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Entry: 3UTT
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HEADER    IMMUNE SYSTEM                           26-NOV-11   3UTT              
TITLE     1E6-A*0201-ALWGPDPAAA COMPLEX, TRICLINIC                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN;   
COMPND   3 CHAIN: A, F;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 25-299;                                       
COMPND   5 SYNONYM: MHC CLASS I HEAVY CHAIN, MHC CLASS I ANTIGEN A*2;           
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   9 CHAIN: B, G;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 21-119;                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: INSULIN;                                                   
COMPND  14 CHAIN: C, H;                                                         
COMPND  15 FRAGMENT: PRE-PRO-INSULIN DERIVED PEPTIDE (UNP RESIDUES 15-24);      
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: 1E6 TCR ALPHA CHAIN;                                       
COMPND  19 CHAIN: D, I;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: 1E6 TCR BETA CHAIN;                                        
COMPND  23 CHAIN: E, J;                                                         
COMPND  24 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: HLA-A, HLAA;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;                               
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: B2M, CDABP0092, HDCMA22P;                                      
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;                               
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 SYNTHETIC: YES;                                                      
SOURCE  19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  20 ORGANISM_COMMON: HUMAN;                                              
SOURCE  21 ORGANISM_TAXID: 9606;                                                
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;                               
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  31 ORGANISM_COMMON: HUMAN;                                              
SOURCE  32 ORGANISM_TAXID: 9606;                                                
SOURCE  33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  34 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  35 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3                                
KEYWDS    MAJOR HISTOCOMPATIBILITY COMPLEX, HUMAN LEUKOCYTE ANTIGEN, TYPE I     
KEYWDS   2 DIABETES, T CELL RECEPTOR, IMMUNE SYSTEM                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.RIZKALLAH,D.K.COLE,A.K.SEWELL,A.M.BULEK,J.ROSSJOHN,S.GRAS         
REVDAT   3   17-JUL-19 3UTT    1       REMARK                                   
REVDAT   2   07-MAR-12 3UTT    1       JRNL                                     
REVDAT   1   25-JAN-12 3UTT    0                                                
JRNL        AUTH   A.M.BULEK,D.K.COLE,A.SKOWERA,G.DOLTON,S.GRAS,F.MADURA,       
JRNL        AUTH 2 A.FULLER,J.J.MILES,E.GOSTICK,D.A.PRICE,J.W.DRIJFHOUT,        
JRNL        AUTH 3 R.R.KNIGHT,G.C.HUANG,N.LISSIN,P.E.MOLLOY,L.WOOLDRIDGE,       
JRNL        AUTH 4 B.K.JAKOBSEN,J.ROSSJOHN,M.PEAKMAN,P.J.RIZKALLAH,A.K.SEWELL   
JRNL        TITL   STRUCTURAL BASIS FOR THE KILLING OF HUMAN BETA CELLS BY      
JRNL        TITL 2 CD8(+) T CELLS IN TYPE 1 DIABETES.                           
JRNL        REF    NAT.IMMUNOL.                  V.  13   283 2012              
JRNL        REFN                   ISSN 1529-2908                               
JRNL        PMID   22245737                                                     
JRNL        DOI    10.1038/NI.2206                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.6.1_357                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.34                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 51877                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2634                            
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 29.3382 -  5.5896    0.97     5364   256  0.1752 0.2293        
REMARK   3     2  5.5896 -  4.4416    0.97     5286   300  0.1398 0.2080        
REMARK   3     3  4.4416 -  3.8816    0.96     5260   287  0.1447 0.2255        
REMARK   3     4  3.8816 -  3.5274    0.95     5190   287  0.1781 0.2660        
REMARK   3     5  3.5274 -  3.2749    0.94     5080   298  0.2049 0.3147        
REMARK   3     6  3.2749 -  3.0820    0.91     5013   291  0.2274 0.3057        
REMARK   3     7  3.0820 -  2.9278    0.88     4810   247  0.2387 0.3499        
REMARK   3     8  2.9278 -  2.8005    0.85     4625   231  0.2740 0.3773        
REMARK   3     9  2.8005 -  2.6927    0.80     4469   220  0.2720 0.3471        
REMARK   3    10  2.6927 -  2.5999    0.77     4146   217  0.2845 0.3788        
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              : 30.40                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.200           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.30580                                             
REMARK   3    B22 (A**2) : 0.79600                                              
REMARK   3    B33 (A**2) : -13.10170                                            
REMARK   3    B12 (A**2) : 4.88570                                              
REMARK   3    B13 (A**2) : 3.96990                                              
REMARK   3    B23 (A**2) : -1.50350                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          13795                                  
REMARK   3   ANGLE     :  0.671          18707                                  
REMARK   3   CHIRALITY :  0.048           1937                                  
REMARK   3   PLANARITY :  0.004           2457                                  
REMARK   3   DIHEDRAL  : 11.956           5051                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 22                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1:181)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.0801   7.3159  -7.9497              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0566 T22:   0.2798                                     
REMARK   3      T33:   0.1495 T12:  -0.0382                                     
REMARK   3      T13:  -0.0890 T23:  -0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0618 L22:   1.1514                                     
REMARK   3      L33:   1.6051 L12:  -0.7412                                     
REMARK   3      L13:   0.6515 L23:  -0.9323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1907 S12:  -0.0687 S13:   0.0665                       
REMARK   3      S21:   0.5648 S22:   0.1262 S23:   0.1061                       
REMARK   3      S31:  -0.2773 S32:   0.2361 S33:   0.0485                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 182:275)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8667   0.7418  26.4945              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3956 T22:   0.3344                                     
REMARK   3      T33:   0.0722 T12:  -0.1054                                     
REMARK   3      T13:  -0.0772 T23:  -0.0422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5608 L22:   0.5765                                     
REMARK   3      L33:   0.6940 L12:   0.4757                                     
REMARK   3      L13:   0.1187 L23:   0.1824                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2720 S12:   0.0855 S13:  -0.0154                       
REMARK   3      S21:   0.5759 S22:  -0.1330 S23:   0.0404                       
REMARK   3      S31:   0.2227 S32:  -0.0318 S33:   0.0123                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 0:42)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9140 -10.8060   8.1687              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1635 T22:   0.2463                                     
REMARK   3      T33:   0.0960 T12:  -0.0922                                     
REMARK   3      T13:   0.0468 T23:   0.0857                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6182 L22:   0.5823                                     
REMARK   3      L33:   1.6839 L12:  -0.0594                                     
REMARK   3      L13:  -0.0903 L23:   0.2757                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0522 S12:  -0.0925 S13:   0.0508                       
REMARK   3      S21:   0.3960 S22:   0.1208 S23:   0.0500                       
REMARK   3      S31:   1.0366 S32:  -0.1656 S33:  -0.0111                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 43:99)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   2.8067 -13.0138   7.4028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2375 T22:   0.2746                                     
REMARK   3      T33:   0.0997 T12:  -0.0338                                     
REMARK   3      T13:   0.0620 T23:   0.0280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4458 L22:   0.4319                                     
REMARK   3      L33:   1.2205 L12:  -0.0550                                     
REMARK   3      L13:  -0.1423 L23:   0.2933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1409 S12:  -0.2320 S13:  -0.1103                       
REMARK   3      S21:   0.3895 S22:  -0.0573 S23:  -0.0390                       
REMARK   3      S31:   0.9467 S32:   0.1787 S33:  -0.0031                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 1:10)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7756  10.2431 -15.1681              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1225 T22:   0.4148                                     
REMARK   3      T33:   0.2795 T12:   0.0873                                     
REMARK   3      T13:  -0.0970 T23:   0.0831                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0610 L22:   0.5678                                     
REMARK   3      L33:   0.4867 L12:  -0.1407                                     
REMARK   3      L13:   0.0019 L23:  -0.3284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1808 S12:   0.0030 S13:   0.0753                       
REMARK   3      S21:   0.1263 S22:  -0.4469 S23:  -0.2693                       
REMARK   3      S31:  -0.0628 S32:   0.7529 S33:  -0.0999                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN D AND RESID 3:109)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6400  30.7149 -31.7865              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5710 T22:  -0.0099                                     
REMARK   3      T33:   0.2892 T12:  -0.0258                                     
REMARK   3      T13:   0.1192 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1640 L22:   0.9805                                     
REMARK   3      L33:   0.3704 L12:   0.1005                                     
REMARK   3      L13:   0.2913 L23:  -0.0634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1341 S12:   0.0313 S13:  -0.1326                       
REMARK   3      S21:  -0.0588 S22:   0.1697 S23:  -0.0584                       
REMARK   3      S31:  -0.7797 S32:  -0.2311 S33:   0.0519                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN D AND RESID 110:176)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4775  38.1922 -62.8503              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1692 T22:   0.0600                                     
REMARK   3      T33:   0.2997 T12:  -0.3140                                     
REMARK   3      T13:   0.0663 T23:  -0.0713                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0783 L22:   0.4468                                     
REMARK   3      L33:   1.4059 L12:  -0.1946                                     
REMARK   3      L13:  -0.2456 L23:   0.4797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1294 S12:   0.1209 S13:   0.0244                       
REMARK   3      S21:  -0.9900 S22:   0.2288 S23:  -0.0430                       
REMARK   3      S31:  -0.2783 S32:   0.5057 S33:  -0.0514                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN D AND RESID 177:199)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   8.4643  46.0918 -67.2639              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8903 T22:   0.1124                                     
REMARK   3      T33:   0.6251 T12:  -0.3032                                     
REMARK   3      T13:  -0.2894 T23:   0.0740                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4925 L22:   0.3009                                     
REMARK   3      L33:   0.6165 L12:   0.0721                                     
REMARK   3      L13:  -0.2981 L23:   0.2428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3723 S12:  -0.3608 S13:   0.4321                       
REMARK   3      S21:  -0.0919 S22:   0.3376 S23:   0.1673                       
REMARK   3      S31:  -0.1512 S32:  -0.1759 S33:   0.0037                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN E AND RESID 3:118)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8340   9.5917 -38.9540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1622 T22:   0.0079                                     
REMARK   3      T33:   0.1960 T12:  -0.1711                                     
REMARK   3      T13:  -0.0373 T23:   0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8288 L22:   0.1490                                     
REMARK   3      L33:   1.7631 L12:   0.0341                                     
REMARK   3      L13:  -0.2505 L23:   0.1907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1808 S12:   0.3369 S13:  -0.1623                       
REMARK   3      S21:  -0.1823 S22:   0.0007 S23:   0.1027                       
REMARK   3      S31:  -0.6607 S32:  -0.2079 S33:   0.0410                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 119:201)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7902  26.9079 -64.1769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2401 T22:   0.1421                                     
REMARK   3      T33:   0.1461 T12:  -0.1230                                     
REMARK   3      T13:   0.2787 T23:   0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5426 L22:   0.4590                                     
REMARK   3      L33:   0.7372 L12:   0.3972                                     
REMARK   3      L13:   0.2077 L23:   0.3514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3623 S12:   0.1794 S13:   0.1492                       
REMARK   3      S21:  -0.1977 S22:   0.1984 S23:   0.0178                       
REMARK   3      S31:  -1.4041 S32:   0.1472 S33:   0.0445                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 202:244)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5077  15.5320 -68.2193              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6140 T22:   0.1722                                     
REMARK   3      T33:   0.2518 T12:  -0.1494                                     
REMARK   3      T13:   0.2500 T23:  -0.1346                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6312 L22:   0.7188                                     
REMARK   3      L33:   1.2666 L12:  -0.4468                                     
REMARK   3      L13:   0.0519 L23:   0.2418                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1309 S12:   0.3413 S13:  -0.3321                       
REMARK   3      S21:  -0.3926 S22:   0.4428 S23:  -0.2556                       
REMARK   3      S31:  -1.3460 S32:   0.0314 S33:   0.0539                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 1:181)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  21.1665 -20.5905 -54.7557              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3337 T22:   0.0362                                     
REMARK   3      T33:   0.1321 T12:   0.1703                                     
REMARK   3      T13:  -0.0616 T23:   0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6654 L22:   1.0649                                     
REMARK   3      L33:   1.0244 L12:   0.6909                                     
REMARK   3      L13:  -0.2792 L23:  -0.4773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4104 S12:  -0.0261 S13:  -0.0858                       
REMARK   3      S21:  -0.6732 S22:   0.1475 S23:  -0.2311                       
REMARK   3      S31:   0.9677 S32:  -0.0235 S33:  -0.3315                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 182:275)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9000 -13.6209 -89.3465              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2388 T22:   0.3448                                     
REMARK   3      T33:   0.1496 T12:   0.0409                                     
REMARK   3      T13:   0.1002 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2497 L22:   0.2379                                     
REMARK   3      L33:   0.7364 L12:  -0.0537                                     
REMARK   3      L13:   0.0467 L23:   0.2516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1701 S12:  -0.1073 S13:   0.2164                       
REMARK   3      S21:  -0.3084 S22:   0.1998 S23:  -0.1352                       
REMARK   3      S31:   0.3538 S32:   0.2673 S33:   0.0001                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN G AND RESID 0:37)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4930  -5.3309 -73.2019              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0185 T22:   0.1689                                     
REMARK   3      T33:   0.1725 T12:   0.0103                                     
REMARK   3      T13:  -0.0231 T23:   0.0599                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6670 L22:   0.4426                                     
REMARK   3      L33:   1.7117 L12:   0.0845                                     
REMARK   3      L13:  -0.0685 L23:   0.1911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2151 S12:   0.1451 S13:  -0.2115                       
REMARK   3      S21:  -0.0493 S22:   0.1145 S23:   0.0030                       
REMARK   3      S31:  -0.2072 S32:  -0.1327 S33:   0.0212                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN G AND RESID 38:99)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5223  -1.9976 -73.4476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1539 T22:   0.1430                                     
REMARK   3      T33:   0.1160 T12:   0.0430                                     
REMARK   3      T13:   0.0044 T23:   0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6216 L22:   0.5633                                     
REMARK   3      L33:   0.7491 L12:  -0.0035                                     
REMARK   3      L13:   0.0488 L23:  -0.1573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1155 S12:   0.1760 S13:  -0.0272                       
REMARK   3      S21:  -0.0125 S22:  -0.0352 S23:   0.0049                       
REMARK   3      S31:  -0.3250 S32:  -0.0544 S33:  -0.0004                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 1:10)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  21.1179 -23.3691 -47.4896              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0041 T22:   0.1639                                     
REMARK   3      T33:   0.1854 T12:  -0.2313                                     
REMARK   3      T13:  -0.1532 T23:  -0.1291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2079 L22:   4.7266                                     
REMARK   3      L33:   0.2799 L12:   0.7297                                     
REMARK   3      L13:  -0.1614 L23:   0.0455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0175 S12:  -0.2900 S13:   0.1763                       
REMARK   3      S21:  -0.1837 S22:  -0.7717 S23:  -0.0594                       
REMARK   3      S31:   0.0504 S32:  -0.2666 S33:  -0.2650                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN I AND RESID 3:109)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7804 -44.2500 -31.3694              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4997 T22:  -0.2552                                     
REMARK   3      T33:   0.1394 T12:  -0.1150                                     
REMARK   3      T13:  -0.0192 T23:  -0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3751 L22:   0.9778                                     
REMARK   3      L33:   1.4216 L12:  -0.4037                                     
REMARK   3      L13:  -0.0733 L23:  -0.3892                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5454 S12:  -0.4147 S13:   0.0921                       
REMARK   3      S21:   0.1345 S22:   0.4009 S23:  -0.0549                       
REMARK   3      S31:   0.9771 S32:  -0.7028 S33:  -0.0132                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN I AND RESID 110:170)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0275 -52.3791  -1.6814              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3889 T22:   0.4618                                     
REMARK   3      T33:   0.5044 T12:   0.1494                                     
REMARK   3      T13:   0.2384 T23:  -0.1025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1352 L22:   0.1705                                     
REMARK   3      L33:   0.1127 L12:  -0.1409                                     
REMARK   3      L13:   0.0599 L23:  -0.0292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1648 S12:  -0.1460 S13:  -0.0435                       
REMARK   3      S21:   0.4665 S22:   0.3649 S23:   0.3719                       
REMARK   3      S31:  -0.2003 S32:   0.3076 S33:  -0.0001                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN I AND RESID 171:199)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7858 -59.2096   0.8830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1379 T22:   0.3704                                     
REMARK   3      T33:   0.7231 T12:   0.1098                                     
REMARK   3      T13:   0.2203 T23:   0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0570 L22:   0.0442                                     
REMARK   3      L33:   0.0249 L12:   0.0340                                     
REMARK   3      L13:  -0.0361 L23:  -0.0424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2889 S12:   0.3058 S13:  -0.3515                       
REMARK   3      S21:  -0.1884 S22:   0.5554 S23:  -0.1308                       
REMARK   3      S31:   0.4206 S32:   0.1198 S33:  -0.0003                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN J AND RESID 2:115)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5508 -25.0110 -27.9148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0588 T22:   0.3465                                     
REMARK   3      T33:   0.1427 T12:   0.0880                                     
REMARK   3      T13:  -0.0300 T23:  -0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6141 L22:   0.3594                                     
REMARK   3      L33:   1.6145 L12:   0.3274                                     
REMARK   3      L13:  -0.0954 L23:   0.3646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0161 S12:  -0.3702 S13:   0.2004                       
REMARK   3      S21:  -0.0609 S22:  -0.1722 S23:   0.1113                       
REMARK   3      S31:  -0.2053 S32:  -0.4689 S33:   0.0008                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: (CHAIN J AND RESID 116:204)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2241 -41.0261  -0.5981              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6570 T22:   0.3705                                     
REMARK   3      T33:   0.1694 T12:   0.1705                                     
REMARK   3      T13:   0.0444 T23:  -0.0631                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5759 L22:   0.7443                                     
REMARK   3      L33:   0.5764 L12:  -0.6092                                     
REMARK   3      L13:  -0.3562 L23:   0.2592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0649 S12:   0.1115 S13:  -0.0510                       
REMARK   3      S21:   0.1783 S22:   0.0359 S23:   0.0145                       
REMARK   3      S31:   1.0740 S32:   0.1896 S33:   0.0011                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: (CHAIN J AND RESID 205:244)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3728 -30.0551   1.4428              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3069 T22:   0.4838                                     
REMARK   3      T33:   0.0741 T12:   0.1169                                     
REMARK   3      T13:   0.0596 T23:  -0.0534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5126 L22:   0.9346                                     
REMARK   3      L33:   1.4666 L12:  -0.3067                                     
REMARK   3      L13:   0.1006 L23:   0.3059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3632 S12:  -0.2505 S13:   0.2538                       
REMARK   3      S21:   0.4329 S22:   0.4941 S23:  -0.1774                       
REMARK   3      S31:   0.9278 S32:  -0.0622 S33:   0.0443                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3UTT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-DEC-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000069199.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9778                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.15                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61204                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.579                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.925                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.73600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG3350, 0.2 M SODIUM CITRATE,   
REMARK 280  0.1 M BIS-TRIS PROPANE, PH 6.5, VAPOR DIFFUSION, TEMPERATURE 291K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, 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 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     ALA E     2                                                      
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    ASP A  29     -109.50     53.89                                   
REMARK 500    ASN A  86       76.20     47.02                                   
REMARK 500    LEU A 110      -83.62    -85.91                                   
REMARK 500    TYR A 123      -67.83   -101.33                                   
REMARK 500    ARG A 131      -27.67   -142.72                                   
REMARK 500    TRP A 133     -143.79   -138.99                                   
REMARK 500    ASP A 137     -166.90   -167.08                                   
REMARK 500    ALA A 193       79.86    -69.98                                   
REMARK 500    SER A 195     -135.40   -151.77                                   
REMARK 500    GLU A 212      109.79    -57.96                                   
REMARK 500    LEU A 230      113.17   -167.48                                   
REMARK 500    ASP A 238       17.53   -145.86                                   
REMARK 500    LYS A 243      110.93   -178.41                                   
REMARK 500    TRP A 274     -163.98     87.20                                   
REMARK 500    HIS B  31      135.90    172.88                                   
REMARK 500    SER B  57     -168.40   -116.12                                   
REMARK 500    TRP B  60       -8.91     70.59                                   
REMARK 500    PRO B  90      113.95    -39.43                                   
REMARK 500    ASP B  98       33.91    -91.97                                   
REMARK 500    ASP C   6      167.71    163.94                                   
REMARK 500    ALA C   8       53.48     72.11                                   
REMARK 500    LEU D  11      116.39     45.58                                   
REMARK 500    ASN D  27      102.69    175.66                                   
REMARK 500    SER D  28     -164.25    -59.49                                   
REMARK 500    ALA D  29      -42.23     76.76                                   
REMARK 500    PHE D  30      108.18    -46.99                                   
REMARK 500    SER D  40     -104.93     43.04                                   
REMARK 500    LEU D  47      -66.90   -108.75                                   
REMARK 500    SER D  52     -179.31   -175.02                                   
REMARK 500    SER D  53      141.72    -39.51                                   
REMARK 500    SER D  82     -120.15    -52.98                                   
REMARK 500    ASP D  83      -46.07     57.33                                   
REMARK 500    ALA D  85      177.82    173.64                                   
REMARK 500    ARG D  92     -163.40   -172.91                                   
REMARK 500    ASP D  94      -92.98     51.69                                   
REMARK 500    LYS D  98      106.24    -46.99                                   
REMARK 500    ASN D 115       79.99   -150.16                                   
REMARK 500    ARG D 124      106.43    -49.86                                   
REMARK 500    SER D 141       41.01    -76.43                                   
REMARK 500    GLN D 147     -150.46    -73.44                                   
REMARK 500    LYS D 149      -75.76    -70.76                                   
REMARK 500    ASP D 152       23.32    -76.74                                   
REMARK 500    ARG D 164     -169.58     56.56                                   
REMARK 500    SER D 165      -90.36     42.46                                   
REMARK 500    MET D 166       92.51    -64.22                                   
REMARK 500    ASP D 167       64.22    -63.00                                   
REMARK 500    SER D 177      151.02    175.62                                   
REMARK 500    PHE D 188       62.59   -109.68                                   
REMARK 500    ILE D 192       71.87    -68.92                                   
REMARK 500    ASN E  51       62.08     63.20                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     119 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UTP   RELATED DB: PDB                                   
REMARK 900 1E6 TCR SPECIFIC FOR HLA-A*0201-ALWGPDPAAA                           
REMARK 900 RELATED ID: 3UTQ   RELATED DB: PDB                                   
REMARK 900 HUMAN HLA-A*0201-ALWGPDPAAA                                          
REMARK 900 RELATED ID: 3UTS   RELATED DB: PDB                                   
REMARK 900 1E6-A*0201-ALWGPDPAAA COMPLEX, MONOCLINIC                            
DBREF  3UTT A    1   275  UNP    P01892   1A02_HUMAN      25    299             
DBREF  3UTT B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  3UTT C    1    10  UNP    P01308   INS_HUMAN       15     24             
DBREF  3UTT F    1   275  UNP    P01892   1A02_HUMAN      25    299             
DBREF  3UTT G    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  3UTT H    1    10  UNP    P01308   INS_HUMAN       15     24             
DBREF  3UTT D    3   201  PDB    3UTT     3UTT             3    201             
DBREF  3UTT I    3   201  PDB    3UTT     3UTT             3    201             
DBREF  3UTT E    2   246  PDB    3UTT     3UTT             2    246             
DBREF  3UTT J    2   246  PDB    3UTT     3UTT             2    246             
SEQADV 3UTT MET B    0  UNP  P61769              INITIATING METHIONINE          
SEQADV 3UTT MET G    0  UNP  P61769              INITIATING METHIONINE          
SEQRES   1 A  275  GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER          
SEQRES   2 A  275  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 A  275  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  275  ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 A  275  GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG          
SEQRES   6 A  275  LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU          
SEQRES   7 A  275  GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 A  275  SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  275  SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA          
SEQRES  10 A  275  TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU          
SEQRES  11 A  275  ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR          
SEQRES  12 A  275  LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU          
SEQRES  13 A  275  ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG          
SEQRES  14 A  275  ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR          
SEQRES  15 A  275  ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER          
SEQRES  16 A  275  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE          
SEQRES  17 A  275  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 A  275  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 A  275  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 A  275  VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 A  275  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 A  275  TRP GLU                                                      
SEQRES   1 B  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 B  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 B  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 B  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 B  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 B  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 B  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 B  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 C   10  ALA LEU TRP GLY PRO ASP PRO ALA ALA ALA                      
SEQRES   1 D  199  GLU VAL GLU GLN ASP PRO GLY PRO LEU SER VAL PRO GLU          
SEQRES   2 D  199  GLY ALA ILE VAL SER LEU ASN CYS THR TYR SER ASN SER          
SEQRES   3 D  199  ALA PHE GLN TYR PHE MET TRP TYR ARG GLN TYR SER ARG          
SEQRES   4 D  199  LYS GLY PRO GLU LEU LEU MET TYR THR TYR SER SER GLY          
SEQRES   5 D  199  ASN LYS GLU ASP GLY ARG PHE THR ALA GLN VAL ASP LYS          
SEQRES   6 D  199  SER SER LYS TYR ILE SER LEU PHE ILE ARG ASP SER GLN          
SEQRES   7 D  199  PRO SER ASP SER ALA THR TYR LEU CYS ALA MET ARG GLY          
SEQRES   8 D  199  ASP SER SER TYR LYS LEU ILE PHE GLY SER GLY THR ARG          
SEQRES   9 D  199  LEU LEU VAL ARG PRO ASP ILE GLN ASN PRO ASP PRO ALA          
SEQRES  10 D  199  VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER          
SEQRES  11 D  199  VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL          
SEQRES  12 D  199  SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS          
SEQRES  13 D  199  CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN          
SEQRES  14 D  199  SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS          
SEQRES  15 D  199  ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR          
SEQRES  16 D  199  PHE PHE PRO SER                                              
SEQRES   1 E  245  ALA GLY VAL ILE GLN SER PRO ARG HIS GLU VAL THR GLU          
SEQRES   2 E  245  MET GLY GLN GLN VAL THR LEU ARG CYS LYS PRO ILE SER          
SEQRES   3 E  245  GLY HIS ASP TYR LEU PHE TRP TYR ARG GLN THR MET MET          
SEQRES   4 E  245  ARG GLY LEU GLU LEU LEU ILE TYR PHE ASN ASN ASN VAL          
SEQRES   5 E  245  PRO ILE ASP ASP SER GLY MET PRO GLU ASP ARG PHE SER          
SEQRES   6 E  245  ALA LYS MET PRO ASN ALA SER PHE SER THR LEU LYS ILE          
SEQRES   7 E  245  GLN PRO SER GLU PRO ARG ASP SER ALA VAL TYR PHE CYS          
SEQRES   8 E  245  ALA SER SER LEU TRP GLU LYS LEU ALA LYS ASN ILE GLN          
SEQRES   9 E  245  TYR PHE GLY ALA GLY THR ARG LEU SER VAL LEU GLU ASP          
SEQRES  10 E  245  LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU          
SEQRES  11 E  245  PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR          
SEQRES  12 E  245  LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL          
SEQRES  13 E  245  GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER          
SEQRES  14 E  245  GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO          
SEQRES  15 E  245  ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU          
SEQRES  16 E  245  ARG VAL SER ALA THR PHE TRP GLN ASP PRO ARG ASN HIS          
SEQRES  17 E  245  PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN          
SEQRES  18 E  245  ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN          
SEQRES  19 E  245  ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP                  
SEQRES   1 F  275  GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER          
SEQRES   2 F  275  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 F  275  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 F  275  ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 F  275  GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG          
SEQRES   6 F  275  LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU          
SEQRES   7 F  275  GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 F  275  SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 F  275  SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA          
SEQRES  10 F  275  TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU          
SEQRES  11 F  275  ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR          
SEQRES  12 F  275  LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU          
SEQRES  13 F  275  ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG          
SEQRES  14 F  275  ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR          
SEQRES  15 F  275  ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER          
SEQRES  16 F  275  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE          
SEQRES  17 F  275  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 F  275  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 F  275  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 F  275  VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 F  275  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 F  275  TRP GLU                                                      
SEQRES   1 G  100  MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG          
SEQRES   2 G  100  HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS          
SEQRES   3 G  100  TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP          
SEQRES   4 G  100  LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS          
SEQRES   5 G  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU          
SEQRES   6 G  100  LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU          
SEQRES   7 G  100  TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO          
SEQRES   8 G  100  LYS ILE VAL LYS TRP ASP ARG ASP MET                          
SEQRES   1 H   10  ALA LEU TRP GLY PRO ASP PRO ALA ALA ALA                      
SEQRES   1 I  199  GLU VAL GLU GLN ASP PRO GLY PRO LEU SER VAL PRO GLU          
SEQRES   2 I  199  GLY ALA ILE VAL SER LEU ASN CYS THR TYR SER ASN SER          
SEQRES   3 I  199  ALA PHE GLN TYR PHE MET TRP TYR ARG GLN TYR SER ARG          
SEQRES   4 I  199  LYS GLY PRO GLU LEU LEU MET TYR THR TYR SER SER GLY          
SEQRES   5 I  199  ASN LYS GLU ASP GLY ARG PHE THR ALA GLN VAL ASP LYS          
SEQRES   6 I  199  SER SER LYS TYR ILE SER LEU PHE ILE ARG ASP SER GLN          
SEQRES   7 I  199  PRO SER ASP SER ALA THR TYR LEU CYS ALA MET ARG GLY          
SEQRES   8 I  199  ASP SER SER TYR LYS LEU ILE PHE GLY SER GLY THR ARG          
SEQRES   9 I  199  LEU LEU VAL ARG PRO ASP ILE GLN ASN PRO ASP PRO ALA          
SEQRES  10 I  199  VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER          
SEQRES  11 I  199  VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL          
SEQRES  12 I  199  SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS          
SEQRES  13 I  199  CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN          
SEQRES  14 I  199  SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS          
SEQRES  15 I  199  ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR          
SEQRES  16 I  199  PHE PHE PRO SER                                              
SEQRES   1 J  245  ALA GLY VAL ILE GLN SER PRO ARG HIS GLU VAL THR GLU          
SEQRES   2 J  245  MET GLY GLN GLN VAL THR LEU ARG CYS LYS PRO ILE SER          
SEQRES   3 J  245  GLY HIS ASP TYR LEU PHE TRP TYR ARG GLN THR MET MET          
SEQRES   4 J  245  ARG GLY LEU GLU LEU LEU ILE TYR PHE ASN ASN ASN VAL          
SEQRES   5 J  245  PRO ILE ASP ASP SER GLY MET PRO GLU ASP ARG PHE SER          
SEQRES   6 J  245  ALA LYS MET PRO ASN ALA SER PHE SER THR LEU LYS ILE          
SEQRES   7 J  245  GLN PRO SER GLU PRO ARG ASP SER ALA VAL TYR PHE CYS          
SEQRES   8 J  245  ALA SER SER LEU TRP GLU LYS LEU ALA LYS ASN ILE GLN          
SEQRES   9 J  245  TYR PHE GLY ALA GLY THR ARG LEU SER VAL LEU GLU ASP          
SEQRES  10 J  245  LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU          
SEQRES  11 J  245  PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR          
SEQRES  12 J  245  LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL          
SEQRES  13 J  245  GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER          
SEQRES  14 J  245  GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO          
SEQRES  15 J  245  ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU          
SEQRES  16 J  245  ARG VAL SER ALA THR PHE TRP GLN ASP PRO ARG ASN HIS          
SEQRES  17 J  245  PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN          
SEQRES  18 J  245  ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN          
SEQRES  19 J  245  ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP                  
FORMUL  11  HOH   *151(H2 O)                                                    
HELIX    1   1 GLY A   56  TYR A   85  1                                  30    
HELIX    2   2 ASP A  137  ALA A  149  1                                  13    
HELIX    3   3 HIS A  151  GLY A  162  1                                  12    
HELIX    4   4 GLY A  162  GLY A  175  1                                  14    
HELIX    5   5 GLY A  175  GLN A  180  1                                   6    
HELIX    6   6 GLN A  253  GLN A  255  5                                   3    
HELIX    7   7 GLU E   83  SER E   87  5                                   5    
HELIX    8   8 LEU E   96  LYS E  102  1                                   7    
HELIX    9   9 ASP E  118  VAL E  122  5                                   5    
HELIX   10  10 SER E  133  THR E  140  1                                   8    
HELIX   11  11 ALA E  200  GLN E  204  1                                   5    
HELIX   12  12 TRP F   51  GLU F   55  5                                   5    
HELIX   13  13 GLY F   56  TYR F   85  1                                  30    
HELIX   14  14 ASP F  137  ALA F  150  1                                  14    
HELIX   15  15 HIS F  151  GLY F  162  1                                  12    
HELIX   16  16 GLY F  162  GLY F  175  1                                  14    
HELIX   17  17 GLY F  175  GLN F  180  1                                   6    
HELIX   18  18 GLN F  253  GLN F  255  5                                   3    
HELIX   19  19 GLN I   80  SER I   84  5                                   5    
HELIX   20  20 ALA I  183  ALA I  187  5                                   5    
HELIX   21  21 GLU J   83  SER J   87  5                                   5    
HELIX   22  22 LEU J   96  ALA J  101  1                                   6    
HELIX   23  23 ASP J  118  VAL J  122  5                                   5    
HELIX   24  24 SER J  133  THR J  140  1                                   8    
HELIX   25  25 ALA J  200  GLN J  204  1                                   5    
SHEET    1   A 7 GLU A  46  PRO A  47  0                                        
SHEET    2   A 7 THR A  31  ASP A  37 -1  N  ARG A  35   O  GLU A  46           
SHEET    3   A 7 ARG A  21  VAL A  28 -1  N  GLY A  26   O  VAL A  34           
SHEET    4   A 7 HIS A   3  VAL A  12 -1  N  THR A  10   O  ILE A  23           
SHEET    5   A 7 THR A  94  VAL A 103 -1  O  VAL A  95   N  SER A  11           
SHEET    6   A 7 PHE A 109  TYR A 118 -1  O  ARG A 111   N  ASP A 102           
SHEET    7   A 7 LYS A 121  ALA A 125 -1  O  TYR A 123   N  TYR A 116           
SHEET    1   B 3 LYS A 186  HIS A 192  0                                        
SHEET    2   B 3 GLU A 198  LEU A 206 -1  O  THR A 200   N  HIS A 192           
SHEET    3   B 3 ALA A 245  PRO A 250 -1  O  ALA A 245   N  CYS A 203           
SHEET    1   C 4 GLU A 222  GLN A 224  0                                        
SHEET    2   C 4 THR A 214  ARG A 219 -1  N  ARG A 219   O  GLU A 222           
SHEET    3   C 4 TYR A 257  HIS A 263 -1  O  THR A 258   N  GLN A 218           
SHEET    4   C 4 LEU A 266  LEU A 272 -1  O  LEU A 272   N  CYS A 259           
SHEET    1   D 2 ARG A 234  PRO A 235  0                                        
SHEET    2   D 2 PHE A 241  GLN A 242 -1  O  GLN A 242   N  ARG A 234           
SHEET    1   E 4 LYS B   6  SER B  11  0                                        
SHEET    2   E 4 ASN B  21  PHE B  30 -1  O  SER B  28   N  LYS B   6           
SHEET    3   E 4 PHE B  62  PHE B  70 -1  O  LEU B  64   N  VAL B  27           
SHEET    4   E 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    1   F 4 LYS B   6  SER B  11  0                                        
SHEET    2   F 4 ASN B  21  PHE B  30 -1  O  SER B  28   N  LYS B   6           
SHEET    3   F 4 PHE B  62  PHE B  70 -1  O  LEU B  64   N  VAL B  27           
SHEET    4   F 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1   G 4 GLU B  44  ARG B  45  0                                        
SHEET    2   G 4 ILE B  35  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3   G 4 TYR B  78  HIS B  84 -1  O  ASN B  83   N  GLU B  36           
SHEET    4   G 4 LYS B  91  LYS B  94 -1  O  LYS B  91   N  VAL B  82           
SHEET    1   H 5 VAL D   4  GLN D   6  0                                        
SHEET    2   H 5 VAL D  19  TYR D  25 -1  O  THR D  24   N  GLU D   5           
SHEET    3   H 5 TYR D  71  ILE D  76 -1  O  LEU D  74   N  LEU D  21           
SHEET    4   H 5 PHE D  61  ASP D  66 -1  N  GLN D  64   O  SER D  73           
SHEET    5   H 5 GLY D  54  ASP D  58 -1  N  ASP D  58   O  PHE D  61           
SHEET    1   I 5 SER D  12  PRO D  14  0                                        
SHEET    2   I 5 THR D 105  ARG D 110  1  O  LEU D 108   N  VAL D  13           
SHEET    3   I 5 ALA D  85  GLY D  93 -1  N  TYR D  87   O  THR D 105           
SHEET    4   I 5 TYR D  32  GLN D  38 -1  N  TYR D  36   O  LEU D  88           
SHEET    5   I 5 GLU D  45  THR D  50 -1  O  LEU D  47   N  TRP D  35           
SHEET    1   J 4 SER D  12  PRO D  14  0                                        
SHEET    2   J 4 THR D 105  ARG D 110  1  O  LEU D 108   N  VAL D  13           
SHEET    3   J 4 ALA D  85  GLY D  93 -1  N  TYR D  87   O  THR D 105           
SHEET    4   J 4 SER D  96  PHE D 101 -1  O  ILE D 100   N  MET D  91           
SHEET    1   K 4 ALA D 119  LEU D 123  0                                        
SHEET    2   K 4 VAL D 133  PHE D 139 -1  O  LEU D 135   N  TYR D 121           
SHEET    3   K 4 LYS D 169  TRP D 176 -1  O  ALA D 175   N  CYS D 134           
SHEET    4   K 4 TYR D 154  ILE D 155 -1  N  TYR D 154   O  TRP D 176           
SHEET    1   L 4 ALA D 119  LEU D 123  0                                        
SHEET    2   L 4 VAL D 133  PHE D 139 -1  O  LEU D 135   N  TYR D 121           
SHEET    3   L 4 LYS D 169  TRP D 176 -1  O  ALA D 175   N  CYS D 134           
SHEET    4   L 4 CYS D 159  ASP D 162 -1  N  CYS D 159   O  SER D 172           
SHEET    1   M 4 ILE E   5  SER E   7  0                                        
SHEET    2   M 4 VAL E  19  LYS E  24 -1  O  ARG E  22   N  SER E   7           
SHEET    3   M 4 PHE E  74  ILE E  79 -1  O  SER E  75   N  CYS E  23           
SHEET    4   M 4 PHE E  65  ASN E  71 -1  N  LYS E  68   O  THR E  76           
SHEET    1   N 6 HIS E  10  GLU E  14  0                                        
SHEET    2   N 6 THR E 111  LEU E 116  1  O  SER E 114   N  GLU E  11           
SHEET    3   N 6 ALA E  88  SER E  95 -1  N  ALA E  88   O  LEU E 113           
SHEET    4   N 6 TYR E  31  GLN E  37 -1  N  TYR E  35   O  PHE E  91           
SHEET    5   N 6 GLU E  44  ASN E  50 -1  O  LEU E  46   N  TRP E  34           
SHEET    6   N 6 VAL E  53  ASP E  56 -1  O  VAL E  53   N  ASN E  50           
SHEET    1   O 4 HIS E  10  GLU E  14  0                                        
SHEET    2   O 4 THR E 111  LEU E 116  1  O  SER E 114   N  GLU E  11           
SHEET    3   O 4 ALA E  88  SER E  95 -1  N  ALA E  88   O  LEU E 113           
SHEET    4   O 4 TYR E 106  PHE E 107 -1  O  TYR E 106   N  SER E  94           
SHEET    1   P 3 LYS E 142  VAL E 146  0                                        
SHEET    2   P 3 SER E 194  SER E 199 -1  O  VAL E 198   N  ALA E 143           
SHEET    3   P 3 VAL E 172  THR E 174 -1  N  CYS E 173   O  ARG E 195           
SHEET    1   Q 4 LYS E 166  GLU E 167  0                                        
SHEET    2   Q 4 VAL E 157  VAL E 163 -1  N  VAL E 163   O  LYS E 166           
SHEET    3   Q 4 HIS E 209  PHE E 216 -1  O  ARG E 211   N  TRP E 162           
SHEET    4   Q 4 GLN E 235  TRP E 242 -1  O  ALA E 239   N  CYS E 212           
SHEET    1   R 2 LEU E 179  LYS E 180  0                                        
SHEET    2   R 2 TYR E 190  ALA E 191 -1  O  ALA E 191   N  LEU E 179           
SHEET    1   S 8 GLU F  46  PRO F  47  0                                        
SHEET    2   S 8 THR F  31  ASP F  37 -1  N  ARG F  35   O  GLU F  46           
SHEET    3   S 8 ARG F  21  VAL F  28 -1  N  GLY F  26   O  VAL F  34           
SHEET    4   S 8 HIS F   3  VAL F  12 -1  N  ARG F   6   O  TYR F  27           
SHEET    5   S 8 THR F  94  VAL F 103 -1  O  ARG F  97   N  PHE F   9           
SHEET    6   S 8 PHE F 109  TYR F 118 -1  O  GLN F 115   N  MET F  98           
SHEET    7   S 8 LYS F 121  LEU F 126 -1  O  LEU F 126   N  HIS F 114           
SHEET    8   S 8 TRP F 133  ALA F 135 -1  O  THR F 134   N  ALA F 125           
SHEET    1   T 4 LYS F 186  ALA F 193  0                                        
SHEET    2   T 4 GLU F 198  PHE F 208 -1  O  TRP F 204   N  HIS F 188           
SHEET    3   T 4 PHE F 241  PRO F 250 -1  O  VAL F 249   N  ALA F 199           
SHEET    4   T 4 ARG F 234  PRO F 235 -1  N  ARG F 234   O  GLN F 242           
SHEET    1   U 4 GLU F 222  ASP F 223  0                                        
SHEET    2   U 4 THR F 214  ARG F 219 -1  N  ARG F 219   O  GLU F 222           
SHEET    3   U 4 TYR F 257  GLN F 262 -1  O  THR F 258   N  GLN F 218           
SHEET    4   U 4 LEU F 270  LEU F 272 -1  O  LEU F 272   N  CYS F 259           
SHEET    1   V 4 VAL G   9  SER G  11  0                                        
SHEET    2   V 4 ASN G  21  PHE G  30 -1  O  ASN G  24   N  TYR G  10           
SHEET    3   V 4 PHE G  62  PHE G  70 -1  O  TYR G  66   N  CYS G  25           
SHEET    4   V 4 GLU G  50  HIS G  51 -1  N  GLU G  50   O  TYR G  67           
SHEET    1   W 4 VAL G   9  SER G  11  0                                        
SHEET    2   W 4 ASN G  21  PHE G  30 -1  O  ASN G  24   N  TYR G  10           
SHEET    3   W 4 PHE G  62  PHE G  70 -1  O  TYR G  66   N  CYS G  25           
SHEET    4   W 4 SER G  55  PHE G  56 -1  N  SER G  55   O  TYR G  63           
SHEET    1   X 4 GLU G  44  ARG G  45  0                                        
SHEET    2   X 4 ILE G  35  LYS G  41 -1  N  LYS G  41   O  GLU G  44           
SHEET    3   X 4 TYR G  78  HIS G  84 -1  O  ALA G  79   N  LEU G  40           
SHEET    4   X 4 LYS G  91  LYS G  94 -1  O  LYS G  91   N  VAL G  82           
SHEET    1   Y 5 VAL I   4  GLN I   6  0                                        
SHEET    2   Y 5 VAL I  19  TYR I  25 -1  O  THR I  24   N  GLU I   5           
SHEET    3   Y 5 TYR I  71  ILE I  76 -1  O  ILE I  72   N  CYS I  23           
SHEET    4   Y 5 PHE I  61  ASP I  66 -1  N  GLN I  64   O  SER I  73           
SHEET    5   Y 5 ASN I  55  ASP I  58 -1  N  ASP I  58   O  PHE I  61           
SHEET    1   Z 5 SER I  12  PRO I  14  0                                        
SHEET    2   Z 5 THR I 105  ARG I 110  1  O  LEU I 108   N  VAL I  13           
SHEET    3   Z 5 ALA I  85  ARG I  92 -1  N  ALA I  85   O  LEU I 107           
SHEET    4   Z 5 TYR I  32  GLN I  38 -1  N  MET I  34   O  ALA I  90           
SHEET    5   Z 5 GLU I  45  THR I  50 -1  O  THR I  50   N  PHE I  33           
SHEET    1  AA 4 SER I  12  PRO I  14  0                                        
SHEET    2  AA 4 THR I 105  ARG I 110  1  O  LEU I 108   N  VAL I  13           
SHEET    3  AA 4 ALA I  85  ARG I  92 -1  N  ALA I  85   O  LEU I 107           
SHEET    4  AA 4 LEU I  99  PHE I 101 -1  O  ILE I 100   N  MET I  91           
SHEET    1  AB 4 ALA I 119  VAL I 120  0                                        
SHEET    2  AB 4 CYS I 134  PHE I 139 -1  O  THR I 137   N  ALA I 119           
SHEET    3  AB 4 ASN I 171  TRP I 176 -1  O  ALA I 173   N  PHE I 136           
SHEET    4  AB 4 TYR I 154  THR I 156 -1  N  TYR I 154   O  TRP I 176           
SHEET    1  AC 2 ARG I 124  ASP I 125  0                                        
SHEET    2  AC 2 PHE J 130  GLU J 131 -1  O  GLU J 131   N  ARG I 124           
SHEET    1  AD 4 ILE J   5  SER J   7  0                                        
SHEET    2  AD 4 LEU J  21  LYS J  24 -1  O  ARG J  22   N  SER J   7           
SHEET    3  AD 4 PHE J  74  ILE J  79 -1  O  LEU J  77   N  LEU J  21           
SHEET    4  AD 4 PHE J  65  ASN J  71 -1  N  SER J  66   O  LYS J  78           
SHEET    1  AE 6 HIS J  10  GLU J  14  0                                        
SHEET    2  AE 6 THR J 111  LEU J 116  1  O  SER J 114   N  GLU J  11           
SHEET    3  AE 6 ALA J  88  SER J  95 -1  N  TYR J  90   O  THR J 111           
SHEET    4  AE 6 TYR J  31  GLN J  37 -1  N  PHE J  33   O  ALA J  93           
SHEET    5  AE 6 LEU J  43  ASN J  50 -1  O  GLU J  44   N  ARG J  36           
SHEET    6  AE 6 VAL J  53  ASP J  56 -1  O  VAL J  53   N  ASN J  50           
SHEET    1  AF 4 HIS J  10  GLU J  14  0                                        
SHEET    2  AF 4 THR J 111  LEU J 116  1  O  SER J 114   N  GLU J  11           
SHEET    3  AF 4 ALA J  88  SER J  95 -1  N  TYR J  90   O  THR J 111           
SHEET    4  AF 4 TYR J 106  PHE J 107 -1  O  TYR J 106   N  SER J  94           
SHEET    1  AG 3 LYS J 142  PHE J 152  0                                        
SHEET    2  AG 3 TYR J 190  SER J 199 -1  O  VAL J 198   N  ALA J 143           
SHEET    3  AG 3 VAL J 172  THR J 174 -1  N  CYS J 173   O  ARG J 195           
SHEET    1  AH 3 LYS J 142  PHE J 152  0                                        
SHEET    2  AH 3 TYR J 190  SER J 199 -1  O  VAL J 198   N  ALA J 143           
SHEET    3  AH 3 LEU J 179  LYS J 180 -1  N  LEU J 179   O  ALA J 191           
SHEET    1  AI 4 LYS J 166  VAL J 168  0                                        
SHEET    2  AI 4 VAL J 157  VAL J 163 -1  N  VAL J 163   O  LYS J 166           
SHEET    3  AI 4 HIS J 209  PHE J 216 -1  O  GLN J 213   N  SER J 160           
SHEET    4  AI 4 GLN J 235  TRP J 242 -1  O  GLN J 235   N  PHE J 216           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.03  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.04  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
SSBOND   4 CYS D   23    CYS D   89                          1555   1555  2.03  
SSBOND   5 CYS D  134    CYS D  184                          1555   1555  2.03  
SSBOND   6 CYS D  159    CYS E  173                          1555   1555  2.03  
SSBOND   7 CYS E   23    CYS E   92                          1555   1555  2.02  
SSBOND   8 CYS E  147    CYS E  212                          1555   1555  2.03  
SSBOND   9 CYS F  101    CYS F  164                          1555   1555  2.03  
SSBOND  10 CYS F  203    CYS F  259                          1555   1555  2.04  
SSBOND  11 CYS G   25    CYS G   80                          1555   1555  2.03  
SSBOND  12 CYS I   23    CYS I   89                          1555   1555  2.03  
SSBOND  13 CYS I  134    CYS I  184                          1555   1555  2.03  
SSBOND  14 CYS I  159    CYS J  173                          1555   1555  2.03  
SSBOND  15 CYS J   23    CYS J   92                          1555   1555  2.03  
SSBOND  16 CYS J  147    CYS J  212                          1555   1555  2.03  
CISPEP   1 TYR A  209    PRO A  210          0        -0.10                     
CISPEP   2 HIS B   31    PRO B   32          0         2.79                     
CISPEP   3 GLY C    4    PRO C    5          0        -0.07                     
CISPEP   4 PRO C    7    ALA C    8          0        13.88                     
CISPEP   5 SER E    7    PRO E    8          0        -2.24                     
CISPEP   6 TYR E  153    PRO E  154          0         2.58                     
CISPEP   7 TYR F  209    PRO F  210          0         3.32                     
CISPEP   8 HIS G   31    PRO G   32          0         2.09                     
CISPEP   9 GLY H    4    PRO H    5          0        -4.69                     
CISPEP  10 PRO H    7    ALA H    8          0        13.87                     
CISPEP  11 PRO I    8    GLY I    9          0         0.05                     
CISPEP  12 ASP I   94    SER I   95          0         6.28                     
CISPEP  13 SER J    7    PRO J    8          0         0.27                     
CISPEP  14 TYR J  153    PRO J  154          0        -1.23                     
CRYST1   41.480   98.440  121.300  97.27  98.16  93.38 P 1           2          
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      0.024108  0.001422  0.003684        0.00000                         
SCALE2      0.000000  0.010176  0.001402        0.00000                         
SCALE3      0.000000  0.000000  0.008407        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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