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Database: PDB
Entry: 6CBX
LinkDB: 6CBX
Original site: 6CBX 
HEADER    TRANSFERASE/INHIBITOR                   05-FEB-18   6CBX              
TITLE     CRYSTAL STRUCTURE OF HUMAN SET AND MYND DOMAIN CONTAINING PROTEIN 2   
TITLE    2 WITH MTF1497                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE SMYD2;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HSKM-B,HISTONE METHYLTRANSFERASE SMYD2,LYSINE N-            
COMPND   5 METHYLTRANSFERASE 3C,SET AND MYND DOMAIN-CONTAINING PROTEIN 2;       
COMPND   6 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   7 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: SMYD2, KMT3C;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFBOH-MHL                                 
KEYWDS    SMYD2 MTF9975 INHIBITOR, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS     
KEYWDS   2 CONSORTIUM, SGC, TRANSFERASE-INHIBITOR COMPLEX                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.ZENG,A.DONG,A.HUTCHINSON,A.SEITOVA,J.TATLOCK,R.KUMPF,A.OWEN,        
AUTHOR   2 A.TAYLOR,A.CASIMIRO-GARCIA,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,     
AUTHOR   3 P.J.BROWN,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)                  
REVDAT   1   14-MAR-18 6CBX    0                                                
JRNL        AUTH   H.ZENG,A.DONG,A.HUTCHINSON,A.SEITOVA,J.TATLOCK,R.KUMPF,      
JRNL        AUTH 2 A.OWEN,A.TAYLOR,A.CASIMIRO-GARCIA,C.BOUNTRA,C.H.ARROWSMITH,  
JRNL        AUTH 3 A.M.EDWARDS,P.J.BROWN,H.WU,                                  
JRNL        AUTH 4 STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN SET AND MYND DOMAIN CONTAINING    
JRNL        TITL 2 PROTEIN 2 WITH MTF1497                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.94 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 61405                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1208                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.94                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4421                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6770                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 106                                     
REMARK   3   SOLVENT ATOMS            : 365                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.48000                                             
REMARK   3    B22 (A**2) : -0.38000                                             
REMARK   3    B33 (A**2) : 0.89000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.34000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.169         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.151         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.113         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.005         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7136 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6643 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9669 ; 1.374 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15338 ; 0.940 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   887 ; 5.738 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   321 ;35.863 ;24.206       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1224 ;13.513 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;17.316 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1035 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8284 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1625 ; 0.002 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6CBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232412.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97926                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62638                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.940                              
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     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.93800                            
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: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M NH4SO4, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       58.51550            
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 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 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     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     HIS A   433                                                      
REMARK 465     HIS B   433                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A   6    CG   CD1  CD2                                       
REMARK 470     ASN A  50    OD1  ND2                                            
REMARK 470     ARG A  58    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 127    CD   CE   NZ                                        
REMARK 470     LYS A 132    CD   CE   NZ                                        
REMARK 470     GLN A 265    CD   OE1  NE2                                       
REMARK 470     LYS A 274    CD   CE   NZ                                        
REMARK 470     GLU A 278    CD   OE1  OE2                                       
REMARK 470     LYS A 281    CG   CD   CE   NZ                                   
REMARK 470     SER A 283    OG                                                  
REMARK 470     ASP A 284    CG   OD1  OD2                                       
REMARK 470     LYS A 287    CG   CD   CE   NZ                                   
REMARK 470     GLU A 289    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 292    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 293    CG   OD1  OD2                                       
REMARK 470     ARG A 296    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 309    CD   CE   NZ                                        
REMARK 470     GLU A 319    CD   OE1  OE2                                       
REMARK 470     MET A 353    CG   SD   CE                                        
REMARK 470     GLU A 357    CD   OE1  OE2                                       
REMARK 470     GLN A 361    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 365    CG   CD   CE   NZ                                   
REMARK 470     LYS A 368    CD   CE   NZ                                        
REMARK 470     LYS A 372    NZ                                                  
REMARK 470     LYS A 403    CD   CE   NZ                                        
REMARK 470     GLU A 431    OE1  OE2                                            
REMARK 470     SER A 432    OG                                                  
REMARK 470     LYS B  80    CE   NZ                                             
REMARK 470     GLN B 265    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 271    CG   OD1  OD2                                       
REMARK 470     LYS B 274    CD   CE   NZ                                        
REMARK 470     LYS B 281    CG   CD   CE   NZ                                   
REMARK 470     SER B 283    OG                                                  
REMARK 470     ASP B 284    CG   OD1  OD2                                       
REMARK 470     GLU B 289    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 292    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 296    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 309    CD   CE   NZ                                        
REMARK 470     GLU B 319    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 323    CG   CD1  CD2                                       
REMARK 470     LYS B 368    CD   CE   NZ                                        
REMARK 470     GLU B 396    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 398    CG   CD   CE   NZ                                   
REMARK 470     LYS B 403    CD   CE   NZ                                        
REMARK 470     GLU B 431    CG   CD   OE1  OE2                                  
REMARK 470     SER B 432    OG                                                  
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    LEU A   6      -43.14   -153.16                                   
REMARK 500    ASN A 101       46.91   -156.20                                   
REMARK 500    CYS A 210       73.26   -118.31                                   
REMARK 500    CYS A 210       69.97   -116.98                                   
REMARK 500    GLU A 431       58.99    -68.81                                   
REMARK 500    ASN B 101       42.23   -152.84                                   
REMARK 500    TYR B 311      -21.54   -144.34                                   
REMARK 500    HIS B 397       71.22   -103.88                                   
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 A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  55   SG  103.3                                              
REMARK 620 3 CYS A  74   SG  100.6  94.2                                        
REMARK 620 4 CYS A  78   SG  111.4 122.1 121.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  65   SG                                                     
REMARK 620 2 CYS A  68   SG  109.1                                              
REMARK 620 3 HIS A  86   NE2 110.6 105.1                                        
REMARK 620 4 CYS A  90   SG  111.0 115.7 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 209   SG                                                     
REMARK 620 2 CYS A 262   SG  116.1                                              
REMARK 620 3 CYS A 264   SG  111.5 103.7                                        
REMARK 620 4 CYS A 267   SG   96.7 115.9 113.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  52   SG                                                     
REMARK 620 2 CYS B  55   SG  106.8                                              
REMARK 620 3 CYS B  74   SG  108.3 101.4                                        
REMARK 620 4 CYS B  78   SG  106.9 118.4 114.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  65   SG                                                     
REMARK 620 2 CYS B  68   SG  112.8                                              
REMARK 620 3 HIS B  86   NE2 106.6 106.6                                        
REMARK 620 4 CYS B  90   SG  110.2 115.4 104.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 209   SG                                                     
REMARK 620 2 CYS B 262   SG  113.8                                              
REMARK 620 3 CYS B 264   SG  109.8 107.5                                        
REMARK 620 4 CYS B 267   SG   98.4 113.6 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EW1 A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EW1 B 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 1007                
DBREF  6CBX A    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
DBREF  6CBX B    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
SEQADV 6CBX GLY A    0  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 6CBX GLU A  165  UNP  Q9NRG4    GLY   165 CONFLICT                       
SEQADV 6CBX GLY B    0  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 6CBX GLU B  165  UNP  Q9NRG4    GLY   165 CONFLICT                       
SEQRES   1 A  434  GLY MET ARG ALA GLU GLY LEU GLY GLY LEU GLU ARG PHE          
SEQRES   2 A  434  CYS SER PRO GLY LYS GLY ARG GLY LEU ARG ALA LEU GLN          
SEQRES   3 A  434  PRO PHE GLN VAL GLY ASP LEU LEU PHE SER CYS PRO ALA          
SEQRES   4 A  434  TYR ALA TYR VAL LEU THR VAL ASN GLU ARG GLY ASN HIS          
SEQRES   5 A  434  CYS GLU TYR CYS PHE THR ARG LYS GLU GLY LEU SER LYS          
SEQRES   6 A  434  CYS GLY ARG CYS LYS GLN ALA PHE TYR CYS ASN VAL GLU          
SEQRES   7 A  434  CYS GLN LYS GLU ASP TRP PRO MET HIS LYS LEU GLU CYS          
SEQRES   8 A  434  SER PRO MET VAL VAL PHE GLY GLU ASN TRP ASN PRO SER          
SEQRES   9 A  434  GLU THR VAL ARG LEU THR ALA ARG ILE LEU ALA LYS GLN          
SEQRES  10 A  434  LYS ILE HIS PRO GLU ARG THR PRO SER GLU LYS LEU LEU          
SEQRES  11 A  434  ALA VAL LYS GLU PHE GLU SER HIS LEU ASP LYS LEU ASP          
SEQRES  12 A  434  ASN GLU LYS LYS ASP LEU ILE GLN SER ASP ILE ALA ALA          
SEQRES  13 A  434  LEU HIS HIS PHE TYR SER LYS HIS LEU GLU PHE PRO ASP          
SEQRES  14 A  434  ASN ASP SER LEU VAL VAL LEU PHE ALA GLN VAL ASN CYS          
SEQRES  15 A  434  ASN GLY PHE THR ILE GLU ASP GLU GLU LEU SER HIS LEU          
SEQRES  16 A  434  GLY SER ALA ILE PHE PRO ASP VAL ALA LEU MET ASN HIS          
SEQRES  17 A  434  SER CYS CYS PRO ASN VAL ILE VAL THR TYR LYS GLY THR          
SEQRES  18 A  434  LEU ALA GLU VAL ARG ALA VAL GLN GLU ILE LYS PRO GLY          
SEQRES  19 A  434  GLU GLU VAL PHE THR SER TYR ILE ASP LEU LEU TYR PRO          
SEQRES  20 A  434  THR GLU ASP ARG ASN ASP ARG LEU ARG ASP SER TYR PHE          
SEQRES  21 A  434  PHE THR CYS GLU CYS GLN GLU CYS THR THR LYS ASP LYS          
SEQRES  22 A  434  ASP LYS ALA LYS VAL GLU ILE ARG LYS LEU SER ASP PRO          
SEQRES  23 A  434  PRO LYS ALA GLU ALA ILE ARG ASP MET VAL ARG TYR ALA          
SEQRES  24 A  434  ARG ASN VAL ILE GLU GLU PHE ARG ARG ALA LYS HIS TYR          
SEQRES  25 A  434  LYS SER PRO SER GLU LEU LEU GLU ILE CYS GLU LEU SER          
SEQRES  26 A  434  GLN GLU LYS MET SER SER VAL PHE GLU ASP SER ASN VAL          
SEQRES  27 A  434  TYR MET LEU HIS MET MET TYR GLN ALA MET GLY VAL CYS          
SEQRES  28 A  434  LEU TYR MET GLN ASP TRP GLU GLY ALA LEU GLN TYR GLY          
SEQRES  29 A  434  GLN LYS ILE ILE LYS PRO TYR SER LYS HIS TYR PRO LEU          
SEQRES  30 A  434  TYR SER LEU ASN VAL ALA SER MET TRP LEU LYS LEU GLY          
SEQRES  31 A  434  ARG LEU TYR MET GLY LEU GLU HIS LYS ALA ALA GLY GLU          
SEQRES  32 A  434  LYS ALA LEU LYS LYS ALA ILE ALA ILE MET GLU VAL ALA          
SEQRES  33 A  434  HIS GLY LYS ASP HIS PRO TYR ILE SER GLU ILE LYS GLN          
SEQRES  34 A  434  GLU ILE GLU SER HIS                                          
SEQRES   1 B  434  GLY MET ARG ALA GLU GLY LEU GLY GLY LEU GLU ARG PHE          
SEQRES   2 B  434  CYS SER PRO GLY LYS GLY ARG GLY LEU ARG ALA LEU GLN          
SEQRES   3 B  434  PRO PHE GLN VAL GLY ASP LEU LEU PHE SER CYS PRO ALA          
SEQRES   4 B  434  TYR ALA TYR VAL LEU THR VAL ASN GLU ARG GLY ASN HIS          
SEQRES   5 B  434  CYS GLU TYR CYS PHE THR ARG LYS GLU GLY LEU SER LYS          
SEQRES   6 B  434  CYS GLY ARG CYS LYS GLN ALA PHE TYR CYS ASN VAL GLU          
SEQRES   7 B  434  CYS GLN LYS GLU ASP TRP PRO MET HIS LYS LEU GLU CYS          
SEQRES   8 B  434  SER PRO MET VAL VAL PHE GLY GLU ASN TRP ASN PRO SER          
SEQRES   9 B  434  GLU THR VAL ARG LEU THR ALA ARG ILE LEU ALA LYS GLN          
SEQRES  10 B  434  LYS ILE HIS PRO GLU ARG THR PRO SER GLU LYS LEU LEU          
SEQRES  11 B  434  ALA VAL LYS GLU PHE GLU SER HIS LEU ASP LYS LEU ASP          
SEQRES  12 B  434  ASN GLU LYS LYS ASP LEU ILE GLN SER ASP ILE ALA ALA          
SEQRES  13 B  434  LEU HIS HIS PHE TYR SER LYS HIS LEU GLU PHE PRO ASP          
SEQRES  14 B  434  ASN ASP SER LEU VAL VAL LEU PHE ALA GLN VAL ASN CYS          
SEQRES  15 B  434  ASN GLY PHE THR ILE GLU ASP GLU GLU LEU SER HIS LEU          
SEQRES  16 B  434  GLY SER ALA ILE PHE PRO ASP VAL ALA LEU MET ASN HIS          
SEQRES  17 B  434  SER CYS CYS PRO ASN VAL ILE VAL THR TYR LYS GLY THR          
SEQRES  18 B  434  LEU ALA GLU VAL ARG ALA VAL GLN GLU ILE LYS PRO GLY          
SEQRES  19 B  434  GLU GLU VAL PHE THR SER TYR ILE ASP LEU LEU TYR PRO          
SEQRES  20 B  434  THR GLU ASP ARG ASN ASP ARG LEU ARG ASP SER TYR PHE          
SEQRES  21 B  434  PHE THR CYS GLU CYS GLN GLU CYS THR THR LYS ASP LYS          
SEQRES  22 B  434  ASP LYS ALA LYS VAL GLU ILE ARG LYS LEU SER ASP PRO          
SEQRES  23 B  434  PRO LYS ALA GLU ALA ILE ARG ASP MET VAL ARG TYR ALA          
SEQRES  24 B  434  ARG ASN VAL ILE GLU GLU PHE ARG ARG ALA LYS HIS TYR          
SEQRES  25 B  434  LYS SER PRO SER GLU LEU LEU GLU ILE CYS GLU LEU SER          
SEQRES  26 B  434  GLN GLU LYS MET SER SER VAL PHE GLU ASP SER ASN VAL          
SEQRES  27 B  434  TYR MET LEU HIS MET MET TYR GLN ALA MET GLY VAL CYS          
SEQRES  28 B  434  LEU TYR MET GLN ASP TRP GLU GLY ALA LEU GLN TYR GLY          
SEQRES  29 B  434  GLN LYS ILE ILE LYS PRO TYR SER LYS HIS TYR PRO LEU          
SEQRES  30 B  434  TYR SER LEU ASN VAL ALA SER MET TRP LEU LYS LEU GLY          
SEQRES  31 B  434  ARG LEU TYR MET GLY LEU GLU HIS LYS ALA ALA GLY GLU          
SEQRES  32 B  434  LYS ALA LEU LYS LYS ALA ILE ALA ILE MET GLU VAL ALA          
SEQRES  33 B  434  HIS GLY LYS ASP HIS PRO TYR ILE SER GLU ILE LYS GLN          
SEQRES  34 B  434  GLU ILE GLU SER HIS                                          
HET     ZN  A1001       1                                                       
HET     ZN  A1002       1                                                       
HET     ZN  A1003       1                                                       
HET    EW1  A1004      36                                                       
HET     CL  A1005       1                                                       
HET    EDO  A1006       4                                                       
HET    EDO  A1007       4                                                       
HET    UNX  A1008       1                                                       
HET    UNX  A1009       1                                                       
HET    UNX  A1010       1                                                       
HET    UNX  A1011       1                                                       
HET    UNX  A1012       1                                                       
HET     ZN  B1001       1                                                       
HET     ZN  B1002       1                                                       
HET     ZN  B1003       1                                                       
HET    EW1  B1004      36                                                       
HET     CL  B1005       1                                                       
HET    EDO  B1006       4                                                       
HET    EDO  B1007       4                                                       
HET    UNX  B1008       1                                                       
HET    UNX  B1009       1                                                       
HET    UNX  B1010       1                                                       
HET    UNX  B1011       1                                                       
HET    UNX  B1012       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     EW1 [3-(4-AMINO-6-METHYL-1H-IMIDAZO[4,5-C]PYRIDIN-1-YL)              
HETNAM   2 EW1  AZETIDIN-1-YL][1-({1-[(1R)-CYCLOHEPT-2-EN-1-                    
HETNAM   3 EW1  YL]PIPERIDIN-4-YL}METHYL)-1H-PYRROL-3-YL]METHANONE              
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     EW1 MTF1497                                                          
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   ZN    6(ZN 2+)                                                     
FORMUL   6  EW1    2(C28 H37 N7 O)                                              
FORMUL   7   CL    2(CL 1-)                                                     
FORMUL   8  EDO    4(C2 H6 O2)                                                  
FORMUL  10  UNX    10(X)                                                        
FORMUL  27  HOH   *365(H2 O)                                                    
HELIX    1 AA1 VAL A   45  ARG A   48  5                                   4    
HELIX    2 AA2 ASN A   75  LYS A   87  1                                  13    
HELIX    3 AA3 GLU A   89  GLY A   97  1                                   9    
HELIX    4 AA4 GLU A   98  TRP A  100  5                                   3    
HELIX    5 AA5 SER A  103  HIS A  119  1                                  17    
HELIX    6 AA6 THR A  123  LYS A  127  5                                   5    
HELIX    7 AA7 ALA A  130  PHE A  134  5                                   5    
HELIX    8 AA8 HIS A  137  LEU A  141  5                                   5    
HELIX    9 AA9 ASP A  142  SER A  161  1                                  20    
HELIX   10 AB1 ASP A  168  GLY A  183  1                                  16    
HELIX   11 AB2 ASP A  201  MET A  205  5                                   5    
HELIX   12 AB3 PRO A  246  PHE A  259  1                                  14    
HELIX   13 AB4 CYS A  264  LYS A  270  1                                   7    
HELIX   14 AB5 LYS A  272  VAL A  277  1                                   6    
HELIX   15 AB6 LYS A  287  LYS A  312  1                                  26    
HELIX   16 AB7 SER A  313  SER A  329  1                                  17    
HELIX   17 AB8 ASN A  336  MET A  353  1                                  18    
HELIX   18 AB9 ASP A  355  TYR A  374  1                                  20    
HELIX   19 AC1 SER A  378  LEU A  395  1                                  18    
HELIX   20 AC2 HIS A  397  HIS A  416  1                                  20    
HELIX   21 AC3 HIS A  420  GLU A  431  1                                  12    
HELIX   22 AC4 VAL B   45  ARG B   48  5                                   4    
HELIX   23 AC5 ASN B   75  LYS B   87  1                                  13    
HELIX   24 AC6 GLU B   89  GLY B   97  1                                   9    
HELIX   25 AC7 GLU B   98  TRP B  100  5                                   3    
HELIX   26 AC8 SER B  103  HIS B  119  1                                  17    
HELIX   27 AC9 ALA B  130  PHE B  134  5                                   5    
HELIX   28 AD1 HIS B  137  LEU B  141  5                                   5    
HELIX   29 AD2 ASP B  142  SER B  161  1                                  20    
HELIX   30 AD3 ASP B  168  GLY B  183  1                                  16    
HELIX   31 AD4 ASP B  201  MET B  205  5                                   5    
HELIX   32 AD5 PRO B  246  PHE B  259  1                                  14    
HELIX   33 AD6 CYS B  264  LYS B  270  1                                   7    
HELIX   34 AD7 LYS B  272  VAL B  277  1                                   6    
HELIX   35 AD8 LYS B  287  LYS B  309  1                                  23    
HELIX   36 AD9 SER B  313  SER B  330  1                                  18    
HELIX   37 AE1 ASN B  336  MET B  353  1                                  18    
HELIX   38 AE2 ASP B  355  TYR B  374  1                                  20    
HELIX   39 AE3 SER B  378  LEU B  395  1                                  18    
HELIX   40 AE4 HIS B  397  HIS B  416  1                                  20    
HELIX   41 AE5 HIS B  420  SER B  432  1                                  13    
SHEET    1 AA1 2 LEU A   9  SER A  14  0                                        
SHEET    2 AA1 2 GLY A  18  ALA A  23 -1  O  GLY A  18   N  SER A  14           
SHEET    1 AA2 3 LEU A  32  PRO A  37  0                                        
SHEET    2 AA2 3 LEU A 221  ALA A 226 -1  O  ALA A 222   N  CYS A  36           
SHEET    3 AA2 3 VAL A 213  LYS A 218 -1  N  THR A 216   O  GLU A 223           
SHEET    1 AA3 3 ALA A  40  LEU A  43  0                                        
SHEET    2 AA3 3 HIS A 193  ILE A 198 -1  O  ILE A 198   N  ALA A  40           
SHEET    3 AA3 3 PHE A 184  GLU A 187 -1  N  PHE A 184   O  ALA A 197           
SHEET    1 AA4 2 SER A  63  LYS A  64  0                                        
SHEET    2 AA4 2 PHE A  72  TYR A  73 -1  O  TYR A  73   N  SER A  63           
SHEET    1 AA5 2 ASN A 206  HIS A 207  0                                        
SHEET    2 AA5 2 PHE A 237  THR A 238  1  O  THR A 238   N  ASN A 206           
SHEET    1 AA6 2 LEU B   9  SER B  14  0                                        
SHEET    2 AA6 2 GLY B  18  ALA B  23 -1  O  ARG B  22   N  GLU B  10           
SHEET    1 AA7 3 LEU B  32  PRO B  37  0                                        
SHEET    2 AA7 3 LEU B 221  ALA B 226 -1  O  VAL B 224   N  PHE B  34           
SHEET    3 AA7 3 VAL B 213  LYS B 218 -1  N  THR B 216   O  GLU B 223           
SHEET    1 AA8 3 ALA B  40  LEU B  43  0                                        
SHEET    2 AA8 3 HIS B 193  ILE B 198 -1  O  ILE B 198   N  ALA B  40           
SHEET    3 AA8 3 PHE B 184  GLU B 187 -1  N  PHE B 184   O  ALA B 197           
SHEET    1 AA9 2 SER B  63  LYS B  64  0                                        
SHEET    2 AA9 2 PHE B  72  TYR B  73 -1  O  TYR B  73   N  SER B  63           
SHEET    1 AB1 2 ASN B 206  HIS B 207  0                                        
SHEET    2 AB1 2 PHE B 237  THR B 238  1  O  THR B 238   N  ASN B 206           
LINK         SG  CYS A  52                ZN    ZN A1001     1555   1555  2.42  
LINK         SG  CYS A  55                ZN    ZN A1001     1555   1555  2.46  
LINK         SG  CYS A  65                ZN    ZN A1002     1555   1555  2.36  
LINK         SG  CYS A  68                ZN    ZN A1002     1555   1555  2.01  
LINK         SG  CYS A  74                ZN    ZN A1001     1555   1555  2.40  
LINK         SG  CYS A  78                ZN    ZN A1001     1555   1555  1.93  
LINK         NE2 HIS A  86                ZN    ZN A1002     1555   1555  2.17  
LINK         SG  CYS A  90                ZN    ZN A1002     1555   1555  2.38  
LINK         SG  CYS A 209                ZN    ZN A1003     1555   1555  2.34  
LINK         SG  CYS A 262                ZN    ZN A1003     1555   1555  2.33  
LINK         SG  CYS A 264                ZN    ZN A1003     1555   1555  2.35  
LINK         SG  CYS A 267                ZN    ZN A1003     1555   1555  2.33  
LINK         SG  CYS B  52                ZN    ZN B1001     1555   1555  2.37  
LINK         SG  CYS B  55                ZN    ZN B1001     1555   1555  2.36  
LINK         SG  CYS B  65                ZN    ZN B1002     1555   1555  2.39  
LINK         SG  CYS B  68                ZN    ZN B1002     1555   1555  2.18  
LINK         SG  CYS B  74                ZN    ZN B1001     1555   1555  2.34  
LINK         SG  CYS B  78                ZN    ZN B1001     1555   1555  2.28  
LINK         NE2 HIS B  86                ZN    ZN B1002     1555   1555  2.08  
LINK         SG  CYS B  90                ZN    ZN B1002     1555   1555  2.32  
LINK         SG  CYS B 209                ZN    ZN B1003     1555   1555  2.37  
LINK         SG  CYS B 262                ZN    ZN B1003     1555   1555  2.28  
LINK         SG  CYS B 264                ZN    ZN B1003     1555   1555  2.34  
LINK         SG  CYS B 267                ZN    ZN B1003     1555   1555  2.26  
SITE     1 AC1  4 CYS A  52  CYS A  55  CYS A  74  CYS A  78                    
SITE     1 AC2  4 CYS A  65  CYS A  68  HIS A  86  CYS A  90                    
SITE     1 AC3  4 CYS A 209  CYS A 262  CYS A 264  CYS A 267                    
SITE     1 AC4 17 GLY A  16  LYS A  17  GLU A 135  HIS A 137                    
SITE     2 AC4 17 CYS A 181  ASN A 182  GLY A 183  PHE A 184                    
SITE     3 AC4 17 ALA A 203  ASN A 206  HIS A 207  TYR A 240                    
SITE     4 AC4 17 TYR A 258  PHE A 260  GLU A 263  HOH A1157                    
SITE     5 AC4 17 HOH A1214                                                     
SITE     1 AC5  2 ILE A 241  ASP A 242                                          
SITE     1 AC6  7 PRO A  37  ALA A  38  LYS A 115  THR A 123                    
SITE     2 AC6  7 PRO A 124  SER A 125  HOH A1166                               
SITE     1 AC7  4 ASP A 242  TYR A 245  TYR A 370  TYR A 374                    
SITE     1 AC8  4 CYS B  52  CYS B  55  CYS B  74  CYS B  78                    
SITE     1 AC9  4 CYS B  65  CYS B  68  HIS B  86  CYS B  90                    
SITE     1 AD1  4 CYS B 209  CYS B 262  CYS B 264  CYS B 267                    
SITE     1 AD2 17 GLY B  16  LYS B  17  GLU B 135  HIS B 137                    
SITE     2 AD2 17 CYS B 181  ASN B 182  GLY B 183  PHE B 184                    
SITE     3 AD2 17 ALA B 203  ASN B 206  HIS B 207  TYR B 240                    
SITE     4 AD2 17 TYR B 258  PHE B 260  GLU B 263  HOH B1154                    
SITE     5 AD2 17 HOH B1185                                                     
SITE     1 AD3  3 ILE B 241  ASP B 242  ARG B 253                               
SITE     1 AD4  5 SER A 329  ARG B  67  LYS B  87  SER B  91                    
SITE     2 AD4  5 HIS B 163                                                     
SITE     1 AD5  4 HIS A 157  HIS B 158  HOH B1105  HOH B1153                    
CRYST1   58.020  117.031   64.444  90.00  92.54  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      0.017235  0.000000  0.000763        0.00000                         
SCALE2      0.000000  0.008545  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015533        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system