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Database: PDB
Entry: 2P28
LinkDB: 2P28
Original site: 2P28 
HEADER    CELL ADHESION                           07-MAR-07   2P28              
TITLE     STRUCTURE OF THE PHE2 AND PHE3 FRAGMENTS OF THE INTEGRIN BETA2 SUBUNIT
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN BETA-2;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PHE2 FRAGMENT;                                             
COMPND   5 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA- 1/CR3/P150,95      
COMPND   6 SUBUNIT BETA, COMPLEMENT RECEPTOR C3 SUBUNIT BETA, CD18 ANTIGEN;     
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-2;                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: PHE3 FRAGMENT;                                             
COMPND  12 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA- 1/CR3/P150,95      
COMPND  13 SUBUNIT BETA, COMPLEMENT RECEPTOR C3 SUBUNIT BETA, CD18 ANTIGEN;     
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293_GNTI;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PIRES2-EGFP;                              
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  16 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HEK293_GNTI;                            
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PIRES2-EGFP                               
KEYWDS    INTEGRIN BETA2 SUBUNIT, HYBRID DOMAIN, PSI DOMAIN, I-EGF DOMAINS,     
KEYWDS   2 CELL ADHESION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SHI,S.Y.FOO,S.M.TAN,E.P.MITCHELL,S.K.A.LAW,J.LESCAR                 
REVDAT   4   13-JUL-11 2P28    1       VERSN                                    
REVDAT   3   24-FEB-09 2P28    1       VERSN                                    
REVDAT   2   17-JUN-08 2P28    1       JRNL                                     
REVDAT   1   14-AUG-07 2P28    0                                                
JRNL        AUTH   M.SHI,S.Y.FOO,S.M.TAN,E.P.MITCHELL,S.K.A.LAW,J.LESCAR        
JRNL        TITL   A STRUCTURAL HYPOTHESIS FOR THE TRANSITION BETWEEN BENT AND  
JRNL        TITL 2 EXTENDED CONFORMATIONS OF THE LEUKOCYTE BETA2 INTEGRINS      
JRNL        REF    J.BIOL.CHEM.                  V. 282 30198 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17673459                                                     
JRNL        DOI    10.1074/JBC.M701670200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 18723                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.263                           
REMARK   3   R VALUE            (WORKING SET) : 0.261                           
REMARK   3   FREE R VALUE                     : 0.308                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 964                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1255                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 70                           
REMARK   3   BIN FREE R VALUE                    : 0.4050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2355                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 199                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : UNVERIFIED                                          
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.16000                                              
REMARK   3    B22 (A**2) : 0.16000                                              
REMARK   3    B33 (A**2) : -0.24000                                             
REMARK   3    B12 (A**2) : 0.08000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.341         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.262         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.196         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.734         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.912                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2408 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2053 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3257 ; 1.223 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4816 ; 0.800 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   305 ; 6.312 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   355 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2710 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   466 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   442 ; 0.174 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2404 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1536 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   142 ; 0.174 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    28 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   100 ; 0.231 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.158 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1532 ; 0.716 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2453 ; 1.337 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   876 ; 1.332 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   804 ; 2.281 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        B   431                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5719  19.7650   9.1114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5006 T22:   0.4081                                     
REMARK   3      T33:   0.4655 T12:   0.0153                                     
REMARK   3      T13:  -0.0505 T23:  -0.0609                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1953 L22:   0.6294                                     
REMARK   3      L33:   2.0810 L12:  -0.3745                                     
REMARK   3      L13:  -0.5242 L23:   0.9519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0357 S12:   0.1246 S13:  -0.0428                       
REMARK   3      S21:   0.1741 S22:   0.0322 S23:  -0.0664                       
REMARK   3      S31:   0.3092 S32:  -0.1245 S33:  -0.0679                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   435        B   466                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.9354  23.4167  42.1519              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7003 T22:   0.2709                                     
REMARK   3      T33:   0.3286 T12:  -0.3067                                     
REMARK   3      T13:   0.0132 T23:  -0.2175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.9432 L22:   6.7843                                     
REMARK   3      L33:  28.2786 L12:  -6.6546                                     
REMARK   3      L13: -12.2910 L23:  11.4915                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2904 S12:  -0.1926 S13:   0.7016                       
REMARK   3      S21:  -0.1336 S22:  -0.8847 S23:   0.3085                       
REMARK   3      S31:   1.7915 S32:  -0.7804 S33:   0.5943                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   470        B   556                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.1695  44.7480  69.1864              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4187 T22:   0.4547                                     
REMARK   3      T33:   0.5230 T12:  -0.0847                                     
REMARK   3      T13:   0.0100 T23:  -0.0696                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7190 L22:   0.5953                                     
REMARK   3      L33:   3.9696 L12:   0.7188                                     
REMARK   3      L13:  -1.6289 L23:   0.3703                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2513 S12:  -0.0634 S13:   0.0195                       
REMARK   3      S21:   0.0830 S22:  -0.1227 S23:  -0.0328                       
REMARK   3      S31:  -0.2204 S32:   0.2268 S33:  -0.1286                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2P28 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041874.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18866                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
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) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
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: PHASES                                                
REMARK 200 STARTING MODEL: 1YUK, 1L3Y                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULPHATE, 15% PEG4000,     
REMARK 280  5% ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      282.61600            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      141.30800            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      211.96200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       70.65400            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      353.27000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      282.61600            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      141.30800            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       70.65400            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      211.96200            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      353.27000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     HIS A    69                                                      
REMARK 465     ASN A    70                                                      
REMARK 465     GLY A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     ASP B   433                                                      
REMARK 465     ARG B   434                                                      
REMARK 465     SER B   467                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG B 466    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 468    OG                                                  
REMARK 470     GLN B 469    CG   CD   OE1  NE2                                  
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 B   557     O    HOH B   594     8665     1.84            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    ASP A  68   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 377   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 515   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
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    GLU A   2      115.44   -176.51                                   
REMARK 500    PHE A   6      -79.35    -75.85                                   
REMARK 500    ASP A  58       74.33   -159.06                                   
REMARK 500    LYS A  74      -76.22    -84.66                                   
REMARK 500    GLU B 444      110.39   -169.10                                   
REMARK 500    GLN B 464     -153.10   -106.24                                   
REMARK 500    ASN B 480       46.12   -108.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER B  431     ARG B  432                 -134.39                    
REMARK 500 SER B  435     LEU B  436                  -58.96                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 413        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH A 428        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH B 563        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH B 617        DISTANCE =  7.10 ANGSTROMS                       
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 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2P26   RELATED DB: PDB                                   
DBREF  2P28 A    1   100  UNP    P05107   ITB2_HUMAN      23    122             
DBREF  2P28 B  340   552  UNP    P05107   ITB2_HUMAN     362    574             
SEQADV 2P28 HIS B  553  UNP  P05107              EXPRESSION TAG                 
SEQADV 2P28 HIS B  554  UNP  P05107              EXPRESSION TAG                 
SEQADV 2P28 HIS B  555  UNP  P05107              EXPRESSION TAG                 
SEQADV 2P28 HIS B  556  UNP  P05107              EXPRESSION TAG                 
SEQRES   1 A  100  GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU          
SEQRES   2 A  100  CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS          
SEQRES   3 A  100  LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG          
SEQRES   4 A  100  CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA          
SEQRES   5 A  100  ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR          
SEQRES   6 A  100  GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO          
SEQRES   7 A  100  GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA          
SEQRES   8 A  100  ALA PHE ASN VAL THR PHE ARG ARG ALA                          
SEQRES   1 B  217  LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA LEU          
SEQRES   2 B  217  PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS SER          
SEQRES   3 B  217  ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP CYS          
SEQRES   4 B  217  ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN VAL          
SEQRES   5 B  217  LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER PHE          
SEQRES   6 B  217  VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR VAL          
SEQRES   7 B  217  GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP GLN          
SEQRES   8 B  217  SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE LEU          
SEQRES   9 B  217  GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE GLY          
SEQRES  10 B  217  LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER GLN          
SEQRES  11 B  217  GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER ILE          
SEQRES  12 B  217  ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN CYS          
SEQRES  13 B  217  LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE TYR          
SEQRES  14 B  217  GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU ARG          
SEQRES  15 B  217  TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY LEU          
SEQRES  16 B  217  CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE GLU          
SEQRES  17 B  217  GLY SER ALA CYS GLN HIS HIS HIS HIS                          
HET    NAG  A 401      15                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3  NAG    C8 H15 N O6                                                  
FORMUL   4  HOH   *199(H2 O)                                                    
HELIX    1   1 SER A   10  GLY A   18  1                                   9    
HELIX    2   2 LYS A   26  THR A   30  5                                   5    
HELIX    3   3 PRO A   35  ILE A   38  5                                   4    
HELIX    4   4 THR A   42  MET A   48  1                                   7    
HELIX    5   5 ALA A   52  ASP A   54  5                                   3    
HELIX    6   6 SER B  468  ARG B  476  5                                   9    
HELIX    7   7 ILE B  482  GLY B  486  5                                   5    
SHEET    1   A 3 CYS A  40  ASP A  41  0                                        
SHEET    2   A 3 THR A  22  CYS A  24 -1  N  THR A  22   O  ASP A  41           
SHEET    3   A 3 ILE A  56  MET A  57 -1  O  MET A  57   N  TRP A  23           
SHEET    1   B 6 LEU A  62  GLU A  67  0                                        
SHEET    2   B 6 LYS A  80  LEU A  85 -1  O  THR A  82   N  GLU A  64           
SHEET    3   B 6 ILE B 414  PRO B 421  1  O  GLN B 418   N  LEU A  83           
SHEET    4   B 6 GLN B 402  ALA B 408 -1  N  GLN B 402   O  VAL B 419           
SHEET    5   B 6 VAL B 345  HIS B 349 -1  N  ASP B 348   O  ARG B 407           
SHEET    6   B 6 GLY B 376  CYS B 378 -1  O  CYS B 378   N  VAL B 345           
SHEET    1   C 5 LEU A  76  SER A  77  0                                        
SHEET    2   C 5 ALA A  91  PHE A  97 -1  O  THR A  96   N  SER A  77           
SHEET    3   C 5 ILE B 387  ALA B 395 -1  O  VAL B 393   N  ALA A  91           
SHEET    4   C 5 LEU B 356  PHE B 363 -1  N  PHE B 363   O  THR B 388           
SHEET    5   C 5 THR B 369  GLN B 373 -1  O  GLN B 373   N  TYR B 360           
SHEET    1   D 2 GLY B 441  GLU B 444  0                                        
SHEET    2   D 2 ILE B 447  CYS B 450 -1  O  ARG B 449   N  PHE B 442           
SHEET    1   E 2 TYR B 454  ILE B 455  0                                        
SHEET    2   E 2 CYS B 461  GLN B 462 -1  O  CYS B 461   N  ILE B 455           
SHEET    1   F 2 GLY B 488  VAL B 491  0                                        
SHEET    2   F 2 GLN B 494  CYS B 497 -1  O  GLN B 494   N  VAL B 491           
SHEET    1   G 2 ILE B 507  TYR B 508  0                                        
SHEET    2   G 2 CYS B 514  ASP B 515 -1  O  CYS B 514   N  TYR B 508           
SHEET    1   H 2 ARG B 521  TYR B 522  0                                        
SHEET    2   H 2 GLN B 525  VAL B 526 -1  O  GLN B 525   N  TYR B 522           
SHEET    1   I 2 GLY B 533  PHE B 536  0                                        
SHEET    2   I 2 LYS B 539  CYS B 542 -1  O  ARG B 541   N  LEU B 534           
SHEET    1   J 2 PHE B 546  GLU B 547  0                                        
SHEET    2   J 2 HIS B 553  HIS B 554 -1  O  HIS B 553   N  GLU B 547           
SSBOND   1 CYS A    3    CYS A   21                          1555   1555  2.06  
SSBOND   2 CYS A   11    CYS B  425                          1555   1555  2.03  
SSBOND   3 CYS A   14    CYS A   40                          1555   1555  2.05  
SSBOND   4 CYS A   24    CYS A   51                          1555   1555  2.04  
SSBOND   5 CYS B  364    CYS B  378                          1555   1555  2.02  
SSBOND   6 CYS B  398    CYS B  423                          1555   1555  2.03  
SSBOND   7 CYS B  427    CYS B  445                          1555   1555  2.03  
SSBOND   8 CYS B  437    CYS B  448                          1555   1555  2.04  
SSBOND   9 CYS B  450    CYS B  459                          1555   1555  2.04  
SSBOND  10 CYS B  461    CYS B  492                          1555   1555  2.07  
SSBOND  11 CYS B  475    CYS B  490                          1555   1555  2.06  
SSBOND  12 CYS B  484    CYS B  495                          1555   1555  2.06  
SSBOND  13 CYS B  497    CYS B  512                          1555   1555  2.06  
SSBOND  14 CYS B  514    CYS B  537                          1555   1555  2.07  
SSBOND  15 CYS B  519    CYS B  535                          1555   1555  2.04  
SSBOND  16 CYS B  527    CYS B  540                          1555   1555  1.83  
SSBOND  17 CYS B  542    CYS B  551                          1555   1555  2.03  
CISPEP   1 SER A   77    PRO A   78          0        -1.55                     
SITE     1 AC1 12 ASN A  94  HOH A 405  HOH A 414  ALA B 351                    
SITE     2 AC1 12 LEU B 352  PRO B 353  ASP B 354  PHE B 363                    
SITE     3 AC1 12 GLN B 390  GLU B 520  HOH B 561  HOH B 653                    
CRYST1   52.260   52.260  423.924  90.00  90.00 120.00 P 65 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019135  0.011048  0.000000        0.00000                         
SCALE2      0.000000  0.022095  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002359        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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