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Database: PDB
Entry: 2P26
LinkDB: 2P26
Original site: 2P26 
HEADER    CELL ADHESION                           06-MAR-07   2P26              
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 AND PHE3;                                             
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                                                      
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                               
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   5   16-AUG-17 2P26    1       SOURCE REMARK                            
REVDAT   4   13-JUL-11 2P26    1       VERSN                                    
REVDAT   3   24-FEB-09 2P26    1       VERSN                                    
REVDAT   2   17-JUN-08 2P26    1       JRNL                                     
REVDAT   1   14-AUG-07 2P26    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.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 21815                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1117                            
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) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.80                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 817                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 48.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 36                           
REMARK   3   BIN FREE R VALUE                    : 0.5920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2156                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 268                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.21000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.26000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.20000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.179         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.870         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2281 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3095 ; 1.169 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   285 ; 5.817 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   109 ;35.744 ;24.220       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   384 ;15.033 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;12.783 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   338 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1740 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   957 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1516 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   207 ; 0.111 ; 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):   157 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    41 ; 0.133 ; 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):  1448 ; 0.378 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2275 ; 0.649 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   907 ; 1.101 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   820 ; 1.794 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 10                                         
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        A    63                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8980  -7.8590 -32.0500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0622 T22:   0.0056                                     
REMARK   3      T33:   0.0181 T12:   0.0117                                     
REMARK   3      T13:  -0.0035 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0658 L22:   2.2788                                     
REMARK   3      L33:   1.7243 L12:   0.1150                                     
REMARK   3      L13:   0.7279 L23:  -0.2921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0247 S12:  -0.0400 S13:  -0.0597                       
REMARK   3      S21:   0.0526 S22:  -0.0008 S23:   0.0902                       
REMARK   3      S31:  -0.0941 S32:  -0.1010 S33:  -0.0240                       
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 :   A    64        A    75                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0320 -18.8270 -11.8320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3017 T22:   0.3394                                     
REMARK   3      T33:   0.4643 T12:   0.0437                                     
REMARK   3      T13:  -0.0759 T23:   0.1047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8094 L22:   2.0915                                     
REMARK   3      L33:   9.0043 L12:  -1.5293                                     
REMARK   3      L13:   2.8790 L23:  -2.5158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5910 S12:  -0.0352 S13:  -1.8147                       
REMARK   3      S21:   0.0828 S22:  -0.2474 S23:  -0.1995                       
REMARK   3      S31:   0.9772 S32:   1.0782 S33:  -0.3436                       
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 :   A    76        A   351                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6760  -7.7560 -11.0730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0689 T22:   0.0287                                     
REMARK   3      T33:  -0.0397 T12:  -0.0193                                     
REMARK   3      T13:  -0.0096 T23:  -0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9144 L22:   1.3659                                     
REMARK   3      L33:   1.3444 L12:  -0.4509                                     
REMARK   3      L13:   0.9498 L23:  -0.0421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0428 S12:  -0.4148 S13:  -0.1406                       
REMARK   3      S21:   0.2024 S22:   0.0556 S23:   0.0413                       
REMARK   3      S31:   0.0195 S32:  -0.0226 S33:  -0.0983                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   352        A   388                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.1490  -2.3460  -5.1440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0431 T22:   0.0937                                     
REMARK   3      T33:  -0.0337 T12:  -0.0103                                     
REMARK   3      T13:  -0.0001 T23:  -0.0809                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2338 L22:   2.6518                                     
REMARK   3      L33:   8.0144 L12:  -0.6692                                     
REMARK   3      L13:   1.3006 L23:  -1.5501                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0421 S12:  -0.6335 S13:   0.2584                       
REMARK   3      S21:   0.2909 S22:   0.2343 S23:   0.0960                       
REMARK   3      S31:  -0.0785 S32:  -0.2294 S33:  -0.1921                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   389        A   426                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9660  -6.9340 -20.7700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0586 T22:   0.0098                                     
REMARK   3      T33:   0.0089 T12:  -0.0193                                     
REMARK   3      T13:  -0.0066 T23:  -0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6964 L22:   0.3879                                     
REMARK   3      L33:   1.2595 L12:  -0.1352                                     
REMARK   3      L13:   1.5244 L23:  -0.0132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0394 S12:   0.0895 S13:  -0.0657                       
REMARK   3      S21:   0.0496 S22:  -0.0321 S23:   0.0536                       
REMARK   3      S31:  -0.0029 S32:   0.1464 S33:  -0.0073                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   427        A   447                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3420 -20.1960 -45.9730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0737 T22:  -0.0050                                     
REMARK   3      T33:  -0.0001 T12:  -0.0058                                     
REMARK   3      T13:  -0.0172 T23:   0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9944 L22:   2.2312                                     
REMARK   3      L33:   3.8742 L12:  -1.8910                                     
REMARK   3      L13:  -0.0582 L23:   0.5789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0916 S12:   0.0142 S13:  -0.0987                       
REMARK   3      S21:  -0.1132 S22:  -0.0895 S23:   0.0570                       
REMARK   3      S31:   0.2312 S32:  -0.0664 S33:  -0.0021                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   448        A   461                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.8670 -12.5890 -52.9150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0536 T22:   0.0600                                     
REMARK   3      T33:  -0.0193 T12:   0.0378                                     
REMARK   3      T13:  -0.0075 T23:   0.0282                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5756 L22:   4.9567                                     
REMARK   3      L33:   5.1811 L12:  -2.8482                                     
REMARK   3      L13:   0.8871 L23:  -0.5513                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1884 S12:   0.3508 S13:   0.4120                       
REMARK   3      S21:  -0.1237 S22:  -0.2035 S23:  -0.1579                       
REMARK   3      S31:  -0.1364 S32:  -0.0458 S33:   0.0151                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   462        A   484                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.1840  -0.7220 -57.0380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2639 T22:   0.2003                                     
REMARK   3      T33:   0.0157 T12:   0.0120                                     
REMARK   3      T13:   0.0995 T23:   0.0687                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3570 L22:   6.2386                                     
REMARK   3      L33:   3.2061 L12:   1.2123                                     
REMARK   3      L13:   2.9453 L23:  -0.8359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3735 S12:   0.3832 S13:   0.4884                       
REMARK   3      S21:  -1.1835 S22:   0.1059 S23:  -0.4308                       
REMARK   3      S31:  -0.6054 S32:   0.6698 S33:  -0.4793                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   485        A   511                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.5940  -5.8630 -45.3240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0273 T22:   0.0824                                     
REMARK   3      T33:  -0.0674 T12:   0.0670                                     
REMARK   3      T13:  -0.0362 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1521 L22:   1.8016                                     
REMARK   3      L33:   4.3139 L12:  -0.6472                                     
REMARK   3      L13:  -2.9893 L23:   1.1772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1389 S12:   0.4367 S13:   0.0610                       
REMARK   3      S21:  -0.1408 S22:  -0.1960 S23:   0.1949                       
REMARK   3      S31:   0.0180 S32:  -0.1287 S33:   0.0571                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   512        A   519                          
REMARK   3    ORIGIN FOR THE GROUP (A): -46.1830  -1.7230 -41.8920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0190 T22:   0.0563                                     
REMARK   3      T33:  -0.0246 T12:  -0.0229                                     
REMARK   3      T13:  -0.0506 T23:   0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1320 L22:   8.2715                                     
REMARK   3      L33:   7.5520 L12:  -6.2355                                     
REMARK   3      L13:  -5.7186 L23:   0.1195                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0468 S12:   0.4270 S13:  -0.2568                       
REMARK   3      S21:   0.0407 S22:   0.2147 S23:   0.7462                       
REMARK   3      S31:   0.3460 S32:  -0.5641 S33:  -0.2614                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 2P26 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000041872.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21822                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.870                             
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1YUK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM ACETATE, 0.1M SODIUM      
REMARK 280  ACETATE, PH4.6, 18% PEG3350, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 291K                                                    
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   O    HOH A   766     O    HOH A   784              2.15            
REMARK 500   O    HOH A   766     O    HOH A   787              2.16            
REMARK 500   O    HOH A   641     O    HOH A   772              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   O    HOH A   766     O    HOH A   783     2454     1.59            
REMARK 500   O7   NAG A   302     O    HOH A   771     1565     2.17            
REMARK 500   NH2  ARG A   466     O    HOH A   688     2453     2.19            
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    CYS A 484   CB    CYS A 484   SG     -0.118                       
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       67.63   -160.57                                   
REMARK 500    HIS A  69      -88.52    -49.57                                   
REMARK 500    HIS A  69      -97.63    -36.65                                   
REMARK 500    LYS A 340      -55.83   -128.75                                   
REMARK 500    ASN A 384       -1.48     72.94                                   
REMARK 500    HIS A 438       18.07     56.12                                   
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 HIS A   69     ASN A   70                  149.61                    
REMARK 500 HIS A   69     ASN A   70                  148.17                    
REMARK 500 GLY A  465     ARG A  466                  130.77                    
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 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 303                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2P28   RELATED DB: PDB                                   
DBREF  2P26 A    1   100  UNP    P05107   ITB2_HUMAN      23    122             
DBREF  2P26 A  340   513  UNP    P05107   ITB2_HUMAN     362    535             
SEQADV 2P26 HIS A  514  UNP  P05107              EXPRESSION TAG                 
SEQADV 2P26 HIS A  515  UNP  P05107              EXPRESSION TAG                 
SEQADV 2P26 HIS A  516  UNP  P05107              EXPRESSION TAG                 
SEQADV 2P26 HIS A  517  UNP  P05107              EXPRESSION TAG                 
SEQADV 2P26 HIS A  518  UNP  P05107              EXPRESSION TAG                 
SEQADV 2P26 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                                  
MODRES 2P26 ASN A   28  ASN  GLYCOSYLATION SITE                                 
MODRES 2P26 ASN A   94  ASN  GLYCOSYLATION SITE                                 
MODRES 2P26 ASN A  479  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 301      14                                                       
HET    NAG  A 302      14                                                       
HET    NAG  A 303      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   5  HOH   *268(H2 O)                                                    
HELIX    1   1 SER A   10  GLU A   16  1                                   7    
HELIX    2   2 PRO A   35  ILE A   38  5                                   4    
HELIX    3   3 THR A   42  ARG A   49  1                                   8    
HELIX    4   4 ALA A   52  ASP A   54  5                                   3    
HELIX    5   5 SER A  435  GLY A  439  5                                   5    
HELIX    6   6 SER A  467  SER A  474  1                                   8    
HELIX    7   7 ILE A  482  GLY A  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  GLN A  66  0                                        
SHEET    2   B 6 LYS A  80  LEU A  85 -1  O  THR A  82   N  GLU A  64           
SHEET    3   B 6 VAL A 415  PRO A 421  1  O  GLN A 418   N  LEU A  83           
SHEET    4   B 6 GLN A 402  ALA A 408 -1  N  GLN A 402   O  VAL A 419           
SHEET    5   B 6 VAL A 345  HIS A 349 -1  N  ASP A 348   O  ARG A 407           
SHEET    6   B 6 GLY A 376  CYS A 378 -1  O  CYS A 378   N  VAL A 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 A 387  ALA A 395 -1  O  VAL A 391   N  PHE A  93           
SHEET    4   C 5 LEU A 356  PHE A 363 -1  N  PHE A 363   O  THR A 388           
SHEET    5   C 5 THR A 369  GLN A 373 -1  O  HIS A 370   N  SER A 362           
SHEET    1   D 2 GLY A 441  GLU A 444  0                                        
SHEET    2   D 2 ILE A 447  CYS A 450 -1  O  ARG A 449   N  PHE A 442           
SHEET    1   E 2 TYR A 454  ILE A 455  0                                        
SHEET    2   E 2 CYS A 461  GLN A 462 -1  O  CYS A 461   N  ILE A 455           
SHEET    1   F 2 GLY A 488  VAL A 491  0                                        
SHEET    2   F 2 GLN A 494  CYS A 497 -1  O  LEU A 496   N  ASP A 489           
SHEET    1   G 2 LEU A 506  TYR A 508  0                                        
SHEET    2   G 2 HIS A 514  HIS A 516 -1  O  HIS A 516   N  LEU A 506           
SSBOND   1 CYS A    3    CYS A   21                          1555   1555  2.04  
SSBOND   2 CYS A   11    CYS A  425                          1555   1555  2.01  
SSBOND   3 CYS A   14    CYS A   40                          1555   1555  2.02  
SSBOND   4 CYS A   24    CYS A   51                          1555   1555  2.04  
SSBOND   5 CYS A  364    CYS A  378                          1555   1555  2.04  
SSBOND   6 CYS A  398    CYS A  423                          1555   1555  2.03  
SSBOND   7 CYS A  427    CYS A  445                          1555   1555  2.02  
SSBOND   8 CYS A  437    CYS A  448                          1555   1555  2.03  
SSBOND   9 CYS A  450    CYS A  459                          1555   1555  2.04  
SSBOND  10 CYS A  461    CYS A  492                          1555   1555  2.03  
SSBOND  11 CYS A  475    CYS A  490                          1555   1555  2.03  
SSBOND  12 CYS A  484    CYS A  495                          1555   1555  2.07  
SSBOND  13 CYS A  497    CYS A  512                          1555   1555  2.03  
LINK         ND2 ASN A  28                 C1  NAG A 303     1555   1555  1.44  
LINK         ND2 ASN A  94                 C1  NAG A 301     1555   1555  1.44  
LINK         ND2 ASN A 479                 C1  NAG A 302     1555   1555  1.45  
CISPEP   1 GLN A    1    GLU A    2          0         6.41                     
CISPEP   2 GLN A    1    GLU A    2          0         0.31                     
CISPEP   3 GLY A   71    GLY A   72          0        24.64                     
CISPEP   4 SER A   77    PRO A   78          0        -2.70                     
CISPEP   5 LEU A  341    SER A  342          0         4.21                     
CISPEP   6 ASN A  366    GLY A  367          0        -6.57                     
CISPEP   7 PRO A  503    GLY A  504          0       -14.71                     
SITE     1 AC1  6 ASN A  94  PHE A 363  GLN A 390  HOH A 593                    
SITE     2 AC1  6 HOH A 695  HOH A 733                                          
SITE     1 AC2  6 SER A 435  HIS A 438  LYS A 440  ASN A 479                    
SITE     2 AC2  6 HOH A 558  HOH A 771                                          
SITE     1 AC3  5 ASN A  28  ASN A 458  ASN A 480  HOH A 693                    
SITE     2 AC3  5 HOH A 739                                                     
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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