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Database: PDB
Entry: 3N71
LinkDB: 3N71
Original site: 3N71 
HEADER    TRANSCRIPTION                           26-MAY-10   3N71              
TITLE     CRYSTAL STRUCTURE OF CARDIAC SPECIFIC HISTONE METHYLTRANSFERASE SMYD1 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE LYSINE METHYLTRANSFERASE SMYD1;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SET AND MYND DOMAIN CONTAINING 1, ISOFORM CRA_B, SMYD1      
COMPND   5 PROTEIN;                                                             
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: MCG_127279, SMYD1;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSUMO                                     
KEYWDS    HISTONE LYSINE METHYLTRANSFERASE, SMYD1, HEART DEVELOPMENT, MYND,     
KEYWDS   2 TRANSCRIPTION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.SIRINUPONG,Z.YANG                                                   
REVDAT   3   05-JAN-11 3N71    1       JRNL                                     
REVDAT   2   27-OCT-10 3N71    1       JRNL                                     
REVDAT   1   13-OCT-10 3N71    0                                                
JRNL        AUTH   N.SIRINUPONG,J.BRUNZELLE,J.YE,A.PIRZADA,L.NICO,Z.YANG        
JRNL        TITL   CRYSTAL STRUCTURE OF CARDIAC-SPECIFIC HISTONE                
JRNL        TITL 2 METHYLTRANSFERASE SMYD1 REVEALS UNUSUAL ACTIVE SITE          
JRNL        TITL 3 ARCHITECTURE.                                                
JRNL        REF    J.BIOL.CHEM.                  V. 285 40635 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20943667                                                     
JRNL        DOI    10.1074/JBC.M110.168187                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 27386                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : 5% RANDOM                       
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1992                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3120                       
REMARK   3   BIN FREE R VALUE                    : 0.3340                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 195                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3786                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 110                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.99                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3N71 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059460.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.28287, 1.27823, 1.28268          
REMARK 200  MONOCHROMATOR                  : KOHZU                              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27582                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.56700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG8000, 2.5% GLYCEROL, 200 MM       
REMARK 280  NDSB-201, 100 MM MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       85.25000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.21911            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       19.03333            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       85.25000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       49.21911            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       19.03333            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       85.25000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       49.21911            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       19.03333            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       98.43822            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       38.06667            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       98.43822            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       38.06667            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       98.43822            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       38.06667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     GLN A   469                                                      
REMARK 465     PRO A   470                                                      
REMARK 465     MET A   471                                                      
REMARK 465     GLN A   472                                                      
REMARK 465     VAL A   473                                                      
REMARK 465     MET A   474                                                      
REMARK 465     ALA A   475                                                      
REMARK 465     GLU A   476                                                      
REMARK 465     PRO A   477                                                      
REMARK 465     SER A   478                                                      
REMARK 465     ASN A   479                                                      
REMARK 465     GLU A   480                                                      
REMARK 465     PRO A   481                                                      
REMARK 465     ALA A   482                                                      
REMARK 465     PRO A   483                                                      
REMARK 465     ALA A   484                                                      
REMARK 465     LEU A   485                                                      
REMARK 465     PHE A   486                                                      
REMARK 465     HIS A   487                                                      
REMARK 465     LYS A   488                                                      
REMARK 465     LYS A   489                                                      
REMARK 465     GLN A   490                                                      
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    ALA A  30       -7.60     80.05                                   
REMARK 500    GLN A  59      149.72   -176.57                                   
REMARK 500    ASN A 101      160.19    -45.61                                   
REMARK 500    THR A 119      154.56    179.77                                   
REMARK 500    ASN A 180        0.78   -150.68                                   
REMARK 500    GLU A 222       82.95   -154.65                                   
REMARK 500    ALA A 223      178.46     66.72                                   
REMARK 500    SER A 226       75.22     53.23                                   
REMARK 500    LEU A 256       61.28    -67.23                                   
REMARK 500    TYR A 271       54.49     37.46                                   
REMARK 500    LYS A 284      -12.45     82.99                                   
REMARK 500    LYS A 296       74.73     64.30                                   
REMARK 500    VAL A 342      -60.62   -105.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    CYS A 125        18.4      L          L   OUTSIDE RANGE           
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 497  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 274   SG                                                     
REMARK 620 2 CYS A 279   SG  121.7                                              
REMARK 620 3 CYS A 276   SG  108.4 113.5                                        
REMARK 620 4 CYS A 208   SG  113.4  94.6 103.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 496  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  68   SG                                                     
REMARK 620 2 HIS A  86   NE2 105.8                                              
REMARK 620 3 CYS A  90   SG  122.5 101.0                                        
REMARK 620 4 CYS A  65   SG  112.1  98.8 112.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 495  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  78   SG                                                     
REMARK 620 2 CYS A  52   SG  111.5                                              
REMARK 620 3 CYS A  55   SG  129.4 112.4                                        
REMARK 620 4 CYS A  74   SG  108.5  92.0  93.7                                  
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 SFG A 491                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 492                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 493                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 494                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 495                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 496                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 497                  
DBREF  3N71 A    1   490  UNP    Q6DFW7   Q6DFW7_MOUSE     1    490             
SEQRES   1 A  490  MET THR ILE GLY SER MET GLU ASN VAL GLU VAL PHE THR          
SEQRES   2 A  490  SER GLU GLY LYS GLY ARG GLY LEU LYS ALA THR LYS GLU          
SEQRES   3 A  490  PHE TRP ALA ALA ASP VAL ILE PHE ALA GLU ARG ALA TYR          
SEQRES   4 A  490  SER ALA VAL VAL PHE ASP SER LEU ILE ASN PHE VAL CYS          
SEQRES   5 A  490  HIS THR CYS PHE LYS ARG GLN GLU LYS LEU HIS ARG CYS          
SEQRES   6 A  490  GLY GLN CYS LYS PHE ALA HIS TYR CYS ASP ARG THR CYS          
SEQRES   7 A  490  GLN LYS ASP ALA TRP LEU ASN HIS LYS ASN GLU CYS ALA          
SEQRES   8 A  490  ALA ILE LYS LYS TYR GLY LYS VAL PRO ASN GLU ASN ILE          
SEQRES   9 A  490  ARG LEU ALA ALA ARG ILE MET TRP ARG VAL GLU ARG GLU          
SEQRES  10 A  490  GLY THR GLY LEU THR GLU GLY CYS LEU VAL SER VAL ASP          
SEQRES  11 A  490  ASP LEU GLN ASN HIS VAL GLU HIS PHE GLY GLU GLU GLU          
SEQRES  12 A  490  GLN LYS GLU LEU ARG VAL ASP VAL ASP THR PHE LEU GLN          
SEQRES  13 A  490  TYR TRP PRO PRO GLN SER GLN GLN PHE SER MET GLN TYR          
SEQRES  14 A  490  ILE SER HIS ILE PHE GLY VAL ILE ASN CYS ASN GLY PHE          
SEQRES  15 A  490  THR LEU SER ASP GLN ARG GLY LEU GLN ALA VAL GLY VAL          
SEQRES  16 A  490  GLY ILE PHE PRO ASN LEU GLY LEU VAL ASN HIS ASP CYS          
SEQRES  17 A  490  TRP PRO ASN CYS THR VAL ILE PHE ASN ASN GLY ASN HIS          
SEQRES  18 A  490  GLU ALA VAL LYS SER MET PHE HIS THR GLN MET ARG ILE          
SEQRES  19 A  490  GLU LEU ARG ALA LEU GLY LYS ILE SER GLU GLY GLU GLU          
SEQRES  20 A  490  LEU THR VAL SER TYR ILE ASP PHE LEU HIS LEU SER GLU          
SEQRES  21 A  490  GLU ARG ARG ARG GLN LEU LYS LYS GLN TYR TYR PHE ASP          
SEQRES  22 A  490  CYS SER CYS GLU HIS CYS GLN LYS GLY LEU LYS ASP ASP          
SEQRES  23 A  490  LEU PHE LEU ALA ALA LYS GLU ASP PRO LYS PRO SER GLN          
SEQRES  24 A  490  GLU VAL VAL LYS GLU MET ILE GLN PHE SER LYS ASP THR          
SEQRES  25 A  490  LEU GLU LYS ILE ASP LYS ALA ARG SER GLU GLY LEU TYR          
SEQRES  26 A  490  HIS GLU VAL VAL LYS LEU CYS ARG GLU CYS LEU GLU LYS          
SEQRES  27 A  490  GLN GLU PRO VAL PHE ALA ASP THR ASN LEU TYR VAL LEU          
SEQRES  28 A  490  ARG LEU LEU SER ILE ALA SER GLU VAL LEU SER TYR LEU          
SEQRES  29 A  490  GLN ALA TYR GLU GLU ALA SER HIS TYR ALA ARG ARG MET          
SEQRES  30 A  490  VAL ASP GLY TYR MET LYS LEU TYR HIS HIS ASN ASN ALA          
SEQRES  31 A  490  GLN LEU GLY MET ALA VAL MET ARG ALA GLY LEU THR ASN          
SEQRES  32 A  490  TRP HIS ALA GLY HIS ILE GLU VAL GLY HIS GLY MET ILE          
SEQRES  33 A  490  CYS LYS ALA TYR ALA ILE LEU LEU VAL THR HIS GLY PRO          
SEQRES  34 A  490  SER HIS PRO ILE THR LYS ASP LEU GLU ALA MET ARG MET          
SEQRES  35 A  490  GLN THR GLU MET GLU LEU ARG MET PHE ARG GLN ASN GLU          
SEQRES  36 A  490  PHE MET TYR HIS LYS MET ARG GLU ALA ALA LEU ASN ASN          
SEQRES  37 A  490  GLN PRO MET GLN VAL MET ALA GLU PRO SER ASN GLU PRO          
SEQRES  38 A  490  ALA PRO ALA LEU PHE HIS LYS LYS GLN                          
HET    SFG  A 491      27                                                       
HET    MES  A 492      12                                                       
HET    GOL  A 493       6                                                       
HET    GOL  A 494       6                                                       
HET     ZN  A 495       1                                                       
HET     ZN  A 496       1                                                       
HET     ZN  A 497       1                                                       
HETNAM     SFG ADENOSYL-ORNITHINE                                               
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     GOL GLYCEROL                                                         
HETNAM      ZN ZINC ION                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SFG    C15 H23 N7 O5                                                
FORMUL   3  MES    C6 H13 N O4 S                                                
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   6   ZN    3(ZN 2+)                                                     
FORMUL   9  HOH   *110(H2 O)                                                    
HELIX    1   1 ASP A   45  ILE A   48  5                                   4    
HELIX    2   2 ASP A   75  GLY A   97  1                                  23    
HELIX    3   3 ASN A  101  GLU A  117  1                                  17    
HELIX    4   4 SER A  128  LEU A  132  5                                   5    
HELIX    5   5 HIS A  135  PHE A  139  5                                   5    
HELIX    6   6 GLY A  140  TRP A  158  1                                  19    
HELIX    7   7 SER A  166  CYS A  179  1                                  14    
HELIX    8   8 ASN A  200  VAL A  204  5                                   5    
HELIX    9   9 MET A  227  GLN A  231  5                                   5    
HELIX   10  10 LEU A  258  TYR A  271  1                                  14    
HELIX   11  11 CYS A  276  GLY A  282  1                                   7    
HELIX   12  12 LYS A  284  LEU A  289  1                                   6    
HELIX   13  13 SER A  298  SER A  321  1                                  24    
HELIX   14  14 LEU A  324  GLU A  340  1                                  17    
HELIX   15  15 ASN A  347  LEU A  364  1                                  18    
HELIX   16  16 ALA A  366  TYR A  385  1                                  20    
HELIX   17  17 ASN A  389  ALA A  406  1                                  18    
HELIX   18  18 HIS A  408  HIS A  427  1                                  20    
HELIX   19  19 HIS A  431  LEU A  466  1                                  36    
SHEET    1   A 2 VAL A   9  THR A  13  0                                        
SHEET    2   A 2 ARG A  19  ALA A  23 -1  O  GLY A  20   N  PHE A  12           
SHEET    1   B 3 VAL A  32  GLU A  36  0                                        
SHEET    2   B 3 ARG A 233  ALA A 238 -1  O  ILE A 234   N  GLU A  36           
SHEET    3   B 3 CYS A 212  ASN A 217 -1  N  ASN A 217   O  ARG A 233           
SHEET    1   C 3 SER A  40  VAL A  43  0                                        
SHEET    2   C 3 ALA A 192  ILE A 197 -1  O  ILE A 197   N  SER A  40           
SHEET    3   C 3 GLY A 181  SER A 185 -1  N  LEU A 184   O  GLY A 194           
SHEET    1   D 2 HIS A  63  ARG A  64  0                                        
SHEET    2   D 2 HIS A  72  TYR A  73 -1  O  TYR A  73   N  HIS A  63           
SHEET    1   E 2 ASN A 205  HIS A 206  0                                        
SHEET    2   E 2 THR A 249  VAL A 250  1  O  VAL A 250   N  ASN A 205           
LINK         SG  CYS A 274                ZN    ZN A 497     1555   1555  2.27  
LINK         SG  CYS A  68                ZN    ZN A 496     1555   1555  2.30  
LINK         NE2 HIS A  86                ZN    ZN A 496     1555   1555  2.37  
LINK         SG  CYS A 279                ZN    ZN A 497     1555   1555  2.37  
LINK         SG  CYS A  78                ZN    ZN A 495     1555   1555  2.40  
LINK         SG  CYS A  52                ZN    ZN A 495     1555   1555  2.45  
LINK         SG  CYS A  55                ZN    ZN A 495     1555   1555  2.52  
LINK         SG  CYS A  90                ZN    ZN A 496     1555   1555  2.53  
LINK         SG  CYS A 276                ZN    ZN A 497     1555   1555  2.54  
LINK         SG  CYS A 208                ZN    ZN A 497     1555   1555  2.60  
LINK         SG  CYS A  74                ZN    ZN A 495     1555   1555  2.65  
LINK         SG  CYS A  65                ZN    ZN A 496     1555   1555  2.66  
SITE     1 AC1 13 LYS A  17  ARG A  19  GLN A 133  HIS A 135                    
SITE     2 AC1 13 ASN A 180  GLY A 202  LEU A 203  VAL A 204                    
SITE     3 AC1 13 ASN A 205  HIS A 206  TYR A 252  TYR A 270                    
SITE     4 AC1 13 PHE A 272                                                     
SITE     1 AC2  5 VAL A 114  ASP A 130  PHE A 165  SER A 166                    
SITE     2 AC2  5 TYR A 169                                                     
SITE     1 AC3  4 PHE A  44  ASP A  45  SER A  46  GLU A 102                    
SITE     1 AC4  3 LEU A  47  ARG A  58  GLN A 191                               
SITE     1 AC5  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC6  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC7  4 CYS A 208  CYS A 274  CYS A 276  CYS A 279                    
CRYST1  170.500  170.500   57.100  90.00  90.00 120.00 H 3           9          
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      0.005865  0.003386  0.000000        0.00000                         
SCALE2      0.000000  0.006772  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017513        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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