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Database: PDB
Entry: 5IWL
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HEADER    CELL ADHESION                           22-MAR-16   5IWL              
TITLE     CD47-DIABODY COMPLEX                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5F9 DIABODY;                                               
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: LEUKOCYTE SURFACE ANTIGEN CD47;                            
COMPND   7 CHAIN: C, D;                                                         
COMPND   8 FRAGMENT: EXTRACELLULAR DOMAIN (UNP RESIDUES 19-132);                
COMPND   9 SYNONYM: ANTIGENIC SURFACE DETERMINANT PROTEIN OA3,INTEGRIN-         
COMPND  10 ASSOCIATED PROTEIN,IAP,PROTEIN MER6;                                 
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: CD47, MER6;                                                    
SOURCE  14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    RECEPTOR, DIABODY, COMPLEX, CELL ADHESION                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.DI,K.M.JUDE,K.C.GARCIA                                              
REVDAT   3   19-FEB-20 5IWL    1       JRNL   REMARK SEQRES                     
REVDAT   2   13-JUL-16 5IWL    1       JRNL                                     
REVDAT   1   29-JUN-16 5IWL    0                                                
JRNL        AUTH   K.WEISKOPF,N.S.JAHCHAN,P.J.SCHNORR,S.CRISTEA,A.M.RING,       
JRNL        AUTH 2 R.L.MAUTE,A.K.VOLKMER,J.P.VOLKMER,J.LIU,J.S.LIM,D.YANG,      
JRNL        AUTH 3 G.SEITZ,T.NGUYEN,D.WU,K.JUDE,H.GUERSTON,A.BARKAL,F.TRAPANI,  
JRNL        AUTH 4 J.GEORGE,J.T.POIRIER,E.E.GARDNER,L.A.MILES,E.DE STANCHINA,   
JRNL        AUTH 5 S.M.LOFGREN,H.VOGEL,M.M.WINSLOW,C.DIVE,R.K.THOMAS,C.M.RUDIN, 
JRNL        AUTH 6 M.VAN DE RIJN,R.MAJETI,K.C.GARCIA,I.L.WEISSMAN,J.SAGE        
JRNL        TITL   CD47-BLOCKING IMMUNOTHERAPIES STIMULATE MACROPHAGE-MEDIATED  
JRNL        TITL 2 DESTRUCTION OF SMALL-CELL LUNG CANCER.                       
JRNL        REF    J.CLIN.INVEST.                V. 126  2610 2016              
JRNL        REFN                   ISSN 0021-9738                               
JRNL        PMID   27294525                                                     
JRNL        DOI    10.1172/JCI81603                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10 R2155                                    
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20382                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.370                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1299                            
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 44.7272 -  5.8208    0.99     2238   150  0.1959 0.2182        
REMARK   3     2  5.8208 -  4.6216    1.00     2149   145  0.1748 0.2243        
REMARK   3     3  4.6216 -  4.0379    1.00     2121   150  0.1827 0.2530        
REMARK   3     4  4.0379 -  3.6689    1.00     2125   142  0.2167 0.2605        
REMARK   3     5  3.6689 -  3.4060    1.00     2090   139  0.2350 0.2761        
REMARK   3     6  3.4060 -  3.2053    1.00     2096   145  0.2653 0.3477        
REMARK   3     7  3.2053 -  3.0448    1.00     2103   145  0.2900 0.3395        
REMARK   3     8  3.0448 -  2.9123    1.00     2092   139  0.3061 0.3207        
REMARK   3     9  2.9123 -  2.8002    1.00     2069   144  0.3434 0.3368        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.330           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           5488                                  
REMARK   3   ANGLE     :  0.617           7479                                  
REMARK   3   CHIRALITY :  0.046            851                                  
REMARK   3   PLANARITY :  0.004            955                                  
REMARK   3   DIHEDRAL  : 12.122           3197                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 125 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5800  23.6659  -0.1524              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4941 T22:   0.2528                                     
REMARK   3      T33:   0.4866 T12:  -0.0087                                     
REMARK   3      T13:  -0.0803 T23:   0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9180 L22:   1.9594                                     
REMARK   3      L33:   4.8413 L12:   2.0577                                     
REMARK   3      L13:  -1.0418 L23:  -0.4111                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1693 S12:  -0.1649 S13:   0.2169                       
REMARK   3      S21:  -0.0053 S22:  -0.0984 S23:  -0.1373                       
REMARK   3      S31:  -0.1409 S32:   0.0416 S33:   0.2414                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 126 THROUGH 233 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.6579  25.8397  11.4597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7151 T22:   0.4426                                     
REMARK   3      T33:   0.6513 T12:  -0.0966                                     
REMARK   3      T13:   0.2201 T23:  -0.0882                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1932 L22:   5.1406                                     
REMARK   3      L33:   3.1590 L12:  -0.0221                                     
REMARK   3      L13:  -1.1425 L23:  -0.8112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5105 S12:   0.2651 S13:  -0.8645                       
REMARK   3      S21:  -0.5891 S22:   0.3617 S23:  -0.3335                       
REMARK   3      S31:   0.8067 S32:   0.3512 S33:   0.1059                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 125 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8411  35.5639  22.3254              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3916 T22:   0.3282                                     
REMARK   3      T33:   0.3793 T12:  -0.0469                                     
REMARK   3      T13:   0.0562 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3115 L22:   1.6318                                     
REMARK   3      L33:   2.0526 L12:   2.0656                                     
REMARK   3      L13:  -0.2493 L23:  -0.4684                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0542 S12:   0.0304 S13:   0.0623                       
REMARK   3      S21:  -0.0666 S22:   0.0426 S23:   0.0566                       
REMARK   3      S31:   0.0536 S32:   0.1177 S33:   0.0468                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 126 THROUGH 233 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.8562   4.7146  10.9803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7301 T22:   0.3010                                     
REMARK   3      T33:   0.5424 T12:   0.0323                                     
REMARK   3      T13:   0.0317 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9938 L22:   2.2639                                     
REMARK   3      L33:   3.0009 L12:  -1.1751                                     
REMARK   3      L13:  -0.0446 L23:  -1.3786                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0415 S12:   0.1479 S13:  -0.4060                       
REMARK   3      S21:  -0.6477 S22:  -0.1820 S23:   0.0802                       
REMARK   3      S31:   1.1297 S32:   0.2635 S33:   0.2222                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 8 )                     
REMARK   3    ORIGIN FOR THE GROUP (A): -55.2435  22.0231   9.5697              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4731 T22:   1.0652                                     
REMARK   3      T33:   0.7015 T12:   0.1721                                     
REMARK   3      T13:   0.1529 T23:   0.3259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9160 L22:   1.7896                                     
REMARK   3      L33:   4.5301 L12:  -2.9435                                     
REMARK   3      L13:  -4.7190 L23:   2.8625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2315 S12:  -0.3537 S13:   0.2601                       
REMARK   3      S21:   0.4811 S22:   0.8810 S23:   0.9966                       
REMARK   3      S31:  -0.6333 S32:  -1.0377 S33:  -0.8378                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 9 THROUGH 21 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -70.1200  16.7613  21.2029              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4748 T22:   1.3274                                     
REMARK   3      T33:   0.7931 T12:  -0.0791                                     
REMARK   3      T13:  -0.0060 T23:   0.3504                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1564 L22:   8.4004                                     
REMARK   3      L33:   7.5889 L12:   2.6323                                     
REMARK   3      L13:   1.1027 L23:   1.7064                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1704 S12:   0.2709 S13:   1.1147                       
REMARK   3      S21:   0.6170 S22:   0.7774 S23:   1.6444                       
REMARK   3      S31:   0.2201 S32:  -2.4501 S33:  -1.0573                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 22 THROUGH 36 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -52.8675  11.0019   4.9160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5809 T22:   0.9196                                     
REMARK   3      T33:   0.5804 T12:  -0.3060                                     
REMARK   3      T13:  -0.0881 T23:   0.1911                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5491 L22:   3.3664                                     
REMARK   3      L33:   8.7240 L12:   1.9625                                     
REMARK   3      L13:  -3.2879 L23:  -5.4428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2348 S12:   0.9298 S13:   0.2208                       
REMARK   3      S21:  -1.2076 S22:   0.0871 S23:   0.0253                       
REMARK   3      S31:   0.9129 S32:  -2.2713 S33:   0.4544                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 37 THROUGH 58 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -52.3273   7.1049  18.8486              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6452 T22:   0.3606                                     
REMARK   3      T33:   0.4527 T12:  -0.0858                                     
REMARK   3      T13:  -0.0222 T23:   0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6174 L22:   5.2186                                     
REMARK   3      L33:   8.3608 L12:  -6.0806                                     
REMARK   3      L13:  -5.5363 L23:   1.9846                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1786 S12:  -0.0518 S13:   0.4468                       
REMARK   3      S21:  -0.2519 S22:   0.5027 S23:  -0.9323                       
REMARK   3      S31:   0.4739 S32:   0.0166 S33:  -0.3251                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 59 THROUGH 79 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -59.4632   7.4098  15.8411              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5647 T22:   0.8797                                     
REMARK   3      T33:   0.3994 T12:  -0.1287                                     
REMARK   3      T13:  -0.1421 T23:  -0.0447                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1303 L22:   5.2222                                     
REMARK   3      L33:   2.6945 L12:  -0.6177                                     
REMARK   3      L13:   0.0631 L23:  -3.5990                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5446 S12:   0.8404 S13:  -0.0109                       
REMARK   3      S21:  -0.4896 S22:   1.0016 S23:   0.6109                       
REMARK   3      S31:  -0.3990 S32:  -1.5365 S33:  -0.6110                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 80 THROUGH 89 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -65.7822  11.3122  25.1110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5634 T22:   0.5418                                     
REMARK   3      T33:   0.6104 T12:  -0.0646                                     
REMARK   3      T13:  -0.0256 T23:   0.1058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3043 L22:   8.4334                                     
REMARK   3      L33:   3.9181 L12:  -1.5647                                     
REMARK   3      L13:  -1.0800 L23:   5.7436                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3402 S12:   0.1429 S13:   0.0561                       
REMARK   3      S21:   0.8296 S22:   0.8389 S23:  -0.4110                       
REMARK   3      S31:   0.2074 S32:  -0.1200 S33:  -1.1455                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 90 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -52.6087  14.8502  16.9790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4545 T22:   0.4666                                     
REMARK   3      T33:   0.5555 T12:   0.0192                                     
REMARK   3      T13:  -0.0951 T23:   0.0652                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5360 L22:   4.2052                                     
REMARK   3      L33:   9.0257 L12:  -3.0261                                     
REMARK   3      L13:  -4.4346 L23:   4.2056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2018 S12:   0.7036 S13:   0.4637                       
REMARK   3      S21:  -0.3337 S22:  -0.0652 S23:   0.0490                       
REMARK   3      S31:  -0.4685 S32:  -1.2593 S33:  -0.1763                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 103 THROUGH 114 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -56.7614  20.0970  17.7973              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5537 T22:   0.6120                                     
REMARK   3      T33:   0.5842 T12:   0.1113                                     
REMARK   3      T13:  -0.0018 T23:   0.1613                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9042 L22:   1.7662                                     
REMARK   3      L33:   7.5800 L12:   0.9045                                     
REMARK   3      L13:  -2.7806 L23:   0.1472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4653 S12:  -0.0719 S13:   1.1807                       
REMARK   3      S21:   0.2391 S22:   0.6421 S23:   0.0171                       
REMARK   3      S31:  -0.1203 S32:  -0.6141 S33:  -0.9093                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 8 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):   8.6848  58.0958  12.7069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5697 T22:   0.5168                                     
REMARK   3      T33:   0.4123 T12:   0.1684                                     
REMARK   3      T13:   0.0267 T23:  -0.1061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9676 L22:   5.3194                                     
REMARK   3      L33:   5.2934 L12:  -2.0371                                     
REMARK   3      L13:   2.1050 L23:  -3.5424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2351 S12:  -0.1836 S13:   0.1837                       
REMARK   3      S21:   0.1180 S22:   0.3242 S23:  -0.4601                       
REMARK   3      S31:  -0.1727 S32:  -0.2804 S33:  -0.3002                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 9 THROUGH 21 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  21.1300  67.6365   0.9079              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6800 T22:   0.4108                                     
REMARK   3      T33:   0.6008 T12:  -0.0593                                     
REMARK   3      T13:   0.1566 T23:   0.0523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6358 L22:   6.1058                                     
REMARK   3      L33:   3.0283 L12:  -5.0694                                     
REMARK   3      L13:   1.4373 L23:   1.3672                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0206 S12:   0.1796 S13:   1.5619                       
REMARK   3      S21:   0.1916 S22:   0.5476 S23:   0.2207                       
REMARK   3      S31:  -1.1011 S32:   0.3964 S33:  -0.6934                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 22 THROUGH 32 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0384  52.4593  17.5271              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3270 T22:   0.5573                                     
REMARK   3      T33:   0.6294 T12:  -0.0613                                     
REMARK   3      T13:   0.1261 T23:  -0.0501                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5332 L22:   8.3270                                     
REMARK   3      L33:   2.4497 L12:  -0.7878                                     
REMARK   3      L13:   1.2042 L23:   1.6359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8419 S12:  -0.1817 S13:  -0.3625                       
REMARK   3      S21:   0.5057 S22:  -0.3589 S23:   0.4127                       
REMARK   3      S31:  -0.0419 S32:   1.1311 S33:  -0.6350                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 33 THROUGH 58 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3734  46.9536   4.9869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2911 T22:   0.4592                                     
REMARK   3      T33:   0.4809 T12:   0.0009                                     
REMARK   3      T13:   0.0841 T23:  -0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3681 L22:   7.7234                                     
REMARK   3      L33:   6.7008 L12:  -1.0463                                     
REMARK   3      L13:  -1.1437 L23:  -4.0184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3339 S12:  -0.1834 S13:  -0.3680                       
REMARK   3      S21:   0.1838 S22:   0.2268 S23:   0.1137                       
REMARK   3      S31:   0.2184 S32:  -0.4862 S33:   0.0679                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 59 THROUGH 79 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1617  53.6847   6.7039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3685 T22:   0.3154                                     
REMARK   3      T33:   0.4816 T12:  -0.0133                                     
REMARK   3      T13:  -0.0897 T23:   0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8368 L22:   2.3625                                     
REMARK   3      L33:   3.0453 L12:  -0.6541                                     
REMARK   3      L13:  -4.0864 L23:  -0.0864                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2413 S12:  -0.0621 S13:   0.3936                       
REMARK   3      S21:  -0.1613 S22:   0.1371 S23:  -0.1264                       
REMARK   3      S31:  -0.0339 S32:   0.6117 S33:  -0.7182                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 80 THROUGH 89 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  23.2103  61.0372  -2.4689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4232 T22:   0.4434                                     
REMARK   3      T33:   0.3791 T12:  -0.0264                                     
REMARK   3      T13:   0.0957 T23:   0.0707                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7441 L22:   5.5341                                     
REMARK   3      L33:   3.1087 L12:   2.1783                                     
REMARK   3      L13:   3.6055 L23:   0.4220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8190 S12:  -1.0028 S13:  -0.8870                       
REMARK   3      S21:   0.0427 S22:  -0.1727 S23:  -0.5754                       
REMARK   3      S31:  -0.1764 S32:  -0.9878 S33:  -0.7501                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 90 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9527  52.1735   5.1104              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3425 T22:   0.4486                                     
REMARK   3      T33:   0.4451 T12:   0.0890                                     
REMARK   3      T13:   0.0114 T23:   0.0173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7057 L22:   3.5466                                     
REMARK   3      L33:   4.4292 L12:   1.8327                                     
REMARK   3      L13:  -1.9580 L23:  -0.1909                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0481 S12:   0.1056 S13:   0.2517                       
REMARK   3      S21:   0.1077 S22:   0.6277 S23:   0.6403                       
REMARK   3      S31:  -0.2951 S32:   0.1295 S33:  -0.7883                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 103 THROUGH 114 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8755  58.9101   4.1182              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4467 T22:   0.3931                                     
REMARK   3      T33:   0.4271 T12:  -0.0010                                     
REMARK   3      T13:   0.0827 T23:  -0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4316 L22:   5.2947                                     
REMARK   3      L33:   9.7173 L12:   3.8385                                     
REMARK   3      L13:  -3.6882 L23:  -5.5401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1400 S12:   0.1993 S13:   0.5842                       
REMARK   3      S21:  -0.4699 S22:   0.4783 S23:   0.5086                       
REMARK   3      S31:   0.3837 S32:  -0.1681 S33:  -0.5053                       
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 5IWL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217168.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.127085                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS JUNE 17, 2015                  
REMARK 200  DATA SCALING SOFTWARE          : XDS JUNE 17, 2015                  
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20405                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
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) : 2.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.80                              
REMARK 200  R MERGE FOR SHELL          (I) : 2.56200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.950                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE PH 6.0, 17% PEG        
REMARK 280  4000, VAPOR DIFFUSION, TEMPERATURE 295K                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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       87.42000            
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       43.71000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       43.71000            
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       87.42000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS B   234                                                      
REMARK 465     LYS A   234                                                      
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     LYS B  65    CG   CD   CE   NZ                                   
REMARK 470     ASP B 187    CG   OD1  OD2                                       
REMARK 470     LYS B 201    CG   CD   CE   NZ                                   
REMARK 470     ARG B 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 206    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 208    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  65    CG   CD   CE   NZ                                   
REMARK 470     ASP A 187    CG   OD1  OD2                                       
REMARK 470     LYS A 201    CG   CD   CE   NZ                                   
REMARK 470     ARG A 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 208    CG   CD   OE1  OE2                                  
REMARK 470     LYS C   6    CG   CD   CE   NZ                                   
REMARK 470     LYS C   8    CG   CD   CE   NZ                                   
REMARK 470     GLN C  31    CG   CD   OE1  NE2                                  
REMARK 470     LYS C  43    CG   CD   CE   NZ                                   
REMARK 470     LYS C  67    CG   CD   CE   NZ                                   
REMARK 470     GLU C  69    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  75    CG   CD   CE   NZ                                   
REMARK 470     LYS C  81    CG   CD   CE   NZ                                   
REMARK 470     LYS C  84    CG   CD   CE   NZ                                   
REMARK 470     LYS C 112    CG   CD   CE   NZ                                   
REMARK 470     ARG C 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D   6    CG   CD   CE   NZ                                   
REMARK 470     LYS D   8    CG   CD   CE   NZ                                   
REMARK 470     GLN D  31    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  43    CG   CD   CE   NZ                                   
REMARK 470     LYS D  67    CG   CD   CE   NZ                                   
REMARK 470     LYS D  84    CG   CD   CE   NZ                                   
REMARK 470     ARG D 114    CG   CD   NE   CZ   NH1  NH2                        
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    GLN B  43     -168.16   -120.58                                   
REMARK 500    ASP B 105      -71.23   -119.19                                   
REMARK 500    SER B 116     -163.19    -77.90                                   
REMARK 500    LEU B 174      -66.02   -108.22                                   
REMARK 500    VAL B 178      -51.07     70.62                                   
REMARK 500    PHE B 182     -168.73    -79.08                                   
REMARK 500    THR A  91      107.74    -57.45                                   
REMARK 500    ASP A 105      -63.03   -120.47                                   
REMARK 500    SER A 116     -130.77    -85.50                                   
REMARK 500    TYR A 159       55.89    -92.13                                   
REMARK 500    VAL A 178      -52.46     67.73                                   
REMARK 500    SER A 183      -72.44    -65.28                                   
REMARK 500    GLU C  29       27.02   -140.46                                   
REMARK 500    PHE C  63       55.69   -113.06                                   
REMARK 500    LEU C 101     -113.16     57.26                                   
REMARK 500    GLU D  29       23.49   -144.72                                   
REMARK 500    PHE D  63       54.44   -118.17                                   
REMARK 500    LEU D 101     -127.35     53.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 201 bound   
REMARK 800  to ASN C 16                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 202 bound   
REMARK 800  to ASN C 32                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 203 bound   
REMARK 800  to ASN C 93                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 202 bound   
REMARK 800  to ASN D 16                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 201 bound   
REMARK 800  to ASN D 32                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 203 bound   
REMARK 800  to ASN D 93                                                         
DBREF  5IWL B    1   234  PDB    5IWL     5IWL             1    234             
DBREF  5IWL A    1   234  PDB    5IWL     5IWL             1    234             
DBREF  5IWL C    1   114  UNP    Q08722   CD47_HUMAN      19    132             
DBREF  5IWL D    1   114  UNP    Q08722   CD47_HUMAN      19    132             
SEQADV 5IWL ASP C   11  UNP  Q08722    GLU    29 CONFLICT                       
SEQADV 5IWL GLY C   15  UNP  Q08722    CYS    33 ENGINEERED MUTATION            
SEQADV 5IWL ASP D   11  UNP  Q08722    GLU    29 CONFLICT                       
SEQADV 5IWL GLY D   15  UNP  Q08722    CYS    33 ENGINEERED MUTATION            
SEQRES   1 B  234  PCA VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 B  234  PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 B  234  TYR THR PHE THR ASN TYR ASN MET HIS TRP VAL ARG GLN          
SEQRES   4 B  234  ALA PRO GLY GLN ARG LEU GLU TRP MET GLY THR ILE TYR          
SEQRES   5 B  234  PRO GLY ASN ASP ASP THR SER TYR ASN GLN LYS PHE LYS          
SEQRES   6 B  234  ASP ARG VAL THR ILE THR ALA ASP THR SER ALA SER THR          
SEQRES   7 B  234  ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 B  234  ALA VAL TYR TYR CYS ALA ARG GLY GLY TYR ARG ALA MET          
SEQRES   9 B  234  ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER          
SEQRES  10 B  234  GLY GLY SER GLY GLY ASP ILE VAL MET THR GLN SER PRO          
SEQRES  11 B  234  LEU SER LEU PRO VAL THR PRO GLY GLU PRO ALA SER ILE          
SEQRES  12 B  234  SER CYS ARG SER SER GLN SER ILE VAL TYR SER ASN GLY          
SEQRES  13 B  234  ASN THR TYR LEU GLY TRP TYR LEU GLN LYS PRO GLY GLN          
SEQRES  14 B  234  SER PRO GLN LEU LEU ILE TYR LYS VAL SER ASN ARG PHE          
SEQRES  15 B  234  SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER GLY          
SEQRES  16 B  234  THR ASP PHE THR LEU LYS ILE SER ARG VAL GLU ALA GLU          
SEQRES  17 B  234  ASP VAL GLY VAL TYR TYR CYS PHE GLN GLY SER HIS VAL          
SEQRES  18 B  234  PRO TYR THR PHE GLY GLN GLY THR LYS LEU GLU ILE LYS          
SEQRES   1 A  234  PCA VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 A  234  PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 A  234  TYR THR PHE THR ASN TYR ASN MET HIS TRP VAL ARG GLN          
SEQRES   4 A  234  ALA PRO GLY GLN ARG LEU GLU TRP MET GLY THR ILE TYR          
SEQRES   5 A  234  PRO GLY ASN ASP ASP THR SER TYR ASN GLN LYS PHE LYS          
SEQRES   6 A  234  ASP ARG VAL THR ILE THR ALA ASP THR SER ALA SER THR          
SEQRES   7 A  234  ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 A  234  ALA VAL TYR TYR CYS ALA ARG GLY GLY TYR ARG ALA MET          
SEQRES   9 A  234  ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER          
SEQRES  10 A  234  GLY GLY SER GLY GLY ASP ILE VAL MET THR GLN SER PRO          
SEQRES  11 A  234  LEU SER LEU PRO VAL THR PRO GLY GLU PRO ALA SER ILE          
SEQRES  12 A  234  SER CYS ARG SER SER GLN SER ILE VAL TYR SER ASN GLY          
SEQRES  13 A  234  ASN THR TYR LEU GLY TRP TYR LEU GLN LYS PRO GLY GLN          
SEQRES  14 A  234  SER PRO GLN LEU LEU ILE TYR LYS VAL SER ASN ARG PHE          
SEQRES  15 A  234  SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER GLY          
SEQRES  16 A  234  THR ASP PHE THR LEU LYS ILE SER ARG VAL GLU ALA GLU          
SEQRES  17 A  234  ASP VAL GLY VAL TYR TYR CYS PHE GLN GLY SER HIS VAL          
SEQRES  18 A  234  PRO TYR THR PHE GLY GLN GLY THR LYS LEU GLU ILE LYS          
SEQRES   1 C  114  PCA LEU LEU PHE ASN LYS THR LYS SER VAL ASP PHE THR          
SEQRES   2 C  114  PHE GLY ASN ASP THR VAL VAL ILE PRO CYS PHE VAL THR          
SEQRES   3 C  114  ASN MET GLU ALA GLN ASN THR THR GLU VAL TYR VAL LYS          
SEQRES   4 C  114  TRP LYS PHE LYS GLY ARG ASP ILE TYR THR PHE ASP GLY          
SEQRES   5 C  114  ALA LEU ASN LYS SER THR VAL PRO THR ASP PHE SER SER          
SEQRES   6 C  114  ALA LYS ILE GLU VAL SER GLN LEU LEU LYS GLY ASP ALA          
SEQRES   7 C  114  SER LEU LYS MET ASP LYS SER ASP ALA VAL SER HIS THR          
SEQRES   8 C  114  GLY ASN TYR THR CYS GLU VAL THR GLU LEU THR ARG GLU          
SEQRES   9 C  114  GLY GLU THR ILE ILE GLU LEU LYS TYR ARG                      
SEQRES   1 D  114  PCA LEU LEU PHE ASN LYS THR LYS SER VAL ASP PHE THR          
SEQRES   2 D  114  PHE GLY ASN ASP THR VAL VAL ILE PRO CYS PHE VAL THR          
SEQRES   3 D  114  ASN MET GLU ALA GLN ASN THR THR GLU VAL TYR VAL LYS          
SEQRES   4 D  114  TRP LYS PHE LYS GLY ARG ASP ILE TYR THR PHE ASP GLY          
SEQRES   5 D  114  ALA LEU ASN LYS SER THR VAL PRO THR ASP PHE SER SER          
SEQRES   6 D  114  ALA LYS ILE GLU VAL SER GLN LEU LEU LYS GLY ASP ALA          
SEQRES   7 D  114  SER LEU LYS MET ASP LYS SER ASP ALA VAL SER HIS THR          
SEQRES   8 D  114  GLY ASN TYR THR CYS GLU VAL THR GLU LEU THR ARG GLU          
SEQRES   9 D  114  GLY GLU THR ILE ILE GLU LEU LYS TYR ARG                      
MODRES 5IWL PCA C    1  GLN  MODIFIED RESIDUE                                   
MODRES 5IWL PCA D    1  GLN  MODIFIED RESIDUE                                   
HET    PCA  B   1       8                                                       
HET    PCA  A   1       8                                                       
HET    PCA  C   1       8                                                       
HET    PCA  D   1       8                                                       
HET    NAG  C 201      14                                                       
HET    NAG  C 202      14                                                       
HET    NAG  C 203      14                                                       
HET    PGE  C 204      10                                                       
HET    NAG  D 201      14                                                       
HET    NAG  D 202      14                                                       
HET    NAG  D 203      14                                                       
HET    PGE  D 204      10                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PGE TRIETHYLENE GLYCOL                                               
FORMUL   1  PCA    4(C5 H7 N O3)                                                
FORMUL   5  NAG    6(C8 H15 N O6)                                               
FORMUL   8  PGE    2(C6 H14 O4)                                                 
FORMUL  13  HOH   *7(H2 O)                                                      
HELIX    1 AA1 THR B   28  TYR B   32  5                                   5    
HELIX    2 AA2 GLN B   62  LYS B   65  5                                   4    
HELIX    3 AA3 ARG B   87  THR B   91  5                                   5    
HELIX    4 AA4 THR A   28  TYR A   32  5                                   5    
HELIX    5 AA5 GLN A   62  LYS A   65  5                                   4    
HELIX    6 AA6 ARG A   87  THR A   91  5                                   5    
HELIX    7 AA7 GLU A  206  VAL A  210  5                                   5    
HELIX    8 AA8 ASN C   32  THR C   34  5                                   3    
HELIX    9 AA9 VAL C   70  LEU C   73  5                                   4    
HELIX   10 AB1 LYS C   84  HIS C   90  1                                   7    
HELIX   11 AB2 ASN D   32  THR D   34  5                                   3    
HELIX   12 AB3 PRO D   60  SER D   64  5                                   5    
HELIX   13 AB4 GLU D   69  LEU D   73  5                                   5    
HELIX   14 AB5 LYS D   84  SER D   89  1                                   6    
SHEET    1 AA1 4 GLN B   3  GLN B   6  0                                        
SHEET    2 AA1 4 VAL B  18  SER B  25 -1  O  LYS B  23   N  VAL B   5           
SHEET    3 AA1 4 THR B  78  LEU B  83 -1  O  ALA B  79   N  CYS B  22           
SHEET    4 AA1 4 VAL B  68  ASP B  73 -1  N  THR B  69   O  GLU B  82           
SHEET    1 AA2 6 GLU B  10  LYS B  12  0                                        
SHEET    2 AA2 6 THR B 111  VAL B 115  1  O  LEU B 112   N  GLU B  10           
SHEET    3 AA2 6 ALA B  92  GLY B  99 -1  N  TYR B  94   O  THR B 111           
SHEET    4 AA2 6 ASN B  33  GLN B  39 -1  N  VAL B  37   O  TYR B  95           
SHEET    5 AA2 6 LEU B  45  TYR B  52 -1  O  MET B  48   N  TRP B  36           
SHEET    6 AA2 6 ASP B  57  TYR B  60 -1  O  ASP B  57   N  TYR B  52           
SHEET    1 AA3 4 GLU B  10  LYS B  12  0                                        
SHEET    2 AA3 4 THR B 111  VAL B 115  1  O  LEU B 112   N  GLU B  10           
SHEET    3 AA3 4 ALA B  92  GLY B  99 -1  N  TYR B  94   O  THR B 111           
SHEET    4 AA3 4 MET B 104  TRP B 107 -1  O  TYR B 106   N  ARG B  98           
SHEET    1 AA4 4 MET B 126  SER B 129  0                                        
SHEET    2 AA4 4 ALA B 141  SER B 147 -1  O  ARG B 146   N  THR B 127           
SHEET    3 AA4 4 ASP B 197  ILE B 202 -1  O  PHE B 198   N  CYS B 145           
SHEET    4 AA4 4 PHE B 189  SER B 194 -1  N  SER B 190   O  LYS B 201           
SHEET    1 AA5 6 SER B 132  PRO B 134  0                                        
SHEET    2 AA5 6 THR B 229  GLU B 232  1  O  LYS B 230   N  LEU B 133           
SHEET    3 AA5 6 GLY B 211  GLN B 217 -1  N  GLY B 211   O  LEU B 231           
SHEET    4 AA5 6 LEU B 160  GLN B 165 -1  N  TYR B 163   O  TYR B 214           
SHEET    5 AA5 6 PRO B 171  TYR B 176 -1  O  LEU B 174   N  TRP B 162           
SHEET    6 AA5 6 ASN B 180  ARG B 181 -1  O  ASN B 180   N  TYR B 176           
SHEET    1 AA6 4 SER B 132  PRO B 134  0                                        
SHEET    2 AA6 4 THR B 229  GLU B 232  1  O  LYS B 230   N  LEU B 133           
SHEET    3 AA6 4 GLY B 211  GLN B 217 -1  N  GLY B 211   O  LEU B 231           
SHEET    4 AA6 4 THR B 224  PHE B 225 -1  O  THR B 224   N  GLN B 217           
SHEET    1 AA7 4 GLN A   3  GLN A   6  0                                        
SHEET    2 AA7 4 VAL A  18  SER A  25 -1  O  LYS A  23   N  VAL A   5           
SHEET    3 AA7 4 THR A  78  LEU A  83 -1  O  MET A  81   N  VAL A  20           
SHEET    4 AA7 4 VAL A  68  ASP A  73 -1  N  ASP A  73   O  THR A  78           
SHEET    1 AA8 6 GLU A  10  LYS A  12  0                                        
SHEET    2 AA8 6 THR A 111  VAL A 115  1  O  LEU A 112   N  GLU A  10           
SHEET    3 AA8 6 ALA A  92  GLY A 100 -1  N  TYR A  94   O  THR A 111           
SHEET    4 AA8 6 ASN A  33  GLN A  39 -1  N  HIS A  35   O  ALA A  97           
SHEET    5 AA8 6 LEU A  45  TYR A  52 -1  O  MET A  48   N  TRP A  36           
SHEET    6 AA8 6 ASP A  57  TYR A  60 -1  O  SER A  59   N  THR A  50           
SHEET    1 AA9 4 GLU A  10  LYS A  12  0                                        
SHEET    2 AA9 4 THR A 111  VAL A 115  1  O  LEU A 112   N  GLU A  10           
SHEET    3 AA9 4 ALA A  92  GLY A 100 -1  N  TYR A  94   O  THR A 111           
SHEET    4 AA9 4 ALA A 103  TRP A 107 -1  O  TYR A 106   N  ARG A  98           
SHEET    1 AB1 4 MET A 126  SER A 129  0                                        
SHEET    2 AB1 4 ALA A 141  SER A 147 -1  O  ARG A 146   N  THR A 127           
SHEET    3 AB1 4 ASP A 197  ILE A 202 -1  O  LEU A 200   N  ILE A 143           
SHEET    4 AB1 4 PHE A 189  SER A 194 -1  N  SER A 190   O  LYS A 201           
SHEET    1 AB2 6 SER A 132  PRO A 134  0                                        
SHEET    2 AB2 6 THR A 229  GLU A 232  1  O  LYS A 230   N  LEU A 133           
SHEET    3 AB2 6 GLY A 211  GLN A 217 -1  N  GLY A 211   O  LEU A 231           
SHEET    4 AB2 6 LEU A 160  GLN A 165 -1  N  GLY A 161   O  PHE A 216           
SHEET    5 AB2 6 GLN A 172  TYR A 176 -1  O  ILE A 175   N  TRP A 162           
SHEET    6 AB2 6 ASN A 180  ARG A 181 -1  O  ASN A 180   N  TYR A 176           
SHEET    1 AB3 4 SER A 132  PRO A 134  0                                        
SHEET    2 AB3 4 THR A 229  GLU A 232  1  O  LYS A 230   N  LEU A 133           
SHEET    3 AB3 4 GLY A 211  GLN A 217 -1  N  GLY A 211   O  LEU A 231           
SHEET    4 AB3 4 THR A 224  PHE A 225 -1  O  THR A 224   N  GLN A 217           
SHEET    1 AB4 6 SER C   9  PHE C  12  0                                        
SHEET    2 AB4 6 ARG C 103  TYR C 113  1  O  GLU C 110   N  VAL C  10           
SHEET    3 AB4 6 GLY C  92  GLU C 100 -1  N  GLY C  92   O  LEU C 111           
SHEET    4 AB4 6 VAL C  36  PHE C  42 -1  N  TYR C  37   O  THR C  99           
SHEET    5 AB4 6 ARG C  45  ASP C  51 -1  O  TYR C  48   N  TRP C  40           
SHEET    6 AB4 6 LYS C  56  THR C  58 -1  O  LYS C  56   N  ASP C  51           
SHEET    1 AB5 3 THR C  18  ILE C  21  0                                        
SHEET    2 AB5 3 LEU C  80  ASP C  83 -1  O  MET C  82   N  VAL C  19           
SHEET    3 AB5 3 LYS C  67  ILE C  68 -1  N  LYS C  67   O  LYS C  81           
SHEET    1 AB6 6 SER D   9  PHE D  12  0                                        
SHEET    2 AB6 6 ARG D 103  TYR D 113  1  O  GLU D 110   N  VAL D  10           
SHEET    3 AB6 6 GLY D  92  GLU D 100 -1  N  GLY D  92   O  LEU D 111           
SHEET    4 AB6 6 VAL D  36  PHE D  42 -1  N  TYR D  37   O  THR D  99           
SHEET    5 AB6 6 ARG D  45  ASP D  51 -1  O  TYR D  48   N  TRP D  40           
SHEET    6 AB6 6 LYS D  56  THR D  58 -1  O  LYS D  56   N  ASP D  51           
SHEET    1 AB7 2 THR D  18  ILE D  21  0                                        
SHEET    2 AB7 2 LEU D  80  ASP D  83 -1  O  MET D  82   N  VAL D  19           
SSBOND   1 CYS B   22    CYS B   96                          1555   1555  2.03  
SSBOND   2 CYS B  145    CYS B  215                          1555   1555  2.04  
SSBOND   3 CYS A   22    CYS A   96                          1555   1555  2.04  
SSBOND   4 CYS A  145    CYS A  215                          1555   1555  2.05  
SSBOND   5 CYS C   23    CYS C   96                          1555   1555  2.03  
SSBOND   6 CYS D   23    CYS D   96                          1555   1555  2.04  
LINK         C   PCA B   1                 N   VAL B   2     1555   1555  1.33  
LINK         C   PCA A   1                 N   VAL A   2     1555   1555  1.33  
LINK         C   PCA C   1                 N   LEU C   2     1555   1555  1.33  
LINK         ND2 ASN C  16                 C1  NAG C 201     1555   1555  1.44  
LINK         ND2 ASN C  32                 C1  NAG C 202     1555   1555  1.45  
LINK         ND2 ASN C  93                 C1  NAG C 203     1555   1555  1.44  
LINK         C   PCA D   1                 N   LEU D   2     1555   1555  1.33  
LINK         ND2 ASN D  16                 C1  NAG D 202     1555   1555  1.44  
LINK         ND2 ASN D  32                 C1  NAG D 201     1555   1555  1.44  
LINK         ND2 ASN D  93                 C1  NAG D 203     1555   1555  1.44  
CISPEP   1 SER B  129    PRO B  130          0         1.62                     
CISPEP   2 VAL B  221    PRO B  222          0         3.10                     
CISPEP   3 SER A  129    PRO A  130          0        -0.87                     
CISPEP   4 VAL A  221    PRO A  222          0         1.28                     
SITE     1 AC1  5 TYR B 101  ARG B 102  LEU C   2  GLU C 104                    
SITE     2 AC1  5 GLU C 106                                                     
SITE     1 AC2  7 TYR A 101  ARG A 102  ASN B 155  GLU D  97                    
SITE     2 AC2  7 GLU D 104  GLY D 105  GLU D 106                               
SITE     1 AC3  4 ASP C  11  ASN C  16  VAL C  19  VAL C  20                    
SITE     1 AC4  1 ASN C  32                                                     
SITE     1 AC5  3 SER B  75  ASN C  93  GLU C 110                               
SITE     1 AC6  5 ASP D  11  PHE D  12  ASN D  16  VAL D  19                    
SITE     2 AC6  5 VAL D  20                                                     
SITE     1 AC7  2 ASN D  32  THR D  34                                          
SITE     1 AC8  2 ASN D  93  GLU D 110                                          
CRYST1  103.280  103.280  131.130  90.00  90.00 120.00 P 32 2 1     12          
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      0.009682  0.005590  0.000000        0.00000                         
SCALE2      0.000000  0.011180  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007626        0.00000                         
HETATM    1  N   PCA B   1     -41.139   8.522  -9.220  1.00 80.09           N  
ANISOU    1  N   PCA B   1    11910  10012   8508  -3889   1154  -1296       N  
HETATM    2  CA  PCA B   1     -39.888   8.647  -9.976  1.00 79.02           C  
ANISOU    2  CA  PCA B   1    11891   9629   8503  -3748   1254  -1333       C  
HETATM    3  CB  PCA B   1     -40.177   8.742 -11.470  1.00 81.56           C  
ANISOU    3  CB  PCA B   1    12158  10315   8517  -4099   1274  -1483       C  
HETATM    4  CG  PCA B   1     -41.658   9.035 -11.623  1.00 83.22           C  
ANISOU    4  CG  PCA B   1    12119  11096   8404  -4374   1084  -1453       C  
HETATM    5  CD  PCA B   1     -42.182   8.771 -10.228  1.00 82.55           C  
ANISOU    5  CD  PCA B   1    12028  10882   8455  -4249   1055  -1373       C  
HETATM    6  OE  PCA B   1     -43.394   8.756  -9.984  1.00 84.14           O  
ANISOU    6  OE  PCA B   1    12055  11462   8453  -4455    956  -1367       O  
HETATM    7  C   PCA B   1     -39.099   9.872  -9.544  1.00 74.70           C  
ANISOU    7  C   PCA B   1    11184   9031   8167  -3262   1034  -1085       C  
HETATM    8  O   PCA B   1     -38.661  10.679 -10.368  1.00 73.56           O  
ANISOU    8  O   PCA B   1    10932   9040   7975  -3186    933  -1030       O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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