLE     STRUCTURE OF THE TRANSPOSASE DOMAIN OF HUMAN HISTONE-LYSINE           
TITLE    2 N-METHYLTRANSFERASE SETMAR                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETMAR;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: TRANSPOSASE DOMAIN;                                        
COMPND   5 SYNONYM: SET DOMAIN AND MARINER TRANSPOSASE FUSION GENE-             
COMPND   6 CONTAINING PROTEIN, METNASE, HSMAR1;                                 
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: LYFA PEPTIDE;                                              
COMPND  11 CHAIN: C;                                                            
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: SETMAR;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES                                                       
KEYWDS    HISTONE-LYSINE N-METHYLTRANSFERASE SETMAR, SET DOMAIN AND             
KEYWDS   2 MARINER TRANSPOSASE FUSION, SET DOMAIN AND MARINER                   
KEYWDS   3 TRANSPOSASE FUSION GENE-CONTAINING PROTEIN, STRUCTURAL               
KEYWDS   4 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, ALTERNATIVE           
KEYWDS   5 SPLICING, CHROMATIN REGULATOR, COILED COIL, DNA DAMAGE, DNA          
KEYWDS   6 REPAIR, DNA-BINDING, METHYLTRANSFERASE, NUCLEUS,                     
KEYWDS   7 PHOSPHOPROTEIN, TRANSFERASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.AMAYA,L.DOMBROVSKI,S.NI,C.BOUNTRA,J.WEIGELT,                      
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOTCHKAREV,J.MIN,                       
AUTHOR   3 A.N.PLOTNIKOV,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)              
REVDAT   3   25-AUG-09 3F2K    1       REMARK                                   
REVDAT   2   24-FEB-09 3F2K    1       VERSN                                    
REVDAT   1   25-NOV-08 3F2K    0                                                
JRNL        AUTH   L.DOMBROVSKI,M.F.AMAYA,S.NI,C.BOUNTRA,J.WEIGELT,             
JRNL        AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOTCHKAREV,J.MIN,               
JRNL        AUTH 3 A.N.PLOTNIKOV,H.WU                                           
JRNL        TITL   THE CRYSTAL STRUCTURE OF TRANSPOSASE DOMAIN OF               
JRNL        TITL 2 HUMAN HISTONE-LYSINE N-METHYLTRANSFERASE SETMAR.             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 34969                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1846                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2593                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 147                          
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3127                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 406                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : 0.24000                                              
REMARK   3    B33 (A**2) : -0.07000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.49000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.162         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.156         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.112         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3214 ; 0.022 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4380 ; 1.729 ; 1.929       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   390 ; 5.741 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   169 ;40.091 ;24.793       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   505 ;12.709 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;21.307 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   471 ; 0.129 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2522 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1676 ; 0.212 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2216 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   326 ; 0.193 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    27 ; 0.165 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.223 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2015 ; 1.254 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3141 ; 1.853 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1388 ; 2.907 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1236 ; 4.056 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3F2K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050066.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E DW                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.504                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36815                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: 2F7T                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PURIFIED SETMAR TRANSPOSASE DOMAIN       
REMARK 280  WAS CRYSTALLIZED IN 20% PEG 3350, 0.2 M DI-NA TARTRATE., PH         
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
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       79.41300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.26050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.41300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.26050            
REMARK 290   SMTRY3   4  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 480 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 10520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 271  LIES ON A SPECIAL POSITION.                          
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     TRP A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ARG A    48                                                      
REMARK 465     ARG A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     ALA A    51                                                      
REMARK 465     GLN A    52                                                      
REMARK 465     TRP A    53                                                      
REMARK 465     LEU A    54                                                      
REMARK 465     ASP A    55                                                      
REMARK 465     GLN A    56                                                      
REMARK 465     GLU A    57                                                      
REMARK 465     GLU A    58                                                      
REMARK 465     ALA A    59                                                      
REMARK 465     PRO A    60                                                      
REMARK 465     LYS A    61                                                      
REMARK 465     HIS A    62                                                      
REMARK 465     PHE A    63                                                      
REMARK 465     PRO A    64                                                      
REMARK 465     LYS A    65                                                      
REMARK 465     PRO A    66                                                      
REMARK 465     ILE A    67                                                      
REMARK 465     LEU A    68                                                      
REMARK 465     ALA A   118                                                      
REMARK 465     LEU A   119                                                      
REMARK 465     VAL A   120                                                      
REMARK 465     ASN A   121                                                      
REMARK 465     ASP A   226                                                      
REMARK 465     TRP B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     TYR B    44                                                      
REMARK 465     ASP B    45                                                      
REMARK 465     ASN B    46                                                      
REMARK 465     ARG B    47                                                      
REMARK 465     ARG B    48                                                      
REMARK 465     ARG B    49                                                      
REMARK 465     SER B    50                                                      
REMARK 465     ALA B    51                                                      
REMARK 465     GLN B    52                                                      
REMARK 465     TRP B    53                                                      
REMARK 465     LEU B    54                                                      
REMARK 465     ASP B    55                                                      
REMARK 465     GLN B    56                                                      
REMARK 465     GLU B    57                                                      
REMARK 465     GLU B    58                                                      
REMARK 465     ALA B    59                                                      
REMARK 465     PRO B    60                                                      
REMARK 465     LYS B    61                                                      
REMARK 465     HIS B    62                                                      
REMARK 465     PHE B    63                                                      
REMARK 465     PRO B    64                                                      
REMARK 465     LYS B    65                                                      
REMARK 465     PRO B    66                                                      
REMARK 465     ILE B    67                                                      
REMARK 465     LEU B    68                                                      
REMARK 465     HIS B    69                                                      
REMARK 465     PRO B    70                                                      
REMARK 465     LEU B    90                                                      
REMARK 465     ASN B    91                                                      
REMARK 465     PRO B    92                                                      
REMARK 465     GLY B    93                                                      
REMARK 465     GLU B    94                                                      
REMARK 465     THR B    95                                                      
REMARK 465     ILE B    96                                                      
REMARK 465     LEU B   117                                                      
REMARK 465     ALA B   118                                                      
REMARK 465     LEU B   119                                                      
REMARK 465     VAL B   120                                                      
REMARK 465     ASN B   121                                                      
REMARK 465     ASP B   226                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   5    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A  69    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A  71    CG   CD   CE   NZ                                   
REMARK 470     ARG A 122    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 177    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 180    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 182    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 193    CG   CD   OE1  OE2                                  
REMARK 470     SER A 197    OG                                                  
REMARK 470     LYS B  40    CG   CD   CE   NZ                                   
REMARK 470     ILE B  42    CG1  CG2  CD1                                       
REMARK 470     LEU B  43    CG   CD1  CD2                                       
REMARK 470     LYS B  71    CG   CD   CE   NZ                                   
REMARK 470     LYS B  72    CG   CD   CE   NZ                                   
REMARK 470     LYS B 100    CG   CD   CE   NZ                                   
REMARK 470     GLN B 103    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 107    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 142    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 180    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B 182    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B 184    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 193    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 209    CG   CD   OE1  NE2                                  
REMARK 470     PHE B 225    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU C  13    CG   CD1  CD2                                       
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   ND2  ASN B   131     O    HOH B   241              1.28            
REMARK 500   O    HOH A   446     O    HOH A   447              1.94            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   379     O    HOH A   441     4545     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  16   CG    GLU A  16   CD      0.100                       
REMARK 500    GLU B  16   CG    GLU B  16   CD      0.138                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B  33   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
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    HIS A 167      -72.52   -112.26                                   
REMARK 500    GLU B  28       79.05   -152.85                                   
REMARK 500    HIS B 167      -66.05   -108.16                                   
REMARK 500    SER B 197       35.25    -83.89                                   
REMARK 500    SER B 199      175.14    -53.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 356        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH B 372        DISTANCE =  9.55 ANGSTROMS                       
REMARK 525    HOH B 375        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH B 381        DISTANCE =  8.38 ANGSTROMS                       
REMARK 525    HOH A 427        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A 445        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A 447        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH A 457        DISTANCE =  5.64 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 227  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  38   OD1                                                    
REMARK 620 2 ASP A 130   OD2  92.2                                              
REMARK 620 3 HOH A 469   O    88.4  86.8                                        
REMARK 620 4 HOH A 242   O   178.0  89.4  92.9                                  
REMARK 620 5 HOH A 259   O    87.4 178.5  94.6  91.0                            
REMARK 620 6 HOH A 241   O    90.9  89.8 176.5  87.8  88.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 227  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  38   OD1                                                    
REMARK 620 2 ASP B 130   OD2 102.5                                              
REMARK 620 3 HOH B 230   O    94.4  93.2                                        
REMARK 620 4 HOH B 331   O   171.3  84.8  89.8                                  
REMARK 620 5 HOH B 259   O    81.9 172.8  92.2  90.4                            
REMARK 620 6 HOH B 260   O    86.2  86.4 179.3  89.7  88.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 227                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 227                  
DBREF  3F2K A    1   226  UNP    Q53H47   SETMR_HUMAN    446    671             
DBREF  3F2K B    1   226  UNP    Q53H47   SETMR_HUMAN    446    671             
DBREF  3F2K C   13    16  PDB    3F2K     3F2K            13     16             
SEQRES   1 A  226  TRP VAL PRO HIS GLU LEU THR GLU ASN GLN LYS ASN ARG          
SEQRES   2 A  226  ARG PHE GLU VAL SER SER SER LEU ILE LEU ARG ASN HIS          
SEQRES   3 A  226  ASN GLU PRO PHE LEU ASP ARG ILE VAL THR CYS ASP GLU          
SEQRES   4 A  226  LYS TRP ILE LEU TYR ASP ASN ARG ARG ARG SER ALA GLN          
SEQRES   5 A  226  TRP LEU ASP GLN GLU GLU ALA PRO LYS HIS PHE PRO LYS          
SEQRES   6 A  226  PRO ILE LEU HIS PRO LYS LYS VAL MSE VAL THR ILE TRP          
SEQRES   7 A  226  TRP SER ALA ALA GLY LEU ILE HIS TYR SER PHE LEU ASN          
SEQRES   8 A  226  PRO GLY GLU THR ILE THR SER GLU LYS TYR ALA GLN GLU          
SEQRES   9 A  226  ILE ASP GLU MSE ASN GLN LYS LEU GLN ARG LEU GLN LEU          
SEQRES  10 A  226  ALA LEU VAL ASN ARG LYS GLY PRO ILE LEU LEU HIS ASP          
SEQRES  11 A  226  ASN ALA ARG PRO HIS VAL ALA GLN PRO THR LEU GLN LYS          
SEQRES  12 A  226  LEU ASN GLU LEU GLY TYR GLU VAL LEU PRO HIS PRO PRO          
SEQRES  13 A  226  TYR SER PRO ASP LEU LEU PRO THR ASN TYR HIS VAL PHE          
SEQRES  14 A  226  LYS HIS LEU ASN ASN PHE LEU GLN GLY LYS ARG PHE HIS          
SEQRES  15 A  226  ASN GLN GLN ASP ALA GLU ASN ALA PHE GLN GLU PHE VAL          
SEQRES  16 A  226  GLU SER GLN SER THR ASP PHE TYR ALA THR GLY ILE ASN          
SEQRES  17 A  226  GLN LEU ILE SER ARG TRP GLN LYS CYS VAL ASP CYS ASN          
SEQRES  18 A  226  GLY SER TYR PHE ASP                                          
SEQRES   1 B  226  TRP VAL PRO HIS GLU LEU THR GLU ASN GLN LYS ASN ARG          
SEQRES   2 B  226  ARG PHE GLU VAL SER SER SER LEU ILE LEU ARG ASN HIS          
SEQRES   3 B  226  ASN GLU PRO PHE LEU ASP ARG ILE VAL THR CYS ASP GLU          
SEQRES   4 B  226  LYS TRP ILE LEU TYR ASP ASN ARG ARG ARG SER ALA GLN          
SEQRES   5 B  226  TRP LEU ASP GLN GLU GLU ALA PRO LYS HIS PHE PRO LYS          
SEQRES   6 B  226  PRO ILE LEU HIS PRO LYS LYS VAL MSE VAL THR ILE TRP          
SEQRES   7 B  226  TRP SER ALA ALA GLY LEU ILE HIS TYR SER PHE LEU ASN          
SEQRES   8 B  226  PRO GLY GLU THR ILE THR SER GLU LYS TYR ALA GLN GLU          
SEQRES   9 B  226  ILE ASP GLU MSE ASN GLN LYS LEU GLN ARG LEU GLN LEU          
SEQRES  10 B  226  ALA LEU VAL ASN ARG LYS GLY PRO ILE LEU LEU HIS ASP          
SEQRES  11 B  226  ASN ALA ARG PRO HIS VAL ALA GLN PRO THR LEU GLN LYS          
SEQRES  12 B  226  LEU ASN GLU LEU GLY TYR GLU VAL LEU PRO HIS PRO PRO          
SEQRES  13 B  226  TYR SER PRO ASP LEU LEU PRO THR ASN TYR HIS VAL PHE          
SEQRES  14 B  226  LYS HIS LEU ASN ASN PHE LEU GLN GLY LYS ARG PHE HIS          
SEQRES  15 B  226  ASN GLN GLN ASP ALA GLU ASN ALA PHE GLN GLU PHE VAL          
SEQRES  16 B  226  GLU SER GLN SER THR ASP PHE TYR ALA THR GLY ILE ASN          
SEQRES  17 B  226  GLN LEU ILE SER ARG TRP GLN LYS CYS VAL ASP CYS ASN          
SEQRES  18 B  226  GLY SER TYR PHE ASP                                          
SEQRES   1 C    4  LEU TYR PHE ALA                                              
MODRES 3F2K MSE A   74  MET  SELENOMETHIONINE                                   
MODRES 3F2K MSE A  108  MET  SELENOMETHIONINE                                   
MODRES 3F2K MSE B   74  MET  SELENOMETHIONINE                                   
MODRES 3F2K MSE B  108  MET  SELENOMETHIONINE                                   
HET    MSE  A  74       8                                                       
HET    MSE  A 108       8                                                       
HET    MSE  B  74       8                                                       
HET    MSE  B 108       8                                                       
HET     MG  A 227       1                                                       
HET     MG  B 227       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  HOH   *406(H2 O)                                                    
HELIX    1   1 THR A    7  GLU A   28  1                                  22    
HELIX    2   2 PHE A   30  ASP A   32  5                                   3    
HELIX    3   3 THR A   97  GLN A  116  1                                  20    
HELIX    4   4 ALA A  132  ALA A  137  1                                   6    
HELIX    5   5 PRO A  139  GLY A  148  1                                  10    
HELIX    6   6 SER A  158  LEU A  161  5                                   4    
HELIX    7   7 LEU A  162  HIS A  167  1                                   6    
HELIX    8   8 HIS A  167  GLN A  177  1                                  11    
HELIX    9   9 ASN A  183  SER A  197  1                                  15    
HELIX   10  10 ASP A  201  GLN A  209  1                                   9    
HELIX   11  11 GLN A  209  CYS A  220  1                                  12    
HELIX   12  12 THR B    7  GLU B   28  1                                  22    
HELIX   13  13 PHE B   30  ASP B   32  5                                   3    
HELIX   14  14 THR B   97  GLN B  116  1                                  20    
HELIX   15  15 ALA B  132  ALA B  137  1                                   6    
HELIX   16  16 ALA B  137  GLY B  148  1                                  12    
HELIX   17  17 SER B  158  LEU B  161  5                                   4    
HELIX   18  18 LEU B  162  HIS B  167  1                                   6    
HELIX   19  19 HIS B  167  GLN B  177  1                                  11    
HELIX   20  20 ASN B  183  SER B  197  1                                  15    
HELIX   21  21 ASP B  201  GLN B  209  1                                   9    
HELIX   22  22 GLN B  209  CYS B  220  1                                  12    
SHEET    1   A 5 GLY A  83  PHE A  89  0                                        
SHEET    2   A 5 LYS A  72  SER A  80 -1  N  TRP A  78   O  HIS A  86           
SHEET    3   A 5 ILE A  34  LEU A  43 -1  N  ILE A  42   O  VAL A  73           
SHEET    4   A 5 ILE A 126  LEU A 128  1  O  ILE A 126   N  VAL A  35           
SHEET    5   A 5 GLU A 150  VAL A 151  1  O  GLU A 150   N  LEU A 127           
SHEET    1   B 5 GLY B  83  SER B  88  0                                        
SHEET    2   B 5 VAL B  73  SER B  80 -1  N  TRP B  78   O  HIS B  86           
SHEET    3   B 5 ILE B  34  ILE B  42 -1  N  LYS B  40   O  VAL B  75           
SHEET    4   B 5 ILE B 126  LEU B 128  1  O  ILE B 126   N  VAL B  35           
SHEET    5   B 5 GLU B 150  VAL B 151  1  O  GLU B 150   N  LEU B 127           
LINK         C   VAL A  73                 N   MSE A  74     1555   1555  1.33  
LINK         C   MSE A  74                 N   VAL A  75     1555   1555  1.33  
LINK         C   GLU A 107                 N   MSE A 108     1555   1555  1.34  
LINK         C   MSE A 108                 N   ASN A 109     1555   1555  1.33  
LINK         C   VAL B  73                 N   MSE B  74     1555   1555  1.33  
LINK         C   MSE B  74                 N   VAL B  75     1555   1555  1.32  
LINK         C   GLU B 107                 N   MSE B 108     1555   1555  1.35  
LINK         C   MSE B 108                 N   ASN B 109     1555   1555  1.35  
LINK         OD1 ASP A  38                MG    MG A 227     1555   1555  2.20  
LINK         OD2 ASP A 130                MG    MG A 227     1555   1555  2.00  
LINK         OD1 ASP B  38                MG    MG B 227     1555   1555  2.10  
LINK         OD2 ASP B 130                MG    MG B 227     1555   1555  2.05  
LINK        MG    MG A 227                 O   HOH A 469     1555   1555  2.21  
LINK        MG    MG A 227                 O   HOH A 242     1555   1555  2.16  
LINK        MG    MG A 227                 O   HOH A 259     1555   1555  2.04  
LINK        MG    MG A 227                 O   HOH A 241     1555   1555  2.16  
LINK        MG    MG B 227                 O   HOH B 230     1555   1555  2.09  
LINK        MG    MG B 227                 O   HOH B 331     1555   1555  2.22  
LINK        MG    MG B 227                 O   HOH B 259     1555   1555  2.19  
LINK        MG    MG B 227                 O   HOH B 260     1555   1555  2.32  
CISPEP   1 GLN A  138    PRO A  139          0         4.26                     
CISPEP   2 GLN A  177    GLY A  178          0         5.15                     
CISPEP   3 GLN B  177    GLY B  178          0        -3.11                     
SITE     1 AC1  6 ASP A  38  ASP A 130  HOH A 241  HOH A 242                    
SITE     2 AC1  6 HOH A 259  HOH A 469                                          
SITE     1 AC2  6 ASP B  38  ASP B 130  HOH B 230  HOH B 259                    
SITE     2 AC2  6 HOH B 260  HOH B 331                                          
CRYST1  158.826   46.521   61.748  90.00  92.04  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      0.006296  0.000000  0.000224        0.00000                         
SCALE2      0.000000  0.021496  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016205        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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