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Database: PDB
Entry: 3OXF
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Original site: 3OXF 
HEADER    TRANSFERASE                             21-SEP-10   3OXF              
TITLE     HUMAN LYSINE METHYLTRANSFERASE SMYD3 IN COMPLEX WITH ADOHCY (FORM I)  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET AND MYND DOMAIN-CONTAINING PROTEIN 3;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ZINC FINGER MYND DOMAIN-CONTAINING PROTEIN 1;               
COMPND   5 EC: 2.1.1.43;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SMYD3, ZMYND1, ZNFN3A1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    SMYD PROTEINS, MYND, SET DOMAIN, HISTONE LYSINE METHYLTRANSFERASE,    
KEYWDS   2 HISTONE METHYLATION, H3K4, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XU,J.WU,B.SUN,C.ZHONG,J.DING                                        
REVDAT   3   08-NOV-17 3OXF    1       REMARK                                   
REVDAT   2   13-JUL-11 3OXF    1       JRNL                                     
REVDAT   1   23-FEB-11 3OXF    0                                                
JRNL        AUTH   S.XU,J.WU,B.SUN,C.ZHONG,J.DING                               
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL STUDIES OF HUMAN LYSINE           
JRNL        TITL 2 METHYLTRANSFERASE SMYD3 REVEAL THE IMPORTANT FUNCTIONAL      
JRNL        TITL 3 ROLES OF ITS POST-SET AND TPR DOMAINS AND THE REGULATION OF  
JRNL        TITL 4 ITS ACTIVITY BY DNA BINDING.                                 
JRNL        REF    NUCLEIC ACIDS RES.            V.  39  4438 2011              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   21266482                                                     
JRNL        DOI    10.1093/NAR/GKR019                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 26293                          
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) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1323                            
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) : 2.82                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.89                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1608                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.74                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.3730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6814                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 24                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.85000                                              
REMARK   3    B22 (A**2) : -4.60000                                             
REMARK   3    B33 (A**2) : 0.74000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.31000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.396         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.884                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6995 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9420 ; 1.065 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   849 ; 4.956 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   326 ;35.303 ;23.865       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1318 ;16.327 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;18.863 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1033 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5216 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  4259 ; 0.344 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6868 ; 0.673 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2736 ; 0.846 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2552 ; 1.534 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 RIDING   
REMARK   3  POSITIONS U VALUES                                                  
REMARK   4                                                                      
REMARK   4 3OXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-OCT-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000061692.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-10                          
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               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99985                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26338                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.12200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33900                            
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: CNS                                                   
REMARK 200 STARTING MODEL: 3MEK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14.4% PEG 8000, 20% GLYCEROL, 160MM      
REMARK 280  CALCIUM ACETATE, AND 80MM SODIUM CACODYLATE, PH 6.5, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       58.99500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 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 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     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     LEU A   429                                                      
REMARK 465     GLU A   430                                                      
REMARK 465     HIS A   431                                                      
REMARK 465     HIS A   432                                                      
REMARK 465     HIS A   433                                                      
REMARK 465     HIS A   434                                                      
REMARK 465     HIS A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   427                                                      
REMARK 465     SER B   428                                                      
REMARK 465     LEU B   429                                                      
REMARK 465     GLU B   430                                                      
REMARK 465     HIS B   431                                                      
REMARK 465     HIS B   432                                                      
REMARK 465     HIS B   433                                                      
REMARK 465     HIS B   434                                                      
REMARK 465     HIS B   435                                                      
REMARK 465     HIS B   436                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU B  318   CD                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  13        9.27   -154.56                                   
REMARK 500    ARG A  14       51.95   -117.22                                   
REMARK 500    GLU A  57      -71.08    -52.59                                   
REMARK 500    LYS A  84      -65.52    -27.21                                   
REMARK 500    PRO A 167     -167.15    -65.09                                   
REMARK 500    ALA A 168      -17.65     60.43                                   
REMARK 500    PHE A 362       61.14   -118.87                                   
REMARK 500    ASN B  13       42.96   -158.11                                   
REMARK 500    ARG B  14       49.21   -153.07                                   
REMARK 500    ARG B  51      -69.93    -91.73                                   
REMARK 500    ASN B 134       25.76    -75.76                                   
REMARK 500    ALA B 168      -22.46     74.76                                   
REMARK 500    LYS B 271       -6.94     89.18                                   
REMARK 500    MET B 385       56.51    -97.81                                   
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 439  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  83   NE2                                                    
REMARK 620 2 CYS A  87   SG   93.6                                              
REMARK 620 3 CYS A  62   SG  111.1 118.8                                        
REMARK 620 4 CYS A  65   SG  106.9  97.9 123.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 439  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  83   NE2                                                    
REMARK 620 2 CYS B  62   SG  107.2                                              
REMARK 620 3 CYS B  87   SG  109.3 112.9                                        
REMARK 620 4 CYS B  65   SG  107.9 105.8 113.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 438  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  71   SG                                                     
REMARK 620 2 CYS A  52   SG  110.8                                              
REMARK 620 3 CYS A  75   SG   98.3 107.8                                        
REMARK 620 4 CYS A  49   SG  118.4 111.0 109.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 440  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 261   SG                                                     
REMARK 620 2 CYS A 266   SG   98.2                                              
REMARK 620 3 CYS A 208   SG  123.1 107.6                                        
REMARK 620 4 CYS A 263   SG  107.7 111.9 107.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 438  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  75   SG                                                     
REMARK 620 2 CYS B  71   SG  104.2                                              
REMARK 620 3 CYS B  52   SG  116.0 108.2                                        
REMARK 620 4 CYS B  49   SG  112.9 105.8 109.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 440  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 266   SG                                                     
REMARK 620 2 CYS B 261   SG  103.8                                              
REMARK 620 3 CYS B 263   SG  131.7 103.2                                        
REMARK 620 4 CYS B 208   SG  101.8 114.1 102.5                                  
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 SAH A 437                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 438                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 439                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 440                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 437                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 438                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 439                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 440                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3OXG   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE EXPERIMENTAL INFO OF UNIPROT (Q9H7B4, SMYD3_HUMAN) SHOWS         
REMARK 999 CONFLICTS K -> N, K -> R AT THE POSITIONS 13, 140 (IN REF.6:         
REMARK 999 AAH31010)                                                            
DBREF  3OXF A    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
DBREF  3OXF B    1   428  UNP    Q9H7B4   SMYD3_HUMAN      1    428             
SEQADV 3OXF ASN A   13  UNP  Q9H7B4    LYS    13 SEE REMARK 999                 
SEQADV 3OXF ARG A  140  UNP  Q9H7B4    LYS   140 SEE REMARK 999                 
SEQADV 3OXF LEU A  429  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF GLU A  430  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS A  431  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS A  432  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS A  433  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS A  434  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS A  435  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS A  436  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF ASN B   13  UNP  Q9H7B4    LYS    13 SEE REMARK 999                 
SEQADV 3OXF ARG B  140  UNP  Q9H7B4    LYS   140 SEE REMARK 999                 
SEQADV 3OXF LEU B  429  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF GLU B  430  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS B  431  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS B  432  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS B  433  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS B  434  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS B  435  UNP  Q9H7B4              EXPRESSION TAG                 
SEQADV 3OXF HIS B  436  UNP  Q9H7B4              EXPRESSION TAG                 
SEQRES   1 A  436  MET GLU PRO LEU LYS VAL GLU LYS PHE ALA THR ALA ASN          
SEQRES   2 A  436  ARG GLY ASN GLY LEU ARG ALA VAL THR PRO LEU ARG PRO          
SEQRES   3 A  436  GLY GLU LEU LEU PHE ARG SER ASP PRO LEU ALA TYR THR          
SEQRES   4 A  436  VAL CYS LYS GLY SER ARG GLY VAL VAL CYS ASP ARG CYS          
SEQRES   5 A  436  LEU LEU GLY LYS GLU LYS LEU MET ARG CYS SER GLN CYS          
SEQRES   6 A  436  ARG VAL ALA LYS TYR CYS SER ALA LYS CYS GLN LYS LYS          
SEQRES   7 A  436  ALA TRP PRO ASP HIS LYS ARG GLU CYS LYS CYS LEU LYS          
SEQRES   8 A  436  SER CYS LYS PRO ARG TYR PRO PRO ASP SER VAL ARG LEU          
SEQRES   9 A  436  LEU GLY ARG VAL VAL PHE LYS LEU MET ASP GLY ALA PRO          
SEQRES  10 A  436  SER GLU SER GLU LYS LEU TYR SER PHE TYR ASP LEU GLU          
SEQRES  11 A  436  SER ASN ILE ASN LYS LEU THR GLU ASP ARG LYS GLU GLY          
SEQRES  12 A  436  LEU ARG GLN LEU VAL MET THR PHE GLN HIS PHE MET ARG          
SEQRES  13 A  436  GLU GLU ILE GLN ASP ALA SER GLN LEU PRO PRO ALA PHE          
SEQRES  14 A  436  ASP LEU PHE GLU ALA PHE ALA LYS VAL ILE CYS ASN SER          
SEQRES  15 A  436  PHE THR ILE CYS ASN ALA GLU MET GLN GLU VAL GLY VAL          
SEQRES  16 A  436  GLY LEU TYR PRO SER ILE SER LEU LEU ASN HIS SER CYS          
SEQRES  17 A  436  ASP PRO ASN CYS SER ILE VAL PHE ASN GLY PRO HIS LEU          
SEQRES  18 A  436  LEU LEU ARG ALA VAL ARG ASP ILE GLU VAL GLY GLU GLU          
SEQRES  19 A  436  LEU THR ILE CYS TYR LEU ASP MET LEU MET THR SER GLU          
SEQRES  20 A  436  GLU ARG ARG LYS GLN LEU ARG ASP GLN TYR CYS PHE GLU          
SEQRES  21 A  436  CYS ASP CYS PHE ARG CYS GLN THR GLN ASP LYS ASP ALA          
SEQRES  22 A  436  ASP MET LEU THR GLY ASP GLU GLN VAL TRP LYS GLU VAL          
SEQRES  23 A  436  GLN GLU SER LEU LYS LYS ILE GLU GLU LEU LYS ALA HIS          
SEQRES  24 A  436  TRP LYS TRP GLU GLN VAL LEU ALA MET CYS GLN ALA ILE          
SEQRES  25 A  436  ILE SER SER ASN SER GLU ARG LEU PRO ASP ILE ASN ILE          
SEQRES  26 A  436  TYR GLN LEU LYS VAL LEU ASP CYS ALA MET ASP ALA CYS          
SEQRES  27 A  436  ILE ASN LEU GLY LEU LEU GLU GLU ALA LEU PHE TYR GLY          
SEQRES  28 A  436  THR ARG THR MET GLU PRO TYR ARG ILE PHE PHE PRO GLY          
SEQRES  29 A  436  SER HIS PRO VAL ARG GLY VAL GLN VAL MET LYS VAL GLY          
SEQRES  30 A  436  LYS LEU GLN LEU HIS GLN GLY MET PHE PRO GLN ALA MET          
SEQRES  31 A  436  LYS ASN LEU ARG LEU ALA PHE ASP ILE MET ARG VAL THR          
SEQRES  32 A  436  HIS GLY ARG GLU HIS SER LEU ILE GLU ASP LEU ILE LEU          
SEQRES  33 A  436  LEU LEU GLU GLU CYS ASP ALA ASN ILE ARG ALA SER LEU          
SEQRES  34 A  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  436  MET GLU PRO LEU LYS VAL GLU LYS PHE ALA THR ALA ASN          
SEQRES   2 B  436  ARG GLY ASN GLY LEU ARG ALA VAL THR PRO LEU ARG PRO          
SEQRES   3 B  436  GLY GLU LEU LEU PHE ARG SER ASP PRO LEU ALA TYR THR          
SEQRES   4 B  436  VAL CYS LYS GLY SER ARG GLY VAL VAL CYS ASP ARG CYS          
SEQRES   5 B  436  LEU LEU GLY LYS GLU LYS LEU MET ARG CYS SER GLN CYS          
SEQRES   6 B  436  ARG VAL ALA LYS TYR CYS SER ALA LYS CYS GLN LYS LYS          
SEQRES   7 B  436  ALA TRP PRO ASP HIS LYS ARG GLU CYS LYS CYS LEU LYS          
SEQRES   8 B  436  SER CYS LYS PRO ARG TYR PRO PRO ASP SER VAL ARG LEU          
SEQRES   9 B  436  LEU GLY ARG VAL VAL PHE LYS LEU MET ASP GLY ALA PRO          
SEQRES  10 B  436  SER GLU SER GLU LYS LEU TYR SER PHE TYR ASP LEU GLU          
SEQRES  11 B  436  SER ASN ILE ASN LYS LEU THR GLU ASP ARG LYS GLU GLY          
SEQRES  12 B  436  LEU ARG GLN LEU VAL MET THR PHE GLN HIS PHE MET ARG          
SEQRES  13 B  436  GLU GLU ILE GLN ASP ALA SER GLN LEU PRO PRO ALA PHE          
SEQRES  14 B  436  ASP LEU PHE GLU ALA PHE ALA LYS VAL ILE CYS ASN SER          
SEQRES  15 B  436  PHE THR ILE CYS ASN ALA GLU MET GLN GLU VAL GLY VAL          
SEQRES  16 B  436  GLY LEU TYR PRO SER ILE SER LEU LEU ASN HIS SER CYS          
SEQRES  17 B  436  ASP PRO ASN CYS SER ILE VAL PHE ASN GLY PRO HIS LEU          
SEQRES  18 B  436  LEU LEU ARG ALA VAL ARG ASP ILE GLU VAL GLY GLU GLU          
SEQRES  19 B  436  LEU THR ILE CYS TYR LEU ASP MET LEU MET THR SER GLU          
SEQRES  20 B  436  GLU ARG ARG LYS GLN LEU ARG ASP GLN TYR CYS PHE GLU          
SEQRES  21 B  436  CYS ASP CYS PHE ARG CYS GLN THR GLN ASP LYS ASP ALA          
SEQRES  22 B  436  ASP MET LEU THR GLY ASP GLU GLN VAL TRP LYS GLU VAL          
SEQRES  23 B  436  GLN GLU SER LEU LYS LYS ILE GLU GLU LEU LYS ALA HIS          
SEQRES  24 B  436  TRP LYS TRP GLU GLN VAL LEU ALA MET CYS GLN ALA ILE          
SEQRES  25 B  436  ILE SER SER ASN SER GLU ARG LEU PRO ASP ILE ASN ILE          
SEQRES  26 B  436  TYR GLN LEU LYS VAL LEU ASP CYS ALA MET ASP ALA CYS          
SEQRES  27 B  436  ILE ASN LEU GLY LEU LEU GLU GLU ALA LEU PHE TYR GLY          
SEQRES  28 B  436  THR ARG THR MET GLU PRO TYR ARG ILE PHE PHE PRO GLY          
SEQRES  29 B  436  SER HIS PRO VAL ARG GLY VAL GLN VAL MET LYS VAL GLY          
SEQRES  30 B  436  LYS LEU GLN LEU HIS GLN GLY MET PHE PRO GLN ALA MET          
SEQRES  31 B  436  LYS ASN LEU ARG LEU ALA PHE ASP ILE MET ARG VAL THR          
SEQRES  32 B  436  HIS GLY ARG GLU HIS SER LEU ILE GLU ASP LEU ILE LEU          
SEQRES  33 B  436  LEU LEU GLU GLU CYS ASP ALA ASN ILE ARG ALA SER LEU          
SEQRES  34 B  436  GLU HIS HIS HIS HIS HIS HIS                                  
HET    SAH  A 437      26                                                       
HET     ZN  A 438       1                                                       
HET     ZN  A 439       1                                                       
HET     ZN  A 440       1                                                       
HET    SAH  B 437      26                                                       
HET     ZN  B 438       1                                                       
HET     ZN  B 439       1                                                       
HET     ZN  B 440       1                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM      ZN ZINC ION                                                         
FORMUL   3  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   4   ZN    6(ZN 2+)                                                     
FORMUL  11  HOH   *24(H2 O)                                                     
HELIX    1   1 LYS A   42  ARG A   45  5                                   4    
HELIX    2   2 SER A   72  LYS A   84  1                                  13    
HELIX    3   3 GLU A   86  LYS A   94  1                                   9    
HELIX    4   4 PRO A   99  LEU A  112  1                                  14    
HELIX    5   5 SER A  118  LYS A  122  5                                   5    
HELIX    6   6 ASN A  132  LEU A  136  5                                   5    
HELIX    7   7 THR A  137  MET A  155  1                                  19    
HELIX    8   8 ASP A  161  LEU A  165  5                                   5    
HELIX    9   9 ASP A  170  SER A  182  1                                  13    
HELIX   10  10 SER A  200  LEU A  204  5                                   5    
HELIX   11  11 THR A  245  CYS A  258  1                                  14    
HELIX   12  12 CYS A  263  THR A  268  1                                   6    
HELIX   13  13 LYS A  271  LEU A  276  1                                   6    
HELIX   14  14 ASP A  279  HIS A  299  1                                  21    
HELIX   15  15 LYS A  301  SER A  317  1                                  17    
HELIX   16  16 ASN A  324  GLY A  342  1                                  19    
HELIX   17  17 LEU A  343  ARG A  353  1                                  11    
HELIX   18  18 THR A  354  PHE A  362  1                                   9    
HELIX   19  19 HIS A  366  GLN A  383  1                                  18    
HELIX   20  20 MET A  385  HIS A  404  1                                  20    
HELIX   21  21 SER A  409  SER A  428  1                                  20    
HELIX   22  22 SER B   72  ALA B   79  1                                   8    
HELIX   23  23 ALA B   79  LYS B   84  1                                   6    
HELIX   24  24 GLU B   86  SER B   92  1                                   7    
HELIX   25  25 PRO B   99  LEU B  112  1                                  14    
HELIX   26  26 SER B  118  LYS B  122  5                                   5    
HELIX   27  27 ASN B  132  LEU B  136  5                                   5    
HELIX   28  28 THR B  137  MET B  155  1                                  19    
HELIX   29  29 ASP B  161  LEU B  165  5                                   5    
HELIX   30  30 ASP B  170  SER B  182  1                                  13    
HELIX   31  31 SER B  200  LEU B  204  5                                   5    
HELIX   32  32 THR B  245  GLN B  256  1                                  12    
HELIX   33  33 CYS B  263  GLN B  269  1                                   7    
HELIX   34  34 LYS B  271  LEU B  276  1                                   6    
HELIX   35  35 ASP B  279  HIS B  299  1                                  21    
HELIX   36  36 LYS B  301  SER B  317  1                                  17    
HELIX   37  37 ASN B  324  GLY B  342  1                                  19    
HELIX   38  38 LEU B  343  PHE B  362  1                                  20    
HELIX   39  39 HIS B  366  GLN B  383  1                                  18    
HELIX   40  40 MET B  385  HIS B  404  1                                  20    
HELIX   41  41 HIS B  408  ASN B  424  1                                  17    
SHEET    1   A 2 VAL A   6  ALA A  10  0                                        
SHEET    2   A 2 ASN A  16  ALA A  20 -1  O  GLY A  17   N  PHE A   9           
SHEET    1   B 3 LEU A  29  SER A  33  0                                        
SHEET    2   B 3 HIS A 220  ALA A 225 -1  O  LEU A 223   N  LEU A  30           
SHEET    3   B 3 CYS A 212  ASN A 217 -1  N  ASN A 217   O  HIS A 220           
SHEET    1   C 3 ALA A  37  VAL A  40  0                                        
SHEET    2   C 3 GLU A 192  LEU A 197 -1  O  LEU A 197   N  ALA A  37           
SHEET    3   C 3 PHE A 183  CYS A 186 -1  N  PHE A 183   O  GLY A 196           
SHEET    1   D 2 MET A  60  ARG A  61  0                                        
SHEET    2   D 2 LYS A  69  TYR A  70 -1  O  TYR A  70   N  MET A  60           
SHEET    1   E 2 ASN A 205  HIS A 206  0                                        
SHEET    2   E 2 THR A 236  ILE A 237  1  O  ILE A 237   N  ASN A 205           
SHEET    1   F 4 VAL B   6  ALA B  10  0                                        
SHEET    2   F 4 ASN B  16  ALA B  20 -1  O  ARG B  19   N  GLU B   7           
SHEET    3   F 4 GLU B 234  ILE B 237 -1  O  LEU B 235   N  LEU B  18           
SHEET    4   F 4 ASN B 205  HIS B 206  1  N  ASN B 205   O  ILE B 237           
SHEET    1   G 3 LEU B  29  SER B  33  0                                        
SHEET    2   G 3 HIS B 220  ALA B 225 -1  O  LEU B 221   N  SER B  33           
SHEET    3   G 3 CYS B 212  ASN B 217 -1  N  ASN B 217   O  HIS B 220           
SHEET    1   H 3 ALA B  37  VAL B  40  0                                        
SHEET    2   H 3 GLU B 192  LEU B 197 -1  O  VAL B 195   N  THR B  39           
SHEET    3   H 3 PHE B 183  CYS B 186 -1  N  PHE B 183   O  GLY B 196           
SHEET    1   I 2 MET B  60  ARG B  61  0                                        
SHEET    2   I 2 LYS B  69  TYR B  70 -1  O  TYR B  70   N  MET B  60           
LINK         NE2 HIS A  83                ZN    ZN A 439     1555   1555  2.08  
LINK         NE2 HIS B  83                ZN    ZN B 439     1555   1555  2.12  
LINK         SG  CYS A  71                ZN    ZN A 438     1555   1555  2.20  
LINK         SG  CYS B  62                ZN    ZN B 439     1555   1555  2.21  
LINK         SG  CYS B  87                ZN    ZN B 439     1555   1555  2.21  
LINK         SG  CYS A 261                ZN    ZN A 440     1555   1555  2.21  
LINK         SG  CYS A  87                ZN    ZN A 439     1555   1555  2.21  
LINK         SG  CYS A 266                ZN    ZN A 440     1555   1555  2.21  
LINK         SG  CYS B  75                ZN    ZN B 438     1555   1555  2.22  
LINK         SG  CYS A 208                ZN    ZN A 440     1555   1555  2.22  
LINK         SG  CYS A 263                ZN    ZN A 440     1555   1555  2.22  
LINK         SG  CYS A  52                ZN    ZN A 438     1555   1555  2.23  
LINK         SG  CYS B 266                ZN    ZN B 440     1555   1555  2.24  
LINK         SG  CYS A  62                ZN    ZN A 439     1555   1555  2.25  
LINK         SG  CYS B  71                ZN    ZN B 438     1555   1555  2.28  
LINK         SG  CYS A  65                ZN    ZN A 439     1555   1555  2.28  
LINK         SG  CYS A  75                ZN    ZN A 438     1555   1555  2.32  
LINK         SG  CYS A  49                ZN    ZN A 438     1555   1555  2.32  
LINK         SG  CYS B  65                ZN    ZN B 439     1555   1555  2.32  
LINK         SG  CYS B 261                ZN    ZN B 440     1555   1555  2.34  
LINK         SG  CYS B  52                ZN    ZN B 438     1555   1555  2.37  
LINK         SG  CYS B 263                ZN    ZN B 440     1555   1555  2.37  
LINK         SG  CYS B  49                ZN    ZN B 438     1555   1555  2.43  
LINK         SG  CYS B 208                ZN    ZN B 440     1555   1555  2.46  
CISPEP   1 LYS A   94    PRO A   95          0        -1.09                     
CISPEP   2 LYS B   94    PRO B   95          0         9.10                     
SITE     1 AC1 14 ARG A  14  GLY A  15  ASN A  16  TYR A 124                    
SITE     2 AC1 14 GLU A 130  ASN A 132  ASN A 181  SER A 202                    
SITE     3 AC1 14 ASN A 205  HIS A 206  TYR A 239  TYR A 257                    
SITE     4 AC1 14 PHE A 259  HOH A 450                                          
SITE     1 AC2  4 CYS A  49  CYS A  52  CYS A  71  CYS A  75                    
SITE     1 AC3  4 CYS A  62  CYS A  65  HIS A  83  CYS A  87                    
SITE     1 AC4  4 CYS A 208  CYS A 261  CYS A 263  CYS A 266                    
SITE     1 AC5 12 ARG B  14  GLY B  15  ASN B  16  TYR B 124                    
SITE     2 AC5 12 ASN B 132  SER B 202  LEU B 204  ASN B 205                    
SITE     3 AC5 12 HIS B 206  TYR B 239  TYR B 257  PHE B 259                    
SITE     1 AC6  4 CYS B  49  CYS B  52  CYS B  71  CYS B  75                    
SITE     1 AC7  4 CYS B  62  CYS B  65  HIS B  83  CYS B  87                    
SITE     1 AC8  4 CYS B 208  CYS B 261  CYS B 263  CYS B 266                    
CRYST1   57.991  117.990   82.808  90.00  91.78  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017244  0.000000  0.000536        0.00000                         
SCALE2      0.000000  0.008475  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012082        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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