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Database: PDB
Entry: 6KMS
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HEADER    TRANSFERASE                             01-AUG-19   6KMS              
TITLE     CRYSTAL STRUCTURE OF HUMAN N6AMT1-TRM112 IN COMPLEX WITH SAM (SPACE   
TITLE    2 GROUP I422)                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHYLTRANSFERASE N6AMT1;                                  
COMPND   3 CHAIN: C, D;                                                         
COMPND   4 SYNONYM: HEMK METHYLTRANSFERASE FAMILY MEMBER 2,M.HSAHEMK2P,         
COMPND   5 METHYLARSONITE METHYLTRANSFERASE N6AMT1,N(6)-ADENINE-SPECIFIC DNA    
COMPND   6 METHYLTRANSFERASE 1,PROTEIN N(5)-GLUTAMINE METHYLTRANSFERASE;        
COMPND   7 EC: 2.1.1.-,2.1.1.72;                                                
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: MULTIFUNCTIONAL METHYLTRANSFERASE SUBUNIT TRM112-LIKE      
COMPND  11 PROTEIN;                                                             
COMPND  12 CHAIN: A, B;                                                         
COMPND  13 SYNONYM: TRNA METHYLTRANSFERASE 112 HOMOLOG;                         
COMPND  14 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: N6AMT1, C21ORF127, HEMK2, PRED28;                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: TRMT112, AD-001, HSPC152, HSPC170;                             
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 83333                                       
KEYWDS    METHYLTRANSFERASE, COMPLEX, PROTEIN TRANSLATION, POLYPEPTIDE RELEASE  
KEYWDS   2 FACTOR ERF1, TRANSFERASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.J.LI,Y.SHI,T.L.ZHANG,J.YE,J.P.DING                                  
REVDAT   2   06-NOV-19 6KMS    1       JRNL                                     
REVDAT   1   18-SEP-19 6KMS    0                                                
JRNL        AUTH   W.LI,Y.SHI,T.ZHANG,J.YE,J.DING                               
JRNL        TITL   STRUCTURAL INSIGHT INTO HUMAN N6AMT1-TRM112 COMPLEX          
JRNL        TITL 2 FUNCTIONING AS A PROTEIN METHYLTRANSFERASE.                  
JRNL        REF    CELL DISCOV                   V.   5    51 2019              
JRNL        REFN                   ESSN 2056-5968                               
JRNL        PMID   31636962                                                     
JRNL        DOI    10.1038/S41421-019-0121-Y                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 39482                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1978                            
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 39.3860 -  7.6947    1.00     2864   143  0.1653 0.2019        
REMARK   3     2  7.6947 -  6.1149    1.00     2742   141  0.2123 0.2490        
REMARK   3     3  6.1149 -  5.3441    1.00     2713   138  0.2245 0.2948        
REMARK   3     4  5.3441 -  4.8564    1.00     2704   130  0.2120 0.2509        
REMARK   3     5  4.8564 -  4.5089    1.00     2673   151  0.2076 0.2260        
REMARK   3     6  4.5089 -  4.2434    1.00     2648   143  0.2170 0.2229        
REMARK   3     7  4.2434 -  4.0311    1.00     2683   128  0.2430 0.3205        
REMARK   3     8  4.0311 -  3.8558    1.00     2640   145  0.2646 0.2902        
REMARK   3     9  3.8558 -  3.7074    1.00     2660   146  0.2669 0.2602        
REMARK   3    10  3.7074 -  3.5796    1.00     2642   133  0.2836 0.3451        
REMARK   3    11  3.5796 -  3.4677    1.00     2614   163  0.2954 0.3416        
REMARK   3    12  3.4677 -  3.3687    1.00     2622   156  0.3072 0.3621        
REMARK   3    13  3.3687 -  3.2800    1.00     2647   142  0.3477 0.3854        
REMARK   3    14  3.2800 -  3.2000    1.00     2652   119  0.3611 0.3588        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.880           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 83.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 81.66                          
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      :  0.012           5209                                  
REMARK   3   ANGLE     :  1.374           7094                                  
REMARK   3   CHIRALITY :  0.072            827                                  
REMARK   3   PLANARITY :  0.009            922                                  
REMARK   3   DIHEDRAL  : 21.871           3114                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESID 0 THROUGH 43 OR         
REMARK   3                          (RESID 44 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 45       
REMARK   3                          THROUGH 67 OR (RESID 68 AND (NAME N OR      
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 69 THROUGH 75 OR (RESID 76 AND     
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 77 THROUGH 88 OR        
REMARK   3                          (RESID 89 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 90       
REMARK   3                          THROUGH 120))                               
REMARK   3     SELECTION          : (CHAIN B AND RESID 0 THROUGH 120)           
REMARK   3     ATOM PAIRS NUMBER  : 953                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN C AND (RESID 6 THROUGH 15 OR         
REMARK   3                          (RESID 16 AND (NAME N OR NAME CA OR NAME    
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 17       
REMARK   3                          THROUGH 114 OR (RESID 115 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 116 THROUGH 145 OR (RESID 146      
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME    
REMARK   3                          O OR NAME CB )) OR RESID 147 THROUGH 167    
REMARK   3                          OR (RESID 168 AND (NAME N OR NAME CA OR     
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID     
REMARK   3                          169 THROUGH 174 OR (RESID 175 AND (NAME N   
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESID 176 THROUGH 183 OR (RESID 184   
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME    
REMARK   3                          O OR NAME CB )) OR RESID 185 THROUGH 186    
REMARK   3                          OR (RESID 187 AND (NAME N OR NAME CA OR     
REMARK   3                          NAME C OR NAME O OR NAME CB )) OR RESID     
REMARK   3                          188 THROUGH 190 OR (RESID 191 AND (NAME N   
REMARK   3                          OR NAME CA OR NAME C OR NAME O OR NAME CB   
REMARK   3                          )) OR RESID 192 THROUGH 198 OR (RESID 199   
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME    
REMARK   3                          O OR NAME CB )) OR RESID 200 THROUGH 202    
REMARK   3                          OR (RESID 203 THROUGH 204 AND (NAME N OR    
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 205 THROUGH 212 OR (RESID 213      
REMARK   3                          AND (NAME N OR NAME CA OR NAME C OR NAME    
REMARK   3                          O OR NAME CB )) OR RESID 214))              
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 1670                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6KMS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-AUG-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300013184.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39672                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 28.80                              
REMARK 200  R MERGE                    (I) : 0.23400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.6700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 28.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 2.20300                            
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: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 83.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M (NH4)2SO4, 0.1M MES, PH 6.5, 10%    
REMARK 280  1,4-DIOXANE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
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                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       97.67700            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       97.67700            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      123.27550            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       97.67700            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       97.67700            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000      123.27550            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       97.67700            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       97.67700            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      123.27550            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       97.67700            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       97.67700            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000      123.27550            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       97.67700            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       97.67700            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000      123.27550            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       97.67700            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       97.67700            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      123.27550            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       97.67700            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       97.67700            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000      123.27550            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       97.67700            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       97.67700            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      123.27550            
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: 2450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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     MSE C   -13                                                      
REMARK 465     GLY C   -12                                                      
REMARK 465     SER C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     SER C    -3                                                      
REMARK 465     GLN C    -2                                                      
REMARK 465     ASP C    -1                                                      
REMARK 465     PRO C     0                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     GLU A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     THR A   123                                                      
REMARK 465     GLU A   124                                                      
REMARK 465     SER A   125                                                      
REMARK 465     SER B   125                                                      
REMARK 465     MSE D   -13                                                      
REMARK 465     GLY D   -12                                                      
REMARK 465     SER D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     SER D    -3                                                      
REMARK 465     GLN D    -2                                                      
REMARK 465     ASP D    -1                                                      
REMARK 465     PRO D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     GLU D     4                                                      
REMARK 465     ASN D     5                                                      
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 C 166    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  68    CG   CD   CE   NZ                                   
REMARK 470     GLU B  76    CG   CD   OE1  OE2                                  
REMARK 470     LEU B  89    CG   CD1  CD2                                       
REMARK 470     ARG D  16    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 115    CG   CD   CE   NZ                                   
REMARK 470     ARG D 146    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 166    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 168    CG   CD1  CD2                                       
REMARK 470     LYS D 175    CG   CD   CE   NZ                                   
REMARK 470     LYS D 184    CG   CD   CE   NZ                                   
REMARK 470     LYS D 187    CG   CD   CE   NZ                                   
REMARK 470     LEU D 191    CG   CD1  CD2                                       
REMARK 470     ARG D 199    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 203    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 204    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 213    CG   CD   CE   NZ                                   
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    PHE C   6      -70.11   -128.92                                   
REMARK 500    HIS C  11       46.74   -145.92                                   
REMARK 500    PRO C  69        7.40    -67.93                                   
REMARK 500    LEU C 104      -96.70     59.14                                   
REMARK 500    GLU C 114       27.88     49.80                                   
REMARK 500    ASN C 178       68.14     72.04                                   
REMARK 500    SER C 198      155.79    178.58                                   
REMARK 500    ALA C 201      138.01   -172.58                                   
REMARK 500    GLN A  65       79.15   -112.81                                   
REMARK 500    HIS D  11       46.16   -146.25                                   
REMARK 500    ASP D  21       30.85    -93.88                                   
REMARK 500    PRO D  69       14.38    -66.79                                   
REMARK 500    CYS D  75      144.41    177.33                                   
REMARK 500    LEU D 104      -98.70     61.82                                   
REMARK 500    SER D 135      165.25    -49.32                                   
REMARK 500    ARG D 166       30.42    -83.64                                   
REMARK 500    ASN D 178       63.26     71.38                                   
REMARK 500    SER D 198      165.62    174.75                                   
REMARK 500    ALA D 201      145.05   -174.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM D 301                 
DBREF  6KMS C    1   214  UNP    Q9Y5N5   N6MT1_HUMAN      1    214             
DBREF  6KMS A    1   125  UNP    Q9UI30   TR112_HUMAN      1    125             
DBREF  6KMS B    1   125  UNP    Q9UI30   TR112_HUMAN      1    125             
DBREF  6KMS D    1   214  UNP    Q9Y5N5   N6MT1_HUMAN      1    214             
SEQADV 6KMS MSE C  -13  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS GLY C  -12  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS SER C  -11  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS SER C  -10  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS C   -9  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS C   -8  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS C   -7  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS C   -6  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS C   -5  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS C   -4  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS SER C   -3  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS GLN C   -2  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS ASP C   -1  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS PRO C    0  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS MSE A    0  UNP  Q9UI30              INITIATING METHIONINE          
SEQADV 6KMS MSE B    0  UNP  Q9UI30              INITIATING METHIONINE          
SEQADV 6KMS MSE D  -13  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS GLY D  -12  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS SER D  -11  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS SER D  -10  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS D   -9  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS D   -8  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS D   -7  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS D   -6  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS D   -5  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS HIS D   -4  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS SER D   -3  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS GLN D   -2  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS ASP D   -1  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQADV 6KMS PRO D    0  UNP  Q9Y5N5              EXPRESSION TAG                 
SEQRES   1 C  228  MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 C  228  PRO MSE ALA GLY GLU ASN PHE ALA THR PRO PHE HIS GLY          
SEQRES   3 C  228  HIS VAL GLY ARG GLY ALA PHE SER ASP VAL TYR GLU PRO          
SEQRES   4 C  228  ALA GLU ASP THR PHE LEU LEU LEU ASP ALA LEU GLU ALA          
SEQRES   5 C  228  ALA ALA ALA GLU LEU ALA GLY VAL GLU ILE CYS LEU GLU          
SEQRES   6 C  228  VAL GLY SER GLY SER GLY VAL VAL SER ALA PHE LEU ALA          
SEQRES   7 C  228  SER MSE ILE GLY PRO GLN ALA LEU TYR MSE CYS THR ASP          
SEQRES   8 C  228  ILE ASN PRO GLU ALA ALA ALA CYS THR LEU GLU THR ALA          
SEQRES   9 C  228  ARG CYS ASN LYS VAL HIS ILE GLN PRO VAL ILE THR ASP          
SEQRES  10 C  228  LEU VAL LYS GLY LEU LEU PRO ARG LEU THR GLU LYS VAL          
SEQRES  11 C  228  ASP LEU LEU VAL PHE ASN PRO PRO TYR VAL VAL THR PRO          
SEQRES  12 C  228  PRO GLN GLU VAL GLY SER HIS GLY ILE GLU ALA ALA TRP          
SEQRES  13 C  228  ALA GLY GLY ARG ASN GLY ARG GLU VAL MSE ASP ARG PHE          
SEQRES  14 C  228  PHE PRO LEU VAL PRO ASP LEU LEU SER PRO ARG GLY LEU          
SEQRES  15 C  228  PHE TYR LEU VAL THR ILE LYS GLU ASN ASN PRO GLU GLU          
SEQRES  16 C  228  ILE LEU LYS ILE MSE LYS THR LYS GLY LEU GLN GLY THR          
SEQRES  17 C  228  THR ALA LEU SER ARG GLN ALA GLY GLN GLU THR LEU SER          
SEQRES  18 C  228  VAL LEU LYS PHE THR LYS SER                                  
SEQRES   1 A  126  MSE MSE LYS LEU LEU THR HIS ASN LEU LEU SER SER HIS          
SEQRES   2 A  126  VAL ARG GLY VAL GLY SER ARG GLY PHE PRO LEU ARG LEU          
SEQRES   3 A  126  GLN ALA THR GLU VAL ARG ILE CYS PRO VAL GLU PHE ASN          
SEQRES   4 A  126  PRO ASN PHE VAL ALA ARG MSE ILE PRO LYS VAL GLU TRP          
SEQRES   5 A  126  SER ALA PHE LEU GLU ALA ALA ASP ASN LEU ARG LEU ILE          
SEQRES   6 A  126  GLN VAL PRO LYS GLY PRO VAL GLU GLY TYR GLU GLU ASN          
SEQRES   7 A  126  GLU GLU PHE LEU ARG THR MSE HIS HIS LEU LEU LEU GLU          
SEQRES   8 A  126  VAL GLU VAL ILE GLU GLY THR LEU GLN CYS PRO GLU SER          
SEQRES   9 A  126  GLY ARG MSE PHE PRO ILE SER ARG GLY ILE PRO ASN MSE          
SEQRES  10 A  126  LEU LEU SER GLU GLU GLU THR GLU SER                          
SEQRES   1 B  126  MSE MSE LYS LEU LEU THR HIS ASN LEU LEU SER SER HIS          
SEQRES   2 B  126  VAL ARG GLY VAL GLY SER ARG GLY PHE PRO LEU ARG LEU          
SEQRES   3 B  126  GLN ALA THR GLU VAL ARG ILE CYS PRO VAL GLU PHE ASN          
SEQRES   4 B  126  PRO ASN PHE VAL ALA ARG MSE ILE PRO LYS VAL GLU TRP          
SEQRES   5 B  126  SER ALA PHE LEU GLU ALA ALA ASP ASN LEU ARG LEU ILE          
SEQRES   6 B  126  GLN VAL PRO LYS GLY PRO VAL GLU GLY TYR GLU GLU ASN          
SEQRES   7 B  126  GLU GLU PHE LEU ARG THR MSE HIS HIS LEU LEU LEU GLU          
SEQRES   8 B  126  VAL GLU VAL ILE GLU GLY THR LEU GLN CYS PRO GLU SER          
SEQRES   9 B  126  GLY ARG MSE PHE PRO ILE SER ARG GLY ILE PRO ASN MSE          
SEQRES  10 B  126  LEU LEU SER GLU GLU GLU THR GLU SER                          
SEQRES   1 D  228  MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 D  228  PRO MSE ALA GLY GLU ASN PHE ALA THR PRO PHE HIS GLY          
SEQRES   3 D  228  HIS VAL GLY ARG GLY ALA PHE SER ASP VAL TYR GLU PRO          
SEQRES   4 D  228  ALA GLU ASP THR PHE LEU LEU LEU ASP ALA LEU GLU ALA          
SEQRES   5 D  228  ALA ALA ALA GLU LEU ALA GLY VAL GLU ILE CYS LEU GLU          
SEQRES   6 D  228  VAL GLY SER GLY SER GLY VAL VAL SER ALA PHE LEU ALA          
SEQRES   7 D  228  SER MSE ILE GLY PRO GLN ALA LEU TYR MSE CYS THR ASP          
SEQRES   8 D  228  ILE ASN PRO GLU ALA ALA ALA CYS THR LEU GLU THR ALA          
SEQRES   9 D  228  ARG CYS ASN LYS VAL HIS ILE GLN PRO VAL ILE THR ASP          
SEQRES  10 D  228  LEU VAL LYS GLY LEU LEU PRO ARG LEU THR GLU LYS VAL          
SEQRES  11 D  228  ASP LEU LEU VAL PHE ASN PRO PRO TYR VAL VAL THR PRO          
SEQRES  12 D  228  PRO GLN GLU VAL GLY SER HIS GLY ILE GLU ALA ALA TRP          
SEQRES  13 D  228  ALA GLY GLY ARG ASN GLY ARG GLU VAL MSE ASP ARG PHE          
SEQRES  14 D  228  PHE PRO LEU VAL PRO ASP LEU LEU SER PRO ARG GLY LEU          
SEQRES  15 D  228  PHE TYR LEU VAL THR ILE LYS GLU ASN ASN PRO GLU GLU          
SEQRES  16 D  228  ILE LEU LYS ILE MSE LYS THR LYS GLY LEU GLN GLY THR          
SEQRES  17 D  228  THR ALA LEU SER ARG GLN ALA GLY GLN GLU THR LEU SER          
SEQRES  18 D  228  VAL LEU LYS PHE THR LYS SER                                  
MODRES 6KMS MSE C   66  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE C   74  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE C  152  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE C  186  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE A    1  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE A   45  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE A   84  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE A  106  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE A  116  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE B    1  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE B   45  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE B   84  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE B  106  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE B  116  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE D   66  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE D   74  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE D  152  MET  MODIFIED RESIDUE                                   
MODRES 6KMS MSE D  186  MET  MODIFIED RESIDUE                                   
HET    MSE  C  66       8                                                       
HET    MSE  C  74       8                                                       
HET    MSE  C 152       8                                                       
HET    MSE  C 186       8                                                       
HET    MSE  A   0       8                                                       
HET    MSE  A   1       8                                                       
HET    MSE  A  45       8                                                       
HET    MSE  A  84       8                                                       
HET    MSE  A 106       8                                                       
HET    MSE  A 116       8                                                       
HET    MSE  B   0       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  45       8                                                       
HET    MSE  B  84       8                                                       
HET    MSE  B 106       8                                                       
HET    MSE  B 116       8                                                       
HET    MSE  D  66       8                                                       
HET    MSE  D  74       8                                                       
HET    MSE  D 152       8                                                       
HET    MSE  D 186       8                                                       
HET    SAM  C 301      27                                                       
HET    SAM  D 301      27                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   1  MSE    20(C5 H11 N O2 SE)                                           
FORMUL   5  SAM    2(C15 H22 N6 O5 S)                                           
HELIX    1 AA1 ARG C   16  SER C   20  5                                   5    
HELIX    2 AA2 ALA C   26  ALA C   39  1                                  14    
HELIX    3 AA3 ALA C   41  VAL C   46  5                                   6    
HELIX    4 AA4 GLY C   57  GLY C   68  1                                  12    
HELIX    5 AA5 ASN C   79  ASN C   93  1                                  15    
HELIX    6 AA6 PRO C  129  VAL C  133  5                                   5    
HELIX    7 AA7 ILE C  138  ALA C  143  1                                   6    
HELIX    8 AA8 GLY C  145  GLY C  148  5                                   4    
HELIX    9 AA9 ARG C  149  PHE C  156  1                                   8    
HELIX   10 AB1 LEU C  158  LEU C  162  1                                   5    
HELIX   11 AB2 ILE C  174  ASN C  177  5                                   4    
HELIX   12 AB3 ASN C  178  THR C  188  1                                  11    
HELIX   13 AB4 LEU A    3  ASN A    7  1                                   5    
HELIX   14 AB5 VAL A   16  PHE A   21  5                                   6    
HELIX   15 AB6 ASN A   38  ILE A   46  1                                   9    
HELIX   16 AB7 GLU A   50  LEU A   61  1                                  12    
HELIX   17 AB8 ASN A   77  GLU A   90  1                                  14    
HELIX   18 AB9 LYS B    2  ASN B    7  1                                   6    
HELIX   19 AC1 VAL B   16  GLY B   20  5                                   5    
HELIX   20 AC2 ASN B   38  ILE B   46  1                                   9    
HELIX   21 AC3 GLU B   50  LEU B   61  1                                  12    
HELIX   22 AC4 ASN B   77  GLU B   90  1                                  14    
HELIX   23 AC5 ALA D   26  ALA D   39  1                                  14    
HELIX   24 AC6 GLY D   57  GLY D   68  1                                  12    
HELIX   25 AC7 ASN D   79  ASN D   93  1                                  15    
HELIX   26 AC8 GLY D  137  ALA D  141  5                                   5    
HELIX   27 AC9 GLY D  145  GLY D  148  5                                   4    
HELIX   28 AD1 ARG D  149  PHE D  156  1                                   8    
HELIX   29 AD2 PRO D  157  LEU D  162  1                                   6    
HELIX   30 AD3 ASN D  178  LYS D  189  1                                  12    
SHEET    1 AA1 7 ILE C  97  ILE C 101  0                                        
SHEET    2 AA1 7 LEU C  72  ASP C  77  1  N  TYR C  73   O  GLN C  98           
SHEET    3 AA1 7 ILE C  48  VAL C  52  1  N  CYS C  49   O  MSE C  74           
SHEET    4 AA1 7 VAL C 116  PHE C 121  1  O  VAL C 120   N  LEU C  50           
SHEET    5 AA1 7 LEU C 163  THR C 173  1  O  LEU C 168   N  ASP C 117           
SHEET    6 AA1 7 GLU C 204  LYS C 213 -1  O  LEU C 209   N  LEU C 171           
SHEET    7 AA1 7 LEU C 191  THR C 194 -1  N  THR C 194   O  LYS C 210           
SHEET    1 AA2 7 ILE C  97  ILE C 101  0                                        
SHEET    2 AA2 7 LEU C  72  ASP C  77  1  N  TYR C  73   O  GLN C  98           
SHEET    3 AA2 7 ILE C  48  VAL C  52  1  N  CYS C  49   O  MSE C  74           
SHEET    4 AA2 7 VAL C 116  PHE C 121  1  O  VAL C 120   N  LEU C  50           
SHEET    5 AA2 7 LEU C 163  THR C 173  1  O  LEU C 168   N  ASP C 117           
SHEET    6 AA2 7 GLU C 204  LYS C 213 -1  O  LEU C 209   N  LEU C 171           
SHEET    7 AA2 7 ARG C 199  ALA C 201 -1  N  ALA C 201   O  GLU C 204           
SHEET    1 AA3 3 MSE A   1  LYS A   2  0                                        
SHEET    2 AA3 3 VAL A  91  GLN A  99 -1  O  VAL A  93   N  MSE A   1           
SHEET    3 AA3 3 ARG A  24  ILE A  32 -1  N  GLU A  29   O  ILE A  94           
SHEET    1 AA4 4 MSE A   1  LYS A   2  0                                        
SHEET    2 AA4 4 VAL A  91  GLN A  99 -1  O  VAL A  93   N  MSE A   1           
SHEET    3 AA4 4 MSE A 106  SER A 110 -1  O  PHE A 107   N  LEU A  98           
SHEET    4 AA4 4 ILE A 113  PRO A 114 -1  O  ILE A 113   N  SER A 110           
SHEET    1 AA5 4 ARG B  24  ILE B  32  0                                        
SHEET    2 AA5 4 VAL B  91  GLN B  99 -1  O  GLN B  99   N  ARG B  24           
SHEET    3 AA5 4 MSE B 106  SER B 110 -1  O  PHE B 107   N  LEU B  98           
SHEET    4 AA5 4 ILE B 113  PRO B 114 -1  O  ILE B 113   N  SER B 110           
SHEET    1 AA6 6 ILE D  97  VAL D 100  0                                        
SHEET    2 AA6 6 LEU D  72  THR D  76  1  N  TYR D  73   O  GLN D  98           
SHEET    3 AA6 6 ILE D  48  LEU D  50  1  N  CYS D  49   O  LEU D  72           
SHEET    4 AA6 6 VAL D 116  PHE D 121  1  O  VAL D 120   N  LEU D  50           
SHEET    5 AA6 6 LEU D 163  THR D 173  1  O  SER D 164   N  VAL D 116           
SHEET    6 AA6 6 SER D 207  VAL D 208 -1  O  SER D 207   N  THR D 173           
SHEET    1 AA7 6 ILE D  97  VAL D 100  0                                        
SHEET    2 AA7 6 LEU D  72  THR D  76  1  N  TYR D  73   O  GLN D  98           
SHEET    3 AA7 6 ILE D  48  LEU D  50  1  N  CYS D  49   O  LEU D  72           
SHEET    4 AA7 6 VAL D 116  PHE D 121  1  O  VAL D 120   N  LEU D  50           
SHEET    5 AA7 6 LEU D 163  THR D 173  1  O  SER D 164   N  VAL D 116           
SHEET    6 AA7 6 PHE D 211  THR D 212 -1  O  PHE D 211   N  PHE D 169           
LINK         C   SER C  65                 N   MSE C  66     1555   1555  1.32  
LINK         C   MSE C  66                 N   ILE C  67     1555   1555  1.33  
LINK         C   TYR C  73                 N   MSE C  74     1555   1555  1.32  
LINK         C   MSE C  74                 N   CYS C  75     1555   1555  1.32  
LINK         C   VAL C 151                 N   MSE C 152     1555   1555  1.34  
LINK         C   MSE C 152                 N   ASP C 153     1555   1555  1.34  
LINK         C   ILE C 185                 N   MSE C 186     1555   1555  1.33  
LINK         C   MSE C 186                 N   LYS C 187     1555   1555  1.34  
LINK         C   MSE A   0                 N   MSE A   1     1555   1555  1.35  
LINK         C   MSE A   1                 N   LYS A   2     1555   1555  1.33  
LINK         C   ARG A  44                 N   MSE A  45     1555   1555  1.34  
LINK         C   MSE A  45                 N   ILE A  46     1555   1555  1.34  
LINK         C   THR A  83                 N   MSE A  84     1555   1555  1.33  
LINK         C   MSE A  84                 N   HIS A  85     1555   1555  1.34  
LINK         C   ARG A 105                 N   MSE A 106     1555   1555  1.32  
LINK         C   MSE A 106                 N   PHE A 107     1555   1555  1.32  
LINK         C   ASN A 115                 N   MSE A 116     1555   1555  1.32  
LINK         C   MSE A 116                 N   LEU A 117     1555   1555  1.33  
LINK         C   MSE B   0                 N   MSE B   1     1555   1555  1.35  
LINK         C   MSE B   1                 N   LYS B   2     1555   1555  1.33  
LINK         C   ARG B  44                 N   MSE B  45     1555   1555  1.33  
LINK         C   MSE B  45                 N   ILE B  46     1555   1555  1.33  
LINK         C   THR B  83                 N   MSE B  84     1555   1555  1.33  
LINK         C   MSE B  84                 N   HIS B  85     1555   1555  1.33  
LINK         C   ARG B 105                 N   MSE B 106     1555   1555  1.32  
LINK         C   MSE B 106                 N   PHE B 107     1555   1555  1.33  
LINK         C   ASN B 115                 N   MSE B 116     1555   1555  1.33  
LINK         C   MSE B 116                 N   LEU B 117     1555   1555  1.33  
LINK         C   SER D  65                 N   MSE D  66     1555   1555  1.32  
LINK         C   MSE D  66                 N   ILE D  67     1555   1555  1.34  
LINK         C   TYR D  73                 N   MSE D  74     1555   1555  1.33  
LINK         C   MSE D  74                 N   CYS D  75     1555   1555  1.34  
LINK         C   VAL D 151                 N   MSE D 152     1555   1555  1.32  
LINK         C   MSE D 152                 N   ASP D 153     1555   1555  1.34  
LINK         C   ILE D 185                 N   MSE D 186     1555   1555  1.33  
LINK         C   MSE D 186                 N   LYS D 187     1555   1555  1.34  
CISPEP   1 LEU C  109    PRO C  110          0         6.45                     
CISPEP   2 PHE A   21    PRO A   22          0        -1.91                     
CISPEP   3 PHE B   21    PRO B   22          0        -0.94                     
CISPEP   4 LEU D  109    PRO D  110          0         3.79                     
SITE     1 AC1 15 TYR C  23  THR C  29  GLU C  51  GLY C  53                    
SITE     2 AC1 15 SER C  54  GLY C  55  SER C  56  ASP C  77                    
SITE     3 AC1 15 ILE C  78  ASP C 103  LEU C 104  ASN C 122                    
SITE     4 AC1 15 PRO C 124  ALA C 140  ALA C 141                               
SITE     1 AC2 13 TYR D  23  THR D  29  GLU D  51  GLY D  53                    
SITE     2 AC2 13 GLY D  55  VAL D  59  ASP D  77  ILE D  78                    
SITE     3 AC2 13 LEU D 104  ASN D 122  ALA D 140  ALA D 141                    
SITE     4 AC2 13 ARG D 154                                                     
CRYST1  195.354  195.354  246.551  90.00  90.00  90.00 I 4 2 2      32          
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      0.005119  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005119  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004056        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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