GenomeNet

Database: PDB
Entry: 3HYM
LinkDB: 3HYM
Original site: 3HYM 
HEADER    CELL CYCLE, LIGASE                      22-JUN-09   3HYM              
TITLE     INSIGHTS INTO ANAPHASE PROMOTING COMPLEX TPR SUBDOMAIN                
TITLE    2 ASSEMBLY FROM A CDC26-APC6 STRUCTURE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANAPHASE-PROMOTING COMPLEX SUBUNIT CDC26;                  
COMPND   3 CHAIN: A, C, E, G, I, K;                                             
COMPND   4 FRAGMENT: CDC26N;                                                    
COMPND   5 SYNONYM: CELL DIVISION CYCLE PROTEIN 26 HOMOLOG;                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CELL DIVISION CYCLE PROTEIN 16 HOMOLOG;                    
COMPND   9 CHAIN: B, D, F, H, J, L;                                             
COMPND  10 FRAGMENT: APC6TPR;                                                   
COMPND  11 SYNONYM: CDC16HS, ANAPHASE-PROMOTING COMPLEX SUBUNIT 6,              
COMPND  12 APC6, CYCLOSOME SUBUNIT 6;                                           
COMPND  13 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: CDC26, C9ORF17;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CDC16, ANAPC6;                                                 
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    APC, ANAPHASE PROMOTING COMPLEX, CELL CYCLE, MITOSIS,                 
KEYWDS   2 CYCLOSOME, TPR, UBIQUITIN, UBIQUITIN LIGASE, E3, TWINNING,           
KEYWDS   3 ALTERNATIVE SPLICING, CELL DIVISION, PHOSPHOPROTEIN, TPR             
KEYWDS   4 REPEAT, UBL CONJUGATION PATHWAY, COILED COIL, NUCLEUS,               
KEYWDS   5 LIGASE                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.WANG,B.T.DYE,K.R.RAJASHANKAR,I.KURINOV,B.A.SCHULMAN                 
REVDAT   2   15-SEP-09 3HYM    1       JRNL                                     
REVDAT   1   11-AUG-09 3HYM    0                                                
JRNL        AUTH   J.WANG,B.T.DYE,K.R.RAJASHANKAR,I.KURINOV,                    
JRNL        AUTH 2 B.A.SCHULMAN                                                 
JRNL        TITL   INSIGHTS INTO ANAPHASE PROMOTING COMPLEX TPR                 
JRNL        TITL 2 SUBDOMAIN ASSEMBLY FROM A CDC26-APC6 STRUCTURE.              
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16   987 2009              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19668213                                                     
JRNL        DOI    10.1038/NSMB.1645                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.40                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.020                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 197777                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.920                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9730                            
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 49.4172 -  7.5929    0.98     9507   496  0.1524 0.1677        
REMARK   3     2  7.5929 -  6.0301    0.98     9562   487  0.1804 0.1959        
REMARK   3     3  6.0301 -  5.2689    0.98     9585   489  0.2064 0.2206        
REMARK   3     4  5.2689 -  4.7876    0.98     9541   492  0.1612 0.1969        
REMARK   3     5  4.7876 -  4.4447    0.98     9471   489  0.1411 0.1761        
REMARK   3     6  4.4447 -  4.1828    0.98     9608   490  0.1469 0.1732        
REMARK   3     7  4.1828 -  3.9734    0.98     9538   482  0.1551 0.1914        
REMARK   3     8  3.9734 -  3.8005    0.98     9571   488  0.1665 0.1762        
REMARK   3     9  3.8005 -  3.6542    0.98     9595   486  0.1771 0.2194        
REMARK   3    10  3.6542 -  3.5282    0.98     9571   491  0.1949 0.2239        
REMARK   3    11  3.5282 -  3.4179    0.98     9518   483  0.1958 0.2201        
REMARK   3    12  3.4179 -  3.3202    0.98     9476   479  0.2135 0.2490        
REMARK   3    13  3.3202 -  3.2328    0.98     9522   482  0.2216 0.2702        
REMARK   3    14  3.2328 -  3.1539    0.98     9481   486  0.2306 0.2917        
REMARK   3    15  3.1539 -  3.0823    0.98     9282   476  0.2433 0.2934        
REMARK   3    16  3.0823 -  3.0167    0.98     9405   485  0.2474 0.2831        
REMARK   3    17  3.0167 -  2.9563    0.98     9242   464  0.2552 0.3219        
REMARK   3    18  2.9563 -  2.9005    0.98     9197   470  0.2632 0.3263        
REMARK   3    19  2.9005 -  2.8488    0.98     9048   456  0.2742 0.3339        
REMARK   3    20  2.8488 -  2.8005    0.98     8446   440  0.2859 0.3209        
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              : 0.33                                          
REMARK   3   B_SOL              : 60.28                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 65.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 229:421)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -87.4690-102.3084 -23.5773              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0876 T22:  -0.2353                                     
REMARK   3      T33:  -0.1428 T12:   0.2521                                     
REMARK   3      T13:  -0.0139 T23:   0.1956                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0288 L22:   0.1036                                     
REMARK   3      L33:   0.0349 L12:  -0.0612                                     
REMARK   3      L13:  -0.0225 L23:  -0.0154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0903 S12:   0.0644 S13:   0.1133                       
REMARK   3      S21:   0.0922 S22:   0.1511 S23:   0.0903                       
REMARK   3      S31:  -0.0715 S32:  -0.0426 S33:  -0.0458                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 422:529)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -76.2797-119.7765  -1.9350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0634 T22:   0.1374                                     
REMARK   3      T33:  -0.1383 T12:   0.1499                                     
REMARK   3      T13:   0.3281 T23:   0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0516 L22:  -0.0085                                     
REMARK   3      L33:   0.0342 L12:  -0.0162                                     
REMARK   3      L13:  -0.0531 L23:   0.0232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0462 S12:   0.0133 S13:   0.0396                       
REMARK   3      S21:   0.0147 S22:   0.0035 S23:  -0.0702                       
REMARK   3      S31:  -0.0734 S32:   0.1092 S33:  -0.0471                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN D AND RESID 229:421)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -87.4402 -73.2947  -6.5783              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0529 T22:  -0.2720                                     
REMARK   3      T33:   0.2133 T12:   0.3252                                     
REMARK   3      T13:  -0.1165 T23:   0.3583                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0431 L22:  -0.1459                                     
REMARK   3      L33:   0.0259 L12:   0.0283                                     
REMARK   3      L13:   0.0086 L23:   0.0504                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1846 S12:   0.0081 S13:   0.0624                       
REMARK   3      S21:   0.0215 S22:  -0.0838 S23:   0.0296                       
REMARK   3      S31:   0.1767 S32:   0.1346 S33:  -0.3348                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D AND RESID 422:529)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -75.4882 -56.2151 -28.1260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1922 T22:   0.3108                                     
REMARK   3      T33:   0.4714 T12:  -0.0908                                     
REMARK   3      T13:  -0.3857 T23:   0.4918                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1952 L22:   0.0093                                     
REMARK   3      L33:   0.2326 L12:  -0.0194                                     
REMARK   3      L13:   0.2234 L23:  -0.0300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0026 S12:   0.1272 S13:   0.0002                       
REMARK   3      S21:   0.0566 S22:  -0.0905 S23:  -0.0318                       
REMARK   3      S31:  -0.0487 S32:   0.2877 S33:   0.1274                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN F AND RESID 229:421)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -43.5320-128.5834  -7.9323              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1134 T22:   0.2304                                     
REMARK   3      T33:  -0.1870 T12:  -0.0236                                     
REMARK   3      T13:  -0.1229 T23:  -0.1443                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1858 L22:   0.2239                                     
REMARK   3      L33:   0.2545 L12:   0.1572                                     
REMARK   3      L13:   0.1223 L23:   0.2723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0693 S12:   0.0973 S13:  -0.0760                       
REMARK   3      S21:   0.1609 S22:   0.0778 S23:  -0.0782                       
REMARK   3      S31:   0.0853 S32:   0.0177 S33:   0.2126                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN F AND RESID 422:529)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -62.8019-125.3845 -30.8117              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0154 T22:   0.1600                                     
REMARK   3      T33:  -0.3400 T12:   0.0219                                     
REMARK   3      T13:   0.0537 T23:  -0.1029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0614 L22:   0.0386                                     
REMARK   3      L33:   0.4636 L12:  -0.0151                                     
REMARK   3      L13:   0.0294 L23:   0.0690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0435 S12:   0.1274 S13:  -0.0396                       
REMARK   3      S21:   0.0056 S22:   0.1013 S23:  -0.0329                       
REMARK   3      S31:  -0.1234 S32:   0.1939 S33:   0.3404                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN H AND RESID 229:421)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -16.7355-113.2311 -22.0816              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3529 T22:   0.3043                                     
REMARK   3      T33:   0.2110 T12:  -0.0931                                     
REMARK   3      T13:  -0.4264 T23:  -0.2706                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0098 L22:  -0.0362                                     
REMARK   3      L33:   0.0474 L12:   0.0036                                     
REMARK   3      L13:   0.0325 L23:  -0.0303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0739 S12:  -0.0266 S13:  -0.0992                       
REMARK   3      S21:   0.0425 S22:  -0.0204 S23:  -0.1359                       
REMARK   3      S31:   0.0300 S32:  -0.2071 S33:  -0.1715                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN H AND RESID 422:529)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3520 -95.5626   1.1380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3018 T22:   0.0119                                     
REMARK   3      T33:   0.2962 T12:   0.3170                                     
REMARK   3      T13:  -0.5683 T23:  -0.1287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0311 L22:   0.0095                                     
REMARK   3      L33:   0.0240 L12:  -0.0152                                     
REMARK   3      L13:   0.0036 L23:  -0.0304                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1205 S12:   0.0091 S13:  -0.0026                       
REMARK   3      S21:   0.1251 S22:   0.0193 S23:  -0.1334                       
REMARK   3      S31:  -0.2089 S32:  -0.0768 S33:   0.0219                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN J AND RESID 229:421)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -17.2208 -62.1656  -5.6335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0346 T22:   0.0807                                     
REMARK   3      T33:  -0.0560 T12:   0.4941                                     
REMARK   3      T13:  -0.4075 T23:  -0.0281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0852 L22:   0.4091                                     
REMARK   3      L33:   0.2583 L12:   0.0546                                     
REMARK   3      L13:   0.0124 L23:   0.0815                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1576 S12:   0.1224 S13:  -0.0822                       
REMARK   3      S21:   0.3650 S22:   0.2866 S23:  -0.3273                       
REMARK   3      S31:   0.1206 S32:   0.1057 S33:   0.7882                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN J AND RESID 422:529)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5327 -79.9247 -28.3425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2067 T22:   0.3173                                     
REMARK   3      T33:   0.6029 T12:  -0.1793                                     
REMARK   3      T13:  -0.0460 T23:  -0.4591                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0189 L22:   0.1126                                     
REMARK   3      L33:   0.2256 L12:   0.0618                                     
REMARK   3      L13:   0.1109 L23:   0.0565                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0160 S12:  -0.0546 S13:   0.1381                       
REMARK   3      S21:  -0.0350 S22:   0.3384 S23:  -0.2674                       
REMARK   3      S31:   0.0813 S32:   0.0328 S33:   0.1014                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 229:421)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -43.1883 -47.3509 -21.1080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2222 T22:   0.2340                                     
REMARK   3      T33:   0.1641 T12:   0.3186                                     
REMARK   3      T13:  -0.0931 T23:   0.4383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3069 L22:   0.3273                                     
REMARK   3      L33:   0.1429 L12:   0.0476                                     
REMARK   3      L13:  -0.1021 L23:  -0.0184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0953 S12:   0.1458 S13:   0.0863                       
REMARK   3      S21:   0.1293 S22:   0.4893 S23:   0.3263                       
REMARK   3      S31:   0.0132 S32:  -0.1766 S33:   0.3291                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 422:529)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -62.9398 -50.1951   1.7209              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1198 T22:   0.0700                                     
REMARK   3      T33:   0.3500 T12:   0.3907                                     
REMARK   3      T13:   0.0855 T23:   0.1161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0739 L22:   0.1373                                     
REMARK   3      L33:   0.1087 L12:  -0.0465                                     
REMARK   3      L13:  -0.0127 L23:  -0.0721                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1803 S12:   0.1361 S13:   0.1856                       
REMARK   3      S21:   0.0382 S22:   0.0297 S23:  -0.0132                       
REMARK   3      S31:  -0.0701 S32:  -0.1389 S33:   0.2404                       
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 B and (resseq 229:347 or resseq       
REMARK   3                          350:422 or resseq 444:528)                  
REMARK   3     SELECTION          : chain D and (resseq 229:347 or resseq       
REMARK   3                          350:422 or resseq 444:528)                  
REMARK   3     ATOM PAIRS NUMBER  : 2166                                        
REMARK   3     RMSD               : 0.461                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 229:347 or resseq       
REMARK   3                          350:422 or resseq 444:528)                  
REMARK   3     SELECTION          : chain F and (resseq 229:347 or resseq       
REMARK   3                          350:422 or resseq 444:528)                  
REMARK   3     ATOM PAIRS NUMBER  : 2175                                        
REMARK   3     RMSD               : 0.626                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 229:347 or resseq       
REMARK   3                          350:422 or resseq 444:528)                  
REMARK   3     SELECTION          : chain H and (resseq 229:347 or resseq       
REMARK   3                          350:422 or resseq 444:528)                  
REMARK   3     ATOM PAIRS NUMBER  : 2162                                        
REMARK   3     RMSD               : 0.597                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 229:347 or resseq       
REMARK   3                          350:422 or resseq 444:528)                  
REMARK   3     SELECTION          : chain J and (resseq 229:347 or resseq       
REMARK   3                          350:422 or resseq 444:528)                  
REMARK   3     ATOM PAIRS NUMBER  : 2171                                        
REMARK   3     RMSD               : 0.613                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 229:347 or resseq       
REMARK   3                          350:422 or resseq 444:528)                  
REMARK   3     SELECTION          : chain L and (resseq 229:347 or resseq       
REMARK   3                          350:422 or resseq 444:528)                  
REMARK   3     ATOM PAIRS NUMBER  : 2153                                        
REMARK   3     RMSD               : 0.609                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A                                     
REMARK   3     SELECTION          : chain C                                     
REMARK   3     ATOM PAIRS NUMBER  : 199                                         
REMARK   3     RMSD               : 0.568                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: chain A                                     
REMARK   3     SELECTION          : chain E                                     
REMARK   3     ATOM PAIRS NUMBER  : 203                                         
REMARK   3     RMSD               : 0.538                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: chain A                                     
REMARK   3     SELECTION          : chain G                                     
REMARK   3     ATOM PAIRS NUMBER  : 204                                         
REMARK   3     RMSD               : 0.750                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: chain A                                     
REMARK   3     SELECTION          : chain I                                     
REMARK   3     ATOM PAIRS NUMBER  : 203                                         
REMARK   3     RMSD               : 0.601                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: chain A                                     
REMARK   3     SELECTION          : chain K                                     
REMARK   3     ATOM PAIRS NUMBER  : 183                                         
REMARK   3     RMSD               : 0.557                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  TWIN OPERATOR: K, H, -L                                             
REMARK   3  TWIN FRACTION: 0.44                                                 
REMARK   4                                                                      
REMARK   4 3HYM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053742.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97926                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 197947                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.600                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.12700                            
REMARK 200  R SYM                      (I) : 0.12700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.47500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXS                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 MIX WITH WELL BUFFER:  0.2M          
REMARK 280  MGCL2, 7% ISOPROPANOL, 0.1 M TRIS-CL PH 8.4, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 297K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.08400            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       40.08400            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       40.08400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10                           
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: 3400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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: 3360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 3320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 4                                                       
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: 3370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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: 5                                                       
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: 3410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
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: 6                                                       
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: 3380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
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: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
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: 8                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, K, L                            
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: 9                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J                            
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: 10                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 31960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 79910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -184.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L                               
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     GLU A    27                                                      
REMARK 465     THR A    28                                                      
REMARK 465     ARG A    29                                                      
REMARK 465     GLY B   210                                                      
REMARK 465     SER B   211                                                      
REMARK 465     TYR B   212                                                      
REMARK 465     ASN B   213                                                      
REMARK 465     LYS B   214                                                      
REMARK 465     PRO B   215                                                      
REMARK 465     SER B   216                                                      
REMARK 465     GLU B   217                                                      
REMARK 465     THR B   218                                                      
REMARK 465     VAL B   219                                                      
REMARK 465     ILE B   220                                                      
REMARK 465     PRO B   221                                                      
REMARK 465     GLU B   222                                                      
REMARK 465     SER B   223                                                      
REMARK 465     VAL B   224                                                      
REMARK 465     ASP B   225                                                      
REMARK 465     GLY B   226                                                      
REMARK 465     LEU B   227                                                      
REMARK 465     GLN B   228                                                      
REMARK 465     SER B   530                                                      
REMARK 465     GLU B   531                                                      
REMARK 465     ALA B   532                                                      
REMARK 465     TYR B   533                                                      
REMARK 465     ILE B   534                                                      
REMARK 465     GLY B   535                                                      
REMARK 465     ALA B   536                                                      
REMARK 465     ASP B   537                                                      
REMARK 465     ILE B   538                                                      
REMARK 465     LYS B   539                                                      
REMARK 465     LYS C    24                                                      
REMARK 465     ASP C    25                                                      
REMARK 465     LEU C    26                                                      
REMARK 465     GLU C    27                                                      
REMARK 465     THR C    28                                                      
REMARK 465     ARG C    29                                                      
REMARK 465     GLY D   210                                                      
REMARK 465     SER D   211                                                      
REMARK 465     TYR D   212                                                      
REMARK 465     ASN D   213                                                      
REMARK 465     LYS D   214                                                      
REMARK 465     PRO D   215                                                      
REMARK 465     SER D   216                                                      
REMARK 465     GLU D   217                                                      
REMARK 465     THR D   218                                                      
REMARK 465     VAL D   219                                                      
REMARK 465     ILE D   220                                                      
REMARK 465     PRO D   221                                                      
REMARK 465     GLU D   222                                                      
REMARK 465     SER D   223                                                      
REMARK 465     VAL D   224                                                      
REMARK 465     ASP D   225                                                      
REMARK 465     GLY D   226                                                      
REMARK 465     LEU D   227                                                      
REMARK 465     GLN D   228                                                      
REMARK 465     SER D   530                                                      
REMARK 465     GLU D   531                                                      
REMARK 465     ALA D   532                                                      
REMARK 465     TYR D   533                                                      
REMARK 465     ILE D   534                                                      
REMARK 465     GLY D   535                                                      
REMARK 465     ALA D   536                                                      
REMARK 465     ASP D   537                                                      
REMARK 465     ILE D   538                                                      
REMARK 465     LYS D   539                                                      
REMARK 465     GLU E    27                                                      
REMARK 465     THR E    28                                                      
REMARK 465     ARG E    29                                                      
REMARK 465     GLY F   210                                                      
REMARK 465     SER F   211                                                      
REMARK 465     TYR F   212                                                      
REMARK 465     ASN F   213                                                      
REMARK 465     LYS F   214                                                      
REMARK 465     PRO F   215                                                      
REMARK 465     SER F   216                                                      
REMARK 465     GLU F   217                                                      
REMARK 465     THR F   218                                                      
REMARK 465     VAL F   219                                                      
REMARK 465     ILE F   220                                                      
REMARK 465     PRO F   221                                                      
REMARK 465     GLU F   222                                                      
REMARK 465     SER F   223                                                      
REMARK 465     VAL F   224                                                      
REMARK 465     ASP F   225                                                      
REMARK 465     GLY F   226                                                      
REMARK 465     LEU F   227                                                      
REMARK 465     GLN F   228                                                      
REMARK 465     SER F   530                                                      
REMARK 465     GLU F   531                                                      
REMARK 465     ALA F   532                                                      
REMARK 465     TYR F   533                                                      
REMARK 465     ILE F   534                                                      
REMARK 465     GLY F   535                                                      
REMARK 465     ALA F   536                                                      
REMARK 465     ASP F   537                                                      
REMARK 465     ILE F   538                                                      
REMARK 465     LYS F   539                                                      
REMARK 465     LEU G    26                                                      
REMARK 465     GLU G    27                                                      
REMARK 465     THR G    28                                                      
REMARK 465     ARG G    29                                                      
REMARK 465     GLY H   210                                                      
REMARK 465     SER H   211                                                      
REMARK 465     TYR H   212                                                      
REMARK 465     ASN H   213                                                      
REMARK 465     LYS H   214                                                      
REMARK 465     PRO H   215                                                      
REMARK 465     SER H   216                                                      
REMARK 465     GLU H   217                                                      
REMARK 465     THR H   218                                                      
REMARK 465     VAL H   219                                                      
REMARK 465     ILE H   220                                                      
REMARK 465     PRO H   221                                                      
REMARK 465     GLU H   222                                                      
REMARK 465     SER H   223                                                      
REMARK 465     VAL H   224                                                      
REMARK 465     ASP H   225                                                      
REMARK 465     GLY H   226                                                      
REMARK 465     LEU H   227                                                      
REMARK 465     SER H   530                                                      
REMARK 465     GLU H   531                                                      
REMARK 465     ALA H   532                                                      
REMARK 465     TYR H   533                                                      
REMARK 465     ILE H   534                                                      
REMARK 465     GLY H   535                                                      
REMARK 465     ALA H   536                                                      
REMARK 465     ASP H   537                                                      
REMARK 465     ILE H   538                                                      
REMARK 465     LYS H   539                                                      
REMARK 465     GLU I    27                                                      
REMARK 465     THR I    28                                                      
REMARK 465     ARG I    29                                                      
REMARK 465     GLY J   210                                                      
REMARK 465     SER J   211                                                      
REMARK 465     TYR J   212                                                      
REMARK 465     ASN J   213                                                      
REMARK 465     LYS J   214                                                      
REMARK 465     PRO J   215                                                      
REMARK 465     SER J   216                                                      
REMARK 465     GLU J   217                                                      
REMARK 465     THR J   218                                                      
REMARK 465     VAL J   219                                                      
REMARK 465     ILE J   220                                                      
REMARK 465     PRO J   221                                                      
REMARK 465     GLU J   222                                                      
REMARK 465     SER J   223                                                      
REMARK 465     VAL J   224                                                      
REMARK 465     ASP J   225                                                      
REMARK 465     GLY J   226                                                      
REMARK 465     LEU J   227                                                      
REMARK 465     GLN J   228                                                      
REMARK 465     SER J   530                                                      
REMARK 465     GLU J   531                                                      
REMARK 465     ALA J   532                                                      
REMARK 465     TYR J   533                                                      
REMARK 465     ILE J   534                                                      
REMARK 465     GLY J   535                                                      
REMARK 465     ALA J   536                                                      
REMARK 465     ASP J   537                                                      
REMARK 465     ILE J   538                                                      
REMARK 465     LYS J   539                                                      
REMARK 465     LYS K    24                                                      
REMARK 465     ASP K    25                                                      
REMARK 465     LEU K    26                                                      
REMARK 465     GLU K    27                                                      
REMARK 465     THR K    28                                                      
REMARK 465     ARG K    29                                                      
REMARK 465     GLY L   210                                                      
REMARK 465     SER L   211                                                      
REMARK 465     TYR L   212                                                      
REMARK 465     ASN L   213                                                      
REMARK 465     LYS L   214                                                      
REMARK 465     PRO L   215                                                      
REMARK 465     SER L   216                                                      
REMARK 465     GLU L   217                                                      
REMARK 465     THR L   218                                                      
REMARK 465     VAL L   219                                                      
REMARK 465     ILE L   220                                                      
REMARK 465     PRO L   221                                                      
REMARK 465     GLU L   222                                                      
REMARK 465     SER L   223                                                      
REMARK 465     VAL L   224                                                      
REMARK 465     ASP L   225                                                      
REMARK 465     GLY L   226                                                      
REMARK 465     LEU L   227                                                      
REMARK 465     GLN L   228                                                      
REMARK 465     VAL L   439                                                      
REMARK 465     THR L   440                                                      
REMARK 465     SER L   530                                                      
REMARK 465     GLU L   531                                                      
REMARK 465     ALA L   532                                                      
REMARK 465     TYR L   533                                                      
REMARK 465     ILE L   534                                                      
REMARK 465     GLY L   535                                                      
REMARK 465     ALA L   536                                                      
REMARK 465     ASP L   537                                                      
REMARK 465     ILE L   538                                                      
REMARK 465     LYS L   539                                                      
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     GLU A  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  24    CG   CD   CE   NZ                                   
REMARK 470     ASP A  25    CG   OD1  OD2                                       
REMARK 470     LEU A  26    CG   CD1  CD2                                       
REMARK 470     GLU B 229    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 240    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 315    CG   CD   CE   NZ                                   
REMARK 470     LYS B 325    CG   CD   CE   NZ                                   
REMARK 470     LYS B 419    CG   CD   CE   NZ                                   
REMARK 470     LYS B 431    CG   CD   CE   NZ                                   
REMARK 470     ILE B 432    CG1  CG2  CD1                                       
REMARK 470     LYS B 433    CG   CD   CE   NZ                                   
REMARK 470     ILE B 435    CG1  CG2  CD1                                       
REMARK 470     ASN B 437    CG   OD1  ND2                                       
REMARK 470     GLU B 438    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 439    CG1  CG2                                            
REMARK 470     THR B 440    OG1  CG2                                            
REMARK 470     VAL B 441    CG1  CG2                                            
REMARK 470     ASP B 442    CG   OD1  OD2                                       
REMARK 470     LYS B 443    CG   CD   CE   NZ                                   
REMARK 470     ARG B 509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 510    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  17    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 229    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 240    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 290    CG   CD   CE   NZ                                   
REMARK 470     LYS D 315    CG   CD   CE   NZ                                   
REMARK 470     LYS D 431    CG   CD   CE   NZ                                   
REMARK 470     ILE D 432    CG1  CG2  CD1                                       
REMARK 470     LYS D 433    CG   CD   CE   NZ                                   
REMARK 470     ILE D 435    CG1  CG2  CD1                                       
REMARK 470     ASN D 437    CG   OD1  ND2                                       
REMARK 470     GLU D 438    CG   CD   OE1  OE2                                  
REMARK 470     VAL D 439    CG1  CG2                                            
REMARK 470     THR D 440    OG1  CG2                                            
REMARK 470     VAL D 441    CG1  CG2                                            
REMARK 470     ASP D 442    CG   OD1  OD2                                       
REMARK 470     LYS D 443    CG   CD   CE   NZ                                   
REMARK 470     ARG D 509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 510    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E  17    CG   CD   OE1  OE2                                  
REMARK 470     ARG E  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E  24    CG   CD   CE   NZ                                   
REMARK 470     ASP E  25    CG   OD1  OD2                                       
REMARK 470     LEU E  26    CG   CD1  CD2                                       
REMARK 470     GLU F 229    CG   CD   OE1  OE2                                  
REMARK 470     ARG F 240    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 315    CG   CD   CE   NZ                                   
REMARK 470     LYS F 325    CG   CD   CE   NZ                                   
REMARK 470     LYS F 419    CG   CD   CE   NZ                                   
REMARK 470     LYS F 431    CG   CD   CE   NZ                                   
REMARK 470     ILE F 432    CG1  CG2  CD1                                       
REMARK 470     LYS F 433    CG   CD   CE   NZ                                   
REMARK 470     ILE F 435    CG1  CG2  CD1                                       
REMARK 470     ASN F 437    CG   OD1  ND2                                       
REMARK 470     GLU F 438    CG   CD   OE1  OE2                                  
REMARK 470     VAL F 439    CG1  CG2                                            
REMARK 470     THR F 440    OG1  CG2                                            
REMARK 470     VAL F 441    CG1  CG2                                            
REMARK 470     ASP F 442    CG   OD1  OD2                                       
REMARK 470     LYS F 443    CG   CD   CE   NZ                                   
REMARK 470     LYS G  24    CG   CD   CE   NZ                                   
REMARK 470     ASP G  25    CG   OD1  OD2                                       
REMARK 470     GLN H 228    CG   CD   OE1  NE2                                  
REMARK 470     ARG H 240    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 260    CG   CD   CE   NZ                                   
REMARK 470     LYS H 290    CG   CD   CE   NZ                                   
REMARK 470     LYS H 315    CG   CD   CE   NZ                                   
REMARK 470     LYS H 325    CG   CD   CE   NZ                                   
REMARK 470     LYS H 419    CG   CD   CE   NZ                                   
REMARK 470     LYS H 431    CG   CD   CE   NZ                                   
REMARK 470     ILE H 432    CG1  CG2  CD1                                       
REMARK 470     LYS H 433    CG   CD   CE   NZ                                   
REMARK 470     ILE H 435    CG1  CG2  CD1                                       
REMARK 470     ASN H 437    CG   OD1  ND2                                       
REMARK 470     GLU H 438    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 439    CG1  CG2                                            
REMARK 470     THR H 440    OG1  CG2                                            
REMARK 470     VAL H 441    CG1  CG2                                            
REMARK 470     ASP H 442    CG   OD1  OD2                                       
REMARK 470     LYS H 443    CG   CD   CE   NZ                                   
REMARK 470     ARG H 509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H 510    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU I  17    CG   CD   OE1  OE2                                  
REMARK 470     ARG I  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS I  24    CG   CD   CE   NZ                                   
REMARK 470     ASP I  25    CG   OD1  OD2                                       
REMARK 470     LEU I  26    CG   CD1  CD2                                       
REMARK 470     GLU J 229    CG   CD   OE1  OE2                                  
REMARK 470     ARG J 240    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS J 290    CG   CD   CE   NZ                                   
REMARK 470     LYS J 315    CG   CD   CE   NZ                                   
REMARK 470     LYS J 325    CG   CD   CE   NZ                                   
REMARK 470     LYS J 419    CG   CD   CE   NZ                                   
REMARK 470     LYS J 431    CG   CD   CE   NZ                                   
REMARK 470     ILE J 432    CG1  CG2  CD1                                       
REMARK 470     LYS J 433    CG   CD   CE   NZ                                   
REMARK 470     ILE J 435    CG1  CG2  CD1                                       
REMARK 470     ASN J 437    CG   OD1  ND2                                       
REMARK 470     GLU J 438    CG   CD   OE1  OE2                                  
REMARK 470     VAL J 439    CG1  CG2                                            
REMARK 470     THR J 440    OG1  CG2                                            
REMARK 470     VAL J 441    CG1  CG2                                            
REMARK 470     ASP J 442    CG   OD1  OD2                                       
REMARK 470     LYS J 443    CG   CD   CE   NZ                                   
REMARK 470     ARG J 509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG K  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU L 229    CG   CD   OE1  OE2                                  
REMARK 470     ARG L 240    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS L 290    CG   CD   CE   NZ                                   
REMARK 470     LYS L 315    CG   CD   CE   NZ                                   
REMARK 470     LYS L 325    CG   CD   CE   NZ                                   
REMARK 470     LYS L 419    CG   CD   CE   NZ                                   
REMARK 470     LYS L 423    CG   CD   CE   NZ                                   
REMARK 470     LYS L 431    CG   CD   CE   NZ                                   
REMARK 470     ILE L 432    CG1  CG2  CD1                                       
REMARK 470     ILE L 435    CG1  CG2  CD1                                       
REMARK 470     ASN L 437    CG   OD1  ND2                                       
REMARK 470     GLU L 438    CG   CD   OE1  OE2                                  
REMARK 470     VAL L 441    CG1  CG2                                            
REMARK 470     ASP L 442    CG   OD1  OD2                                       
REMARK 470     LYS L 443    CG   CD   CE   NZ                                   
REMARK 470     GLU L 445    CG   CD   OE1  OE2                                  
REMARK 470     ARG L 509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU L 524    CG   CD   OE1  OE2                                  
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    LYS A   5      129.31    -37.30                                   
REMARK 500    ASP A  25      -77.15    -68.59                                   
REMARK 500    LYS B 260      -85.50    -86.48                                   
REMARK 500    TYR B 295       51.19   -150.27                                   
REMARK 500    PRO B 296       32.80    -78.89                                   
REMARK 500    HIS B 314       33.88    -85.50                                   
REMARK 500    LYS B 315       49.41    -68.21                                   
REMARK 500    THR B 328       39.95    -79.22                                   
REMARK 500    LEU B 329      -16.40   -153.68                                   
REMARK 500    GLU B 330       83.43   -173.15                                   
REMARK 500    SER B 348       -0.21     86.31                                   
REMARK 500    ASN B 382       13.90     85.93                                   
REMARK 500    ASN B 383       51.75    -90.20                                   
REMARK 500    SER B 396       38.79    -90.10                                   
REMARK 500    ILE B 397      -66.65   -146.65                                   
REMARK 500    ALA B 398       78.68   -112.22                                   
REMARK 500    LYS B 433     -115.07    -67.56                                   
REMARK 500    ILE B 435      -95.20    -64.57                                   
REMARK 500    GLU B 438       13.24    179.94                                   
REMARK 500    THR B 440        8.27    -64.29                                   
REMARK 500    LYS B 443       26.05     49.98                                   
REMARK 500    GLU B 445      -29.50   -178.58                                   
REMARK 500    PRO B 446      -82.67    -42.61                                   
REMARK 500    LEU B 447      -65.97      2.39                                   
REMARK 500    LYS B 459       15.02     55.62                                   
REMARK 500    LYS B 460       41.28    -82.78                                   
REMARK 500    PRO B 476       26.40    -73.94                                   
REMARK 500    GLN B 477       15.66   -146.69                                   
REMARK 500    THR B 504       22.83    -70.14                                   
REMARK 500    LEU B 508      -65.72    -96.49                                   
REMARK 500    THR C   7      111.40    -36.12                                   
REMARK 500    ASP C  14        7.73    -67.28                                   
REMARK 500    CYS D 245       27.29     80.10                                   
REMARK 500    ASP D 246       64.89   -103.43                                   
REMARK 500    LYS D 260      -85.41    -88.45                                   
REMARK 500    PHE D 263       26.50    -69.77                                   
REMARK 500    TYR D 295       44.96   -156.88                                   
REMARK 500    HIS D 314       27.43    -67.03                                   
REMARK 500    LYS D 315       42.09    -73.83                                   
REMARK 500    SER D 348       13.20     81.61                                   
REMARK 500    ASN D 382       11.54     80.10                                   
REMARK 500    ILE D 397      -69.93    -91.08                                   
REMARK 500    ALA D 398       79.75   -104.20                                   
REMARK 500    ASN D 415        2.99    -69.95                                   
REMARK 500    GLU D 430      -71.28    -54.72                                   
REMARK 500    ALA D 434     -146.88    -76.75                                   
REMARK 500    ILE D 435      141.22    -36.25                                   
REMARK 500    GLU D 438     -159.82   -134.23                                   
REMARK 500    VAL D 441       27.24   -176.30                                   
REMARK 500    LYS D 443       -5.38     62.21                                   
REMARK 500    GLU D 445       -9.21    175.75                                   
REMARK 500    ALA D 464      -72.53    -60.78                                   
REMARK 500    VAL D 473      -43.82    -28.47                                   
REMARK 500    HIS D 503      -70.06    -61.25                                   
REMARK 500    LEU D 508      -77.75    -99.14                                   
REMARK 500    ASP E  25      -81.19    -58.80                                   
REMARK 500    PHE F 263       15.05    -67.80                                   
REMARK 500    HIS F 264       94.59    -53.56                                   
REMARK 500    LYS F 280       57.54    -67.08                                   
REMARK 500    ASN F 282      -70.80    -71.10                                   
REMARK 500    TYR F 295       46.08   -156.24                                   
REMARK 500    PRO F 296       39.43    -70.96                                   
REMARK 500    HIS F 314       31.85    -70.52                                   
REMARK 500    LYS F 315       36.54    -77.50                                   
REMARK 500    THR F 328       41.84    -83.11                                   
REMARK 500    LEU F 329      -40.47   -135.58                                   
REMARK 500    SER F 348      -34.97     93.79                                   
REMARK 500    GLU F 349      103.01    -47.16                                   
REMARK 500    ASN F 383       45.72    -89.35                                   
REMARK 500    SER F 396       44.17    -78.07                                   
REMARK 500    ILE F 397      -42.29   -150.31                                   
REMARK 500    GLU F 430      -73.82    -51.78                                   
REMARK 500    LYS F 431      -70.32    -45.59                                   
REMARK 500    ILE F 432      -14.59    -49.62                                   
REMARK 500    GLU F 438        4.76   -154.41                                   
REMARK 500    VAL F 439       45.49     80.27                                   
REMARK 500    THR F 440       -4.54    -58.88                                   
REMARK 500    VAL F 441        4.20    -61.69                                   
REMARK 500    ASP F 442       96.15    -51.95                                   
REMARK 500    GLU F 445      -36.74   -170.20                                   
REMARK 500    LYS F 460       31.95    -74.93                                   
REMARK 500    TYR F 461      -45.21    -27.83                                   
REMARK 500    LEU F 508      -90.03   -121.70                                   
REMARK 500    ASP F 511       51.31    -92.46                                   
REMARK 500    ARG G  23      -72.55    -68.60                                   
REMARK 500    GLU H 229       99.68   -166.11                                   
REMARK 500    CYS H 245       36.99     72.87                                   
REMARK 500    PHE H 263       30.35    -71.11                                   
REMARK 500    LYS H 280       61.23    -68.52                                   
REMARK 500    ASN H 282      -72.75    -57.61                                   
REMARK 500    TYR H 295       57.92   -166.92                                   
REMARK 500    PRO H 296       31.79    -78.73                                   
REMARK 500    HIS H 314       27.77    -64.26                                   
REMARK 500    LYS H 315       45.88    -75.43                                   
REMARK 500    GLU H 330       95.31   -162.93                                   
REMARK 500    LEU H 380       20.91    -79.30                                   
REMARK 500    SER H 396       37.71    -80.61                                   
REMARK 500    ILE H 397      -63.89   -144.48                                   
REMARK 500    GLU H 430       46.77    -81.24                                   
REMARK 500    LYS H 431      -42.57   -158.30                                   
REMARK 500    ILE H 435      -27.83   -159.92                                   
REMARK 500    ASP H 442       20.29     41.88                                   
REMARK 500    TRP H 444     -158.06    -54.75                                   
REMARK 500    GLU H 445      -12.47   -172.38                                   
REMARK 500    LEU H 447      -55.51    -25.18                                   
REMARK 500    LYS H 459       -0.99     70.11                                   
REMARK 500    LYS H 460       36.70    -64.47                                   
REMARK 500    TYR H 461      -39.94    -29.90                                   
REMARK 500    LEU H 508      -65.67   -145.29                                   
REMARK 500    ASP H 511       45.65    -86.83                                   
REMARK 500    PHE J 263       30.21    -70.19                                   
REMARK 500    TYR J 295       59.76   -140.87                                   
REMARK 500    PRO J 296       31.14    -76.64                                   
REMARK 500    PRO J 299        0.79    -58.90                                   
REMARK 500    HIS J 314       14.95     35.99                                   
REMARK 500    LYS J 315       45.26    -73.38                                   
REMARK 500    HIS J 342      -39.84    -39.10                                   
REMARK 500    ASN J 383       56.01    -91.66                                   
REMARK 500    ILE J 397      -71.23    -97.18                                   
REMARK 500    ALA J 398       78.96   -111.13                                   
REMARK 500    LYS J 431      -24.79    169.71                                   
REMARK 500    LYS J 433        7.26   -151.66                                   
REMARK 500    GLU J 438       62.83   -156.45                                   
REMARK 500    THR J 440       95.21    -49.73                                   
REMARK 500    VAL J 441      -16.24   -163.35                                   
REMARK 500    GLU J 445      -44.30    164.13                                   
REMARK 500    PRO J 446      -68.20    -28.42                                   
REMARK 500    LEU J 447      -66.94    -19.18                                   
REMARK 500    LYS J 459       -9.43     76.27                                   
REMARK 500    LYS J 460       78.88    -61.27                                   
REMARK 500    GLN J 477       34.45    -98.57                                   
REMARK 500    ASN J 494       41.10    -96.56                                   
REMARK 500    LEU J 508      -70.33   -146.35                                   
REMARK 500    GLU K  20      -70.28    -47.68                                   
REMARK 500    ASN K  21       20.01    -68.54                                   
REMARK 500    ASP L 246       78.22   -100.65                                   
REMARK 500    LYS L 260      -82.38    -76.34                                   
REMARK 500    PHE L 263       31.61    -72.20                                   
REMARK 500    LYS L 280       58.91    -64.43                                   
REMARK 500    LEU L 291      -18.15    -48.75                                   
REMARK 500    TYR L 295       48.81   -149.50                                   
REMARK 500    PRO L 296       20.29    -65.87                                   
REMARK 500    HIS L 314       33.73    -67.79                                   
REMARK 500    LYS L 315       46.09    -79.32                                   
REMARK 500    THR L 328       48.53    -74.16                                   
REMARK 500    LEU L 329      -46.93   -141.66                                   
REMARK 500    SER L 348       -0.64     82.97                                   
REMARK 500    THR L 381       14.71   -145.80                                   
REMARK 500    ASN L 382       11.88     80.67                                   
REMARK 500    SER L 396       -5.78    -55.69                                   
REMARK 500    ILE L 397      -69.43    -97.84                                   
REMARK 500    GLU L 400       51.73    -96.36                                   
REMARK 500    LYS L 423      -73.34    -52.73                                   
REMARK 500    GLU L 430       79.88    -68.08                                   
REMARK 500    LYS L 431      -38.56    162.76                                   
REMARK 500    ILE L 432     -102.81    -63.56                                   
REMARK 500    ILE L 435     -102.90    -77.59                                   
REMARK 500    GLU L 445      -36.94   -145.53                                   
REMARK 500    PRO L 446     -130.92    -61.64                                   
REMARK 500    LEU L 447      -77.25     45.75                                   
REMARK 500    LYS L 460       49.91    -74.84                                   
REMARK 500    GLN L 477       36.32    -96.15                                   
REMARK 500    LEU L 508      -74.03   -152.37                                   
REMARK 500    ASP L 512       87.00    -66.29                                   
REMARK 500    ILE L 527       82.78    -68.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3HYM A    1    29  UNP    Q8NHZ8   CDC26_HUMAN      1     29             
DBREF  3HYM B  212   539  UNP    Q13042   CDC16_HUMAN    212    539             
DBREF  3HYM C    1    29  UNP    Q8NHZ8   CDC26_HUMAN      1     29             
DBREF  3HYM D  212   539  UNP    Q13042   CDC16_HUMAN    212    539             
DBREF  3HYM E    1    29  UNP    Q8NHZ8   CDC26_HUMAN      1     29             
DBREF  3HYM F  212   539  UNP    Q13042   CDC16_HUMAN    212    539             
DBREF  3HYM G    1    29  UNP    Q8NHZ8   CDC26_HUMAN      1     29             
DBREF  3HYM H  212   539  UNP    Q13042   CDC16_HUMAN    212    539             
DBREF  3HYM I    1    29  UNP    Q8NHZ8   CDC26_HUMAN      1     29             
DBREF  3HYM J  212   539  UNP    Q13042   CDC16_HUMAN    212    539             
DBREF  3HYM K    1    29  UNP    Q8NHZ8   CDC26_HUMAN      1     29             
DBREF  3HYM L  212   539  UNP    Q13042   CDC16_HUMAN    212    539             
SEQADV 3HYM GLY B  210  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM SER B  211  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM GLY D  210  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM SER D  211  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM GLY F  210  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM SER F  211  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM GLY H  210  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM SER H  211  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM GLY J  210  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM SER J  211  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM GLY L  210  UNP  Q13042              EXPRESSION TAG                 
SEQADV 3HYM SER L  211  UNP  Q13042              EXPRESSION TAG                 
SEQRES   1 A   29  MSE LEU ARG ARG LYS PRO THR ARG LEU GLU LEU LYS LEU          
SEQRES   2 A   29  ASP ASP ILE GLU GLU PHE GLU ASN ILE ARG LYS ASP LEU          
SEQRES   3 A   29  GLU THR ARG                                                  
SEQRES   1 B  330  GLY SER TYR ASN LYS PRO SER GLU THR VAL ILE PRO GLU          
SEQRES   2 B  330  SER VAL ASP GLY LEU GLN GLU ASN LEU ASP VAL VAL VAL          
SEQRES   3 B  330  SER LEU ALA GLU ARG HIS TYR TYR ASN CYS ASP PHE LYS          
SEQRES   4 B  330  MSE CYS TYR LYS LEU THR SER VAL VAL MSE GLU LYS ASP          
SEQRES   5 B  330  PRO PHE HIS ALA SER CYS LEU PRO VAL HIS ILE GLY THR          
SEQRES   6 B  330  LEU VAL GLU LEU ASN LYS ALA ASN GLU LEU PHE TYR LEU          
SEQRES   7 B  330  SER HIS LYS LEU VAL ASP LEU TYR PRO SER ASN PRO VAL          
SEQRES   8 B  330  SER TRP PHE ALA VAL GLY CYS TYR TYR LEU MSE VAL GLY          
SEQRES   9 B  330  HIS LYS ASN GLU HIS ALA ARG ARG TYR LEU SER LYS ALA          
SEQRES  10 B  330  THR THR LEU GLU LYS THR TYR GLY PRO ALA TRP ILE ALA          
SEQRES  11 B  330  TYR GLY HIS SER PHE ALA VAL GLU SER GLU HIS ASP GLN          
SEQRES  12 B  330  ALA MSE ALA ALA TYR PHE THR ALA ALA GLN LEU MSE LYS          
SEQRES  13 B  330  GLY CYS HIS LEU PRO MSE LEU TYR ILE GLY LEU GLU TYR          
SEQRES  14 B  330  GLY LEU THR ASN ASN SER LYS LEU ALA GLU ARG PHE PHE          
SEQRES  15 B  330  SER GLN ALA LEU SER ILE ALA PRO GLU ASP PRO PHE VAL          
SEQRES  16 B  330  MSE HIS GLU VAL GLY VAL VAL ALA PHE GLN ASN GLY GLU          
SEQRES  17 B  330  TRP LYS THR ALA GLU LYS TRP PHE LEU ASP ALA LEU GLU          
SEQRES  18 B  330  LYS ILE LYS ALA ILE GLY ASN GLU VAL THR VAL ASP LYS          
SEQRES  19 B  330  TRP GLU PRO LEU LEU ASN ASN LEU GLY HIS VAL CYS ARG          
SEQRES  20 B  330  LYS LEU LYS LYS TYR ALA GLU ALA LEU ASP TYR HIS ARG          
SEQRES  21 B  330  GLN ALA LEU VAL LEU ILE PRO GLN ASN ALA SER THR TYR          
SEQRES  22 B  330  SER ALA ILE GLY TYR ILE HIS SER LEU MSE GLY ASN PHE          
SEQRES  23 B  330  GLU ASN ALA VAL ASP TYR PHE HIS THR ALA LEU GLY LEU          
SEQRES  24 B  330  ARG ARG ASP ASP THR PHE SER VAL THR MSE LEU GLY HIS          
SEQRES  25 B  330  CYS ILE GLU MSE TYR ILE GLY ASP SER GLU ALA TYR ILE          
SEQRES  26 B  330  GLY ALA ASP ILE LYS                                          
SEQRES   1 C   29  MSE LEU ARG ARG LYS PRO THR ARG LEU GLU LEU LYS LEU          
SEQRES   2 C   29  ASP ASP ILE GLU GLU PHE GLU ASN ILE ARG LYS ASP LEU          
SEQRES   3 C   29  GLU THR ARG                                                  
SEQRES   1 D  330  GLY SER TYR ASN LYS PRO SER GLU THR VAL ILE PRO GLU          
SEQRES   2 D  330  SER VAL ASP GLY LEU GLN GLU ASN LEU ASP VAL VAL VAL          
SEQRES   3 D  330  SER LEU ALA GLU ARG HIS TYR TYR ASN CYS ASP PHE LYS          
SEQRES   4 D  330  MSE CYS TYR LYS LEU THR SER VAL VAL MSE GLU LYS ASP          
SEQRES   5 D  330  PRO PHE HIS ALA SER CYS LEU PRO VAL HIS ILE GLY THR          
SEQRES   6 D  330  LEU VAL GLU LEU ASN LYS ALA ASN GLU LEU PHE TYR LEU          
SEQRES   7 D  330  SER HIS LYS LEU VAL ASP LEU TYR PRO SER ASN PRO VAL          
SEQRES   8 D  330  SER TRP PHE ALA VAL GLY CYS TYR TYR LEU MSE VAL GLY          
SEQRES   9 D  330  HIS LYS ASN GLU HIS ALA ARG ARG TYR LEU SER LYS ALA          
SEQRES  10 D  330  THR THR LEU GLU LYS THR TYR GLY PRO ALA TRP ILE ALA          
SEQRES  11 D  330  TYR GLY HIS SER PHE ALA VAL GLU SER GLU HIS ASP GLN          
SEQRES  12 D  330  ALA MSE ALA ALA TYR PHE THR ALA ALA GLN LEU MSE LYS          
SEQRES  13 D  330  GLY CYS HIS LEU PRO MSE LEU TYR ILE GLY LEU GLU TYR          
SEQRES  14 D  330  GLY LEU THR ASN ASN SER LYS LEU ALA GLU ARG PHE PHE          
SEQRES  15 D  330  SER GLN ALA LEU SER ILE ALA PRO GLU ASP PRO PHE VAL          
SEQRES  16 D  330  MSE HIS GLU VAL GLY VAL VAL ALA PHE GLN ASN GLY GLU          
SEQRES  17 D  330  TRP LYS THR ALA GLU LYS TRP PHE LEU ASP ALA LEU GLU          
SEQRES  18 D  330  LYS ILE LYS ALA ILE GLY ASN GLU VAL THR VAL ASP LYS          
SEQRES  19 D  330  TRP GLU PRO LEU LEU ASN ASN LEU GLY HIS VAL CYS ARG          
SEQRES  20 D  330  LYS LEU LYS LYS TYR ALA GLU ALA LEU ASP TYR HIS ARG          
SEQRES  21 D  330  GLN ALA LEU VAL LEU ILE PRO GLN ASN ALA SER THR TYR          
SEQRES  22 D  330  SER ALA ILE GLY TYR ILE HIS SER LEU MSE GLY ASN PHE          
SEQRES  23 D  330  GLU ASN ALA VAL ASP TYR PHE HIS THR ALA LEU GLY LEU          
SEQRES  24 D  330  ARG ARG ASP ASP THR PHE SER VAL THR MSE LEU GLY HIS          
SEQRES  25 D  330  CYS ILE GLU MSE TYR ILE GLY ASP SER GLU ALA TYR ILE          
SEQRES  26 D  330  GLY ALA ASP ILE LYS                                          
SEQRES   1 E   29  MSE LEU ARG ARG LYS PRO THR ARG LEU GLU LEU LYS LEU          
SEQRES   2 E   29  ASP ASP ILE GLU GLU PHE GLU ASN ILE ARG LYS ASP LEU          
SEQRES   3 E   29  GLU THR ARG                                                  
SEQRES   1 F  330  GLY SER TYR ASN LYS PRO SER GLU THR VAL ILE PRO GLU          
SEQRES   2 F  330  SER VAL ASP GLY LEU GLN GLU ASN LEU ASP VAL VAL VAL          
SEQRES   3 F  330  SER LEU ALA GLU ARG HIS TYR TYR ASN CYS ASP PHE LYS          
SEQRES   4 F  330  MSE CYS TYR LYS LEU THR SER VAL VAL MSE GLU LYS ASP          
SEQRES   5 F  330  PRO PHE HIS ALA SER CYS LEU PRO VAL HIS ILE GLY THR          
SEQRES   6 F  330  LEU VAL GLU LEU ASN LYS ALA ASN GLU LEU PHE TYR LEU          
SEQRES   7 F  330  SER HIS LYS LEU VAL ASP LEU TYR PRO SER ASN PRO VAL          
SEQRES   8 F  330  SER TRP PHE ALA VAL GLY CYS TYR TYR LEU MSE VAL GLY          
SEQRES   9 F  330  HIS LYS ASN GLU HIS ALA ARG ARG TYR LEU SER LYS ALA          
SEQRES  10 F  330  THR THR LEU GLU LYS THR TYR GLY PRO ALA TRP ILE ALA          
SEQRES  11 F  330  TYR GLY HIS SER PHE ALA VAL GLU SER GLU HIS ASP GLN          
SEQRES  12 F  330  ALA MSE ALA ALA TYR PHE THR ALA ALA GLN LEU MSE LYS          
SEQRES  13 F  330  GLY CYS HIS LEU PRO MSE LEU TYR ILE GLY LEU GLU TYR          
SEQRES  14 F  330  GLY LEU THR ASN ASN SER LYS LEU ALA GLU ARG PHE PHE          
SEQRES  15 F  330  SER GLN ALA LEU SER ILE ALA PRO GLU ASP PRO PHE VAL          
SEQRES  16 F  330  MSE HIS GLU VAL GLY VAL VAL ALA PHE GLN ASN GLY GLU          
SEQRES  17 F  330  TRP LYS THR ALA GLU LYS TRP PHE LEU ASP ALA LEU GLU          
SEQRES  18 F  330  LYS ILE LYS ALA ILE GLY ASN GLU VAL THR VAL ASP LYS          
SEQRES  19 F  330  TRP GLU PRO LEU LEU ASN ASN LEU GLY HIS VAL CYS ARG          
SEQRES  20 F  330  LYS LEU LYS LYS TYR ALA GLU ALA LEU ASP TYR HIS ARG          
SEQRES  21 F  330  GLN ALA LEU VAL LEU ILE PRO GLN ASN ALA SER THR TYR          
SEQRES  22 F  330  SER ALA ILE GLY TYR ILE HIS SER LEU MSE GLY ASN PHE          
SEQRES  23 F  330  GLU ASN ALA VAL ASP TYR PHE HIS THR ALA LEU GLY LEU          
SEQRES  24 F  330  ARG ARG ASP ASP THR PHE SER VAL THR MSE LEU GLY HIS          
SEQRES  25 F  330  CYS ILE GLU MSE TYR ILE GLY ASP SER GLU ALA TYR ILE          
SEQRES  26 F  330  GLY ALA ASP ILE LYS                                          
SEQRES   1 G   29  MSE LEU ARG ARG LYS PRO THR ARG LEU GLU LEU LYS LEU          
SEQRES   2 G   29  ASP ASP ILE GLU GLU PHE GLU ASN ILE ARG LYS ASP LEU          
SEQRES   3 G   29  GLU THR ARG                                                  
SEQRES   1 H  330  GLY SER TYR ASN LYS PRO SER GLU THR VAL ILE PRO GLU          
SEQRES   2 H  330  SER VAL ASP GLY LEU GLN GLU ASN LEU ASP VAL VAL VAL          
SEQRES   3 H  330  SER LEU ALA GLU ARG HIS TYR TYR ASN CYS ASP PHE LYS          
SEQRES   4 H  330  MSE CYS TYR LYS LEU THR SER VAL VAL MSE GLU LYS ASP          
SEQRES   5 H  330  PRO PHE HIS ALA SER CYS LEU PRO VAL HIS ILE GLY THR          
SEQRES   6 H  330  LEU VAL GLU LEU ASN LYS ALA ASN GLU LEU PHE TYR LEU          
SEQRES   7 H  330  SER HIS LYS LEU VAL ASP LEU TYR PRO SER ASN PRO VAL          
SEQRES   8 H  330  SER TRP PHE ALA VAL GLY CYS TYR TYR LEU MSE VAL GLY          
SEQRES   9 H  330  HIS LYS ASN GLU HIS ALA ARG ARG TYR LEU SER LYS ALA          
SEQRES  10 H  330  THR THR LEU GLU LYS THR TYR GLY PRO ALA TRP ILE ALA          
SEQRES  11 H  330  TYR GLY HIS SER PHE ALA VAL GLU SER GLU HIS ASP GLN          
SEQRES  12 H  330  ALA MSE ALA ALA TYR PHE THR ALA ALA GLN LEU MSE LYS          
SEQRES  13 H  330  GLY CYS HIS LEU PRO MSE LEU TYR ILE GLY LEU GLU TYR          
SEQRES  14 H  330  GLY LEU THR ASN ASN SER LYS LEU ALA GLU ARG PHE PHE          
SEQRES  15 H  330  SER GLN ALA LEU SER ILE ALA PRO GLU ASP PRO PHE VAL          
SEQRES  16 H  330  MSE HIS GLU VAL GLY VAL VAL ALA PHE GLN ASN GLY GLU          
SEQRES  17 H  330  TRP LYS THR ALA GLU LYS TRP PHE LEU ASP ALA LEU GLU          
SEQRES  18 H  330  LYS ILE LYS ALA ILE GLY ASN GLU VAL THR VAL ASP LYS          
SEQRES  19 H  330  TRP GLU PRO LEU LEU ASN ASN LEU GLY HIS VAL CYS ARG          
SEQRES  20 H  330  LYS LEU LYS LYS TYR ALA GLU ALA LEU ASP TYR HIS ARG          
SEQRES  21 H  330  GLN ALA LEU VAL LEU ILE PRO GLN ASN ALA SER THR TYR          
SEQRES  22 H  330  SER ALA ILE GLY TYR ILE HIS SER LEU MSE GLY ASN PHE          
SEQRES  23 H  330  GLU ASN ALA VAL ASP TYR PHE HIS THR ALA LEU GLY LEU          
SEQRES  24 H  330  ARG ARG ASP ASP THR PHE SER VAL THR MSE LEU GLY HIS          
SEQRES  25 H  330  CYS ILE GLU MSE TYR ILE GLY ASP SER GLU ALA TYR ILE          
SEQRES  26 H  330  GLY ALA ASP ILE LYS                                          
SEQRES   1 I   29  MSE LEU ARG ARG LYS PRO THR ARG LEU GLU LEU LYS LEU          
SEQRES   2 I   29  ASP ASP ILE GLU GLU PHE GLU ASN ILE ARG LYS ASP LEU          
SEQRES   3 I   29  GLU THR ARG                                                  
SEQRES   1 J  330  GLY SER TYR ASN LYS PRO SER GLU THR VAL ILE PRO GLU          
SEQRES   2 J  330  SER VAL ASP GLY LEU GLN GLU ASN LEU ASP VAL VAL VAL          
SEQRES   3 J  330  SER LEU ALA GLU ARG HIS TYR TYR ASN CYS ASP PHE LYS          
SEQRES   4 J  330  MSE CYS TYR LYS LEU THR SER VAL VAL MSE GLU LYS ASP          
SEQRES   5 J  330  PRO PHE HIS ALA SER CYS LEU PRO VAL HIS ILE GLY THR          
SEQRES   6 J  330  LEU VAL GLU LEU ASN LYS ALA ASN GLU LEU PHE TYR LEU          
SEQRES   7 J  330  SER HIS LYS LEU VAL ASP LEU TYR PRO SER ASN PRO VAL          
SEQRES   8 J  330  SER TRP PHE ALA VAL GLY CYS TYR TYR LEU MSE VAL GLY          
SEQRES   9 J  330  HIS LYS ASN GLU HIS ALA ARG ARG TYR LEU SER LYS ALA          
SEQRES  10 J  330  THR THR LEU GLU LYS THR TYR GLY PRO ALA TRP ILE ALA          
SEQRES  11 J  330  TYR GLY HIS SER PHE ALA VAL GLU SER GLU HIS ASP GLN          
SEQRES  12 J  330  ALA MSE ALA ALA TYR PHE THR ALA ALA GLN LEU MSE LYS          
SEQRES  13 J  330  GLY CYS HIS LEU PRO MSE LEU TYR ILE GLY LEU GLU TYR          
SEQRES  14 J  330  GLY LEU THR ASN ASN SER LYS LEU ALA GLU ARG PHE PHE          
SEQRES  15 J  330  SER GLN ALA LEU SER ILE ALA PRO GLU ASP PRO PHE VAL          
SEQRES  16 J  330  MSE HIS GLU VAL GLY VAL VAL ALA PHE GLN ASN GLY GLU          
SEQRES  17 J  330  TRP LYS THR ALA GLU LYS TRP PHE LEU ASP ALA LEU GLU          
SEQRES  18 J  330  LYS ILE LYS ALA ILE GLY ASN GLU VAL THR VAL ASP LYS          
SEQRES  19 J  330  TRP GLU PRO LEU LEU ASN ASN LEU GLY HIS VAL CYS ARG          
SEQRES  20 J  330  LYS LEU LYS LYS TYR ALA GLU ALA LEU ASP TYR HIS ARG          
SEQRES  21 J  330  GLN ALA LEU VAL LEU ILE PRO GLN ASN ALA SER THR TYR          
SEQRES  22 J  330  SER ALA ILE GLY TYR ILE HIS SER LEU MSE GLY ASN PHE          
SEQRES  23 J  330  GLU ASN ALA VAL ASP TYR PHE HIS THR ALA LEU GLY LEU          
SEQRES  24 J  330  ARG ARG ASP ASP THR PHE SER VAL THR MSE LEU GLY HIS          
SEQRES  25 J  330  CYS ILE GLU MSE TYR ILE GLY ASP SER GLU ALA TYR ILE          
SEQRES  26 J  330  GLY ALA ASP ILE LYS                                          
SEQRES   1 K   29  MSE LEU ARG ARG LYS PRO THR ARG LEU GLU LEU LYS LEU          
SEQRES   2 K   29  ASP ASP ILE GLU GLU PHE GLU ASN ILE ARG LYS ASP LEU          
SEQRES   3 K   29  GLU THR ARG                                                  
SEQRES   1 L  330  GLY SER TYR ASN LYS PRO SER GLU THR VAL ILE PRO GLU          
SEQRES   2 L  330  SER VAL ASP GLY LEU GLN GLU ASN LEU ASP VAL VAL VAL          
SEQRES   3 L  330  SER LEU ALA GLU ARG HIS TYR TYR ASN CYS ASP PHE LYS          
SEQRES   4 L  330  MSE CYS TYR LYS LEU THR SER VAL VAL MSE GLU LYS ASP          
SEQRES   5 L  330  PRO PHE HIS ALA SER CYS LEU PRO VAL HIS ILE GLY THR          
SEQRES   6 L  330  LEU VAL GLU LEU ASN LYS ALA ASN GLU LEU PHE TYR LEU          
SEQRES   7 L  330  SER HIS LYS LEU VAL ASP LEU TYR PRO SER ASN PRO VAL          
SEQRES   8 L  330  SER TRP PHE ALA VAL GLY CYS TYR TYR LEU MSE VAL GLY          
SEQRES   9 L  330  HIS LYS ASN GLU HIS ALA ARG ARG TYR LEU SER LYS ALA          
SEQRES  10 L  330  THR THR LEU GLU LYS THR TYR GLY PRO ALA TRP ILE ALA          
SEQRES  11 L  330  TYR GLY HIS SER PHE ALA VAL GLU SER GLU HIS ASP GLN          
SEQRES  12 L  330  ALA MSE ALA ALA TYR PHE THR ALA ALA GLN LEU MSE LYS          
SEQRES  13 L  330  GLY CYS HIS LEU PRO MSE LEU TYR ILE GLY LEU GLU TYR          
SEQRES  14 L  330  GLY LEU THR ASN ASN SER LYS LEU ALA GLU ARG PHE PHE          
SEQRES  15 L  330  SER GLN ALA LEU SER ILE ALA PRO GLU ASP PRO PHE VAL          
SEQRES  16 L  330  MSE HIS GLU VAL GLY VAL VAL ALA PHE GLN ASN GLY GLU          
SEQRES  17 L  330  TRP LYS THR ALA GLU LYS TRP PHE LEU ASP ALA LEU GLU          
SEQRES  18 L  330  LYS ILE LYS ALA ILE GLY ASN GLU VAL THR VAL ASP LYS          
SEQRES  19 L  330  TRP GLU PRO LEU LEU ASN ASN LEU GLY HIS VAL CYS ARG          
SEQRES  20 L  330  LYS LEU LYS LYS TYR ALA GLU ALA LEU ASP TYR HIS ARG          
SEQRES  21 L  330  GLN ALA LEU VAL LEU ILE PRO GLN ASN ALA SER THR TYR          
SEQRES  22 L  330  SER ALA ILE GLY TYR ILE HIS SER LEU MSE GLY ASN PHE          
SEQRES  23 L  330  GLU ASN ALA VAL ASP TYR PHE HIS THR ALA LEU GLY LEU          
SEQRES  24 L  330  ARG ARG ASP ASP THR PHE SER VAL THR MSE LEU GLY HIS          
SEQRES  25 L  330  CYS ILE GLU MSE TYR ILE GLY ASP SER GLU ALA TYR ILE          
SEQRES  26 L  330  GLY ALA ASP ILE LYS                                          
MODRES 3HYM MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE B  249  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE B  258  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE B  311  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE B  354  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE B  364  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE B  371  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE B  405  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE B  492  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE B  518  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE B  525  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE D  249  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE D  258  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE D  311  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE D  354  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE D  364  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE D  371  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE D  405  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE D  492  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE D  518  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE D  525  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE E    1  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE F  249  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE F  258  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE F  311  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE F  354  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE F  364  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE F  371  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE F  405  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE F  492  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE F  518  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE F  525  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE G    1  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE H  249  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE H  258  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE H  311  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE H  354  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE H  364  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE H  371  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE H  405  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE H  492  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE H  518  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE H  525  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE I    1  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE J  249  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE J  258  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE J  311  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE J  354  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE J  364  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE J  371  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE J  405  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE J  492  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE J  518  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE J  525  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE K    1  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE L  249  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE L  258  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE L  311  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE L  354  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE L  364  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE L  371  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE L  405  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE L  492  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE L  518  MET  SELENOMETHIONINE                                   
MODRES 3HYM MSE L  525  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  B 249       8                                                       
HET    MSE  B 258       8                                                       
HET    MSE  B 311       8                                                       
HET    MSE  B 354       8                                                       
HET    MSE  B 364       8                                                       
HET    MSE  B 371       8                                                       
HET    MSE  B 405       8                                                       
HET    MSE  B 492       8                                                       
HET    MSE  B 518       8                                                       
HET    MSE  B 525       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  D 249       8                                                       
HET    MSE  D 258       8                                                       
HET    MSE  D 311       8                                                       
HET    MSE  D 354       8                                                       
HET    MSE  D 364       8                                                       
HET    MSE  D 371       8                                                       
HET    MSE  D 405       8                                                       
HET    MSE  D 492       8                                                       
HET    MSE  D 518       8                                                       
HET    MSE  D 525       8                                                       
HET    MSE  E   1       8                                                       
HET    MSE  F 249       8                                                       
HET    MSE  F 258       8                                                       
HET    MSE  F 311       8                                                       
HET    MSE  F 354       8                                                       
HET    MSE  F 364       8                                                       
HET    MSE  F 371       8                                                       
HET    MSE  F 405       8                                                       
HET    MSE  F 492       8                                                       
HET    MSE  F 518       8                                                       
HET    MSE  F 525       8                                                       
HET    MSE  G   1       8                                                       
HET    MSE  H 249       8                                                       
HET    MSE  H 258       8                                                       
HET    MSE  H 311       8                                                       
HET    MSE  H 354       8                                                       
HET    MSE  H 364       8                                                       
HET    MSE  H 371       8                                                       
HET    MSE  H 405       8                                                       
HET    MSE  H 492       8                                                       
HET    MSE  H 518       8                                                       
HET    MSE  H 525       8                                                       
HET    MSE  I   1       8                                                       
HET    MSE  J 249       8                                                       
HET    MSE  J 258       8                                                       
HET    MSE  J 311       8                                                       
HET    MSE  J 354       8                                                       
HET    MSE  J 364       8                                                       
HET    MSE  J 371       8                                                       
HET    MSE  J 405       8                                                       
HET    MSE  J 492       8                                                       
HET    MSE  J 518       8                                                       
HET    MSE  J 525       8                                                       
HET    MSE  K   1       8                                                       
HET    MSE  L 249       8                                                       
HET    MSE  L 258       8                                                       
HET    MSE  L 311       8                                                       
HET    MSE  L 354       8                                                       
HET    MSE  L 364       8                                                       
HET    MSE  L 371       8                                                       
HET    MSE  L 405       8                                                       
HET    MSE  L 492       8                                                       
HET    MSE  L 518       8                                                       
HET    MSE  L 525       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    66(C5 H11 N O2 SE)                                           
FORMUL  13  HOH   *211(H2 O)                                                    
HELIX    1   1 LEU A   13  ASP A   15  5                                   3    
HELIX    2   2 ILE A   16  LEU A   26  1                                  11    
HELIX    3   3 VAL B  233  ASN B  244  1                                  12    
HELIX    4   4 ASP B  246  ASP B  261  1                                  16    
HELIX    5   5 CYS B  267  ASN B  279  1                                  13    
HELIX    6   6 LYS B  280  TYR B  295  1                                  16    
HELIX    7   7 PRO B  299  VAL B  312  1                                  14    
HELIX    8   8 LYS B  315  THR B  328  1                                  14    
HELIX    9   9 GLY B  334  SER B  348  1                                  15    
HELIX   10  10 GLU B  349  MSE B  364  1                                  16    
HELIX   11  11 HIS B  368  THR B  381  1                                  14    
HELIX   12  12 ASN B  383  SER B  396  1                                  14    
HELIX   13  13 ASP B  401  ASN B  415  1                                  15    
HELIX   14  14 GLU B  417  LYS B  433  1                                  17    
HELIX   15  15 GLU B  445  LEU B  458  1                                  14    
HELIX   16  16 LYS B  460  ILE B  475  1                                  16    
HELIX   17  17 ALA B  479  GLY B  493  1                                  15    
HELIX   18  18 ASN B  494  THR B  504  1                                  11    
HELIX   19  19 ASP B  512  MSE B  525  1                                  14    
HELIX   20  20 ILE C   16  ILE C   22  1                                   7    
HELIX   21  21 LEU D  231  CYS D  245  1                                  15    
HELIX   22  22 ASP D  246  ASP D  261  1                                  16    
HELIX   23  23 CYS D  267  LEU D  278  1                                  12    
HELIX   24  24 LYS D  280  TYR D  295  1                                  16    
HELIX   25  25 PRO D  299  MSE D  311  1                                  13    
HELIX   26  26 LYS D  315  GLU D  330  1                                  16    
HELIX   27  27 TYR D  333  VAL D  346  1                                  14    
HELIX   28  28 GLU D  349  MSE D  364  1                                  16    
HELIX   29  29 HIS D  368  LEU D  380  1                                  13    
HELIX   30  30 ASN D  383  ALA D  398  1                                  16    
HELIX   31  31 ASP D  401  ASN D  415  1                                  15    
HELIX   32  32 LYS D  419  ALA D  434  1                                  16    
HELIX   33  33 GLU D  445  LYS D  459  1                                  15    
HELIX   34  34 LYS D  460  ILE D  475  1                                  16    
HELIX   35  35 ASN D  478  GLY D  493  1                                  16    
HELIX   36  36 ASN D  494  GLY D  507  1                                  14    
HELIX   37  37 ASP D  512  MSE D  525  1                                  14    
HELIX   38  38 LYS E   12  ASP E   15  5                                   4    
HELIX   39  39 ILE E   16  LEU E   26  1                                  11    
HELIX   40  40 LEU F  231  ASN F  244  1                                  14    
HELIX   41  41 ASP F  246  ASP F  261  1                                  16    
HELIX   42  42 CYS F  267  LEU F  278  1                                  12    
HELIX   43  43 ASN F  282  TYR F  295  1                                  14    
HELIX   44  44 PRO F  299  CYS F  307  1                                   9    
HELIX   45  45 LYS F  315  THR F  328  1                                  14    
HELIX   46  46 TYR F  333  SER F  348  1                                  16    
HELIX   47  47 GLU F  349  MSE F  364  1                                  16    
HELIX   48  48 HIS F  368  LEU F  380  1                                  13    
HELIX   49  49 ASN F  383  SER F  396  1                                  14    
HELIX   50  50 ASP F  401  GLN F  414  1                                  14    
HELIX   51  51 GLU F  417  ALA F  434  1                                  18    
HELIX   52  52 GLU F  445  LEU F  458  1                                  14    
HELIX   53  53 LYS F  460  ILE F  475  1                                  16    
HELIX   54  54 ASN F  478  GLY F  493  1                                  16    
HELIX   55  55 ASN F  494  GLY F  507  1                                  14    
HELIX   56  56 ASP F  512  MSE F  525  1                                  14    
HELIX   57  57 ILE G   16  ASP G   25  1                                  10    
HELIX   58  58 VAL H  233  ASN H  244  1                                  12    
HELIX   59  59 ASP H  246  ASP H  261  1                                  16    
HELIX   60  60 CYS H  267  LEU H  278  1                                  12    
HELIX   61  61 LYS H  280  TYR H  295  1                                  16    
HELIX   62  62 PRO H  299  VAL H  312  1                                  14    
HELIX   63  63 LYS H  315  THR H  328  1                                  14    
HELIX   64  64 TYR H  333  GLU H  347  1                                  15    
HELIX   65  65 GLU H  349  MSE H  364  1                                  16    
HELIX   66  66 HIS H  368  LEU H  380  1                                  13    
HELIX   67  67 ASN H  383  SER H  396  1                                  14    
HELIX   68  68 ASP H  401  ASN H  415  1                                  15    
HELIX   69  69 GLU H  417  ALA H  428  1                                  12    
HELIX   70  70 THR H  440  TRP H  444  5                                   5    
HELIX   71  71 GLU H  445  LEU H  458  1                                  14    
HELIX   72  72 LYS H  460  ILE H  475  1                                  16    
HELIX   73  73 ASN H  478  GLY H  493  1                                  16    
HELIX   74  74 ASN H  494  GLY H  507  1                                  14    
HELIX   75  75 ASP H  512  ILE H  527  1                                  16    
HELIX   76  76 LEU I   13  ASP I   15  5                                   3    
HELIX   77  77 ILE I   16  LEU I   26  1                                  11    
HELIX   78  78 LEU J  231  ASN J  244  1                                  14    
HELIX   79  79 ASP J  246  ASP J  261  1                                  16    
HELIX   80  80 CYS J  267  LEU J  278  1                                  12    
HELIX   81  81 LYS J  280  TYR J  295  1                                  16    
HELIX   82  82 PRO J  299  VAL J  312  1                                  14    
HELIX   83  83 LYS J  315  THR J  328  1                                  14    
HELIX   84  84 TYR J  333  VAL J  346  1                                  14    
HELIX   85  85 GLU J  349  MSE J  364  1                                  16    
HELIX   86  86 HIS J  368  LEU J  380  1                                  13    
HELIX   87  87 ASN J  383  SER J  396  1                                  14    
HELIX   88  88 ASP J  401  GLY J  416  1                                  16    
HELIX   89  89 GLU J  417  ALA J  428  1                                  12    
HELIX   90  90 ALA J  428  LYS J  433  1                                   6    
HELIX   91  91 PRO J  446  ARG J  456  1                                  11    
HELIX   92  92 TYR J  461  ILE J  475  1                                  15    
HELIX   93  93 ASN J  478  GLY J  493  1                                  16    
HELIX   94  94 ASN J  494  ALA J  505  1                                  12    
HELIX   95  95 ASP J  512  ILE J  527  1                                  16    
HELIX   96  96 LEU K   13  ASP K   15  5                                   3    
HELIX   97  97 ILE K   16  ASN K   21  1                                   6    
HELIX   98  98 LEU L  231  ASN L  244  1                                  14    
HELIX   99  99 ASP L  246  ASP L  261  1                                  16    
HELIX  100 100 SER L  266  LEU L  278  1                                  13    
HELIX  101 101 LYS L  280  TYR L  295  1                                  16    
HELIX  102 102 PRO L  299  VAL L  312  1                                  14    
HELIX  103 103 LYS L  315  THR L  328  1                                  14    
HELIX  104 104 TYR L  333  VAL L  346  1                                  14    
HELIX  105 105 GLU L  349  MSE L  364  1                                  16    
HELIX  106 106 HIS L  368  LEU L  380  1                                  13    
HELIX  107 107 ASN L  383  SER L  396  1                                  14    
HELIX  108 108 ASP L  401  GLY L  416  1                                  16    
HELIX  109 109 GLU L  417  ALA L  428  1                                  12    
HELIX  110 110 LEU L  447  LYS L  457  1                                  11    
HELIX  111 111 LYS L  460  ILE L  475  1                                  16    
HELIX  112 112 ASN L  478  GLY L  493  1                                  16    
HELIX  113 113 ASN L  494  GLY L  507  1                                  14    
HELIX  114 114 ASP L  512  MSE L  525  1                                  14    
LINK         C   LYS B 248                 N   MSE B 249     1555   1555  1.33  
LINK         C   MSE B 249                 N   CYS B 250     1555   1555  1.33  
LINK         C   VAL B 257                 N   MSE B 258     1555   1555  1.33  
LINK         C   MSE B 258                 N   GLU B 259     1555   1555  1.33  
LINK         C   LEU B 310                 N   MSE B 311     1555   1555  1.33  
LINK         C   MSE B 311                 N   VAL B 312     1555   1555  1.33  
LINK         C   ALA B 353                 N   MSE B 354     1555   1555  1.33  
LINK         C   MSE B 354                 N   ALA B 355     1555   1555  1.33  
LINK         C   LEU B 363                 N   MSE B 364     1555   1555  1.33  
LINK         C   MSE B 364                 N   LYS B 365     1555   1555  1.33  
LINK         C   PRO B 370                 N   MSE B 371     1555   1555  1.33  
LINK         C   MSE B 371                 N   LEU B 372     1555   1555  1.33  
LINK         C   VAL B 404                 N   MSE B 405     1555   1555  1.33  
LINK         C   MSE B 405                 N   HIS B 406     1555   1555  1.33  
LINK         C   LEU B 491                 N   MSE B 492     1555   1555  1.33  
LINK         C   MSE B 492                 N   GLY B 493     1555   1555  1.33  
LINK         C   THR B 517                 N   MSE B 518     1555   1555  1.33  
LINK         C   MSE B 518                 N   LEU B 519     1555   1555  1.33  
LINK         C   GLU B 524                 N   MSE B 525     1555   1555  1.33  
LINK         C   MSE B 525                 N   TYR B 526     1555   1555  1.33  
LINK         C   LYS D 248                 N   MSE D 249     1555   1555  1.33  
LINK         C   MSE D 249                 N   CYS D 250     1555   1555  1.33  
LINK         C   VAL D 257                 N   MSE D 258     1555   1555  1.33  
LINK         C   MSE D 258                 N   GLU D 259     1555   1555  1.34  
LINK         C   LEU D 310                 N   MSE D 311     1555   1555  1.34  
LINK         C   MSE D 311                 N   VAL D 312     1555   1555  1.33  
LINK         C   ALA D 353                 N   MSE D 354     1555   1555  1.33  
LINK         C   MSE D 354                 N   ALA D 355     1555   1555  1.33  
LINK         C   LEU D 363                 N   MSE D 364     1555   1555  1.33  
LINK         C   MSE D 364                 N   LYS D 365     1555   1555  1.33  
LINK         C   PRO D 370                 N   MSE D 371     1555   1555  1.33  
LINK         C   MSE D 371                 N   LEU D 372     1555   1555  1.33  
LINK         C   VAL D 404                 N   MSE D 405     1555   1555  1.33  
LINK         C   MSE D 405                 N   HIS D 406     1555   1555  1.33  
LINK         C   LEU D 491                 N   MSE D 492     1555   1555  1.33  
LINK         C   MSE D 492                 N   GLY D 493     1555   1555  1.33  
LINK         C   THR D 517                 N   MSE D 518     1555   1555  1.33  
LINK         C   MSE D 518                 N   LEU D 519     1555   1555  1.33  
LINK         C   GLU D 524                 N   MSE D 525     1555   1555  1.33  
LINK         C   MSE D 525                 N   TYR D 526     1555   1555  1.33  
LINK         C   LYS F 248                 N   MSE F 249     1555   1555  1.33  
LINK         C   MSE F 249                 N   CYS F 250     1555   1555  1.33  
LINK         C   VAL F 257                 N   MSE F 258     1555   1555  1.33  
LINK         C   MSE F 258                 N   GLU F 259     1555   1555  1.33  
LINK         C   LEU F 310                 N   MSE F 311     1555   1555  1.33  
LINK         C   MSE F 311                 N   VAL F 312     1555   1555  1.33  
LINK         C   ALA F 353                 N   MSE F 354     1555   1555  1.33  
LINK         C   MSE F 354                 N   ALA F 355     1555   1555  1.33  
LINK         C   LEU F 363                 N   MSE F 364     1555   1555  1.33  
LINK         C   MSE F 364                 N   LYS F 365     1555   1555  1.33  
LINK         C   PRO F 370                 N   MSE F 371     1555   1555  1.33  
LINK         C   MSE F 371                 N   LEU F 372     1555   1555  1.33  
LINK         C   VAL F 404                 N   MSE F 405     1555   1555  1.33  
LINK         C   MSE F 405                 N   HIS F 406     1555   1555  1.34  
LINK         C   LEU F 491                 N   MSE F 492     1555   1555  1.33  
LINK         C   MSE F 492                 N   GLY F 493     1555   1555  1.33  
LINK         C   THR F 517                 N   MSE F 518     1555   1555  1.33  
LINK         C   MSE F 518                 N   LEU F 519     1555   1555  1.33  
LINK         C   GLU F 524                 N   MSE F 525     1555   1555  1.33  
LINK         C   MSE F 525                 N   TYR F 526     1555   1555  1.33  
LINK         C   LYS H 248                 N   MSE H 249     1555   1555  1.33  
LINK         C   MSE H 249                 N   CYS H 250     1555   1555  1.33  
LINK         C   VAL H 257                 N   MSE H 258     1555   1555  1.33  
LINK         C   MSE H 258                 N   GLU H 259     1555   1555  1.33  
LINK         C   LEU H 310                 N   MSE H 311     1555   1555  1.33  
LINK         C   MSE H 311                 N   VAL H 312     1555   1555  1.33  
LINK         C   ALA H 353                 N   MSE H 354     1555   1555  1.33  
LINK         C   MSE H 354                 N   ALA H 355     1555   1555  1.33  
LINK         C   LEU H 363                 N   MSE H 364     1555   1555  1.33  
LINK         C   MSE H 364                 N   LYS H 365     1555   1555  1.33  
LINK         C   PRO H 370                 N   MSE H 371     1555   1555  1.33  
LINK         C   MSE H 371                 N   LEU H 372     1555   1555  1.33  
LINK         C   VAL H 404                 N   MSE H 405     1555   1555  1.33  
LINK         C   MSE H 405                 N   HIS H 406     1555   1555  1.33  
LINK         C   LEU H 491                 N   MSE H 492     1555   1555  1.33  
LINK         C   MSE H 492                 N   GLY H 493     1555   1555  1.33  
LINK         C   THR H 517                 N   MSE H 518     1555   1555  1.33  
LINK         C   MSE H 518                 N   LEU H 519     1555   1555  1.33  
LINK         C   GLU H 524                 N   MSE H 525     1555   1555  1.33  
LINK         C   MSE H 525                 N   TYR H 526     1555   1555  1.33  
LINK         C   LYS J 248                 N   MSE J 249     1555   1555  1.33  
LINK         C   MSE J 249                 N   CYS J 250     1555   1555  1.33  
LINK         C   VAL J 257                 N   MSE J 258     1555   1555  1.33  
LINK         C   MSE J 258                 N   GLU J 259     1555   1555  1.33  
LINK         C   LEU J 310                 N   MSE J 311     1555   1555  1.33  
LINK         C   MSE J 311                 N   VAL J 312     1555   1555  1.33  
LINK         C   ALA J 353                 N   MSE J 354     1555   1555  1.32  
LINK         C   MSE J 354                 N   ALA J 355     1555   1555  1.33  
LINK         C   LEU J 363                 N   MSE J 364     1555   1555  1.33  
LINK         C   MSE J 364                 N   LYS J 365     1555   1555  1.33  
LINK         C   PRO J 370                 N   MSE J 371     1555   1555  1.33  
LINK         C   MSE J 371                 N   LEU J 372     1555   1555  1.33  
LINK         C   VAL J 404                 N   MSE J 405     1555   1555  1.33  
LINK         C   MSE J 405                 N   HIS J 406     1555   1555  1.33  
LINK         C   LEU J 491                 N   MSE J 492     1555   1555  1.34  
LINK         C   MSE J 492                 N   GLY J 493     1555   1555  1.33  
LINK         C   THR J 517                 N   MSE J 518     1555   1555  1.33  
LINK         C   MSE J 518                 N   LEU J 519     1555   1555  1.33  
LINK         C   GLU J 524                 N   MSE J 525     1555   1555  1.33  
LINK         C   MSE J 525                 N   TYR J 526     1555   1555  1.33  
LINK         C   LYS L 248                 N   MSE L 249     1555   1555  1.33  
LINK         C   MSE L 249                 N   CYS L 250     1555   1555  1.33  
LINK         C   VAL L 257                 N   MSE L 258     1555   1555  1.33  
LINK         C   MSE L 258                 N   GLU L 259     1555   1555  1.33  
LINK         C   LEU L 310                 N   MSE L 311     1555   1555  1.33  
LINK         C   MSE L 311                 N   VAL L 312     1555   1555  1.33  
LINK         C   ALA L 353                 N   MSE L 354     1555   1555  1.33  
LINK         C   MSE L 354                 N   ALA L 355     1555   1555  1.33  
LINK         C   LEU L 363                 N   MSE L 364     1555   1555  1.33  
LINK         C   MSE L 364                 N   LYS L 365     1555   1555  1.33  
LINK         C   PRO L 370                 N   MSE L 371     1555   1555  1.33  
LINK         C   MSE L 371                 N   LEU L 372     1555   1555  1.33  
LINK         C   VAL L 404                 N   MSE L 405     1555   1555  1.34  
LINK         C   MSE L 405                 N   HIS L 406     1555   1555  1.33  
LINK         C   LEU L 491                 N   MSE L 492     1555   1555  1.33  
LINK         C   MSE L 492                 N   GLY L 493     1555   1555  1.33  
LINK         C   THR L 517                 N   MSE L 518     1555   1555  1.33  
LINK         C   MSE L 518                 N   LEU L 519     1555   1555  1.33  
LINK         C   MSE L 525                 N   TYR L 526     1555   1555  1.33  
LINK         C   GLU L 524                 N   MSE L 525     1555   1555  1.33  
LINK         C   MSE A   1                 N   LEU A   2     1555   1555  1.33  
LINK         C   MSE C   1                 N   LEU C   2     1555   1555  1.33  
LINK         C   MSE E   1                 N   LEU E   2     1555   1555  1.34  
LINK         C   MSE G   1                 N   LEU G   2     1555   1555  1.33  
LINK         C   MSE I   1                 N   LEU I   2     1555   1555  1.34  
LINK         C   MSE K   1                 N   LEU K   2     1555   1555  1.34  
CISPEP   1 GLY B  313    HIS B  314          0        -5.83                     
CRYST1  301.897  301.897   80.168  90.00  90.00 120.00 P 63         36          
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      0.003312  0.001912  0.000000        0.00000                         
SCALE2      0.000000  0.003825  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012474        0.00000                         
HETATM    1  N   MSE A   1     -90.420-100.749 -26.191  1.00 79.97           N  
HETATM    2  CA  MSE A   1     -90.559-102.078 -25.611  1.00 77.27           C  
HETATM    3  C   MSE A   1     -89.201-102.761 -25.457  1.00 89.98           C  
HETATM    4  O   MSE A   1     -88.660-103.303 -26.418  1.00 97.70           O  
HETATM    5  CB  MSE A   1     -91.495-102.947 -26.463  1.00 62.69           C  
HETATM    6  CG  MSE A   1     -92.953-102.489 -26.485  1.00 61.49           C  
HETATM    7 SE   MSE A   1     -93.305-101.013 -27.728  1.00218.55          SE  
HETATM    8  CE  MSE A   1     -95.168-100.635 -27.264  1.00 88.98           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system