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Entry: 3IJE
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HEADER    PROTEIN BINDING                         04-AUG-09   3IJE              
TITLE     CRYSTAL STRUCTURE OF THE COMPLETE INTEGRIN ALHAVBETA3 ECTODOMAIN PLUS 
TITLE    2 AN ALPHA/BETA TRANSMEMBRANE FRAGMENT                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-V;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: VITRONECTIN RECEPTOR SUBUNIT ALPHA, INTEGRIN ALPHA-V HEAVY  
COMPND   5 CHAIN, INTEGRIN ALPHA-V LIGHT CHAIN;                                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ALPHAV;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HI-5;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PACUW31;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: 1TM-AVB3 PACUW31;                         
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: ITGB3, GP3A;                                                   
SOURCE  16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: HI-5                                       
KEYWDS    INTEGRIN STRUCTURE, ACTIVATION, EGF DOMAINS, FLIM, CELL SIGNALING,    
KEYWDS   2 CELL ADHESION, CLEAVAGE ON PAIR OF BASIC RESIDUES, DISULFIDE BOND,   
KEYWDS   3 GLYCOPROTEIN, HOST-VIRUS INTERACTION, INTEGRIN, MEMBRANE, RECEPTOR,  
KEYWDS   4 TRANSMEMBRANE, DISEASE MUTATION, PHOSPHOPROTEIN, PROTEIN BINDING     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-P.XIONG,B.MAHALINGHAM,X.RUI,B.T.HYMAN,S.L.GOODMAN,M.A.ARNAOUT      
REVDAT   4   24-JAN-18 3IJE    1       AUTHOR REMARK                            
REVDAT   3   13-JUL-11 3IJE    1       VERSN                                    
REVDAT   2   10-NOV-09 3IJE    1       JRNL                                     
REVDAT   1   29-SEP-09 3IJE    0                                                
JRNL        AUTH   J.P.XIONG,B.MAHALINGHAM,J.L.ALONSO,L.A.BORRELLI,X.RUI,       
JRNL        AUTH 2 S.ANAND,B.T.HYMAN,T.RYSIOK,D.MULLER-POMPALLA,S.L.GOODMAN,    
JRNL        AUTH 3 M.A.ARNAOUT                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE COMPLETE INTEGRIN ALPHAVBETA3       
JRNL        TITL 2 ECTODOMAIN PLUS AN ALPHA/BETA TRANSMEMBRANE FRAGMENT.        
JRNL        REF    J.CELL BIOL.                  V. 186   589 2009              
JRNL        REFN                   ISSN 0021-9525                               
JRNL        PMID   19704023                                                     
JRNL        DOI    10.1083/JCB.200905085                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 59083                          
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) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2917                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1983                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 11                           
REMARK   3   BIN FREE R VALUE                    : 0.4920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12632                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 455                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
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) : 45.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.45000                                             
REMARK   3    B22 (A**2) : -1.45000                                             
REMARK   3    B33 (A**2) : 2.18000                                              
REMARK   3    B12 (A**2) : -0.73000                                             
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): 1.004         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.395         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.338         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 38.790        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.869                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13407 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  9089 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18230 ; 1.130 ; 2.002       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22024 ; 0.808 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1630 ; 6.415 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   597 ;35.540 ;24.908       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2178 ;17.241 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    70 ;11.941 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2072 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14626 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2521 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3183 ; 0.198 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  9993 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6655 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  7519 ; 0.092 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   325 ; 0.148 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.002 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    16 ; 0.130 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    27 ; 0.123 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    52 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.099 ; 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):  8399 ; 0.243 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3315 ; 0.028 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13113 ; 0.455 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5672 ; 0.740 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5117 ; 1.476 ; 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  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   438                          
REMARK   3    RESIDUE RANGE :   A  4005        A  4007                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.4780  54.0090  19.7770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0818 T22:  -0.1186                                     
REMARK   3      T33:  -0.0772 T12:  -0.1693                                     
REMARK   3      T13:  -0.0452 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1688 L22:   2.4134                                     
REMARK   3      L33:   1.4265 L12:   0.5763                                     
REMARK   3      L13:   0.4580 L23:  -0.4357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2438 S12:   0.2083 S13:   0.2143                       
REMARK   3      S21:  -0.2135 S22:   0.1810 S23:   0.1958                       
REMARK   3      S31:  -0.1387 S32:   0.0340 S33:   0.0628                       
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   439        A   593                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.6930  47.9810  -7.6940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5733 T22:   0.3244                                     
REMARK   3      T33:   0.4314 T12:  -0.2060                                     
REMARK   3      T13:  -0.3482 T23:   0.1130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.5228 L22:   2.2703                                     
REMARK   3      L33:   1.6609 L12:   6.1272                                     
REMARK   3      L13:   3.6459 L23:   0.5608                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8359 S12:   1.4085 S13:   0.1893                       
REMARK   3      S21:  -0.4005 S22:   0.5030 S23:  -0.1183                       
REMARK   3      S31:  -0.1093 S32:   0.4426 S33:   0.3329                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   594        A   738                          
REMARK   3    RESIDUE RANGE :   A  4008        A  4008                          
REMARK   3    ORIGIN FOR THE GROUP (A): -51.8010  42.8180  23.4450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3939 T22:   0.2618                                     
REMARK   3      T33:   0.3996 T12:   0.0183                                     
REMARK   3      T13:  -0.1558 T23:   0.0644                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0553 L22:   0.4989                                     
REMARK   3      L33:  18.7879 L12:  -1.0189                                     
REMARK   3      L13:   5.7570 L23:  -0.5225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5635 S12:  -0.4787 S13:   0.3055                       
REMARK   3      S21:   0.2662 S22:  -0.0016 S23:   0.3009                       
REMARK   3      S31:   0.0431 S32:   0.5216 S33:   0.5652                       
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   739        A   956                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.6490  34.5560  74.5080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2367 T22:  -0.0284                                     
REMARK   3      T33:   0.1184 T12:   0.1547                                     
REMARK   3      T13:   0.0634 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2582 L22:   5.0781                                     
REMARK   3      L33:   6.3786 L12:  -2.6082                                     
REMARK   3      L13:   2.2512 L23:  -2.4551                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3213 S12:  -0.4103 S13:  -0.1681                       
REMARK   3      S21:   0.6397 S22:   0.2154 S23:  -0.2427                       
REMARK   3      S31:   0.1298 S32:   0.1583 S33:   0.1059                       
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 :   B     1        B    57                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.8880   4.6670   7.4740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1336 T22:   0.6137                                     
REMARK   3      T33:   0.8134 T12:  -0.1649                                     
REMARK   3      T13:  -0.4013 T23:  -0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.9394 L22:   3.2524                                     
REMARK   3      L33:   4.4817 L12:   1.8596                                     
REMARK   3      L13:   4.5621 L23:   0.8706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2966 S12:   0.5277 S13:  -1.4143                       
REMARK   3      S21:  -1.1616 S22:  -0.3282 S23:   0.9338                       
REMARK   3      S31:   0.6362 S32:  -1.1905 S33:   0.0315                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    58        B   109                          
REMARK   3    RESIDUE RANGE :   B   353        B   434                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0690   7.7260  26.9700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4343 T22:  -0.2715                                     
REMARK   3      T33:   0.2379 T12:  -0.1531                                     
REMARK   3      T13:   0.0768 T23:   0.0907                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1514 L22:   4.0733                                     
REMARK   3      L33:   8.0313 L12:   0.1717                                     
REMARK   3      L13:   2.9430 L23:  -1.3613                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0264 S12:   0.2655 S13:  -0.1472                       
REMARK   3      S21:  -0.2283 S22:  -0.0721 S23:  -0.1743                       
REMARK   3      S31:  -0.2521 S32:   0.1550 S33:   0.0986                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   110        B   352                          
REMARK   3    RESIDUE RANGE :   B  4002        B  4002                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6810  25.3360  35.3470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1429 T22:  -0.0048                                     
REMARK   3      T33:   0.3197 T12:  -0.0939                                     
REMARK   3      T13:  -0.1062 T23:   0.0693                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1022 L22:   2.9599                                     
REMARK   3      L33:   2.6758 L12:   0.2185                                     
REMARK   3      L13:   0.2604 L23:  -1.2024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1657 S12:  -0.1981 S13:  -0.6318                       
REMARK   3      S21:   0.2863 S22:  -0.0768 S23:  -0.6956                       
REMARK   3      S31:   0.1973 S32:   0.4592 S33:  -0.0889                       
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 :   B   435        B   474                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.0970  10.8830  -9.3640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9425 T22:   0.6053                                     
REMARK   3      T33:   0.5666 T12:  -0.4388                                     
REMARK   3      T13:  -0.1656 T23:  -0.0459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  24.5280 L22:  14.0095                                     
REMARK   3      L33:  31.8880 L12: -10.5749                                     
REMARK   3      L13:   5.7185 L23:  -4.0743                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3057 S12:   1.3705 S13:  -0.8896                       
REMARK   3      S21:  -1.1771 S22:  -0.1758 S23:   0.0373                       
REMARK   3      S31:  -1.2827 S32:   0.5829 S33:  -0.1299                       
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 :   B   475        B   524                          
REMARK   3    ORIGIN FOR THE GROUP (A): -51.3960  23.7020   2.4620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9930 T22:   0.5673                                     
REMARK   3      T33:   1.1048 T12:   0.0909                                     
REMARK   3      T13:  -0.3349 T23:  -0.1789                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2504 L22:   4.0759                                     
REMARK   3      L33:  12.6477 L12:  -1.7707                                     
REMARK   3      L13:  -0.6028 L23:  -4.6860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3933 S12:   0.7605 S13:   0.2543                       
REMARK   3      S21:  -0.3606 S22:  -0.0850 S23:  -0.2925                       
REMARK   3      S31:   0.4787 S32:  -1.1569 S33:  -0.3084                       
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 :   B   525        B   562                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.4000  28.5510  22.5540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4204 T22:   0.2423                                     
REMARK   3      T33:   0.9755 T12:  -0.0643                                     
REMARK   3      T13:  -0.2357 T23:  -0.0680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7307 L22:   2.5198                                     
REMARK   3      L33:  11.7129 L12:  -0.4721                                     
REMARK   3      L13:   8.0421 L23:  -1.8190                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8344 S12:   0.0814 S13:   1.9876                       
REMARK   3      S21:  -0.6916 S22:  -0.4343 S23:   1.4418                       
REMARK   3      S31:  -0.6359 S32:  -1.5376 S33:   1.2687                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   563        B   603                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.3210  26.4100  46.7270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4445 T22:   0.1708                                     
REMARK   3      T33:   0.4372 T12:   0.0636                                     
REMARK   3      T13:   0.1260 T23:  -0.1527                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1263 L22:   2.5160                                     
REMARK   3      L33:  39.5386 L12:  -0.5125                                     
REMARK   3      L13:  -0.1008 L23:   4.5592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6346 S12:  -0.1290 S13:  -0.2701                       
REMARK   3      S21:   0.2634 S22:   0.0593 S23:  -0.2919                       
REMARK   3      S31:   2.3657 S32:   0.5669 S33:   0.5753                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   604        B   688                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0790  13.0690  67.9600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3037 T22:   0.0399                                     
REMARK   3      T33:   0.6011 T12:   0.1632                                     
REMARK   3      T13:   0.0809 T23:   0.0860                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7741 L22:   6.2077                                     
REMARK   3      L33:  10.4742 L12:  -1.3088                                     
REMARK   3      L13:   1.6687 L23:  -0.5574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2172 S12:   0.0768 S13:   0.8886                       
REMARK   3      S21:  -0.1114 S22:   0.3308 S23:  -0.7417                       
REMARK   3      S31:  -0.5599 S32:   0.5752 S33:  -0.1136                       
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   : 1.20                                          
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 3IJE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054485.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSE                   
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66702                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
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: CNS                                                   
REMARK 200 STARTING MODEL: 1JV2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG3350, 0.1M NA ACETATE, 0.8M       
REMARK 280  NACL, 2.5MM CACL2, PH 4.8, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 298.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      203.93333            
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      101.96667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      101.96667            
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      203.93333            
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS ONE BIOLOGICAL UNIT             
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: 13520 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 76530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 59.0 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     GLN A   839                                                      
REMARK 465     THR A   840                                                      
REMARK 465     THR A   841                                                      
REMARK 465     GLU A   842                                                      
REMARK 465     LYS A   843                                                      
REMARK 465     ASN A   844                                                      
REMARK 465     ASP A   845                                                      
REMARK 465     THR A   846                                                      
REMARK 465     VAL A   847                                                      
REMARK 465     ALA A   848                                                      
REMARK 465     GLY A   849                                                      
REMARK 465     GLN A   850                                                      
REMARK 465     GLY A   851                                                      
REMARK 465     GLU A   852                                                      
REMARK 465     ARG A   853                                                      
REMARK 465     ASP A   854                                                      
REMARK 465     HIS A   855                                                      
REMARK 465     LEU A   856                                                      
REMARK 465     ILE A   857                                                      
REMARK 465     THR A   858                                                      
REMARK 465     LYS A   859                                                      
REMARK 465     ARG A   860                                                      
REMARK 465     ASP A   861                                                      
REMARK 465     LEU A   862                                                      
REMARK 465     ALA A   863                                                      
REMARK 465     LEU A   864                                                      
REMARK 465     SER A   865                                                      
REMARK 465     GLU A   866                                                      
REMARK 465     GLY A   867                                                      
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    SER A  62       75.20    -52.26                                   
REMARK 500    SER A  63     -144.92     55.90                                   
REMARK 500    THR A  64       90.55     28.12                                   
REMARK 500    ASP A  84       76.55   -165.80                                   
REMARK 500    GLN A 102     -128.41     61.59                                   
REMARK 500    ALA A 166     -151.51     71.09                                   
REMARK 500    ASN A 206       42.46   -102.46                                   
REMARK 500    PHE A 231      -38.46   -131.79                                   
REMARK 500    MET A 261       52.25    -90.43                                   
REMARK 500    ALA A 273       -7.90     74.12                                   
REMARK 500    PHE A 276      109.53    -57.72                                   
REMARK 500    THR A 283      143.96   -172.53                                   
REMARK 500    PHE A 337       -5.20     71.60                                   
REMARK 500    ASP A 368      101.49     53.04                                   
REMARK 500    LYS A 369       69.50    -58.81                                   
REMARK 500    SER A 399      -72.67   -166.79                                   
REMARK 500    ASP A 415     -160.68   -108.20                                   
REMARK 500    ASN A 458       92.77    -69.39                                   
REMARK 500    LYS A 503      -42.80   -168.61                                   
REMARK 500    LYS A 505       85.49    -53.37                                   
REMARK 500    LYS A 523      107.39   -163.90                                   
REMARK 500    ARG A 529      -87.28     68.33                                   
REMARK 500    LEU A 532       81.79    -65.89                                   
REMARK 500    MET A 533       88.00    -67.87                                   
REMARK 500    SER A 546       25.99    -60.63                                   
REMARK 500    GLU A 547      -22.51    166.71                                   
REMARK 500    ALA A 568      -33.77    159.78                                   
REMARK 500    ASP A 570     -153.08    -84.01                                   
REMARK 500    THR A 572       33.68    -95.65                                   
REMARK 500    PHE A 581       47.44    -98.28                                   
REMARK 500    ASP A 595     -132.09     66.81                                   
REMARK 500    LEU A 649       26.05    -69.17                                   
REMARK 500    ASN A 660      116.56   -170.13                                   
REMARK 500    ASN A 674      115.34     62.96                                   
REMARK 500    GLN A 675      -30.85     70.27                                   
REMARK 500    ARG A 677       83.50   -154.27                                   
REMARK 500    ASN A 685      -70.84    -67.17                                   
REMARK 500    GLN A 703       88.64     -4.52                                   
REMARK 500    GLU A 706       51.52    -92.39                                   
REMARK 500    MET A 707     -132.38    -75.07                                   
REMARK 500    ALA A 741       79.99    -54.42                                   
REMARK 500    PRO A 756       81.99    -59.04                                   
REMARK 500    THR A 768      157.63     67.06                                   
REMARK 500    ASN A 804     -107.43     53.13                                   
REMARK 500    LEU A 808     -105.42     28.53                                   
REMARK 500    ILE A 835      -49.48   -168.82                                   
REMARK 500    SER A 836      -98.51     52.88                                   
REMARK 500    ASN A 910      102.64    -50.62                                   
REMARK 500    ASN A 913      107.94   -177.73                                   
REMARK 500    GLN A 914      -85.92     49.37                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     126 RAMACHANDRAN OUTLIERS.                        
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 A  546     GLU A  547                  149.61                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A 2821                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 230   OD2                                                    
REMARK 620 2 ASN A 232   OD1  86.3                                              
REMARK 620 3 ILE A 236   O    85.5 146.0                                        
REMARK 620 4 ASP A 238   OD1 111.8  78.0  74.7                                  
REMARK 620 5 ASP A 238   OD2  68.4  61.4  85.0  45.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 284   OD2                                                    
REMARK 620 2 ASN A 286   OD1  77.6                                              
REMARK 620 3 ASP A 288   OD1  72.5  88.4                                        
REMARK 620 4 TYR A 290   O    70.8 143.4  99.0                                  
REMARK 620 5 ASP A 292   OD1 117.1 104.6 165.0  75.1                            
REMARK 620 6 ASP A 292   OD2  73.2  76.1 144.7  77.5  48.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 349   OD2                                                    
REMARK 620 2 ASP A 351   OD1  76.6                                              
REMARK 620 3 ASP A 353   OD2  70.3  90.9                                        
REMARK 620 4 PHE A 355   O    67.9 144.3  80.2                                  
REMARK 620 5 ASP A 357   OD1  81.5  78.8 151.5  92.8                            
REMARK 620 6 ASP A 357   OD2 128.2 108.9 154.9  91.3  51.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 413   OD1                                                    
REMARK 620 2 ASP A 415   OD1  73.2                                              
REMARK 620 3 ASN A 417   ND2  90.9  66.3                                        
REMARK 620 4 TYR A 419   O    86.1 157.2 124.7                                  
REMARK 620 5 ASP A 421   OD1  92.3  71.1 134.2 101.1                            
REMARK 620 6 ASP A 421   OD2 131.9 107.5 134.7  79.2  47.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4008  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 596   O                                                      
REMARK 620 2 ASP A 599   OD1  71.2                                              
REMARK 620 3 VAL A 601   O    74.6  85.1                                        
REMARK 620 4 GLU A 636   OE1  82.7 151.2  76.4                                  
REMARK 620 5 GLU A 636   OE2  66.3 126.5 112.3  46.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B4002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 123   O                                                      
REMARK 620 2 ASP B 126   OD2  76.8                                              
REMARK 620 3 ASP B 127   OD1  99.4  74.9                                        
REMARK 620 4 MET B 335   O   169.5 107.9  73.4                                  
REMARK 620 N                    1     2     3                                   
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 2044                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2045                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2046                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2047                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2048                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2260                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2261                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2266                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2267                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2268                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2269                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2270                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2271                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2458                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2459                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2524                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2585                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2586                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2805                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2821                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2822                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2943                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2944                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2950                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2951                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2952                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3099                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3452                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3559                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3560                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 3561                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4008                 
DBREF  3IJE A    1   967  UNP    P06756   ITAV_HUMAN      31    997             
DBREF  3IJE B    1   695  UNP    P05106   ITB3_HUMAN      27    721             
SEQRES   1 A  967  PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY          
SEQRES   2 A  967  PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE          
SEQRES   3 A  967  VAL PRO SER ALA SER SER ARG MET PHE LEU LEU VAL GLY          
SEQRES   4 A  967  ALA PRO LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU          
SEQRES   5 A  967  GLY GLY GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG          
SEQRES   6 A  967  ARG CYS GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG          
SEQRES   7 A  967  ASP TYR ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS          
SEQRES   8 A  967  GLN TRP PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS          
SEQRES   9 A  967  ILE LEU ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU          
SEQRES  10 A  967  MET LYS GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU          
SEQRES  11 A  967  GLN ASP GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG          
SEQRES  12 A  967  SER GLN ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN          
SEQRES  13 A  967  GLY GLY PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL          
SEQRES  14 A  967  LEU LEU GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN          
SEQRES  15 A  967  LEU ILE SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR          
SEQRES  16 A  967  ASP PRO ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU          
SEQRES  17 A  967  ALA THR ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR          
SEQRES  18 A  967  LEU GLY TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP          
SEQRES  19 A  967  GLY ILE ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA          
SEQRES  20 A  967  ARG THR LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN          
SEQRES  21 A  967  MET SER SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA          
SEQRES  22 A  967  ALA TYR PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN          
SEQRES  23 A  967  GLY ASP ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU          
SEQRES  24 A  967  PHE MET ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL          
SEQRES  25 A  967  GLY GLN VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP          
SEQRES  26 A  967  PHE GLN THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA          
SEQRES  27 A  967  ARG PHE GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP          
SEQRES  28 A  967  GLN ASP GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR          
SEQRES  29 A  967  GLY GLY GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN          
SEQRES  30 A  967  GLY ARG SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE          
SEQRES  31 A  967  LEU GLU GLY GLN TRP ALA ALA ARG SER MET PRO PRO SER          
SEQRES  32 A  967  PHE GLY TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS          
SEQRES  33 A  967  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL          
SEQRES  34 A  967  ASP ARG ALA ILE LEU TYR ARG ALA ARG PRO VAL ILE THR          
SEQRES  35 A  967  VAL ASN ALA GLY LEU GLU VAL TYR PRO SER ILE LEU ASN          
SEQRES  36 A  967  GLN ASP ASN LYS THR CYS SER LEU PRO GLY THR ALA LEU          
SEQRES  37 A  967  LYS VAL SER CYS PHE ASN VAL ARG PHE CYS LEU LYS ALA          
SEQRES  38 A  967  ASP GLY LYS GLY VAL LEU PRO ARG LYS LEU ASN PHE GLN          
SEQRES  39 A  967  VAL GLU LEU LEU LEU ASP LYS LEU LYS GLN LYS GLY ALA          
SEQRES  40 A  967  ILE ARG ARG ALA LEU PHE LEU TYR SER ARG SER PRO SER          
SEQRES  41 A  967  HIS SER LYS ASN MET THR ILE SER ARG GLY GLY LEU MET          
SEQRES  42 A  967  GLN CYS GLU GLU LEU ILE ALA TYR LEU ARG ASP GLU SER          
SEQRES  43 A  967  GLU PHE ARG ASP LYS LEU THR PRO ILE THR ILE PHE MET          
SEQRES  44 A  967  GLU TYR ARG LEU ASP TYR ARG THR ALA ALA ASP THR THR          
SEQRES  45 A  967  GLY LEU GLN PRO ILE LEU ASN GLN PHE THR PRO ALA ASN          
SEQRES  46 A  967  ILE SER ARG GLN ALA HIS ILE LEU LEU ASP CYS GLY GLU          
SEQRES  47 A  967  ASP ASN VAL CYS LYS PRO LYS LEU GLU VAL SER VAL ASP          
SEQRES  48 A  967  SER ASP GLN LYS LYS ILE TYR ILE GLY ASP ASP ASN PRO          
SEQRES  49 A  967  LEU THR LEU ILE VAL LYS ALA GLN ASN GLN GLY GLU GLY          
SEQRES  50 A  967  ALA TYR GLU ALA GLU LEU ILE VAL SER ILE PRO LEU GLN          
SEQRES  51 A  967  ALA ASP PHE ILE GLY VAL VAL ARG ASN ASN GLU ALA LEU          
SEQRES  52 A  967  ALA ARG LEU SER CYS ALA PHE LYS THR GLU ASN GLN THR          
SEQRES  53 A  967  ARG GLN VAL VAL CYS ASP LEU GLY ASN PRO MET LYS ALA          
SEQRES  54 A  967  GLY THR GLN LEU LEU ALA GLY LEU ARG PHE SER VAL HIS          
SEQRES  55 A  967  GLN GLN SER GLU MET ASP THR SER VAL LYS PHE ASP LEU          
SEQRES  56 A  967  GLN ILE GLN SER SER ASN LEU PHE ASP LYS VAL SER PRO          
SEQRES  57 A  967  VAL VAL SER HIS LYS VAL ASP LEU ALA VAL LEU ALA ALA          
SEQRES  58 A  967  VAL GLU ILE ARG GLY VAL SER SER PRO ASP HIS VAL PHE          
SEQRES  59 A  967  LEU PRO ILE PRO ASN TRP GLU HIS LYS GLU ASN PRO GLU          
SEQRES  60 A  967  THR GLU GLU ASP VAL GLY PRO VAL VAL GLN HIS ILE TYR          
SEQRES  61 A  967  GLU LEU ARG ASN ASN GLY PRO SER SER PHE SER LYS ALA          
SEQRES  62 A  967  MET LEU HIS LEU GLN TRP PRO TYR LYS TYR ASN ASN ASN          
SEQRES  63 A  967  THR LEU LEU TYR ILE LEU HIS TYR ASP ILE ASP GLY PRO          
SEQRES  64 A  967  MET ASN CYS THR SER ASP MET GLU ILE ASN PRO LEU ARG          
SEQRES  65 A  967  ILE LYS ILE SER SER LEU GLN THR THR GLU LYS ASN ASP          
SEQRES  66 A  967  THR VAL ALA GLY GLN GLY GLU ARG ASP HIS LEU ILE THR          
SEQRES  67 A  967  LYS ARG ASP LEU ALA LEU SER GLU GLY ASP ILE HIS THR          
SEQRES  68 A  967  LEU GLY CYS GLY VAL ALA GLN CYS LEU LYS ILE VAL CYS          
SEQRES  69 A  967  GLN VAL GLY ARG LEU ASP ARG GLY LYS SER ALA ILE LEU          
SEQRES  70 A  967  TYR VAL LYS SER LEU LEU TRP THR GLU THR PHE MET ASN          
SEQRES  71 A  967  LYS GLU ASN GLN ASN HIS SER TYR SER LEU LYS SER SER          
SEQRES  72 A  967  ALA SER PHE ASN VAL ILE GLU PHE PRO TYR LYS ASN LEU          
SEQRES  73 A  967  PRO ILE GLU ASP ILE THR ASN SER THR LEU VAL THR THR          
SEQRES  74 A  967  ASN VAL THR TRP GLY ILE GLN PRO ALA PRO MET PRO VAL          
SEQRES  75 A  967  PRO VAL TRP VAL ILE                                          
SEQRES   1 B  695  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  695  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  695  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  695  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  695  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  695  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  695  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  695  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  695  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  695  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  695  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  695  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  695  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  695  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  695  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  695  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  695  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  695  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  695  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  695  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  695  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  695  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  695  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  695  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  695  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  695  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  695  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  695  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  695  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  695  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  695  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  695  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  695  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  695  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  695  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  695  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  695  SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG PRO SER          
SEQRES  38 B  695  GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN PRO VAL          
SEQRES  39 B  695  CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL          
SEQRES  40 B  695  CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY LYS TYR          
SEQRES  41 B  695  CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR LYS GLY          
SEQRES  42 B  695  GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS GLY ASP          
SEQRES  43 B  695  CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR CYS ASN          
SEQRES  44 B  695  CYS THR THR ARG THR ASP THR CYS MET SER SER ASN GLY          
SEQRES  45 B  695  LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS GLY SER          
SEQRES  46 B  695  CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP THR CYS          
SEQRES  47 B  695  GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR PHE LYS          
SEQRES  48 B  695  LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG GLY ALA          
SEQRES  49 B  695  LEU HIS ASP GLU ASN THR CYS ASN ARG TYR CYS ARG ASP          
SEQRES  50 B  695  GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR GLY LYS          
SEQRES  51 B  695  ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP ASP CYS          
SEQRES  52 B  695  VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER GLY LYS          
SEQRES  53 B  695  SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS PRO LYS          
SEQRES  54 B  695  GLY PRO ASP ILE LEU VAL                                      
MODRES 3IJE ASN A   44  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN A  260  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN A  266  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN A  458  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN A  524  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN A  585  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN A  805  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN A  943  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN A  950  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN B  452  ASN  GLYCOSYLATION SITE                                 
MODRES 3IJE ASN B  559  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A2044      14                                                       
HET    NAG  A2045      14                                                       
HET    BMA  A2046      11                                                       
HET    MAN  A2047      11                                                       
HET    MAN  A2048      11                                                       
HET    NAG  A2260      14                                                       
HET    NAG  A2261      14                                                       
HET    NAG  A2266      14                                                       
HET    NAG  A2267      14                                                       
HET    BMA  A2268      11                                                       
HET    MAN  A2269      11                                                       
HET    MAN  A2270      11                                                       
HET    MAN  A2271      11                                                       
HET    NAG  A2458      14                                                       
HET    NAG  A2459      14                                                       
HET    NAG  A2524      14                                                       
HET    NAG  A2585      14                                                       
HET    NAG  A2586      14                                                       
HET    NAG  A2805      14                                                       
HET    NAG  A2821      14                                                       
HET    NAG  A2822      14                                                       
HET    NAG  A2943      14                                                       
HET    NAG  A2944      14                                                       
HET    NAG  A2950      14                                                       
HET    NAG  A2951      14                                                       
HET    BMA  A2952      11                                                       
HET     CA  A4004       1                                                       
HET     CA  A4005       1                                                       
HET     CA  A4006       1                                                       
HET     CA  A4007       1                                                       
HET     CA  A4008       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    NAG  B3452      14                                                       
HET    NAG  B3559      14                                                       
HET    NAG  B3560      14                                                       
HET    BMA  B3561      11                                                       
HET     CA  B4002       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  NAG    25(C8 H15 N O6)                                              
FORMUL   3  BMA    4(C6 H12 O6)                                                 
FORMUL   3  MAN    5(C6 H12 O6)                                                 
FORMUL  13   CA    6(CA 2+)                                                     
HELIX    1   1 GLY A  175  GLN A  180  1                                   6    
HELIX    2   2 VAL A  188  TYR A  195  1                                   8    
HELIX    3   3 GLN A  214  ASP A  218  5                                   5    
HELIX    4   4 ARG A  245  LEU A  250  1                                   6    
HELIX    5   5 ASP A  500  LYS A  505  1                                   6    
HELIX    6   6 TRP A  904  MET A  909  1                                   6    
HELIX    7   7 ILE B    4  GLY B    9  1                                   6    
HELIX    8   8 SER B   12  SER B   20  1                                   9    
HELIX    9   9 LYS B   41  ASP B   47  1                                   7    
HELIX   10  10 SER B  121  SER B  123  5                                   3    
HELIX   11  11 MET B  124  GLN B  132  1                                   9    
HELIX   12  12 GLY B  135  THR B  146  1                                  12    
HELIX   13  13 GLU B  171  ASN B  175  5                                   5    
HELIX   14  14 VAL B  200  GLN B  210  1                                  11    
HELIX   15  15 GLY B  221  CYS B  232  1                                  12    
HELIX   16  16 CYS B  232  GLY B  237  1                                   6    
HELIX   17  17 LEU B  258  LEU B  262  5                                   5    
HELIX   18  18 SER B  291  LYS B  302  1                                  12    
HELIX   19  19 VAL B  314  ILE B  325  1                                  12    
HELIX   20  20 ASN B  339  ARG B  352  1                                  14    
HELIX   21  21 LEU B  573  GLY B  577  5                                   5    
HELIX   22  22 ASP B  606  ASP B  621  1                                  16    
HELIX   23  23 GLY B  623  GLU B  628  1                                   6    
HELIX   24  24 THR B  630  CYS B  635  1                                   6    
SHEET    1   A 4 ALA A   9  SER A  12  0                                        
SHEET    2   A 4 ARG A 431  TYR A 435 -1  O  ALA A 432   N  TYR A  11           
SHEET    3   A 4 ASP A 421  ALA A 426 -1  N  LEU A 422   O  TYR A 435           
SHEET    4   A 4 PHE A 404  THR A 412 -1  N  LYS A 409   O  ILE A 423           
SHEET    1   B 4 VAL A  23  PHE A  26  0                                        
SHEET    2   B 4 PHE A  35  ALA A  40 -1  O  LEU A  37   N  ASP A  24           
SHEET    3   B 4 GLN A  55  ASP A  60 -1  O  GLN A  55   N  ALA A  40           
SHEET    4   B 4 CYS A  67  PRO A  69 -1  O  GLN A  68   N  LYS A  58           
SHEET    1   C 2 ASP A  79  ALA A  81  0                                        
SHEET    2   C 2 ASP A  84  PRO A  85 -1  O  ASP A  84   N  TYR A  80           
SHEET    1   D 2 GLU A  87  PHE A  88  0                                        
SHEET    2   D 2 HIS A 113  TRP A 114 -1  O  HIS A 113   N  PHE A  88           
SHEET    1   E 4 VAL A  98  LYS A 101  0                                        
SHEET    2   E 4 LYS A 104  ALA A 109 -1  O  LEU A 106   N  ARG A  99           
SHEET    3   E 4 THR A 127  ASP A 132 -1  O  THR A 127   N  ALA A 109           
SHEET    4   E 4 LYS A 135  TYR A 139 -1  O  VAL A 137   N  LEU A 130           
SHEET    1   F 4 ILE A 161  PHE A 163  0                                        
SHEET    2   F 4 ARG A 168  GLY A 173 -1  O  LEU A 170   N  ASP A 162           
SHEET    3   F 4 GLN A 182  GLN A 187 -1  O  GLN A 182   N  GLY A 173           
SHEET    4   F 4 LEU A 208  ALA A 209 -1  O  LEU A 208   N  SER A 185           
SHEET    1   G 4 SER A 225  GLY A 229  0                                        
SHEET    2   G 4 ASP A 238  VAL A 243 -1  O  VAL A 240   N  ALA A 227           
SHEET    3   G 4 MET A 252  TYR A 256 -1  O  MET A 252   N  VAL A 243           
SHEET    4   G 4 SER A 263  THR A 268 -1  O  LEU A 264   N  ILE A 255           
SHEET    1   H 4 VAL A 280  THR A 283  0                                        
SHEET    2   H 4 ASP A 292  ALA A 297 -1  O  PHE A 294   N  ALA A 281           
SHEET    3   H 4 GLN A 314  LEU A 319 -1  O  SER A 318   N  VAL A 293           
SHEET    4   H 4 GLN A 327  ASN A 332 -1  O  LEU A 331   N  VAL A 315           
SHEET    1   I 2 MET A 301  ARG A 303  0                                        
SHEET    2   I 2 LEU A 309  GLU A 311 -1  O  GLN A 310   N  ASP A 302           
SHEET    1   J 4 ALA A 343  GLY A 348  0                                        
SHEET    2   J 4 ASP A 357  ALA A 362 -1  O  ASP A 357   N  GLY A 348           
SHEET    3   J 4 ILE A 372  ARG A 379 -1  O  TYR A 374   N  ILE A 360           
SHEET    4   J 4 GLY A 382  LEU A 383 -1  O  GLY A 382   N  ARG A 379           
SHEET    1   K 4 ALA A 343  GLY A 348  0                                        
SHEET    2   K 4 ASP A 357  ALA A 362 -1  O  ASP A 357   N  GLY A 348           
SHEET    3   K 4 ILE A 372  ARG A 379 -1  O  TYR A 374   N  ILE A 360           
SHEET    4   K 4 GLN A 389  GLU A 392 -1  O  LEU A 391   N  VAL A 373           
SHEET    1   L 5 ALA A 511  PHE A 513  0                                        
SHEET    2   L 5 GLN A 534  LEU A 542 -1  O  TYR A 541   N  LEU A 512           
SHEET    3   L 5 SER A 471  ASP A 482 -1  N  VAL A 475   O  LEU A 538           
SHEET    4   L 5 VAL A 440  VAL A 449 -1  N  THR A 442   O  ASP A 482           
SHEET    5   L 5 ILE A 577  LEU A 578  1  O  ILE A 577   N  ILE A 441           
SHEET    1   M 5 ILE A 453  LEU A 454  0                                        
SHEET    2   M 5 ASN A 585  ILE A 592  1  O  HIS A 591   N  LEU A 454           
SHEET    3   M 5 ILE A 555  LEU A 563 -1  N  ILE A 555   O  ALA A 590           
SHEET    4   M 5 LYS A 490  LEU A 499 -1  N  GLN A 494   O  ARG A 562           
SHEET    5   M 5 SER A 520  SER A 528 -1  O  MET A 525   N  PHE A 493           
SHEET    1   N 4 LEU A 606  ASP A 611  0                                        
SHEET    2   N 4 ASN A 623  ASN A 633 -1  O  LYS A 630   N  SER A 609           
SHEET    3   N 4 GLN A 692  VAL A 701 -1  O  ALA A 695   N  VAL A 629           
SHEET    4   N 4 ALA A 651  VAL A 656 -1  N  ASP A 652   O  SER A 700           
SHEET    1   O 6 LYS A 616  TYR A 618  0                                        
SHEET    2   O 6 VAL A 730  ALA A 737  1  O  ALA A 737   N  ILE A 617           
SHEET    3   O 6 SER A 710  GLN A 718 -1  N  LEU A 715   O  VAL A 730           
SHEET    4   O 6 GLU A 642  SER A 646 -1  N  SER A 646   O  ASP A 714           
SHEET    5   O 6 GLN A 678  ASP A 682 -1  O  VAL A 679   N  VAL A 645           
SHEET    6   O 6 SER A 667  LYS A 671 -1  N  ALA A 669   O  VAL A 680           
SHEET    1   P 4 VAL A 742  SER A 748  0                                        
SHEET    2   P 4 VAL A 775  ASN A 784 -1  O  ARG A 783   N  GLU A 743           
SHEET    3   P 4 LYS A 893  LEU A 903 -1  O  SER A 901   N  VAL A 776           
SHEET    4   P 4 LEU A 809  ASP A 817 -1  N  TYR A 810   O  LEU A 902           
SHEET    1   Q 6 HIS A 752  PHE A 754  0                                        
SHEET    2   Q 6 ILE A 941  THR A 952  1  O  ASN A 950   N  VAL A 753           
SHEET    3   Q 6 TYR A 918  GLU A 930 -1  N  TYR A 918   O  VAL A 951           
SHEET    4   Q 6 LYS A 792  LYS A 802 -1  N  GLN A 798   O  SER A 923           
SHEET    5   Q 6 GLN A 878  VAL A 886 -1  O  GLN A 878   N  LYS A 802           
SHEET    6   Q 6 MET A 820  SER A 824 -1  N  THR A 823   O  VAL A 883           
SHEET    1   R 4 HIS A 752  PHE A 754  0                                        
SHEET    2   R 4 ILE A 941  THR A 952  1  O  ASN A 950   N  VAL A 753           
SHEET    3   R 4 TYR A 918  GLU A 930 -1  N  TYR A 918   O  VAL A 951           
SHEET    4   R 4 THR A 871  LEU A 872  1  N  LEU A 872   O  SER A 919           
SHEET    1   S 6 GLU B  60  GLU B  65  0                                        
SHEET    2   S 6 ARG B  87  LEU B  92 -1  O  ALA B  89   N  ARG B  62           
SHEET    3   S 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4   S 6 LYS B 412  PRO B 418 -1  N  LYS B 412   O  VAL B 429           
SHEET    5   S 6 VAL B 355  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6   S 6 SER B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1   T 4 SER B  97  ARG B 105  0                                        
SHEET    2   T 4 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    3   T 4 LEU B 366  LEU B 375 -1  N  THR B 373   O  SER B 396           
SHEET    4   T 4 GLU B 378  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1   U 6 TYR B 190  THR B 197  0                                        
SHEET    2   U 6 LEU B 149  PHE B 156 -1  N  ALA B 155   O  LYS B 191           
SHEET    3   U 6 VAL B 112  ASP B 119  1  N  TYR B 116   O  GLY B 154           
SHEET    4   U 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5   U 6 ILE B 304  THR B 311  1  O  ILE B 307   N  PHE B 248           
SHEET    6   U 6 THR B 329  LEU B 333  1  O  LEU B 333   N  VAL B 310           
SHEET    1   V 2 THR B 454  GLU B 456  0                                        
SHEET    2   V 2 VAL B 459  ARG B 461 -1  O  VAL B 459   N  GLU B 456           
SHEET    1   W 2 GLU B 500  LEU B 502  0                                        
SHEET    2   W 2 GLN B 505  VAL B 507 -1  O  VAL B 507   N  GLU B 500           
SHEET    1   X 2 ILE B 516  THR B 517  0                                        
SHEET    2   X 2 CYS B 523  ASP B 524 -1  O  CYS B 523   N  THR B 517           
SHEET    1   Y 2 GLY B 540  CYS B 542  0                                        
SHEET    2   Y 2 CYS B 547  CYS B 549 -1  O  LEU B 548   N  GLN B 541           
SHEET    1   Z 2 TRP B 553  THR B 554  0                                        
SHEET    2   Z 2 CYS B 560  THR B 561 -1  O  CYS B 560   N  THR B 554           
SHEET    1  AA 2 GLY B 579  CYS B 581  0                                        
SHEET    2  AA 2 CYS B 586  CYS B 588 -1  O  VAL B 587   N  LYS B 580           
SHEET    1  AB 4 GLU B 638  GLU B 640  0                                        
SHEET    2  AB 4 ILE B 678  VAL B 681  1  O  LEU B 679   N  GLU B 638           
SHEET    3  AB 4 VAL B 664  TYR B 670 -1  N  TYR B 670   O  ILE B 678           
SHEET    4  AB 4 ASN B 654  LYS B 658 -1  N  CYS B 655   O  PHE B 667           
SSBOND   1 CYS A   59    CYS A   67                          1555   1555  2.05  
SSBOND   2 CYS A  108    CYS A  128                          1555   1555  2.05  
SSBOND   3 CYS A  142    CYS A  155                          1555   1555  2.03  
SSBOND   4 CYS A  461    CYS A  472                          1555   1555  2.04  
SSBOND   5 CYS A  478    CYS A  535                          1555   1555  2.04  
SSBOND   6 CYS A  596    CYS A  602                          1555   1555  2.74  
SSBOND   7 CYS A  668    CYS A  681                          1555   1555  2.04  
SSBOND   8 CYS A  822    CYS A  884                          1555   1555  2.03  
SSBOND   9 CYS A  874    CYS A  879                          1555   1555  2.06  
SSBOND  10 CYS B    5    CYS B   23                          1555   1555  2.04  
SSBOND  11 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND  12 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND  13 CYS B   26    CYS B   49                          1555   1555  2.04  
SSBOND  14 CYS B  177    CYS B  184                          1555   1555  2.05  
SSBOND  15 CYS B  232    CYS B  273                          1555   1555  2.05  
SSBOND  16 CYS B  374    CYS B  386                          1555   1555  1.99  
SSBOND  17 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  18 CYS B  437    CYS B  457                          1555   1555  2.04  
SSBOND  19 CYS B  448    CYS B  460                          1555   1555  2.05  
SSBOND  20 CYS B  462    CYS B  471                          1555   1555  2.04  
SSBOND  21 CYS B  486    CYS B  501                          1555   1555  2.04  
SSBOND  22 CYS B  495    CYS B  506                          1555   1555  2.03  
SSBOND  23 CYS B  508    CYS B  521                          1555   1555  2.04  
SSBOND  24 CYS B  523    CYS B  544                          1555   1555  2.03  
SSBOND  25 CYS B  528    CYS B  542                          1555   1555  2.02  
SSBOND  26 CYS B  536    CYS B  547                          1555   1555  2.04  
SSBOND  27 CYS B  549    CYS B  558                          1555   1555  2.04  
SSBOND  28 CYS B  560    CYS B  583                          1555   1555  2.04  
SSBOND  29 CYS B  567    CYS B  581                          1555   1555  2.04  
SSBOND  30 CYS B  575    CYS B  586                          1555   1555  2.04  
SSBOND  31 CYS B  588    CYS B  598                          1555   1555  2.71  
SSBOND  32 CYS B  601    CYS B  604                          1555   1555  2.03  
SSBOND  33 CYS B  608    CYS B  655                          1555   1555  2.04  
SSBOND  34 CYS B  614    CYS B  635                          1555   1555  2.03  
SSBOND  35 CYS B  617    CYS B  631                          1555   1555  2.03  
SSBOND  36 CYS B  663    CYS B  687                          1555   1555  2.04  
LINK         ND2 ASN A  44                 C1  NAG A2044     1555   1555  1.45  
LINK         OD2 ASP A 230                CA    CA A4004     1555   1555  2.60  
LINK         OD1 ASN A 232                CA    CA A4004     1555   1555  2.13  
LINK         O   ILE A 236                CA    CA A4004     1555   1555  2.35  
LINK         OD1 ASP A 238                CA    CA A4004     1555   1555  2.51  
LINK         OD2 ASP A 238                CA    CA A4004     1555   1555  2.99  
LINK         ND2 ASN A 260                 C1  NAG A2260     1555   1555  1.45  
LINK         ND2 ASN A 266                 C1  NAG A2266     1555   1555  1.46  
LINK         OD2 ASP A 284                CA    CA A4005     1555   1555  2.51  
LINK         OD1 ASN A 286                CA    CA A4005     1555   1555  2.19  
LINK         OD1 ASP A 288                CA    CA A4005     1555   1555  2.38  
LINK         O   TYR A 290                CA    CA A4005     1555   1555  2.40  
LINK         OD1 ASP A 292                CA    CA A4005     1555   1555  2.53  
LINK         OD2 ASP A 292                CA    CA A4005     1555   1555  2.78  
LINK         OD2 ASP A 349                CA    CA A4006     1555   1555  2.62  
LINK         OD1 ASP A 351                CA    CA A4006     1555   1555  2.22  
LINK         OD2 ASP A 353                CA    CA A4006     1555   1555  2.27  
LINK         O   PHE A 355                CA    CA A4006     1555   1555  2.37  
LINK         OD1 ASP A 357                CA    CA A4006     1555   1555  2.63  
LINK         OD2 ASP A 357                CA    CA A4006     1555   1555  2.39  
LINK         OD1 ASP A 413                CA    CA A4007     1555   1555  2.43  
LINK         OD1 ASP A 415                CA    CA A4007     1555   1555  2.28  
LINK         ND2 ASN A 417                CA    CA A4007     1555   1555  2.44  
LINK         O   TYR A 419                CA    CA A4007     1555   1555  2.32  
LINK         OD1 ASP A 421                CA    CA A4007     1555   1555  2.85  
LINK         OD2 ASP A 421                CA    CA A4007     1555   1555  2.56  
LINK         ND2 ASN A 458                 C1  NAG A2458     1555   1555  1.46  
LINK         ND2 ASN A 524                 C1  NAG A2524     1555   1555  1.46  
LINK         ND2 ASN A 585                 C1  NAG A2585     1555   1555  1.44  
LINK         O   CYS A 596                CA    CA A4008     1555   1555  2.43  
LINK         OD1 ASP A 599                CA    CA A4008     1555   1555  2.47  
LINK         O   VAL A 601                CA    CA A4008     1555   1555  2.32  
LINK         OE1 GLU A 636                CA    CA A4008     1555   1555  2.49  
LINK         OE2 GLU A 636                CA    CA A4008     1555   1555  2.94  
LINK         ND2 ASN A 805                 C1  NAG A2805     1555   1555  1.46  
LINK         ND2 ASN A 943                 C1  NAG A2943     1555   1555  1.44  
LINK         ND2 ASN A 950                 C1  NAG A2950     1555   1555  1.44  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.45  
LINK         O   SER B 123                CA    CA B4002     1555   1555  2.38  
LINK         OD2 ASP B 126                CA    CA B4002     1555   1555  2.44  
LINK         OD1 ASP B 127                CA    CA B4002     1555   1555  2.33  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         O   MET B 335                CA    CA B4002     1555   1555  2.35  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.46  
LINK         ND2 ASN B 452                 C1  NAG B3452     1555   1555  1.44  
LINK         ND2 ASN B 559                 C1  NAG B3559     1555   1555  1.45  
LINK         O4  NAG A2044                 C1  NAG A2045     1555   1555  1.44  
LINK         O4  NAG A2045                 C1  BMA A2046     1555   1555  1.46  
LINK         O3  BMA A2046                 C1  MAN A2048     1555   1555  1.46  
LINK         O6  BMA A2046                 C1  MAN A2047     1555   1555  1.44  
LINK         O4  NAG A2260                 C1  NAG A2261     1555   1555  1.44  
LINK         O4  NAG A2266                 C1  NAG A2267     1555   1555  1.43  
LINK         O4  NAG A2267                 C1  BMA A2268     1555   1555  1.44  
LINK         O3  BMA A2268                 C1  MAN A2269     1555   1555  1.44  
LINK         O6  BMA A2268                 C1  MAN A2270     1555   1555  1.45  
LINK         O4  MAN A2270                 C1  MAN A2271     1555   1555  1.45  
LINK         O4  NAG A2458                 C1  NAG A2459     1555   1555  1.45  
LINK         O4  NAG A2585                 C1  NAG A2586     1555   1555  1.45  
LINK         O4  NAG A2821                 C1  NAG A2822     1555   1555  1.45  
LINK         O4  NAG A2943                 C1  NAG A2944     1555   1555  1.45  
LINK         O4  NAG A2950                 C1  NAG A2951     1555   1555  1.44  
LINK         O4  NAG A2951                 C1  BMA A2952     1555   1555  1.44  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.45  
LINK         O4  NAG B3559                 C1  NAG B3560     1555   1555  1.45  
LINK         O4  NAG B3560                 C1  BMA B3561     1555   1555  1.45  
SITE     1 AC1  5 GLY A  16  LYS A  42  ASN A  44  GLU A  52                    
SITE     2 AC1  5 NAG A2045                                                     
SITE     1 AC2  4 VAL A  51  NAG A2044  BMA A2046  MAN A2048                    
SITE     1 AC3  3 NAG A2045  MAN A2047  MAN A2048                               
SITE     1 AC4  1 BMA A2046                                                     
SITE     1 AC5  2 NAG A2045  BMA A2046                                          
SITE     1 AC6  3 ASP A 257  ASN A 260  NAG A2261                               
SITE     1 AC7  1 NAG A2260                                                     
SITE     1 AC8  7 PHE A 217  MET A 252  TYR A 254  SER A 263                    
SITE     2 AC8  7 LEU A 264  ASN A 266  NAG A2267                               
SITE     1 AC9  5 ALA A 213  GLN A 214  PHE A 217  NAG A2266                    
SITE     2 AC9  5 BMA A2268                                                     
SITE     1 BC1  5 GLN A 214  NAG A2267  MAN A2269  MAN A2270                    
SITE     2 BC1  5 MAN A2271                                                     
SITE     1 BC2  1 BMA A2268                                                     
SITE     1 BC3  2 BMA A2268  MAN A2271                                          
SITE     1 BC4  2 BMA A2268  MAN A2270                                          
SITE     1 BC5  4 ASN A 458  THR A 460  CYS A 472  NAG A2459                    
SITE     1 BC6  2 TYR A 450  NAG A2458                                          
SITE     1 BC7  1 ASN A 524                                                     
SITE     1 BC8  4 PHE A 558  PRO A 583  ASN A 585  NAG A2586                    
SITE     1 BC9  1 NAG A2585                                                     
SITE     1 CC1  2 ASN A 804  ASN A 805                                          
SITE     1 CC2  2 ASN A 821  NAG A2822                                          
SITE     1 CC3  1 NAG A2821                                                     
SITE     1 CC4  3 THR A 942  ASN A 943  NAG A2944                               
SITE     1 CC5  1 NAG A2943                                                     
SITE     1 CC6  3 ASP A 751  ASN A 950  NAG A2951                               
SITE     1 CC7  2 NAG A2950  BMA A2952                                          
SITE     1 CC8  1 NAG A2951                                                     
SITE     1 CC9  2 ASN B  99  SER B 398                                          
SITE     1 DC1  4 ARG A 248  ASN B 316  ASN B 320  GLU B 323                    
SITE     1 DC2  6 SER B 369  ASN B 371  SER B 398  ILE B 399                    
SITE     2 DC2  6 GLU B 400  NAG B3372                                          
SITE     1 DC3  1 NAG B3371                                                     
SITE     1 DC4  2 SER B 445  ASN B 452                                          
SITE     1 DC5  4 TYR B 531  TYR B 557  ASN B 559  NAG B3560                    
SITE     1 DC6  4 PRO A 624  TYR B 557  NAG B3559  BMA B3561                    
SITE     1 DC7  1 NAG B3560                                                     
SITE     1 DC8  4 SER B 123  ASP B 126  ASP B 127  MET B 335                    
SITE     1 DC9  5 ASP A 230  ASN A 232  ASP A 234  ILE A 236                    
SITE     2 DC9  5 ASP A 238                                                     
SITE     1 EC1  5 ASP A 284  ASN A 286  ASP A 288  TYR A 290                    
SITE     2 EC1  5 ASP A 292                                                     
SITE     1 EC2  5 ASP A 349  ASP A 351  ASP A 353  PHE A 355                    
SITE     2 EC2  5 ASP A 357                                                     
SITE     1 EC3  5 ASP A 413  ASP A 415  ASN A 417  TYR A 419                    
SITE     2 EC3  5 ASP A 421                                                     
SITE     1 EC4  5 CYS A 596  ASP A 599  VAL A 601  LYS A 603                    
SITE     2 EC4  5 GLU A 636                                                     
CRYST1  129.870  129.870  305.900  90.00  90.00 120.00 P 32 2 1      6          
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      0.007700  0.004446  0.000000        0.00000                         
SCALE2      0.000000  0.008891  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003269        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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