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Database: PDB
Entry: 6MON
LinkDB: 6MON
Original site: 6MON 
HEADER    TRANSFERASE                             04-OCT-18   6MON              
TITLE     CRYSTAL STRUCTURE OF HUMAN SMYD2 IN COMPLEX WITH NLE-PEPTIDE INHIBITOR
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;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: LYS-LEU-NLE-SER-LYS-ARG-GLY;                               
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 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: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  12 ORGANISM_TAXID: 32630                                                
KEYWDS    METHYLTRANSFERASE, NORLEUCINE, COMPLEX, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.SPELLMON,E.CORNETT,J.BRUNZELLE,S.ROTHBART,Z.YANG                    
REVDAT   1   12-DEC-18 6MON    0                                                
JRNL        AUTH   E.M.CORNETT,B.M.DICKSON,K.KRAJEWSKI,N.SPELLMON,A.UMSTEAD,    
JRNL        AUTH 2 R.M.VAUGHAN,K.M.SHAW,P.P.VERSLUIS,M.W.COWLES,J.BRUNZELLE,    
JRNL        AUTH 3 Z.YANG,I.E.VEGA,Z.W.SUN,S.B.ROTHBART                         
JRNL        TITL   A FUNCTIONAL PROTEOMICS PLATFORM TO REVEAL THE SEQUENCE      
JRNL        TITL 2 DETERMINANTS OF LYSINE METHYLTRANSFERASE SUBSTRATE           
JRNL        TITL 3 SELECTIVITY.                                                 
JRNL        REF    SCI ADV                       V.   4 V2623 2018              
JRNL        REFN                   ESSN 2375-2548                               
JRNL        PMID   30498785                                                     
JRNL        DOI    10.1126/SCIADV.AAV2623                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.24                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.310                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34396                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.650                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1601                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 51.2518 -  6.0265    0.99     3070   155  0.1730 0.1876        
REMARK   3     2  6.0265 -  4.7845    1.00     3002   159  0.1848 0.1954        
REMARK   3     3  4.7845 -  4.1800    1.00     2965   171  0.1704 0.1732        
REMARK   3     4  4.1800 -  3.7980    1.00     2956   180  0.1987 0.2395        
REMARK   3     5  3.7980 -  3.5258    1.00     3011   122  0.2204 0.2448        
REMARK   3     6  3.5258 -  3.3180    1.00     2973   115  0.2378 0.2757        
REMARK   3     7  3.3180 -  3.1519    1.00     2977   131  0.2663 0.3122        
REMARK   3     8  3.1519 -  3.0147    1.00     2967   146  0.2706 0.2944        
REMARK   3     9  3.0147 -  2.8986    1.00     2992   118  0.2853 0.2975        
REMARK   3    10  2.8986 -  2.7986    1.00     2901   171  0.3016 0.3213        
REMARK   3    11  2.7986 -  2.7111    1.00     2981   133  0.3247 0.3481        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           7244                                  
REMARK   3   ANGLE     :  1.056           9725                                  
REMARK   3   CHIRALITY :  0.045           1035                                  
REMARK   3   PLANARITY :  0.006           1248                                  
REMARK   3   DIHEDRAL  : 16.095           2758                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 182 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 160.6270 436.6044 -34.9646              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4469 T22:   0.2818                                     
REMARK   3      T33:   0.4736 T12:   0.1231                                     
REMARK   3      T13:  -0.0478 T23:  -0.0429                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7870 L22:   0.7752                                     
REMARK   3      L33:   1.7087 L12:   0.0162                                     
REMARK   3      L13:   0.7322 L23:  -0.2750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2105 S12:  -0.0442 S13:   0.1547                       
REMARK   3      S21:   0.1648 S22:  -0.0683 S23:   0.1937                       
REMARK   3      S31:   0.0070 S32:  -0.2208 S33:  -0.0146                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 310 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 183.5995 441.0895 -32.6549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5413 T22:   0.4386                                     
REMARK   3      T33:   0.5291 T12:   0.0123                                     
REMARK   3      T13:  -0.0933 T23:   0.1142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4586 L22:   0.2048                                     
REMARK   3      L33:   1.0514 L12:   0.0389                                     
REMARK   3      L13:   0.0508 L23:   0.4670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2550 S12:  -0.0012 S13:   0.1131                       
REMARK   3      S21:   0.0657 S22:   0.0453 S23:  -0.0209                       
REMARK   3      S31:  -0.2176 S32:   0.4592 S33:  -0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 311 THROUGH 397 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 190.1495 433.3076 -47.2260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4328 T22:   0.9796                                     
REMARK   3      T33:   0.5214 T12:   0.0745                                     
REMARK   3      T13:   0.0303 T23:   0.2193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2715 L22:   0.6890                                     
REMARK   3      L33:   1.1410 L12:  -0.0731                                     
REMARK   3      L13:   0.1976 L23:   0.1838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3423 S12:   0.2999 S13:  -0.2265                       
REMARK   3      S21:  -0.3263 S22:   0.0080 S23:  -0.2333                       
REMARK   3      S31:  -0.2172 S32:   1.5270 S33:  -0.0519                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 398 THROUGH 433 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 183.1133 415.9733 -37.1261              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8207 T22:   0.5896                                     
REMARK   3      T33:   0.6865 T12:   0.3814                                     
REMARK   3      T13:   0.1195 T23:   0.0589                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2253 L22:   0.4414                                     
REMARK   3      L33:   0.8105 L12:   0.0750                                     
REMARK   3      L13:   0.1385 L23:   0.5869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2445 S12:   0.1534 S13:  -0.2407                       
REMARK   3      S21:   0.0125 S22:  -0.3850 S23:  -0.0701                       
REMARK   3      S31:   0.8761 S32:   0.0416 S33:  -0.0011                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 212 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 223.9984 409.8576 -62.0576              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3810 T22:   0.2086                                     
REMARK   3      T33:   0.3946 T12:   0.0777                                     
REMARK   3      T13:  -0.0281 T23:  -0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7559 L22:   0.8328                                     
REMARK   3      L33:   2.7431 L12:  -0.0492                                     
REMARK   3      L13:  -0.5979 L23:  -0.0259                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2456 S12:  -0.0305 S13:   0.0298                       
REMARK   3      S21:   0.1483 S22:  -0.0372 S23:  -0.1547                       
REMARK   3      S31:  -0.0767 S32:   0.1432 S33:  -0.0044                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 213 THROUGH 355 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 198.2864 406.5906 -66.4398              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3570 T22:   0.6995                                     
REMARK   3      T33:   0.3199 T12:   0.0493                                     
REMARK   3      T13:   0.0176 T23:  -0.2126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0828 L22:   1.9953                                     
REMARK   3      L33:   1.0710 L12:  -0.0223                                     
REMARK   3      L13:   0.0089 L23:  -0.4016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1744 S12:   0.1991 S13:  -0.1739                       
REMARK   3      S21:  -0.0605 S22:  -0.0018 S23:   0.0088                       
REMARK   3      S31:   0.0201 S32:  -0.8970 S33:  -0.5524                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 356 THROUGH 433 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 200.9247 426.5383 -68.0112              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6299 T22:   0.6511                                     
REMARK   3      T33:   0.5265 T12:   0.8977                                     
REMARK   3      T13:  -0.2412 T23:  -0.2391                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8577 L22:   0.3081                                     
REMARK   3      L33:   2.0299 L12:  -0.3838                                     
REMARK   3      L13:   0.3964 L23:  -0.2849                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6147 S12:   0.2362 S13:   0.5352                       
REMARK   3      S21:   0.2879 S22:  -0.3763 S23:  -0.0360                       
REMARK   3      S31:  -1.6238 S32:  -1.2059 S33:  -1.6702                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID -1 THROUGH 3 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): 176.1692 437.2696 -35.9839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9075 T22:   0.7882                                     
REMARK   3      T33:   0.8565 T12:  -0.1868                                     
REMARK   3      T13:  -0.0093 T23:   0.1354                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6648 L22:   0.1665                                     
REMARK   3      L33:   0.1040 L12:  -0.3323                                     
REMARK   3      L13:  -0.1512 L23:   0.0700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0204 S12:   0.3030 S13:  -0.2018                       
REMARK   3      S21:  -0.2505 S22:  -0.2916 S23:  -0.3019                       
REMARK   3      S31:   0.3258 S32:   0.3095 S33:  -0.0180                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID -2 THROUGH 4 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): 210.9291 409.1537 -64.5535              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8552 T22:   0.9904                                     
REMARK   3      T33:   1.0616 T12:  -0.2538                                     
REMARK   3      T13:   0.1155 T23:  -0.2085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3316 L22:   1.1425                                     
REMARK   3      L33:   4.1274 L12:  -0.4424                                     
REMARK   3      L13:  -1.0054 L23:   2.1112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1940 S12:   0.1859 S13:   0.6170                       
REMARK   3      S21:  -0.2820 S22:  -0.2322 S23:   0.4020                       
REMARK   3      S31:  -0.6114 S32:  -0.2924 S33:   0.0941                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 4304                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6MON COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237317.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-AUG-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.32                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34429                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.710                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 153.730                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.05200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: 5KJK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.5% PEG 3350, 5.9% ETHANOL, 0.1M       
REMARK 280  TRIS PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z+1/2                                              
REMARK 290       4555   Y,-X,Z+1/2                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       26.72850            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       26.72850            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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     LYS C    -2                                                      
REMARK 465     GLY C     4                                                      
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    CYS A  90      -71.61    -53.94                                   
REMARK 500    ASN A 101       43.18   -144.29                                   
REMARK 500    VAL A 277       50.19   -107.47                                   
REMARK 500    TYR A 311      -15.40   -143.67                                   
REMARK 500    CYS B  90      -71.90    -53.75                                   
REMARK 500    ASN B 101       43.38   -144.30                                   
REMARK 500    VAL B 277       50.18   -107.25                                   
REMARK 500    TYR B 311      -15.26   -143.70                                   
REMARK 500    ARG D   3     -129.04   -114.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  52   SG                                                     
REMARK 620 2 CYS A  55   SG  105.5                                              
REMARK 620 3 CYS A  74   SG  106.3  98.7                                        
REMARK 620 4 CYS A  78   SG  102.3 127.7 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  65   SG                                                     
REMARK 620 2 CYS A  68   SG  106.4                                              
REMARK 620 3 HIS A  86   NE2 117.5  94.6                                        
REMARK 620 4 CYS A  90   SG  119.9 108.5 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 209   SG                                                     
REMARK 620 2 CYS A 262   SG  116.2                                              
REMARK 620 3 CYS A 264   SG  112.6 102.3                                        
REMARK 620 4 CYS A 267   SG  100.0 112.0 114.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  52   SG                                                     
REMARK 620 2 CYS B  55   SG  103.8                                              
REMARK 620 3 CYS B  74   SG   98.7  97.0                                        
REMARK 620 4 CYS B  78   SG  104.3 130.0 118.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  65   SG                                                     
REMARK 620 2 CYS B  68   SG  103.1                                              
REMARK 620 3 HIS B  86   NE2 120.3  96.8                                        
REMARK 620 4 CYS B  90   SG  121.5 107.3 104.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 209   SG                                                     
REMARK 620 2 CYS B 262   SG  118.0                                              
REMARK 620 3 CYS B 264   SG  109.3 102.3                                        
REMARK 620 4 CYS B 267   SG  100.1 112.2 115.6                                  
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide NLE C 0 and SER C 1    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide LEU C -1 and NLE C 0   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide NLE D 0 and SER D 1    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide LEU D -1 and NLE D 0   
DBREF  6MON A    5   433  UNP    Q9NRG4   SMYD2_HUMAN      5    433             
DBREF  6MON B    5   433  UNP    Q9NRG4   SMYD2_HUMAN      5    433             
DBREF  6MON C   -2     4  PDB    6MON     6MON            -2      4             
DBREF  6MON D   -2     4  PDB    6MON     6MON            -2      4             
SEQADV 6MON GLU A  165  UNP  Q9NRG4    GLY   165 VARIANT                        
SEQADV 6MON GLU B  165  UNP  Q9NRG4    GLY   165 VARIANT                        
SEQRES   1 A  429  GLY LEU GLY GLY LEU GLU ARG PHE CYS SER PRO GLY LYS          
SEQRES   2 A  429  GLY ARG GLY LEU ARG ALA LEU GLN PRO PHE GLN VAL GLY          
SEQRES   3 A  429  ASP LEU LEU PHE SER CYS PRO ALA TYR ALA TYR VAL LEU          
SEQRES   4 A  429  THR VAL ASN GLU ARG GLY ASN HIS CYS GLU TYR CYS PHE          
SEQRES   5 A  429  THR ARG LYS GLU GLY LEU SER LYS CYS GLY ARG CYS LYS          
SEQRES   6 A  429  GLN ALA PHE TYR CYS ASN VAL GLU CYS GLN LYS GLU ASP          
SEQRES   7 A  429  TRP PRO MET HIS LYS LEU GLU CYS SER PRO MET VAL VAL          
SEQRES   8 A  429  PHE GLY GLU ASN TRP ASN PRO SER GLU THR VAL ARG LEU          
SEQRES   9 A  429  THR ALA ARG ILE LEU ALA LYS GLN LYS ILE HIS PRO GLU          
SEQRES  10 A  429  ARG THR PRO SER GLU LYS LEU LEU ALA VAL LYS GLU PHE          
SEQRES  11 A  429  GLU SER HIS LEU ASP LYS LEU ASP ASN GLU LYS LYS ASP          
SEQRES  12 A  429  LEU ILE GLN SER ASP ILE ALA ALA LEU HIS HIS PHE TYR          
SEQRES  13 A  429  SER LYS HIS LEU GLU PHE PRO ASP ASN ASP SER LEU VAL          
SEQRES  14 A  429  VAL LEU PHE ALA GLN VAL ASN CYS ASN GLY PHE THR ILE          
SEQRES  15 A  429  GLU ASP GLU GLU LEU SER HIS LEU GLY SER ALA ILE PHE          
SEQRES  16 A  429  PRO ASP VAL ALA LEU MET ASN HIS SER CYS CYS PRO ASN          
SEQRES  17 A  429  VAL ILE VAL THR TYR LYS GLY THR LEU ALA GLU VAL ARG          
SEQRES  18 A  429  ALA VAL GLN GLU ILE LYS PRO GLY GLU GLU VAL PHE THR          
SEQRES  19 A  429  SER TYR ILE ASP LEU LEU TYR PRO THR GLU ASP ARG ASN          
SEQRES  20 A  429  ASP ARG LEU ARG ASP SER TYR PHE PHE THR CYS GLU CYS          
SEQRES  21 A  429  GLN GLU CYS THR THR LYS ASP LYS ASP LYS ALA LYS VAL          
SEQRES  22 A  429  GLU ILE ARG LYS LEU SER ASP PRO PRO LYS ALA GLU ALA          
SEQRES  23 A  429  ILE ARG ASP MET VAL ARG TYR ALA ARG ASN VAL ILE GLU          
SEQRES  24 A  429  GLU PHE ARG ARG ALA LYS HIS TYR LYS SER PRO SER GLU          
SEQRES  25 A  429  LEU LEU GLU ILE CYS GLU LEU SER GLN GLU LYS MET SER          
SEQRES  26 A  429  SER VAL PHE GLU ASP SER ASN VAL TYR MET LEU HIS MET          
SEQRES  27 A  429  MET TYR GLN ALA MET GLY VAL CYS LEU TYR MET GLN ASP          
SEQRES  28 A  429  TRP GLU GLY ALA LEU GLN TYR GLY GLN LYS ILE ILE LYS          
SEQRES  29 A  429  PRO TYR SER LYS HIS TYR PRO LEU TYR SER LEU ASN VAL          
SEQRES  30 A  429  ALA SER MET TRP LEU LYS LEU GLY ARG LEU TYR MET GLY          
SEQRES  31 A  429  LEU GLU HIS LYS ALA ALA GLY GLU LYS ALA LEU LYS LYS          
SEQRES  32 A  429  ALA ILE ALA ILE MET GLU VAL ALA HIS GLY LYS ASP HIS          
SEQRES  33 A  429  PRO TYR ILE SER GLU ILE LYS GLN GLU ILE GLU SER HIS          
SEQRES   1 B  429  GLY LEU GLY GLY LEU GLU ARG PHE CYS SER PRO GLY LYS          
SEQRES   2 B  429  GLY ARG GLY LEU ARG ALA LEU GLN PRO PHE GLN VAL GLY          
SEQRES   3 B  429  ASP LEU LEU PHE SER CYS PRO ALA TYR ALA TYR VAL LEU          
SEQRES   4 B  429  THR VAL ASN GLU ARG GLY ASN HIS CYS GLU TYR CYS PHE          
SEQRES   5 B  429  THR ARG LYS GLU GLY LEU SER LYS CYS GLY ARG CYS LYS          
SEQRES   6 B  429  GLN ALA PHE TYR CYS ASN VAL GLU CYS GLN LYS GLU ASP          
SEQRES   7 B  429  TRP PRO MET HIS LYS LEU GLU CYS SER PRO MET VAL VAL          
SEQRES   8 B  429  PHE GLY GLU ASN TRP ASN PRO SER GLU THR VAL ARG LEU          
SEQRES   9 B  429  THR ALA ARG ILE LEU ALA LYS GLN LYS ILE HIS PRO GLU          
SEQRES  10 B  429  ARG THR PRO SER GLU LYS LEU LEU ALA VAL LYS GLU PHE          
SEQRES  11 B  429  GLU SER HIS LEU ASP LYS LEU ASP ASN GLU LYS LYS ASP          
SEQRES  12 B  429  LEU ILE GLN SER ASP ILE ALA ALA LEU HIS HIS PHE TYR          
SEQRES  13 B  429  SER LYS HIS LEU GLU PHE PRO ASP ASN ASP SER LEU VAL          
SEQRES  14 B  429  VAL LEU PHE ALA GLN VAL ASN CYS ASN GLY PHE THR ILE          
SEQRES  15 B  429  GLU ASP GLU GLU LEU SER HIS LEU GLY SER ALA ILE PHE          
SEQRES  16 B  429  PRO ASP VAL ALA LEU MET ASN HIS SER CYS CYS PRO ASN          
SEQRES  17 B  429  VAL ILE VAL THR TYR LYS GLY THR LEU ALA GLU VAL ARG          
SEQRES  18 B  429  ALA VAL GLN GLU ILE LYS PRO GLY GLU GLU VAL PHE THR          
SEQRES  19 B  429  SER TYR ILE ASP LEU LEU TYR PRO THR GLU ASP ARG ASN          
SEQRES  20 B  429  ASP ARG LEU ARG ASP SER TYR PHE PHE THR CYS GLU CYS          
SEQRES  21 B  429  GLN GLU CYS THR THR LYS ASP LYS ASP LYS ALA LYS VAL          
SEQRES  22 B  429  GLU ILE ARG LYS LEU SER ASP PRO PRO LYS ALA GLU ALA          
SEQRES  23 B  429  ILE ARG ASP MET VAL ARG TYR ALA ARG ASN VAL ILE GLU          
SEQRES  24 B  429  GLU PHE ARG ARG ALA LYS HIS TYR LYS SER PRO SER GLU          
SEQRES  25 B  429  LEU LEU GLU ILE CYS GLU LEU SER GLN GLU LYS MET SER          
SEQRES  26 B  429  SER VAL PHE GLU ASP SER ASN VAL TYR MET LEU HIS MET          
SEQRES  27 B  429  MET TYR GLN ALA MET GLY VAL CYS LEU TYR MET GLN ASP          
SEQRES  28 B  429  TRP GLU GLY ALA LEU GLN TYR GLY GLN LYS ILE ILE LYS          
SEQRES  29 B  429  PRO TYR SER LYS HIS TYR PRO LEU TYR SER LEU ASN VAL          
SEQRES  30 B  429  ALA SER MET TRP LEU LYS LEU GLY ARG LEU TYR MET GLY          
SEQRES  31 B  429  LEU GLU HIS LYS ALA ALA GLY GLU LYS ALA LEU LYS LYS          
SEQRES  32 B  429  ALA ILE ALA ILE MET GLU VAL ALA HIS GLY LYS ASP HIS          
SEQRES  33 B  429  PRO TYR ILE SER GLU ILE LYS GLN GLU ILE GLU SER HIS          
SEQRES   1 C    7  LYS LEU NLE SER LYS ARG GLY                                  
SEQRES   1 D    7  LYS LEU NLE SER LYS ARG GLY                                  
HET    NLE  C   0       8                                                       
HET    NLE  D   0       8                                                       
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET    SAH  A 504      26                                                       
HET    GOL  A 505       6                                                       
HET     ZN  B 501       1                                                       
HET     ZN  B 502       1                                                       
HET     ZN  B 503       1                                                       
HET    SAH  B 504      26                                                       
HETNAM     NLE NORLEUCINE                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NLE    2(C6 H13 N O2)                                               
FORMUL   5   ZN    6(ZN 2+)                                                     
FORMUL   8  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   9  GOL    C3 H8 O3                                                     
FORMUL  14  HOH   *7(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 ALA A  130  PHE A  134  5                                   5    
HELIX    7 AA7 HIS A  137  LEU A  141  5                                   5    
HELIX    8 AA8 ASP A  142  SER A  161  1                                  20    
HELIX    9 AA9 ASP A  168  GLY A  183  1                                  16    
HELIX   10 AB1 ASP A  201  MET A  205  5                                   5    
HELIX   11 AB2 PRO A  246  PHE A  259  1                                  14    
HELIX   12 AB3 CYS A  264  LYS A  270  1                                   7    
HELIX   13 AB4 LYS A  272  VAL A  277  1                                   6    
HELIX   14 AB5 LYS A  287  LYS A  309  1                                  23    
HELIX   15 AB6 SER A  313  SER A  329  1                                  17    
HELIX   16 AB7 ASN A  336  MET A  353  1                                  18    
HELIX   17 AB8 ASP A  355  TYR A  374  1                                  20    
HELIX   18 AB9 SER A  378  LEU A  395  1                                  18    
HELIX   19 AC1 HIS A  397  HIS A  416  1                                  20    
HELIX   20 AC2 HIS A  420  HIS A  433  1                                  14    
HELIX   21 AC3 VAL B   45  ARG B   48  5                                   4    
HELIX   22 AC4 ASN B   75  LYS B   87  1                                  13    
HELIX   23 AC5 GLU B   89  GLY B   97  1                                   9    
HELIX   24 AC6 GLU B   98  TRP B  100  5                                   3    
HELIX   25 AC7 SER B  103  HIS B  119  1                                  17    
HELIX   26 AC8 ALA B  130  PHE B  134  5                                   5    
HELIX   27 AC9 HIS B  137  LEU B  141  5                                   5    
HELIX   28 AD1 ASP B  142  SER B  161  1                                  20    
HELIX   29 AD2 ASP B  168  GLY B  183  1                                  16    
HELIX   30 AD3 ASP B  201  MET B  205  5                                   5    
HELIX   31 AD4 PRO B  246  PHE B  259  1                                  14    
HELIX   32 AD5 CYS B  264  LYS B  270  1                                   7    
HELIX   33 AD6 LYS B  272  VAL B  277  1                                   6    
HELIX   34 AD7 LYS B  287  LYS B  309  1                                  23    
HELIX   35 AD8 SER B  313  SER B  329  1                                  17    
HELIX   36 AD9 ASN B  336  MET B  353  1                                  18    
HELIX   37 AE1 ASP B  355  TYR B  374  1                                  20    
HELIX   38 AE2 SER B  378  LEU B  395  1                                  18    
HELIX   39 AE3 HIS B  397  GLY B  417  1                                  21    
HELIX   40 AE4 HIS B  420  HIS B  433  1                                  14    
SHEET    1 AA1 2 LEU A   9  CYS A  13  0                                        
SHEET    2 AA1 2 ARG A  19  ALA A  23 -1  O  ARG A  22   N  GLU A  10           
SHEET    1 AA2 3 LEU A  32  PRO A  37  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  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  CYS B  13  0                                        
SHEET    2 AA6 2 ARG B  19  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  LEU B  33           
SHEET    3 AA7 3 VAL B 213  LYS B 218 -1  N  LYS B 218   O  LEU B 221           
SHEET    1 AA8 3 ALA B  40  LEU B  43  0                                        
SHEET    2 AA8 3 HIS B 193  ILE B 198 -1  O  SER B 196   N  VAL B  42           
SHEET    3 AA8 3 PHE B 184  GLU B 187 -1  N  ILE B 186   O  LEU B 194           
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 A 501     1555   1555  2.37  
LINK         SG  CYS A  55                ZN    ZN A 501     1555   1555  2.30  
LINK         SG  CYS A  65                ZN    ZN A 502     1555   1555  2.37  
LINK         SG  CYS A  68                ZN    ZN A 502     1555   1555  2.29  
LINK         SG  CYS A  74                ZN    ZN A 501     1555   1555  2.30  
LINK         SG  CYS A  78                ZN    ZN A 501     1555   1555  2.26  
LINK         NE2 HIS A  86                ZN    ZN A 502     1555   1555  2.05  
LINK         SG  CYS A  90                ZN    ZN A 502     1555   1555  2.31  
LINK         SG  CYS A 209                ZN    ZN A 503     1555   1555  2.33  
LINK         SG  CYS A 262                ZN    ZN A 503     1555   1555  2.28  
LINK         SG  CYS A 264                ZN    ZN A 503     1555   1555  2.35  
LINK         SG  CYS A 267                ZN    ZN A 503     1555   1555  2.27  
LINK         SG  CYS B  52                ZN    ZN B 501     1555   1555  2.41  
LINK         SG  CYS B  55                ZN    ZN B 501     1555   1555  2.32  
LINK         SG  CYS B  65                ZN    ZN B 502     1555   1555  2.39  
LINK         SG  CYS B  68                ZN    ZN B 502     1555   1555  2.23  
LINK         SG  CYS B  74                ZN    ZN B 501     1555   1555  2.36  
LINK         SG  CYS B  78                ZN    ZN B 501     1555   1555  2.25  
LINK         NE2 HIS B  86                ZN    ZN B 502     1555   1555  2.05  
LINK         SG  CYS B  90                ZN    ZN B 502     1555   1555  2.31  
LINK         SG  CYS B 209                ZN    ZN B 503     1555   1555  2.30  
LINK         SG  CYS B 262                ZN    ZN B 503     1555   1555  2.19  
LINK         SG  CYS B 264                ZN    ZN B 503     1555   1555  2.37  
LINK         SG  CYS B 267                ZN    ZN B 503     1555   1555  2.26  
LINK         C   LEU C  -1                 N   NLE C   0     1555   1555  1.33  
LINK         C   NLE C   0                 N   SER C   1     1555   1555  1.32  
LINK         C   LEU D  -1                 N   NLE D   0     1555   1555  1.33  
LINK         C   NLE D   0                 N   SER D   1     1555   1555  1.33  
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 14 GLY A  16  LYS A  17  ARG A  19  GLU A 135                    
SITE     2 AC4 14 HIS A 137  CYS A 181  ASN A 182  ALA A 203                    
SITE     3 AC4 14 LEU A 204  ASN A 206  HIS A 207  TYR A 240                    
SITE     4 AC4 14 TYR A 258  PHE A 260                                          
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  ARG B  19  GLU B 135                    
SITE     2 AC8 14 HIS B 137  CYS B 181  ASN B 182  ALA B 203                    
SITE     3 AC8 14 LEU B 204  ASN B 206  HIS B 207  TYR B 240                    
SITE     4 AC8 14 TYR B 258  PHE B 260                                          
SITE     1 AC9 10 GLY A 183  PHE A 184  THR A 185  GLU A 187                    
SITE     2 AC9 10 TYR A 240  ILE A 241  TYR A 258  LEU C  -1                    
SITE     3 AC9 10 LYS C   2  ARG C   3                                          
SITE     1 AD1  7 VAL A 179  GLY A 183  PHE A 184  THR A 185                    
SITE     2 AD1  7 TYR A 240  TYR A 258  SER C   1                               
SITE     1 AD2 11 GLY B 183  PHE B 184  THR B 185  GLU B 187                    
SITE     2 AD2 11 TYR B 240  ILE B 241  TYR B 258  LEU D  -1                    
SITE     3 AD2 11 LYS D   2  ARG D   3  GLY D   4                               
SITE     1 AD3  8 VAL B 179  GLY B 183  PHE B 184  THR B 185                    
SITE     2 AD3  8 TYR B 240  TYR B 258  LYS D  -2  SER D   1                    
CRYST1  153.728  153.728   53.457  90.00  90.00  90.00 P 42          8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006505  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006505  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018707        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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