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Database: PDB
Entry: 5IHB
LinkDB: 5IHB
Original site: 5IHB 
HEADER    IMMUNE SYSTEM                           29-FEB-16   5IHB              
TITLE     STRUCTURE OF THE IMMUNE RECEPTOR CD33                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYELOID CELL SURFACE ANTIGEN CD33;                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 21-232;                                       
COMPND   5 SYNONYM: SIALIC ACID-BINDING IG-LIKE LECTIN 3,SIGLEC-3,GP67;         
COMPND   6 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: CD33, SIGLEC3;                                                 
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-F;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    IMMUNE RECEPTOR, SIGLEC, IG-LIKE, SIALIC-ACID BINDING, IMMUNE SYSTEM  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.B.DODD                                                              
REVDAT   3   29-JUL-20 5IHB    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE                                     
REVDAT   2   02-OCT-19 5IHB    1       REMARK                                   
REVDAT   1   29-MAR-17 5IHB    0                                                
JRNL        AUTH   R.B.DODD,W.MEADOWS,S.QAMAR,C.M.JOHNSON,                      
JRNL        AUTH 2 D.KRONENBERG-VERSTEEG,P.ST GEORGE-HYSLOP                     
JRNL        TITL   STRUCTURE OF LIGAND BOUND CD33 RECEPTOR ASSOCIATED WITH      
JRNL        TITL 2 ALZHEIMER'S DISEASE                                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2313)                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.32                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.780                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 56515                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2792                            
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  2.2786 -  2.2400    0.98     2652   121  0.3088 0.3483        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.720           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.38                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.33                          
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      :  0.008           7008                                  
REMARK   3   ANGLE     :  0.779           9583                                  
REMARK   3   CHIRALITY :  0.053           1098                                  
REMARK   3   PLANARITY :  0.006           1234                                  
REMARK   3   DIHEDRAL  :  9.739           4172                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 51 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  43.6547 103.2078  55.2625              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3720 T22:   0.4568                                     
REMARK   3      T33:   0.3982 T12:  -0.0043                                     
REMARK   3      T13:   0.0084 T23:   0.0443                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5166 L22:   0.6600                                     
REMARK   3      L33:   2.0630 L12:  -0.4295                                     
REMARK   3      L13:  -0.2450 L23:   0.4399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1814 S12:   0.3508 S13:   0.0552                       
REMARK   3      S21:  -0.0306 S22:   0.0950 S23:   0.0724                       
REMARK   3      S31:  -0.0251 S32:  -0.1904 S33:  -0.1590                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 78 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  55.3643 102.4229  53.8423              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3429 T22:   0.4932                                     
REMARK   3      T33:   0.4157 T12:  -0.0021                                     
REMARK   3      T13:   0.0310 T23:  -0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9009 L22:   2.2192                                     
REMARK   3      L33:   2.9203 L12:   0.8782                                     
REMARK   3      L13:   0.1568 L23:  -0.6353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1997 S12:   0.3614 S13:   0.2589                       
REMARK   3      S21:   0.0449 S22:  -0.2067 S23:  -0.0861                       
REMARK   3      S31:   0.0348 S32:   0.3437 S33:   0.0313                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 92 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  57.8387  97.6573  62.8226              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5007 T22:   0.5838                                     
REMARK   3      T33:   0.5542 T12:   0.0879                                     
REMARK   3      T13:  -0.0376 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8178 L22:   3.0107                                     
REMARK   3      L33:   6.0497 L12:   0.2591                                     
REMARK   3      L13:  -1.4619 L23:  -0.7789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1241 S12:  -0.5263 S13:  -0.6388                       
REMARK   3      S21:   0.0947 S22:  -0.0272 S23:  -0.6028                       
REMARK   3      S31:   0.4534 S32:   1.2249 S33:   0.0923                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 113 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  48.1964  98.7853  62.9163              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3780 T22:   0.4563                                     
REMARK   3      T33:   0.4955 T12:   0.0175                                     
REMARK   3      T13:   0.0191 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2635 L22:   2.1724                                     
REMARK   3      L33:   6.0525 L12:  -0.2866                                     
REMARK   3      L13:   0.3460 L23:  -0.4488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0961 S12:   0.1185 S13:  -0.1253                       
REMARK   3      S21:   0.1447 S22:   0.0227 S23:  -0.1604                       
REMARK   3      S31:   0.6641 S32:   0.2541 S33:  -0.1143                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 114 THROUGH 128 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  51.5997 105.4198  50.4231              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3364 T22:   0.5309                                     
REMARK   3      T33:   0.4603 T12:   0.0110                                     
REMARK   3      T13:   0.0209 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6519 L22:   1.1310                                     
REMARK   3      L33:   3.8914 L12:   0.0921                                     
REMARK   3      L13:  -0.5530 L23:   0.2926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0830 S12:   0.4526 S13:   0.1564                       
REMARK   3      S21:  -0.2063 S22:   0.0903 S23:  -0.0302                       
REMARK   3      S31:  -0.1909 S32:   0.3334 S33:  -0.1284                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 164 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  40.1814  91.2859  81.2577              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3579 T22:   0.4949                                     
REMARK   3      T33:   0.4436 T12:  -0.0309                                     
REMARK   3      T13:  -0.0138 T23:  -0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6337 L22:   1.7228                                     
REMARK   3      L33:   2.2786 L12:  -0.4623                                     
REMARK   3      L13:   0.2445 L23:  -1.2778                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0990 S12:  -0.3177 S13:   0.0041                       
REMARK   3      S21:   0.4003 S22:   0.1804 S23:   0.2293                       
REMARK   3      S31:  -0.3240 S32:  -0.4342 S33:  -0.1882                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 232 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.1627  84.9219  90.0731              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4056 T22:   0.5079                                     
REMARK   3      T33:   0.3751 T12:  -0.0698                                     
REMARK   3      T13:  -0.0323 T23:   0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2152 L22:   2.2231                                     
REMARK   3      L33:   2.5972 L12:  -0.3244                                     
REMARK   3      L13:  -0.9456 L23:  -0.0829                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1201 S12:  -0.5860 S13:  -0.1298                       
REMARK   3      S21:   0.1269 S22:  -0.0115 S23:   0.0378                       
REMARK   3      S31:  -0.1574 S32:   0.0354 S33:  -0.1053                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7598  58.4818  68.9239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4613 T22:   0.3592                                     
REMARK   3      T33:   0.5184 T12:  -0.0746                                     
REMARK   3      T13:  -0.0333 T23:   0.0197                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7422 L22:   4.3543                                     
REMARK   3      L33:   2.5953 L12:   1.9409                                     
REMARK   3      L13:   1.8403 L23:   2.7030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1330 S12:  -0.2663 S13:   0.0656                       
REMARK   3      S21:   0.1513 S22:  -0.2382 S23:   0.0112                       
REMARK   3      S31:   0.0499 S32:  -0.3578 S33:   0.0392                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 103 THROUGH 149 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.5439  54.5831  59.4579              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3870 T22:   0.4000                                     
REMARK   3      T33:   0.4511 T12:  -0.0662                                     
REMARK   3      T13:  -0.0536 T23:   0.0620                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6152 L22:   2.9459                                     
REMARK   3      L33:   1.9420 L12:   0.8275                                     
REMARK   3      L13:   0.7588 L23:   1.4078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0434 S12:   0.1888 S13:   0.3159                       
REMARK   3      S21:  -0.3266 S22:  -0.2364 S23:   0.1393                       
REMARK   3      S31:  -0.4229 S32:  -0.1636 S33:   0.2576                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 232 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.6099  25.1509  48.4134              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4657 T22:   0.3966                                     
REMARK   3      T33:   0.4378 T12:  -0.0133                                     
REMARK   3      T13:   0.0293 T23:  -0.1169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7911 L22:   2.3052                                     
REMARK   3      L33:   2.1982 L12:   0.6387                                     
REMARK   3      L13:   0.6109 L23:  -0.2209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0415 S12:   0.4574 S13:  -0.4936                       
REMARK   3      S21:   0.1566 S22:   0.0734 S23:  -0.1702                       
REMARK   3      S31:   0.3078 S32:   0.1366 S33:  -0.0795                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 21 THROUGH 51 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  44.5597  25.5429  54.9595              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4372 T22:   0.5258                                     
REMARK   3      T33:   0.4379 T12:   0.0501                                     
REMARK   3      T13:   0.0272 T23:  -0.1042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3208 L22:   2.4439                                     
REMARK   3      L33:   2.3338 L12:  -0.4396                                     
REMARK   3      L13:   0.2391 L23:   0.4320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0539 S12:   0.5445 S13:  -0.2990                       
REMARK   3      S21:   0.2758 S22:  -0.2260 S23:   0.1199                       
REMARK   3      S31:   0.5198 S32:   0.1859 S33:   0.3275                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 52 THROUGH 83 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  57.5523  24.0496  55.1679              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5378 T22:   0.7455                                     
REMARK   3      T33:   0.6223 T12:   0.0652                                     
REMARK   3      T13:   0.0177 T23:  -0.0819                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7091 L22:   2.9465                                     
REMARK   3      L33:   3.5712 L12:   0.2619                                     
REMARK   3      L13:   0.3441 L23:  -0.3685                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0871 S12:   0.1809 S13:  -0.1915                       
REMARK   3      S21:  -0.2851 S22:  -0.0997 S23:  -0.5174                       
REMARK   3      S31:   0.3211 S32:   0.9364 S33:   0.0460                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 84 THROUGH 95 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  54.7099  26.6609  65.1958              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6244 T22:   0.6581                                     
REMARK   3      T33:   0.6496 T12:   0.0960                                     
REMARK   3      T13:  -0.1534 T23:  -0.0501                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5187 L22:   2.9479                                     
REMARK   3      L33:   6.2910 L12:  -0.6868                                     
REMARK   3      L13:   2.3075 L23:   2.3378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0192 S12:   0.4206 S13:  -0.1099                       
REMARK   3      S21:   1.1230 S22:   0.3858 S23:  -0.7845                       
REMARK   3      S31:   0.8373 S32:   1.2036 S33:  -0.0799                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 96 THROUGH 128 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  50.9328  26.6567  57.0396              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4618 T22:   0.5235                                     
REMARK   3      T33:   0.5082 T12:   0.0324                                     
REMARK   3      T13:  -0.0235 T23:  -0.0715                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0956 L22:   2.7479                                     
REMARK   3      L33:   3.7504 L12:  -0.1411                                     
REMARK   3      L13:  -0.2832 L23:   1.7476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1022 S12:   0.3612 S13:  -0.1382                       
REMARK   3      S21:   0.3920 S22:   0.2696 S23:  -0.4622                       
REMARK   3      S31:   0.4124 S32:   0.6322 S33:  -0.1311                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 129 THROUGH 149 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  43.8376  37.4916  69.1371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3696 T22:   0.4432                                     
REMARK   3      T33:   0.5106 T12:   0.0226                                     
REMARK   3      T13:  -0.0518 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2728 L22:   1.9668                                     
REMARK   3      L33:   5.6049 L12:   0.1179                                     
REMARK   3      L13:   0.5123 L23:  -0.3028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1075 S12:   0.1663 S13:   0.0013                       
REMARK   3      S21:  -0.1082 S22:  -0.0886 S23:  -0.1097                       
REMARK   3      S31:  -1.3562 S32:   0.0064 S33:   0.2196                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 150 THROUGH 232 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  43.7225  36.9800  93.6204              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4091 T22:   0.4621                                     
REMARK   3      T33:   0.3884 T12:   0.0802                                     
REMARK   3      T13:  -0.0328 T23:  -0.0863                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4929 L22:   3.7908                                     
REMARK   3      L33:   3.1334 L12:  -0.9841                                     
REMARK   3      L13:   0.9524 L23:  -0.3547                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0058 S12:  -0.5447 S13:   0.2276                       
REMARK   3      S21:   0.0008 S22:   0.0933 S23:   0.1563                       
REMARK   3      S31:  -0.2988 S32:  -0.4767 S33:  -0.1089                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 23 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  70.2130  74.1070  55.3183              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9568 T22:   0.7148                                     
REMARK   3      T33:   0.7933 T12:  -0.0921                                     
REMARK   3      T13:   0.1999 T23:  -0.1531                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5176 L22:   1.9183                                     
REMARK   3      L33:   3.9523 L12:   0.4541                                     
REMARK   3      L13:  -0.9380 L23:  -0.6207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0196 S12:   0.7215 S13:  -0.1164                       
REMARK   3      S21:  -0.9204 S22:   0.2108 S23:  -0.4012                       
REMARK   3      S31:   0.1808 S32:   0.4014 S33:  -0.2074                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 103 THROUGH 231 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  62.2025  78.1783  81.3167              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3764 T22:   0.3742                                     
REMARK   3      T33:   0.4807 T12:  -0.0552                                     
REMARK   3      T13:  -0.0297 T23:   0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1970 L22:   1.6862                                     
REMARK   3      L33:   3.4293 L12:   0.2808                                     
REMARK   3      L13:  -0.9049 L23:   0.6905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0016 S12:  -0.3485 S13:  -0.3847                       
REMARK   3      S21:  -0.2103 S22:   0.0431 S23:  -0.2622                       
REMARK   3      S31:  -0.0494 S32:   0.2143 S33:  -0.0238                       
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 5IHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217843.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.920                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56518                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.240                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 62.320                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.06960                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.78500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: MODEL DERIVED FROM 2ZG2 BY SCULPTOR                  
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% PEG 20,000, 4% PEG MME 500, 100 MM    
REMARK 280  BICINE/TRIS BASE PH 8.5, 1XMORPHEUS AMINO ACIDS, VAPOR DIFFUSION,   
REMARK 280  SITTING DROP, TEMPERATURE 295.15K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000       32.48000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.52000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.52000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.52000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.48000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.52000            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       32.48000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       63.52000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      143.04000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     GLY A   233                                                      
REMARK 465     THR A   234                                                      
REMARK 465     LYS A   235                                                      
REMARK 465     HIS A   236                                                      
REMARK 465     HIS A   237                                                      
REMARK 465     HIS A   238                                                      
REMARK 465     HIS A   239                                                      
REMARK 465     HIS A   240                                                      
REMARK 465     HIS A   241                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     GLY B   233                                                      
REMARK 465     THR B   234                                                      
REMARK 465     LYS B   235                                                      
REMARK 465     HIS B   236                                                      
REMARK 465     HIS B   237                                                      
REMARK 465     HIS B   238                                                      
REMARK 465     HIS B   239                                                      
REMARK 465     HIS B   240                                                      
REMARK 465     HIS B   241                                                      
REMARK 465     GLU C    18                                                      
REMARK 465     THR C    19                                                      
REMARK 465     GLY C    20                                                      
REMARK 465     GLY C   233                                                      
REMARK 465     THR C   234                                                      
REMARK 465     LYS C   235                                                      
REMARK 465     HIS C   236                                                      
REMARK 465     HIS C   237                                                      
REMARK 465     HIS C   238                                                      
REMARK 465     HIS C   239                                                      
REMARK 465     HIS C   240                                                      
REMARK 465     HIS C   241                                                      
REMARK 465     GLU D    18                                                      
REMARK 465     THR D    19                                                      
REMARK 465     GLY D    20                                                      
REMARK 465     PHE D    21                                                      
REMARK 465     TRP D    22                                                      
REMARK 465     THR D   232                                                      
REMARK 465     GLY D   233                                                      
REMARK 465     THR D   234                                                      
REMARK 465     LYS D   235                                                      
REMARK 465     HIS D   236                                                      
REMARK 465     HIS D   237                                                      
REMARK 465     HIS D   238                                                      
REMARK 465     HIS D   239                                                      
REMARK 465     HIS D   240                                                      
REMARK 465     HIS D   241                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  HH22  ARG B   110     OD1  ASP B   140              1.51            
REMARK 500   HD1  HIS D   206     O    ASN D   230              1.59            
REMARK 500   H    THR A   222     O    HOH A   403              1.59            
REMARK 500   H    THR C   222     O    HOH C   404              1.59            
REMARK 500   NH2  ARG B   110     OD1  ASP B   140              1.96            
REMARK 500   NH2  ARG A   110     OD1  ASP A   140              2.14            
REMARK 500   NH2  ARG C   110     OD1  ASP C   140              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  HH22  ARG B   225     OE2  GLU D   154     2664     1.34            
REMARK 500   OH   TYR A    49     O6   NAG C   302     2664     2.03            
REMARK 500   NH2  ARG B   225     OE2  GLU D   154     2664     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG B 225   CZ    ARG B 225   NH1     0.086                       
REMARK 500    ARG B 225   CZ    ARG B 225   NH2     0.089                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LEU A  35     -167.37   -102.20                                   
REMARK 500    VAL A 221       69.24   -119.24                                   
REMARK 500    LEU B  35     -166.04   -103.41                                   
REMARK 500    LEU C  35     -167.59   -102.39                                   
REMARK 500    VAL C 221       63.47   -116.59                                   
REMARK 500    ASN C 230       60.61   -114.26                                   
REMARK 500    VAL C 231      108.37    -58.96                                   
REMARK 500    LEU D  35     -166.55   -104.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5IHB A   21   232  UNP    P20138   CD33_HUMAN      21    232             
DBREF  5IHB B   21   232  UNP    P20138   CD33_HUMAN      21    232             
DBREF  5IHB C   21   232  UNP    P20138   CD33_HUMAN      21    232             
DBREF  5IHB D   21   232  UNP    P20138   CD33_HUMAN      21    232             
SEQADV 5IHB GLU A   18  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB THR A   19  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLY A   20  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLY A   69  UNP  P20138    ARG    69 CONFLICT                       
SEQADV 5IHB GLY A  233  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB THR A  234  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB LYS A  235  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS A  236  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS A  237  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS A  238  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS A  239  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS A  240  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS A  241  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLU B   18  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB THR B   19  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLY B   20  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLY B   69  UNP  P20138    ARG    69 CONFLICT                       
SEQADV 5IHB GLY B  233  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB THR B  234  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB LYS B  235  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS B  236  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS B  237  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS B  238  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS B  239  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS B  240  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS B  241  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLU C   18  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB THR C   19  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLY C   20  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLY C   69  UNP  P20138    ARG    69 CONFLICT                       
SEQADV 5IHB GLY C  233  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB THR C  234  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB LYS C  235  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS C  236  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS C  237  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS C  238  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS C  239  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS C  240  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS C  241  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLU D   18  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB THR D   19  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLY D   20  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB GLY D   69  UNP  P20138    ARG    69 CONFLICT                       
SEQADV 5IHB GLY D  233  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB THR D  234  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB LYS D  235  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS D  236  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS D  237  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS D  238  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS D  239  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS D  240  UNP  P20138              EXPRESSION TAG                 
SEQADV 5IHB HIS D  241  UNP  P20138              EXPRESSION TAG                 
SEQRES   1 A  224  GLU THR GLY PHE TRP LEU GLN VAL GLN GLU SER VAL THR          
SEQRES   2 A  224  VAL GLN GLU GLY LEU CYS VAL LEU VAL PRO CYS THR PHE          
SEQRES   3 A  224  PHE HIS PRO ILE PRO TYR TYR ASP LYS ASN SER PRO VAL          
SEQRES   4 A  224  HIS GLY TYR TRP PHE ARG GLU GLY ALA ILE ILE SER GLY          
SEQRES   5 A  224  ASP SER PRO VAL ALA THR ASN LYS LEU ASP GLN GLU VAL          
SEQRES   6 A  224  GLN GLU GLU THR GLN GLY ARG PHE ARG LEU LEU GLY ASP          
SEQRES   7 A  224  PRO SER ARG ASN ASN CYS SER LEU SER ILE VAL ASP ALA          
SEQRES   8 A  224  ARG ARG ARG ASP ASN GLY SER TYR PHE PHE ARG MET GLU          
SEQRES   9 A  224  ARG GLY SER THR LYS TYR SER TYR LYS SER PRO GLN LEU          
SEQRES  10 A  224  SER VAL HIS VAL THR ASP LEU THR HIS ARG PRO LYS ILE          
SEQRES  11 A  224  LEU ILE PRO GLY THR LEU GLU PRO GLY HIS SER LYS ASN          
SEQRES  12 A  224  LEU THR CYS SER VAL SER TRP ALA CYS GLU GLN GLY THR          
SEQRES  13 A  224  PRO PRO ILE PHE SER TRP LEU SER ALA ALA PRO THR SER          
SEQRES  14 A  224  LEU GLY PRO ARG THR THR HIS SER SER VAL LEU ILE ILE          
SEQRES  15 A  224  THR PRO ARG PRO GLN ASP HIS GLY THR ASN LEU THR CYS          
SEQRES  16 A  224  GLN VAL LYS PHE ALA GLY ALA GLY VAL THR THR GLU ARG          
SEQRES  17 A  224  THR ILE GLN LEU ASN VAL THR GLY THR LYS HIS HIS HIS          
SEQRES  18 A  224  HIS HIS HIS                                                  
SEQRES   1 B  224  GLU THR GLY PHE TRP LEU GLN VAL GLN GLU SER VAL THR          
SEQRES   2 B  224  VAL GLN GLU GLY LEU CYS VAL LEU VAL PRO CYS THR PHE          
SEQRES   3 B  224  PHE HIS PRO ILE PRO TYR TYR ASP LYS ASN SER PRO VAL          
SEQRES   4 B  224  HIS GLY TYR TRP PHE ARG GLU GLY ALA ILE ILE SER GLY          
SEQRES   5 B  224  ASP SER PRO VAL ALA THR ASN LYS LEU ASP GLN GLU VAL          
SEQRES   6 B  224  GLN GLU GLU THR GLN GLY ARG PHE ARG LEU LEU GLY ASP          
SEQRES   7 B  224  PRO SER ARG ASN ASN CYS SER LEU SER ILE VAL ASP ALA          
SEQRES   8 B  224  ARG ARG ARG ASP ASN GLY SER TYR PHE PHE ARG MET GLU          
SEQRES   9 B  224  ARG GLY SER THR LYS TYR SER TYR LYS SER PRO GLN LEU          
SEQRES  10 B  224  SER VAL HIS VAL THR ASP LEU THR HIS ARG PRO LYS ILE          
SEQRES  11 B  224  LEU ILE PRO GLY THR LEU GLU PRO GLY HIS SER LYS ASN          
SEQRES  12 B  224  LEU THR CYS SER VAL SER TRP ALA CYS GLU GLN GLY THR          
SEQRES  13 B  224  PRO PRO ILE PHE SER TRP LEU SER ALA ALA PRO THR SER          
SEQRES  14 B  224  LEU GLY PRO ARG THR THR HIS SER SER VAL LEU ILE ILE          
SEQRES  15 B  224  THR PRO ARG PRO GLN ASP HIS GLY THR ASN LEU THR CYS          
SEQRES  16 B  224  GLN VAL LYS PHE ALA GLY ALA GLY VAL THR THR GLU ARG          
SEQRES  17 B  224  THR ILE GLN LEU ASN VAL THR GLY THR LYS HIS HIS HIS          
SEQRES  18 B  224  HIS HIS HIS                                                  
SEQRES   1 C  224  GLU THR GLY PHE TRP LEU GLN VAL GLN GLU SER VAL THR          
SEQRES   2 C  224  VAL GLN GLU GLY LEU CYS VAL LEU VAL PRO CYS THR PHE          
SEQRES   3 C  224  PHE HIS PRO ILE PRO TYR TYR ASP LYS ASN SER PRO VAL          
SEQRES   4 C  224  HIS GLY TYR TRP PHE ARG GLU GLY ALA ILE ILE SER GLY          
SEQRES   5 C  224  ASP SER PRO VAL ALA THR ASN LYS LEU ASP GLN GLU VAL          
SEQRES   6 C  224  GLN GLU GLU THR GLN GLY ARG PHE ARG LEU LEU GLY ASP          
SEQRES   7 C  224  PRO SER ARG ASN ASN CYS SER LEU SER ILE VAL ASP ALA          
SEQRES   8 C  224  ARG ARG ARG ASP ASN GLY SER TYR PHE PHE ARG MET GLU          
SEQRES   9 C  224  ARG GLY SER THR LYS TYR SER TYR LYS SER PRO GLN LEU          
SEQRES  10 C  224  SER VAL HIS VAL THR ASP LEU THR HIS ARG PRO LYS ILE          
SEQRES  11 C  224  LEU ILE PRO GLY THR LEU GLU PRO GLY HIS SER LYS ASN          
SEQRES  12 C  224  LEU THR CYS SER VAL SER TRP ALA CYS GLU GLN GLY THR          
SEQRES  13 C  224  PRO PRO ILE PHE SER TRP LEU SER ALA ALA PRO THR SER          
SEQRES  14 C  224  LEU GLY PRO ARG THR THR HIS SER SER VAL LEU ILE ILE          
SEQRES  15 C  224  THR PRO ARG PRO GLN ASP HIS GLY THR ASN LEU THR CYS          
SEQRES  16 C  224  GLN VAL LYS PHE ALA GLY ALA GLY VAL THR THR GLU ARG          
SEQRES  17 C  224  THR ILE GLN LEU ASN VAL THR GLY THR LYS HIS HIS HIS          
SEQRES  18 C  224  HIS HIS HIS                                                  
SEQRES   1 D  224  GLU THR GLY PHE TRP LEU GLN VAL GLN GLU SER VAL THR          
SEQRES   2 D  224  VAL GLN GLU GLY LEU CYS VAL LEU VAL PRO CYS THR PHE          
SEQRES   3 D  224  PHE HIS PRO ILE PRO TYR TYR ASP LYS ASN SER PRO VAL          
SEQRES   4 D  224  HIS GLY TYR TRP PHE ARG GLU GLY ALA ILE ILE SER GLY          
SEQRES   5 D  224  ASP SER PRO VAL ALA THR ASN LYS LEU ASP GLN GLU VAL          
SEQRES   6 D  224  GLN GLU GLU THR GLN GLY ARG PHE ARG LEU LEU GLY ASP          
SEQRES   7 D  224  PRO SER ARG ASN ASN CYS SER LEU SER ILE VAL ASP ALA          
SEQRES   8 D  224  ARG ARG ARG ASP ASN GLY SER TYR PHE PHE ARG MET GLU          
SEQRES   9 D  224  ARG GLY SER THR LYS TYR SER TYR LYS SER PRO GLN LEU          
SEQRES  10 D  224  SER VAL HIS VAL THR ASP LEU THR HIS ARG PRO LYS ILE          
SEQRES  11 D  224  LEU ILE PRO GLY THR LEU GLU PRO GLY HIS SER LYS ASN          
SEQRES  12 D  224  LEU THR CYS SER VAL SER TRP ALA CYS GLU GLN GLY THR          
SEQRES  13 D  224  PRO PRO ILE PHE SER TRP LEU SER ALA ALA PRO THR SER          
SEQRES  14 D  224  LEU GLY PRO ARG THR THR HIS SER SER VAL LEU ILE ILE          
SEQRES  15 D  224  THR PRO ARG PRO GLN ASP HIS GLY THR ASN LEU THR CYS          
SEQRES  16 D  224  GLN VAL LYS PHE ALA GLY ALA GLY VAL THR THR GLU ARG          
SEQRES  17 D  224  THR ILE GLN LEU ASN VAL THR GLY THR LYS HIS HIS HIS          
SEQRES  18 D  224  HIS HIS HIS                                                  
HET    NAG  A 301      28                                                       
HET    NAG  A 302      27                                                       
HET    NAG  A 303      28                                                       
HET    NAG  B 301      28                                                       
HET    NAG  B 302      28                                                       
HET    NAG  B 303      27                                                       
HET    NAG  C 301      28                                                       
HET    NAG  C 302      27                                                       
HET    NAG  C 303      27                                                       
HET    NAG  D 301      28                                                       
HET    NAG  D 302      27                                                       
HET    NAG  D 303      27                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   5  NAG    12(C8 H15 N O6)                                              
FORMUL  17  HOH   *232(H2 O)                                                    
HELIX    1 AA1 PRO A   48  LYS A   52  5                                   5    
HELIX    2 AA2 GLY A   64  GLY A   69  1                                   6    
HELIX    3 AA3 ASP A   95  ASN A   99  5                                   5    
HELIX    4 AA4 ARG A  109  ASN A  113  5                                   5    
HELIX    5 AA5 ARG A  202  HIS A  206  5                                   5    
HELIX    6 AA6 PRO B   48  LYS B   52  5                                   5    
HELIX    7 AA7 ASP B   95  ASN B   99  5                                   5    
HELIX    8 AA8 ARG B  109  ASN B  113  5                                   5    
HELIX    9 AA9 ARG B  202  HIS B  206  5                                   5    
HELIX   10 AB1 ALA B  217  GLY B  220  5                                   4    
HELIX   11 AB2 PRO C   48  LYS C   52  5                                   5    
HELIX   12 AB3 GLY C   64  GLY C   69  1                                   6    
HELIX   13 AB4 GLN C   83  GLN C   87  5                                   5    
HELIX   14 AB5 ASP C   95  ASN C   99  5                                   5    
HELIX   15 AB6 ARG C  109  ASN C  113  5                                   5    
HELIX   16 AB7 ARG C  202  HIS C  206  5                                   5    
HELIX   17 AB8 PRO D   48  LYS D   52  5                                   5    
HELIX   18 AB9 ASP D   95  ASN D   99  5                                   5    
HELIX   19 AC1 ARG D  109  ASN D  113  5                                   5    
HELIX   20 AC2 ARG D  202  HIS D  206  5                                   5    
SHEET    1 AA1 2 TRP A  22  VAL A  25  0                                        
SHEET    2 AA1 2 CYS A  41  PHE A  44 -1  O  THR A  42   N  GLN A  24           
SHEET    1 AA2 5 SER A  28  GLN A  32  0                                        
SHEET    2 AA2 5 LEU A 134  THR A 139  1  O  HIS A 137   N  VAL A  29           
SHEET    3 AA2 5 GLY A 114  ARG A 122 -1  N  GLY A 114   O  VAL A 136           
SHEET    4 AA2 5 VAL A  56  ARG A  62 -1  N  HIS A  57   O  GLU A 121           
SHEET    5 AA2 5 ALA A  74  THR A  75 -1  O  ALA A  74   N  TRP A  60           
SHEET    1 AA3 4 SER A  28  GLN A  32  0                                        
SHEET    2 AA3 4 LEU A 134  THR A 139  1  O  HIS A 137   N  VAL A  29           
SHEET    3 AA3 4 GLY A 114  ARG A 122 -1  N  GLY A 114   O  VAL A 136           
SHEET    4 AA3 4 THR A 125  SER A 128 -1  O  THR A 125   N  ARG A 122           
SHEET    1 AA4 3 VAL A  37  VAL A  39  0                                        
SHEET    2 AA4 3 LEU A 103  ILE A 105 -1  O  LEU A 103   N  VAL A  39           
SHEET    3 AA4 3 PHE A  90  LEU A  92 -1  N  ARG A  91   O  SER A 104           
SHEET    1 AA5 4 LYS A 146  LEU A 148  0                                        
SHEET    2 AA5 4 LYS A 159  SER A 164 -1  O  THR A 162   N  LEU A 148           
SHEET    3 AA5 4 SER A 194  ILE A 199 -1  O  LEU A 197   N  LEU A 161           
SHEET    4 AA5 4 THR A 185  THR A 191 -1  N  SER A 186   O  ILE A 198           
SHEET    1 AA6 6 THR A 222  GLN A 228  0                                        
SHEET    2 AA6 6 ASN A 209  LYS A 215 -1  N  VAL A 214   O  THR A 223           
SHEET    3 AA6 6 ILE A 176  SER A 181 -1  N  SER A 178   O  GLN A 213           
SHEET    4 AA6 6 ILE D 176  SER D 181  1  O  TRP D 179   N  TRP A 179           
SHEET    5 AA6 6 ASN D 209  PHE D 216 -1  O  GLN D 213   N  SER D 178           
SHEET    6 AA6 6 VAL D 221  GLN D 228 -1  O  VAL D 221   N  PHE D 216           
SHEET    1 AA7 2 TRP B  22  VAL B  25  0                                        
SHEET    2 AA7 2 CYS B  41  PHE B  44 -1  O  THR B  42   N  GLN B  24           
SHEET    1 AA8 5 SER B  28  GLN B  32  0                                        
SHEET    2 AA8 5 THR B 125  THR B 139  1  O  HIS B 137   N  VAL B  29           
SHEET    3 AA8 5 GLY B 114  ARG B 122 -1  N  ARG B 122   O  THR B 125           
SHEET    4 AA8 5 VAL B  56  ARG B  62 -1  N  HIS B  57   O  GLU B 121           
SHEET    5 AA8 5 ALA B  74  THR B  75 -1  O  ALA B  74   N  TRP B  60           
SHEET    1 AA9 3 VAL B  37  VAL B  39  0                                        
SHEET    2 AA9 3 LEU B 103  ILE B 105 -1  O  LEU B 103   N  VAL B  39           
SHEET    3 AA9 3 PHE B  90  LEU B  92 -1  N  ARG B  91   O  SER B 104           
SHEET    1 AB1 4 LYS B 146  LEU B 148  0                                        
SHEET    2 AB1 4 LYS B 159  SER B 164 -1  O  THR B 162   N  LEU B 148           
SHEET    3 AB1 4 SER B 194  ILE B 199 -1  O  LEU B 197   N  LEU B 161           
SHEET    4 AB1 4 THR B 185  ARG B 190 -1  N  SER B 186   O  ILE B 198           
SHEET    1 AB2 3 ILE B 176  SER B 181  0                                        
SHEET    2 AB2 3 ASN B 209  PHE B 216 -1  O  LYS B 215   N  ILE B 176           
SHEET    3 AB2 3 VAL B 221  GLN B 228 -1  O  THR B 223   N  VAL B 214           
SHEET    1 AB3 2 TRP C  22  VAL C  25  0                                        
SHEET    2 AB3 2 CYS C  41  PHE C  44 -1  O  THR C  42   N  GLN C  24           
SHEET    1 AB4 5 SER C  28  GLN C  32  0                                        
SHEET    2 AB4 5 LEU C 134  THR C 139  1  O  HIS C 137   N  VAL C  29           
SHEET    3 AB4 5 GLY C 114  ARG C 122 -1  N  GLY C 114   O  VAL C 136           
SHEET    4 AB4 5 VAL C  56  ARG C  62 -1  N  HIS C  57   O  GLU C 121           
SHEET    5 AB4 5 ALA C  74  THR C  75 -1  O  ALA C  74   N  TRP C  60           
SHEET    1 AB5 4 SER C  28  GLN C  32  0                                        
SHEET    2 AB5 4 LEU C 134  THR C 139  1  O  HIS C 137   N  VAL C  29           
SHEET    3 AB5 4 GLY C 114  ARG C 122 -1  N  GLY C 114   O  VAL C 136           
SHEET    4 AB5 4 THR C 125  SER C 128 -1  O  THR C 125   N  ARG C 122           
SHEET    1 AB6 3 VAL C  37  VAL C  39  0                                        
SHEET    2 AB6 3 LEU C 103  ILE C 105 -1  O  LEU C 103   N  VAL C  39           
SHEET    3 AB6 3 PHE C  90  LEU C  92 -1  N  ARG C  91   O  SER C 104           
SHEET    1 AB7 4 LYS C 146  LEU C 148  0                                        
SHEET    2 AB7 4 LYS C 159  SER C 164 -1  O  SER C 164   N  LYS C 146           
SHEET    3 AB7 4 SER C 194  ILE C 199 -1  O  LEU C 197   N  LEU C 161           
SHEET    4 AB7 4 THR C 185  THR C 191 -1  N  GLY C 188   O  VAL C 196           
SHEET    1 AB8 3 ILE C 176  SER C 181  0                                        
SHEET    2 AB8 3 ASN C 209  LYS C 215 -1  O  GLN C 213   N  SER C 178           
SHEET    3 AB8 3 THR C 222  GLN C 228 -1  O  THR C 223   N  VAL C 214           
SHEET    1 AB9 2 GLN D  24  VAL D  25  0                                        
SHEET    2 AB9 2 CYS D  41  THR D  42 -1  O  THR D  42   N  GLN D  24           
SHEET    1 AC1 5 SER D  28  GLN D  32  0                                        
SHEET    2 AC1 5 THR D 125  THR D 139  1  O  HIS D 137   N  VAL D  29           
SHEET    3 AC1 5 GLY D 114  ARG D 122 -1  N  TYR D 116   O  LEU D 134           
SHEET    4 AC1 5 VAL D  56  ARG D  62 -1  N  HIS D  57   O  GLU D 121           
SHEET    5 AC1 5 ALA D  74  THR D  75 -1  O  ALA D  74   N  TRP D  60           
SHEET    1 AC2 3 VAL D  37  VAL D  39  0                                        
SHEET    2 AC2 3 LEU D 103  ILE D 105 -1  O  LEU D 103   N  VAL D  39           
SHEET    3 AC2 3 PHE D  90  LEU D  92 -1  N  ARG D  91   O  SER D 104           
SHEET    1 AC3 4 LYS D 146  LEU D 148  0                                        
SHEET    2 AC3 4 LYS D 159  SER D 164 -1  O  THR D 162   N  LEU D 148           
SHEET    3 AC3 4 SER D 194  ILE D 199 -1  O  SER D 195   N  CYS D 163           
SHEET    4 AC3 4 THR D 185  THR D 191 -1  N  SER D 186   O  ILE D 198           
SSBOND   1 CYS A   36    CYS A  169                          1555   1555  2.07  
SSBOND   2 CYS A   41    CYS A  101                          1555   1555  2.05  
SSBOND   3 CYS A  163    CYS A  212                          1555   1555  2.07  
SSBOND   4 CYS B   36    CYS B  169                          1555   1555  2.07  
SSBOND   5 CYS B   41    CYS B  101                          1555   1555  2.06  
SSBOND   6 CYS B  163    CYS B  212                          1555   1555  2.04  
SSBOND   7 CYS C   36    CYS C  169                          1555   1555  2.07  
SSBOND   8 CYS C   41    CYS C  101                          1555   1555  2.05  
SSBOND   9 CYS C  163    CYS C  212                          1555   1555  2.04  
SSBOND  10 CYS D   36    CYS D  169                          1555   1555  2.07  
SSBOND  11 CYS D   41    CYS D  101                          1555   1555  2.04  
SSBOND  12 CYS D  163    CYS D  212                          1555   1555  2.02  
LINK         ND2 ASN A 100                 C1  NAG A 301     1555   1555  1.44  
LINK         ND2 ASN A 160                 C1  NAG A 302     1555   1555  1.43  
LINK         ND2 ASN A 209                 C1  NAG A 303     1555   1555  1.43  
LINK         ND2 ASN B 100                 C1  NAG B 301     1555   1555  1.43  
LINK         ND2 ASN B 160                 C1  NAG B 302     1555   1555  1.44  
LINK         ND2 ASN B 209                 C1  NAG B 303     1555   1555  1.44  
LINK         ND2 ASN C 100                 C1  NAG C 301     1555   1555  1.44  
LINK         ND2 ASN C 160                 C1  NAG C 302     1555   1555  1.44  
LINK         ND2 ASN C 209                 C1  NAG C 303     1555   1555  1.44  
LINK         ND2 ASN D 100                 C1  NAG D 301     1555   1555  1.44  
LINK         ND2 ASN D 160                 C1  NAG D 302     1555   1555  1.43  
LINK         ND2 ASN D 209                 C1  NAG D 303     1555   1555  1.43  
CISPEP   1 SER A  131    PRO A  132          0        -5.73                     
CISPEP   2 SER B  131    PRO B  132          0        -6.84                     
CISPEP   3 SER C  131    PRO C  132          0        -6.27                     
CISPEP   4 SER D  131    PRO D  132          0        -6.01                     
CRYST1   64.960  127.040  143.040  90.00  90.00  90.00 P 21 21 21   16          
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      0.015394  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007872  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006991        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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