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Database: PDB
Entry: 5E6X
LinkDB: 5E6X
Original site: 5E6X 
HEADER    CELL ADHESION                           10-OCT-15   5E6X              
TITLE     RE-REFINEMENT OF THE CRYSTAL STRUCTURE OF THE PLEXIN-SEMAPHORIN-      
TITLE    2 INTEGRIN DOMAIN/HYBRID DOMAIN/I-EGF1 SEGMENT FROM THE HUMAN INTEGRIN 
TITLE    3 B2 SUBUNIT                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN BETA-2;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 23-122 AND 362 535;                           
COMPND   5 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA-1/CR3/P150,95       
COMPND   6 SUBUNIT BETA,COMPLEMENT RECEPTOR C3 SUBUNIT BETA;                    
COMPND   7 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: ITGB2, CD18, MFI7;                                             
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    CD18 FRAGMENT, CELL ADHESION                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.SPRINGER,M.SEN                                                    
REVDAT   6   27-SEP-17 5E6X    1       REMARK                                   
REVDAT   5   15-MAR-17 5E6X    1       JRNL   REMARK                            
REVDAT   4   20-JUL-16 5E6X    1       REMARK                                   
REVDAT   3   11-MAY-16 5E6X    1       JRNL                                     
REVDAT   2   16-MAR-16 5E6X    1       JRNL                                     
REVDAT   1   02-MAR-16 5E6X    0                                                
JRNL        AUTH   M.SEN,T.A.SPRINGER                                           
JRNL        TITL   LEUKOCYTE INTEGRIN ALPHA L BETA 2 HEADPIECE STRUCTURES: THE  
JRNL        TITL 2 ALPHA I DOMAIN, THE POCKET FOR THE INTERNAL LIGAND, AND      
JRNL        TITL 3 CONCERTED MOVEMENTS OF ITS LOOPS.                            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 113  2940 2016              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   26936951                                                     
JRNL        DOI    10.1073/PNAS.1601379113                                      
REMARK   0                                                                      
REMARK   0 THIS ENTRY 5E6X REFLECTS AN ALTERNATIVE MODELING OF THE              
REMARK   0 STRUCTURAL DATA IN R2P26SF ORIGINAL DATA DETERMINED BY AUTHOR:       
REMARK   0 SHI, M., FOO, S.Y., TAN, S.M., MITCHELL, E.P., LAW, S.K.A.,          
REMARK   0 LESCAR, J.                                                           
REMARK   0 ORIGINAL DATA REFERENCE 1                                            
REMARK   0  PDB ID: 2p26                                                        
REMARK   0  AUTH   M.SHI,S.Y.FOO,S.M.TAN,E.P.MITCHELL,S.K.LAW,J.LESCAR          
REMARK   0  TITL   A STRUCTURAL HYPOTHESIS FOR THE TRANSITION BETWEEN BENT AND  
REMARK   0  TITL 2 EXTENDED CONFORMATIONS OF THE LEUKOCYTE BETA2 INTEGRINS.     
REMARK   0  REF    J. BIOL. CHEM.                V. 282 30198 2007              
REMARK   0  REFN                   ISSN 0021-9258                               
REMARK   0  PMID   17673459                                                     
REMARK   0  DOI    10.1074/JBC.M701670200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
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) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 21812                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1116                            
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 27.8737 -  3.4981    1.00     2923   180  0.1627 0.2129        
REMARK   3     2  3.4981 -  2.7774    1.00     2844   164  0.1881 0.2591        
REMARK   3     3  2.7774 -  2.4265    1.00     2816   161  0.2176 0.2635        
REMARK   3     4  2.4265 -  2.2048    1.00     2813   154  0.2114 0.2246        
REMARK   3     5  2.2048 -  2.0468    1.00     2820   144  0.2194 0.2652        
REMARK   3     6  2.0468 -  1.9261    0.99     2792   141  0.2253 0.2682        
REMARK   3     7  1.9261 -  1.8297    0.78     2168   110  0.2705 0.3367        
REMARK   3     8  1.8297 -  1.7501    0.53     1520    62  0.3288 0.4404        
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           2320                                  
REMARK   3   ANGLE     :  0.725           3129                                  
REMARK   3   CHIRALITY :  0.052            343                                  
REMARK   3   PLANARITY :  0.002            422                                  
REMARK   3   DIHEDRAL  : 11.524            876                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 55 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9977  -7.3953 -32.8185              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1292 T22:   0.1057                                     
REMARK   3      T33:   0.1421 T12:   0.0123                                     
REMARK   3      T13:   0.0046 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9106 L22:   1.0506                                     
REMARK   3      L33:   0.5025 L12:   0.2806                                     
REMARK   3      L13:  -0.3768 L23:  -0.2256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0321 S12:  -0.0132 S13:  -0.0861                       
REMARK   3      S21:   0.0394 S22:   0.0386 S23:   0.0097                       
REMARK   3      S31:  -0.0761 S32:  -0.1135 S33:   0.0001                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 79 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   5.1629 -16.1358 -15.7239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2074 T22:   0.1913                                     
REMARK   3      T33:   0.2683 T12:  -0.0032                                     
REMARK   3      T13:  -0.0643 T23:   0.0294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3002 L22:   0.3171                                     
REMARK   3      L33:   0.5501 L12:   0.2544                                     
REMARK   3      L13:  -0.0788 L23:   0.1926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2592 S12:  -0.0904 S13:  -0.3310                       
REMARK   3      S21:   0.0450 S22:  -0.0644 S23:  -0.1537                       
REMARK   3      S31:   0.3304 S32:   0.1809 S33:   0.0029                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 80 THROUGH 344 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0200  -8.7908 -11.1255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1758 T22:   0.1646                                     
REMARK   3      T33:   0.1216 T12:  -0.0290                                     
REMARK   3      T13:  -0.0301 T23:  -0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5763 L22:   0.5885                                     
REMARK   3      L33:   0.3034 L12:  -0.3507                                     
REMARK   3      L13:  -0.2270 L23:  -0.1570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0389 S12:  -0.2546 S13:  -0.1043                       
REMARK   3      S21:   0.3105 S22:   0.0445 S23:   0.1451                       
REMARK   3      S31:  -0.0610 S32:   0.2203 S33:  -0.0199                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 345 THROUGH 421 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7744  -3.7199 -11.7936              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1704 T22:   0.1997                                     
REMARK   3      T33:   0.1669 T12:  -0.0095                                     
REMARK   3      T13:   0.0147 T23:  -0.0311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2849 L22:   0.3360                                     
REMARK   3      L33:   0.3646 L12:  -0.1270                                     
REMARK   3      L13:   0.0856 L23:  -0.3343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0068 S12:  -0.1980 S13:   0.1565                       
REMARK   3      S21:   0.0833 S22:   0.0623 S23:   0.0185                       
REMARK   3      S31:  -0.1595 S32:   0.0667 S33:   0.0001                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 422 THROUGH 435 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.7849 -19.7209 -39.5005              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2493 T22:   0.1962                                     
REMARK   3      T33:   0.2679 T12:  -0.0103                                     
REMARK   3      T13:  -0.0013 T23:  -0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0858 L22:   0.0442                                     
REMARK   3      L33:   0.2484 L12:  -0.0033                                     
REMARK   3      L13:  -0.0028 L23:   0.0024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0873 S12:  -0.1696 S13:  -0.0679                       
REMARK   3      S21:   0.0854 S22:  -0.0180 S23:  -0.1856                       
REMARK   3      S31:   0.2810 S32:   0.0765 S33:  -0.0020                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 436 THROUGH 473 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.3802 -11.5783 -53.9363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1933 T22:   0.1626                                     
REMARK   3      T33:   0.1235 T12:   0.0765                                     
REMARK   3      T13:   0.0305 T23:   0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9452 L22:   0.3268                                     
REMARK   3      L33:   0.3283 L12:  -0.0373                                     
REMARK   3      L13:   0.2587 L23:   0.2791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2810 S12:   0.0308 S13:  -0.0150                       
REMARK   3      S21:  -0.0835 S22:  -0.0997 S23:  -0.0334                       
REMARK   3      S31:  -0.2023 S32:  -0.0942 S33:   0.1581                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 474 THROUGH 505 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -35.3296  -2.7556 -47.5593              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2152 T22:   0.2674                                     
REMARK   3      T33:   0.1701 T12:   0.0445                                     
REMARK   3      T13:   0.0151 T23:   0.0584                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5541 L22:   0.5087                                     
REMARK   3      L33:   0.4100 L12:  -0.1765                                     
REMARK   3      L13:   0.0601 L23:   0.2211                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1193 S12:   0.2821 S13:   0.1201                       
REMARK   3      S21:   0.0730 S22:   0.0168 S23:   0.0064                       
REMARK   3      S31:  -0.1102 S32:   0.0228 S33:   0.0035                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 506 THROUGH 519 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -44.4822  -2.1595 -44.5483              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2618 T22:   0.2559                                     
REMARK   3      T33:   0.1841 T12:   0.0679                                     
REMARK   3      T13:  -0.0425 T23:   0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3167 L22:   1.9255                                     
REMARK   3      L33:   0.5137 L12:  -0.1573                                     
REMARK   3      L13:   0.6198 L23:   0.5794                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3757 S12:   0.5553 S13:  -0.4142                       
REMARK   3      S21:  -0.0309 S22:  -0.3324 S23:   0.2589                       
REMARK   3      S31:   0.4450 S32:   0.1429 S33:   0.0395                       
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 5E6X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214455.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1YUK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: AUTHOR USED THE SF DATA FROM ENTRY 2P26                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       15.42650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   OD1  ASP A    54     O    HOH A   701              2.12            
REMARK 500   O    HOH A   702     O    HOH A   811              2.15            
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   O    HOH A   712     O    HOH A   764     2454     2.12            
REMARK 500   O    HOH A   703     O    HOH A   712     2444     2.13            
REMARK 500   O    HOH A   708     O    HOH A   772     1565     2.14            
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    ASP A  58       75.26   -160.20                                   
REMARK 500    ASP A  68     -179.69    -67.42                                   
REMARK 500    ALA A 100      -68.06   -106.31                                   
REMARK 500    LYS A 340      -81.91   -122.45                                   
REMARK 500    LEU A 341     -138.68     67.91                                   
REMARK 500    ASP A 429     -161.64   -103.08                                   
REMARK 500    HIS A 438       16.58     57.18                                   
REMARK 500    GLN A 464     -131.04     55.48                                   
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 NAG A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound   
REMARK 800  to ASN A 28                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound   
REMARK 800  to ASN A 94                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2P26   RELATED DB: PDB                                   
REMARK 900 THIS ENTRY 5E6X REFLECTS AN ALTERNATIVE MODELING OF X-RAY DATA       
REMARK 900 R2P26SF                                                              
DBREF  5E6X A    1   100  UNP    P05107   ITB2_HUMAN      23    122             
DBREF  5E6X A  340   513  UNP    P05107   ITB2_HUMAN     362    535             
SEQADV 5E6X HIS A  514  UNP  P05107              EXPRESSION TAG                 
SEQADV 5E6X HIS A  515  UNP  P05107              EXPRESSION TAG                 
SEQADV 5E6X HIS A  516  UNP  P05107              EXPRESSION TAG                 
SEQADV 5E6X HIS A  517  UNP  P05107              EXPRESSION TAG                 
SEQADV 5E6X HIS A  518  UNP  P05107              EXPRESSION TAG                 
SEQADV 5E6X HIS A  519  UNP  P05107              EXPRESSION TAG                 
SEQRES   1 A  280  GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU          
SEQRES   2 A  280  CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS          
SEQRES   3 A  280  LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG          
SEQRES   4 A  280  CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA          
SEQRES   5 A  280  ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR          
SEQRES   6 A  280  GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO          
SEQRES   7 A  280  GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA          
SEQRES   8 A  280  ALA PHE ASN VAL THR PHE ARG ARG ALA LYS LEU SER SER          
SEQRES   9 A  280  ARG VAL PHE LEU ASP HIS ASN ALA LEU PRO ASP THR LEU          
SEQRES  10 A  280  LYS VAL THR TYR ASP SER PHE CYS SER ASN GLY VAL THR          
SEQRES  11 A  280  HIS ARG ASN GLN PRO ARG GLY ASP CYS ASP GLY VAL GLN          
SEQRES  12 A  280  ILE ASN VAL PRO ILE THR PHE GLN VAL LYS VAL THR ALA          
SEQRES  13 A  280  THR GLU CYS ILE GLN GLU GLN SER PHE VAL ILE ARG ALA          
SEQRES  14 A  280  LEU GLY PHE THR ASP ILE VAL THR VAL GLN VAL LEU PRO          
SEQRES  15 A  280  GLN CYS GLU CYS ARG CYS ARG ASP GLN SER ARG ASP ARG          
SEQRES  16 A  280  SER LEU CYS HIS GLY LYS GLY PHE LEU GLU CYS GLY ILE          
SEQRES  17 A  280  CYS ARG CYS ASP THR GLY TYR ILE GLY LYS ASN CYS GLU          
SEQRES  18 A  280  CYS GLN THR GLN GLY ARG SER SER GLN GLU LEU GLU GLY          
SEQRES  19 A  280  SER CYS ARG LYS ASP ASN ASN SER ILE ILE CYS SER GLY          
SEQRES  20 A  280  LEU GLY ASP CYS VAL CYS GLY GLN CYS LEU CYS HIS THR          
SEQRES  21 A  280  SER ASP VAL PRO GLY LYS LEU ILE TYR GLY GLN TYR CYS          
SEQRES  22 A  280  GLU HIS HIS HIS HIS HIS HIS                                  
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   5  HOH   *260(H2 O)                                                    
HELIX    1 AA1 SER A   10  GLU A   16  1                                   7    
HELIX    2 AA2 PRO A   35  ILE A   38  5                                   4    
HELIX    3 AA3 THR A   42  ARG A   49  1                                   8    
HELIX    4 AA4 ALA A   52  ASP A   54  5                                   3    
HELIX    5 AA5 SER A  435  GLY A  439  5                                   5    
HELIX    6 AA6 SER A  467  SER A  474  1                                   8    
HELIX    7 AA7 ILE A  482  GLY A  486  5                                   5    
SHEET    1 AA1 3 CYS A  40  ASP A  41  0                                        
SHEET    2 AA1 3 THR A  22  CYS A  24 -1  N  THR A  22   O  ASP A  41           
SHEET    3 AA1 3 ILE A  56  MET A  57 -1  O  MET A  57   N  TRP A  23           
SHEET    1 AA2 6 LEU A  62  GLN A  66  0                                        
SHEET    2 AA2 6 LYS A  80  LEU A  85 -1  O  THR A  82   N  GLU A  64           
SHEET    3 AA2 6 VAL A 415  PRO A 421  1  O  GLN A 418   N  LEU A  83           
SHEET    4 AA2 6 GLN A 402  ALA A 408 -1  N  GLN A 402   O  VAL A 419           
SHEET    5 AA2 6 VAL A 345  HIS A 349 -1  N  ASP A 348   O  ARG A 407           
SHEET    6 AA2 6 GLY A 376  CYS A 378 -1  O  GLY A 376   N  LEU A 347           
SHEET    1 AA3 5 LEU A  76  SER A  77  0                                        
SHEET    2 AA3 5 ALA A  91  PHE A  97 -1  O  THR A  96   N  SER A  77           
SHEET    3 AA3 5 ILE A 387  ALA A 395 -1  O  VAL A 391   N  PHE A  93           
SHEET    4 AA3 5 LEU A 356  PHE A 363 -1  N  LYS A 357   O  THR A 394           
SHEET    5 AA3 5 THR A 369  GLN A 373 -1  O  GLN A 373   N  TYR A 360           
SHEET    1 AA4 2 GLY A 441  GLU A 444  0                                        
SHEET    2 AA4 2 ILE A 447  CYS A 450 -1  O  ARG A 449   N  PHE A 442           
SHEET    1 AA5 2 TYR A 454  ILE A 455  0                                        
SHEET    2 AA5 2 CYS A 461  GLN A 462 -1  O  CYS A 461   N  ILE A 455           
SHEET    1 AA6 2 GLY A 488  VAL A 491  0                                        
SHEET    2 AA6 2 GLN A 494  CYS A 497 -1  O  LEU A 496   N  ASP A 489           
SHEET    1 AA7 2 GLY A 504  TYR A 508  0                                        
SHEET    2 AA7 2 HIS A 514  HIS A 519 -1  O  HIS A 519   N  GLY A 504           
SSBOND   1 CYS A    3    CYS A   21                          1555   1555  2.03  
SSBOND   2 CYS A   11    CYS A  425                          1555   1555  2.03  
SSBOND   3 CYS A   14    CYS A   40                          1555   1555  2.03  
SSBOND   4 CYS A   24    CYS A   51                          1555   1555  2.03  
SSBOND   5 CYS A  364    CYS A  378                          1555   1555  2.03  
SSBOND   6 CYS A  398    CYS A  423                          1555   1555  2.03  
SSBOND   7 CYS A  427    CYS A  445                          1555   1555  2.03  
SSBOND   8 CYS A  437    CYS A  448                          1555   1555  2.03  
SSBOND   9 CYS A  450    CYS A  459                          1555   1555  2.03  
SSBOND  10 CYS A  461    CYS A  492                          1555   1555  2.04  
SSBOND  11 CYS A  475    CYS A  490                          1555   1555  2.04  
SSBOND  12 CYS A  484    CYS A  495                          1555   1555  2.03  
SSBOND  13 CYS A  497    CYS A  512                          1555   1555  2.03  
LINK         ND2 ASN A  28                 C1  NAG A 603     1555   1555  1.44  
LINK         ND2 ASN A  94                 C1  NAG A 601     1555   1555  1.44  
LINK         ND2 ASN A 479                 C1  NAG A 602     1555   1555  1.44  
CISPEP   1 SER A   77    PRO A   78          0         0.98                     
SITE     1 AC1  5 HIS A 438  LYS A 440  ASN A 479  HOH A 708                    
SITE     2 AC1  5 HOH A 709                                                     
SITE     1 AC2  5 ASN A  28  ASN A 458  ASN A 480  HOH A 721                    
SITE     2 AC2  5 HOH A 769                                                     
SITE     1 AC3  4 ASN A  94  GLN A 390  HOH A 783  HOH A 828                    
CRYST1   58.489   30.853   65.157  90.00  94.29  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017097  0.000000  0.001283        0.00000                         
SCALE2      0.000000  0.032412  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015391        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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