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Database: PDB
Entry: 6CBY
LinkDB: 6CBY
Original site: 6CBY 
HEADER    TRANSFERASE/INHIBITOR                   05-FEB-18   6CBY              
TITLE     CRYSTAL STRUCTURE OF HUMAN SET AND MYND DOMAIN CONTAINING PROTEIN 2   
TITLE    2 WITH MTF9975                                                         
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 6CBY    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 MTF9975                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 28052                          
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)  : 0.201                          
REMARK   3   R VALUE            (WORKING SET)  : 0.199                          
REMARK   3   FREE R VALUE                      : 0.258                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 3.120                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 876                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 14                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.55                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.65                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.02                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2942                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2340                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2853                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2320                   
REMARK   3   BIN FREE R VALUE                        : 0.2820                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 3.03                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : NULL                     
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6408                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 52                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 14.90790                                             
REMARK   3    B22 (A**2) : -2.80510                                             
REMARK   3    B33 (A**2) : -12.10280                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.12460                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.340               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.734               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.306               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.942               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.317               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.911                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.874                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6642   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9039   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2197   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 142    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1035   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6642   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 863    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7663   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.09                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.89                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.70                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    1.9916   -0.9815   23.7422           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0439 T22:   -0.1470                                    
REMARK   3     T33:   -0.1260 T12:    0.0190                                    
REMARK   3     T13:    0.0712 T23:   -0.0241                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0524 L22:    1.7987                                    
REMARK   3     L33:    0.6296 L12:   -0.3683                                    
REMARK   3     L13:   -0.0235 L23:    0.2408                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0281 S12:    0.0782 S13:    0.1269                     
REMARK   3     S21:   -0.0279 S22:   -0.0176 S23:   -0.0954                     
REMARK   3     S31:   -0.0697 S32:   -0.0172 S33:    0.0457                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   29.3382  -31.5926    9.1055           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1319 T22:   -0.1921                                    
REMARK   3     T33:   -0.1401 T12:   -0.0273                                    
REMARK   3     T13:    0.0655 T23:   -0.0724                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3697 L22:    1.0347                                    
REMARK   3     L33:    1.9252 L12:   -0.1992                                    
REMARK   3     L13:   -0.9814 L23:    0.7986                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2316 S12:    0.4997 S13:   -0.0864                     
REMARK   3     S21:    0.0431 S22:    0.0344 S23:    0.0787                     
REMARK   3     S31:    0.2002 S32:   -0.3339 S33:    0.1972                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CBY 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_1000232415.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-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) : 0.97891                            
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   : 28751                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
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                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.20400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.93400                            
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   (%): 44.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
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       58.78950            
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     GLY B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ARG B   280                                                      
REMARK 465     LYS B   281                                                      
REMARK 465     LEU B   282                                                      
REMARK 465     SER B   283                                                      
REMARK 465     ASP B   284                                                      
REMARK 465     PRO B   285                                                      
REMARK 465     PRO B   286                                                      
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     ARG A  58    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  59    CD   CE   NZ                                        
REMARK 470     GLU A  60    CG   CD   OE1  OE2                                  
REMARK 470     SER A  63    OG                                                  
REMARK 470     LYS A  64    CD   CE   NZ                                        
REMARK 470     LYS A  69    CG   CD   CE   NZ                                   
REMARK 470     GLN A  70    OE1  NE2                                            
REMARK 470     GLU A  77    CD   OE1  OE2                                       
REMARK 470     LYS A  80    CG   CD   CE   NZ                                   
REMARK 470     ASN A 101    CG   OD1  ND2                                       
REMARK 470     LYS A 115    CE   NZ                                             
REMARK 470     LYS A 117    CG   CD   CE   NZ                                   
REMARK 470     ILE A 118    CD1                                                 
REMARK 470     LYS A 145    CG   CD   CE   NZ                                   
REMARK 470     LYS A 162    CG   CD   CE   NZ                                   
REMARK 470     HIS A 163    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 165    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 229    CD   OE1  OE2                                       
REMARK 470     LYS A 231    CD   CE   NZ                                        
REMARK 470     GLN A 265    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 272    CD   CE   NZ                                        
REMARK 470     LYS A 274    CG   CD   CE   NZ                                   
REMARK 470     GLU A 278    OE1  OE2                                            
REMARK 470     ARG A 280    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 281    CG   CD   CE   NZ                                   
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     ILE A 291    CD1                                                 
REMARK 470     ARG A 292    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 296    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 303    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 306    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 309    CE   NZ                                             
REMARK 470     GLU A 319    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 322    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 323    CG   CD1  CD2                                       
REMARK 470     SER A 324    OG                                                  
REMARK 470     GLU A 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 327    CG   CD   CE   NZ                                   
REMARK 470     SER A 329    OG                                                  
REMARK 470     SER A 330    OG                                                  
REMARK 470     VAL A 331    CG1  CG2                                            
REMARK 470     GLU A 333    CD   OE1  OE2                                       
REMARK 470     LYS A 365    CD   CE   NZ                                        
REMARK 470     LYS A 368    CD   CE   NZ                                        
REMARK 470     LYS A 372    CD   CE   NZ                                        
REMARK 470     LYS A 387    NZ                                                  
REMARK 470     LYS A 398    CD   CE   NZ                                        
REMARK 470     GLU A 402    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 403    CD   CE   NZ                                        
REMARK 470     LYS A 407    NZ                                                  
REMARK 470     LYS A 418    CE   NZ                                             
REMARK 470     GLN A 428    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 431    CG   CD   OE1  OE2                                  
REMARK 470     SER A 432    OG                                                  
REMARK 470     ARG B  11    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B  53    OE1  OE2                                            
REMARK 470     LYS B  59    CD   CE   NZ                                        
REMARK 470     GLU B  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  64    CG   CD   CE   NZ                                   
REMARK 470     LYS B  69    CG   CD   CE   NZ                                   
REMARK 470     GLU B  77    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  80    NZ                                                  
REMARK 470     GLU B  81    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  87    CE   NZ                                             
REMARK 470     ASN B 101    CG   OD1  ND2                                       
REMARK 470     LYS B 115    CG   CD   CE   NZ                                   
REMARK 470     LYS B 117    CG   CD   CE   NZ                                   
REMARK 470     ILE B 118    CG1  CG2  CD1                                       
REMARK 470     HIS B 119    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU B 121    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 122    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 127    CD   CE   NZ                                        
REMARK 470     LYS B 132    CE   NZ                                             
REMARK 470     LYS B 145    CD   CE   NZ                                        
REMARK 470     LYS B 162    NZ                                                  
REMARK 470     GLU B 165    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 214    CD1                                                 
REMARK 470     LYS B 218    NZ                                                  
REMARK 470     LYS B 231    CD   CE   NZ                                        
REMARK 470     ARG B 253    CZ   NH1  NH2                                       
REMARK 470     GLN B 265    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 270    NZ                                                  
REMARK 470     LYS B 272    CE   NZ                                             
REMARK 470     LYS B 274    CG   CD   CE   NZ                                   
REMARK 470     GLU B 278    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 279    CG1  CG2  CD1                                       
REMARK 470     LYS B 287    CG   CD   CE   NZ                                   
REMARK 470     GLU B 289    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 291    CG1  CG2  CD1                                       
REMARK 470     ARG B 292    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 293    CG   OD1  OD2                                       
REMARK 470     VAL B 295    CG1  CG2                                            
REMARK 470     ARG B 296    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 304    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 309    CG   CD   CE   NZ                                   
REMARK 470     HIS B 310    ND1  CD2  CE1  NE2                                  
REMARK 470     LYS B 312    CE   NZ                                             
REMARK 470     SER B 315    OG                                                  
REMARK 470     GLU B 316    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 318    CG   CD1  CD2                                       
REMARK 470     GLU B 319    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 320    CG1  CG2  CD1                                       
REMARK 470     GLU B 322    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 323    CG   CD1  CD2                                       
REMARK 470     SER B 324    OG                                                  
REMARK 470     GLU B 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 327    CG   CD   CE   NZ                                   
REMARK 470     SER B 329    OG                                                  
REMARK 470     SER B 330    OG                                                  
REMARK 470     VAL B 331    CG1  CG2                                            
REMARK 470     GLU B 333    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 334    CG   OD1  OD2                                       
REMARK 470     SER B 335    OG                                                  
REMARK 470     VAL B 349    CG1  CG2                                            
REMARK 470     GLU B 357    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 360    CG   CD1  CD2                                       
REMARK 470     GLN B 361    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 365    CG   CD   CE   NZ                                   
REMARK 470     ILE B 366    CG1  CG2  CD1                                       
REMARK 470     LYS B 368    CG   CD   CE   NZ                                   
REMARK 470     LYS B 372    CG   CD   CE   NZ                                   
REMARK 470     LEU B 376    CG   CD1  CD2                                       
REMARK 470     LYS B 387    CE   NZ                                             
REMARK 470     LYS B 398    CG   CD   CE   NZ                                   
REMARK 470     LYS B 403    CG   CD   CE   NZ                                   
REMARK 470     LYS B 418    CG   CD   CE   NZ                                   
REMARK 470     GLU B 425    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 427    CG   CD   CE   NZ                                   
REMARK 470     GLN B 428    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 430    CG1  CG2  CD1                                       
REMARK 470     GLU B 431    CG   CD   OE1  OE2                                  
REMARK 470     SER B 432    OG                                                  
REMARK 470     HIS B 433    CG   ND1  CD2  CE1  NE2                             
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       95.54     64.82                                   
REMARK 500    LYS A  17      -71.38   -127.31                                   
REMARK 500    TRP A 100      101.06    -55.04                                   
REMARK 500    ASN A 101       51.76   -140.70                                   
REMARK 500    GLU A 126       50.59   -114.34                                   
REMARK 500    CYS A 210       69.35   -116.76                                   
REMARK 500    VAL A 277       49.42   -107.34                                   
REMARK 500    LYS A 309        8.18    -63.86                                   
REMARK 500    HIS A 397       78.74   -118.28                                   
REMARK 500    LYS B  17      -71.65   -118.68                                   
REMARK 500    ASN B  46       12.00    -65.67                                   
REMARK 500    ASN B 101       47.39   -141.54                                   
REMARK 500    VAL B 277       70.16   -111.06                                   
REMARK 500    TYR B 311      -40.08   -150.51                                   
REMARK 500    LEU B 376      -36.62    -38.24                                   
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   98.1                                              
REMARK 620 3 CYS A  74   SG  104.2 100.0                                        
REMARK 620 4 CYS A  78   SG  106.9 110.8 131.9                                  
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  104.4                                              
REMARK 620 3 HIS A  86   NE2 111.5  96.3                                        
REMARK 620 4 CYS A  90   SG  122.2 117.0 102.4                                  
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  106.5                                              
REMARK 620 3 CYS A 264   SG  107.4 108.8                                        
REMARK 620 4 CYS A 267   SG  100.5 108.6 123.6                                  
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   99.5                                              
REMARK 620 3 CYS B  74   SG   97.3 100.0                                        
REMARK 620 4 CYS B  78   SG  114.9 121.2 119.7                                  
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  100.8                                              
REMARK 620 3 HIS B  86   NE2 112.4  91.9                                        
REMARK 620 4 CYS B  90   SG  121.2 117.3 109.4                                  
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  112.3                                              
REMARK 620 3 CYS B 264   SG  109.2 102.1                                        
REMARK 620 4 CYS B 267   SG   97.9 116.8 118.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 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 EW4 A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EW4 B 1004                
DBREF  6CBY A    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
DBREF  6CBY B    1   433  UNP    Q9NRG4   SMYD2_HUMAN      1    433             
SEQADV 6CBY GLY A    0  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 6CBY GLU A  165  UNP  Q9NRG4    GLY   165 CONFLICT                       
SEQADV 6CBY GLY B    0  UNP  Q9NRG4              EXPRESSION TAG                 
SEQADV 6CBY 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    EW4  A1004      37                                                       
HET     ZN  B1001       1                                                       
HET     ZN  B1002       1                                                       
HET     ZN  B1003       1                                                       
HET    EW4  B1004      37                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     EW4 [3-(4-AMINO-6-METHYL-1H-IMIDAZO[4,5-C]PYRIDIN-1-YL)-3-           
HETNAM   2 EW4  METHYLAZETIDIN-1-YL][1-({1-[(1R)-CYCLOHEPT-2-EN-1-              
HETNAM   3 EW4  YL]PIPERIDIN-4-YL}METHYL)-1H-PYRROL-3-YL]METHANONE              
HETSYN     EW4 MTF9975                                                          
FORMUL   3   ZN    6(ZN 2+)                                                     
FORMUL   6  EW4    2(C29 H39 N7 O)                                              
FORMUL  11  HOH   *52(H2 O)                                                     
HELIX    1 AA1 VAL A   45  ARG A   48  5                                   4    
HELIX    2 AA2 ASN A   75  GLY A   97  1                                  23    
HELIX    3 AA3 GLU A   98  TRP A  100  5                                   3    
HELIX    4 AA4 SER A  103  HIS A  119  1                                  17    
HELIX    5 AA5 ALA A  130  PHE A  134  5                                   5    
HELIX    6 AA6 ASP A  142  SER A  161  1                                  20    
HELIX    7 AA7 ASP A  168  GLY A  183  1                                  16    
HELIX    8 AA8 PHE A  199  MET A  205  1                                   7    
HELIX    9 AA9 PRO A  246  PHE A  259  1                                  14    
HELIX   10 AB1 CYS A  264  LYS A  270  1                                   7    
HELIX   11 AB2 LYS A  272  VAL A  277  1                                   6    
HELIX   12 AB3 LYS A  287  LYS A  309  1                                  23    
HELIX   13 AB4 SER A  313  SER A  329  1                                  17    
HELIX   14 AB5 ASN A  336  GLN A  354  1                                  19    
HELIX   15 AB6 ASP A  355  TYR A  374  1                                  20    
HELIX   16 AB7 SER A  378  LEU A  395  1                                  18    
HELIX   17 AB8 HIS A  397  HIS A  416  1                                  20    
HELIX   18 AB9 HIS A  420  SER A  432  1                                  13    
HELIX   19 AC1 VAL B   45  ARG B   48  5                                   4    
HELIX   20 AC2 ASN B   75  GLY B   97  1                                  23    
HELIX   21 AC3 GLU B   98  TRP B  100  5                                   3    
HELIX   22 AC4 SER B  103  HIS B  119  1                                  17    
HELIX   23 AC5 THR B  123  LYS B  127  5                                   5    
HELIX   24 AC6 HIS B  137  LEU B  141  5                                   5    
HELIX   25 AC7 ASP B  142  SER B  161  1                                  20    
HELIX   26 AC8 ASP B  168  GLY B  183  1                                  16    
HELIX   27 AC9 PHE B  199  LEU B  204  1                                   6    
HELIX   28 AD1 PRO B  246  PHE B  259  1                                  14    
HELIX   29 AD2 CYS B  264  LYS B  270  1                                   7    
HELIX   30 AD3 LYS B  272  VAL B  277  1                                   6    
HELIX   31 AD4 ALA B  288  LYS B  309  1                                  22    
HELIX   32 AD5 SER B  313  SER B  329  1                                  17    
HELIX   33 AD6 ASN B  336  MET B  353  1                                  18    
HELIX   34 AD7 ASP B  355  TYR B  374  1                                  20    
HELIX   35 AD8 SER B  378  GLU B  396  1                                  19    
HELIX   36 AD9 HIS B  397  HIS B  416  1                                  20    
HELIX   37 AE1 HIS B  420  GLU B  431  1                                  12    
SHEET    1 AA1 4 LEU A   9  SER A  14  0                                        
SHEET    2 AA1 4 GLY A  18  ALA A  23 -1  O  GLY A  18   N  SER A  14           
SHEET    3 AA1 4 GLU A 235  THR A 238 -1  O  VAL A 236   N  LEU A  21           
SHEET    4 AA1 4 ASN A 206  HIS A 207  1  N  ASN A 206   O  THR A 238           
SHEET    1 AA2 3 LEU A  32  CYS A  36  0                                        
SHEET    2 AA2 3 LEU A 221  ALA A 226 -1  O  VAL A 224   N  LEU A  33           
SHEET    3 AA2 3 VAL A 213  LYS A 218 -1  N  LYS A 218   O  LEU A 221           
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  ILE A 186   O  LEU A 194           
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 4 LEU B   9  SER B  14  0                                        
SHEET    2 AA5 4 GLY B  18  ALA B  23 -1  O  ARG B  22   N  GLU B  10           
SHEET    3 AA5 4 GLU B 235  THR B 238 -1  O  VAL B 236   N  LEU B  21           
SHEET    4 AA5 4 ASN B 206  HIS B 207  1  N  ASN B 206   O  THR B 238           
SHEET    1 AA6 3 LEU B  32  PRO B  37  0                                        
SHEET    2 AA6 3 LEU B 221  ALA B 226 -1  O  VAL B 224   N  LEU B  33           
SHEET    3 AA6 3 VAL B 213  LYS B 218 -1  N  THR B 216   O  GLU B 223           
SHEET    1 AA7 3 TYR B  41  LEU B  43  0                                        
SHEET    2 AA7 3 HIS B 193  ALA B 197 -1  O  SER B 196   N  VAL B  42           
SHEET    3 AA7 3 PHE B 184  GLU B 187 -1  N  PHE B 184   O  ALA B 197           
SHEET    1 AA8 2 SER B  63  LYS B  64  0                                        
SHEET    2 AA8 2 PHE B  72  TYR B  73 -1  O  TYR B  73   N  SER B  63           
LINK         SG  CYS A  52                ZN    ZN A1001     1555   1555  2.45  
LINK         SG  CYS A  55                ZN    ZN A1001     1555   1555  2.47  
LINK         SG  CYS A  65                ZN    ZN A1002     1555   1555  2.46  
LINK         SG  CYS A  68                ZN    ZN A1002     1555   1555  2.44  
LINK         SG  CYS A  74                ZN    ZN A1001     1555   1555  2.32  
LINK         SG  CYS A  78                ZN    ZN A1001     1555   1555  2.41  
LINK         NE2 HIS A  86                ZN    ZN A1002     1555   1555  2.13  
LINK         SG  CYS A  90                ZN    ZN A1002     1555   1555  2.18  
LINK         SG  CYS A 209                ZN    ZN A1003     1555   1555  2.54  
LINK         SG  CYS A 262                ZN    ZN A1003     1555   1555  2.53  
LINK         SG  CYS A 264                ZN    ZN A1003     1555   1555  2.47  
LINK         SG  CYS A 267                ZN    ZN A1003     1555   1555  2.25  
LINK         SG  CYS B  52                ZN    ZN B1001     1555   1555  2.28  
LINK         SG  CYS B  55                ZN    ZN B1001     1555   1555  2.50  
LINK         SG  CYS B  65                ZN    ZN B1002     1555   1555  2.46  
LINK         SG  CYS B  68                ZN    ZN B1002     1555   1555  2.36  
LINK         SG  CYS B  74                ZN    ZN B1001     1555   1555  2.67  
LINK         SG  CYS B  78                ZN    ZN B1001     1555   1555  2.18  
LINK         NE2 HIS B  86                ZN    ZN B1002     1555   1555  2.13  
LINK         SG  CYS B  90                ZN    ZN B1002     1555   1555  2.66  
LINK         SG  CYS B 209                ZN    ZN B1003     1555   1555  2.45  
LINK         SG  CYS B 262                ZN    ZN B1003     1555   1555  2.58  
LINK         SG  CYS B 264                ZN    ZN B1003     1555   1555  2.36  
LINK         SG  CYS B 267                ZN    ZN B1003     1555   1555  2.24  
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 15 GLY A  16  LYS A  17  HIS A 137  CYS A 181                    
SITE     2 AC4 15 ASN A 182  GLY A 183  THR A 185  ASN A 206                    
SITE     3 AC4 15 HIS A 207  TYR A 240  TYR A 258  PHE A 260                    
SITE     4 AC4 15 GLU A 263  HOH A1106  HOH A1122                               
SITE     1 AC5  4 CYS B  52  CYS B  55  CYS B  74  CYS B  78                    
SITE     1 AC6  4 CYS B  65  CYS B  68  HIS B  86  CYS B  90                    
SITE     1 AC7  4 CYS B 209  CYS B 262  CYS B 264  CYS B 267                    
SITE     1 AC8 14 GLY B  16  LYS B  17  HIS B 137  CYS B 181                    
SITE     2 AC8 14 ASN B 182  GLY B 183  ALA B 203  ASN B 206                    
SITE     3 AC8 14 HIS B 207  TYR B 240  TYR B 258  PHE B 260                    
SITE     4 AC8 14 THR B 261  GLU B 263                                          
CRYST1   57.819  117.579   65.013  90.00  92.42  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      0.017295  0.000000  0.000731        0.00000                         
SCALE2      0.000000  0.008505  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015395        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system