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Database: PDB
Entry: 4G1E
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HEADER    PROTEIN BINDING                         10-JUL-12   4G1E              
TITLE     CRYSTAL STRUCTURE OF INTEGRIN ALPHA V BETA 3 WITH COIL-COILED TAG.    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-V;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 31-989;                                       
COMPND   5 SYNONYM: VITRONECTIN RECEPTOR SUBUNIT ALPHA, INTEGRIN ALPHA-V HEAVY  
COMPND   6 CHAIN, INTEGRIN ALPHA-V LIGHT CHAIN;                                 
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 27-717;                                       
COMPND  12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  13 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: ITGAV, MSK8, VNRA;                                             
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 GENE: ITGB3, GP3A                                                    
KEYWDS    PROTEIN BINDING, CELL SURFACE RECEPTOR                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.DONG,L.MI,J.ZHU,W.WANG,B.LUO,T.A.SPRINGER                           
REVDAT   1   12-DEC-12 4G1E    0                                                
JRNL        AUTH   X.DONG,L.Z.MI,J.ZHU,W.WANG,P.HU,B.H.LUO,T.A.SPRINGER         
JRNL        TITL   ALPHAV BETA3 INTEGRIN CRYSTAL STRUCTURES AND THEIR           
JRNL        TITL 2 FUNCTIONAL IMPLICATIONS                                      
JRNL        REF    BIOCHEMISTRY                  V.  51  8814 2012              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   23106217                                                     
JRNL        DOI    10.1021/BI300734N                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 79656                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.470                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1168                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.6393 -  5.6971    0.98    10243   157  0.2186 0.2410        
REMARK   3     2  5.6971 -  4.5254    0.98     9885   146  0.2035 0.2087        
REMARK   3     3  4.5254 -  3.9544    0.99     9812   145  0.2197 0.2225        
REMARK   3     4  3.9544 -  3.5933    0.99     9730   143  0.2561 0.2923        
REMARK   3     5  3.5933 -  3.3360    0.99     9756   144  0.2750 0.2929        
REMARK   3     6  3.3360 -  3.1395    0.99     9660   144  0.3088 0.3361        
REMARK   3     7  3.1395 -  2.9823    0.99     9688   145  0.3282 0.3694        
REMARK   3     8  2.9823 -  2.8526    0.98     9647   144  0.3570 0.3803        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.560           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.01630                                             
REMARK   3    B22 (A**2) : -2.01630                                             
REMARK   3    B33 (A**2) : 4.03250                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006          13984                                  
REMARK   3   ANGLE     :  0.751          18995                                  
REMARK   3   CHIRALITY :  0.050           2194                                  
REMARK   3   PLANARITY :  0.003           2385                                  
REMARK   3   DIHEDRAL  : 20.153           5415                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A and resseq 1:438                               
REMARK   3    ORIGIN FOR THE GROUP (A):  42.0098 -31.4475  30.3357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5625 T22:   1.5435                                     
REMARK   3      T33:   0.5921 T12:   0.0967                                     
REMARK   3      T13:   0.0603 T23:  -0.0698                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0598 L22:   2.0555                                     
REMARK   3      L33:   0.6088 L12:   1.4626                                     
REMARK   3      L13:   0.0671 L23:  -0.3964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1672 S12:  -0.1234 S13:  -0.3630                       
REMARK   3      S21:   0.0413 S22:  -0.2452 S23:  -0.1794                       
REMARK   3      S31:   0.0455 S32:   0.2085 S33:   0.0686                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain A and resseq 439:594                             
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4587 -68.3949  57.6989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9553 T22:   1.7484                                     
REMARK   3      T33:   0.7126 T12:   0.0771                                     
REMARK   3      T13:   0.0389 T23:   0.2982                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7610 L22:   6.8874                                     
REMARK   3      L33:   2.4053 L12:   6.0753                                     
REMARK   3      L13:  -3.9098 L23:  -3.7896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3628 S12:  -0.6238 S13:  -0.6162                       
REMARK   3      S21:   0.0468 S22:  -0.0857 S23:  -0.4862                       
REMARK   3      S31:   0.0016 S32:   0.1524 S33:   0.3972                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain A and resseq 595:737                             
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5926 -72.6775  27.7060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1434 T22:   1.2164                                     
REMARK   3      T33:   0.8138 T12:   0.0151                                     
REMARK   3      T13:  -0.1478 T23:   0.1739                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9843 L22:   5.2984                                     
REMARK   3      L33:   5.3146 L12:   0.2127                                     
REMARK   3      L13:  -3.7914 L23:   1.1471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4483 S12:  -0.0291 S13:  -0.4427                       
REMARK   3      S21:  -0.1925 S22:  -0.4667 S23:   0.0862                       
REMARK   3      S31:   0.6086 S32:   0.0603 S33:   0.0666                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain A and resseq 738:961                             
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9493 -47.1669 -21.2478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9864 T22:   0.7724                                     
REMARK   3      T33:   0.5922 T12:   0.3188                                     
REMARK   3      T13:   0.0138 T23:  -0.1299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3155 L22:   6.8375                                     
REMARK   3      L33:   6.7776 L12:  -0.8432                                     
REMARK   3      L13:  -0.2283 L23:  -4.0891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0322 S12:   0.1433 S13:   0.1269                       
REMARK   3      S21:  -0.6390 S22:   0.0517 S23:  -0.0387                       
REMARK   3      S31:   0.1544 S32:  -0.0564 S33:  -0.1008                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain A and resseq 969:994                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0758 -46.6782 -43.0887              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7057 T22:   1.9611                                     
REMARK   3      T33:   1.2455 T12:  -0.3033                                     
REMARK   3      T13:   0.1570 T23:  -0.5563                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4679 L22:   3.4875                                     
REMARK   3      L33:   6.0015 L12:  -4.1956                                     
REMARK   3      L13:  -2.8319 L23:  -1.2645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1557 S12:  -0.9188 S13:   1.4971                       
REMARK   3      S21:   2.1838 S22:   0.2001 S23:  -0.3773                       
REMARK   3      S31:  -0.8766 S32:   1.3360 S33:  -0.3167                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain B and resseq 1:56                                
REMARK   3    ORIGIN FOR THE GROUP (A): -20.4170 -46.4633  42.4076              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8454 T22:   1.7157                                     
REMARK   3      T33:   1.3518 T12:  -0.0236                                     
REMARK   3      T13:   0.0687 T23:   0.0688                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6050 L22:   2.5640                                     
REMARK   3      L33:   6.9689 L12:  -3.2216                                     
REMARK   3      L13:  -0.5093 L23:   2.4820                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0257 S12:  -1.3412 S13:  -0.2363                       
REMARK   3      S21:   0.3612 S22:  -0.1845 S23:   1.1576                       
REMARK   3      S31:   0.3198 S32:  -0.7779 S33:   0.0917                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain B and (resseq 57:108 or resseq 353:433)          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3045 -23.0598  22.9768              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5404 T22:   1.3611                                     
REMARK   3      T33:   0.8403 T12:   0.2344                                     
REMARK   3      T13:  -0.1042 T23:  -0.1771                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0276 L22:   9.2150                                     
REMARK   3      L33:   4.5575 L12:   0.1049                                     
REMARK   3      L13:  -0.9725 L23:  -4.3245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2605 S12:   0.2535 S13:   0.0849                       
REMARK   3      S21:   0.0633 S22:  -0.4047 S23:  -0.4676                       
REMARK   3      S31:  -0.0237 S32:   0.3040 S33:   0.1632                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain B and resseq 434:472                             
REMARK   3    ORIGIN FOR THE GROUP (A): -14.2349 -46.8669  58.7079              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2676 T22:   2.0824                                     
REMARK   3      T33:   1.1040 T12:  -0.2875                                     
REMARK   3      T13:   0.0922 T23:   0.1525                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3264 L22:   3.4379                                     
REMARK   3      L33:   8.2744 L12:  -4.8165                                     
REMARK   3      L13:   5.9899 L23:  -5.0727                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2885 S12:  -1.9335 S13:  -0.4846                       
REMARK   3      S21:   1.4441 S22:  -0.8166 S23:   0.0972                       
REMARK   3      S31:  -0.0638 S32:  -0.0186 S33:   0.5480                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain B and (resseq 109:352 or resseq 2001)            
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0559  -6.7622  15.1375              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6330 T22:   1.6140                                     
REMARK   3      T33:   1.1098 T12:   0.0501                                     
REMARK   3      T13:   0.1657 T23:   0.2682                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3999 L22:   2.2365                                     
REMARK   3      L33:   2.0133 L12:  -0.8832                                     
REMARK   3      L13:   2.0570 L23:  -0.1628                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0015 S12:   0.8504 S13:   1.1020                       
REMARK   3      S21:  -0.2169 S22:  -0.0258 S23:  -0.0315                       
REMARK   3      S31:  -0.4080 S32:   0.2780 S33:   0.0123                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain B and resseq 473:522                             
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7887 -63.7726  47.2327              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9019 T22:   1.5636                                     
REMARK   3      T33:   1.0105 T12:   0.0776                                     
REMARK   3      T13:   0.0053 T23:   0.2182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1828 L22:   4.4889                                     
REMARK   3      L33:   2.3853 L12:   0.4781                                     
REMARK   3      L13:   1.7943 L23:   2.3906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3418 S12:  -0.8040 S13:   0.0701                       
REMARK   3      S21:   0.2476 S22:  -0.3893 S23:   0.6520                       
REMARK   3      S31:   0.2303 S32:   0.3287 S33:   0.7316                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain B and resseq 523:559                             
REMARK   3    ORIGIN FOR THE GROUP (A):   2.3794 -50.7485  28.6707              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7557 T22:   1.1465                                     
REMARK   3      T33:   1.0095 T12:   0.1212                                     
REMARK   3      T13:   0.1264 T23:   0.0468                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9194 L22:   8.0231                                     
REMARK   3      L33:   7.1622 L12:   2.4979                                     
REMARK   3      L13:  -1.4506 L23:  -6.9758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0324 S12:  -0.3991 S13:  -0.5174                       
REMARK   3      S21:  -0.7099 S22:  -0.5748 S23:  -1.2182                       
REMARK   3      S31:   0.7594 S32:   0.7371 S33:   0.6884                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain B and resseq 560:600                             
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1217 -38.9320   5.9955              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7045 T22:   0.9122                                     
REMARK   3      T33:   0.6461 T12:   0.1953                                     
REMARK   3      T13:  -0.1429 T23:  -0.1506                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2784 L22:   8.4010                                     
REMARK   3      L33:   5.0782 L12:  -7.2677                                     
REMARK   3      L13:  -6.5558 L23:   6.1947                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3864 S12:  -0.2136 S13:   0.1226                       
REMARK   3      S21:  -1.1112 S22:  -0.5499 S23:   0.2571                       
REMARK   3      S31:  -1.1136 S32:  -1.1294 S33:   0.3054                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain B and resseq 601:692                             
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1092 -24.9055 -15.4971              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0123 T22:   0.8027                                     
REMARK   3      T33:   0.8008 T12:   0.3106                                     
REMARK   3      T13:   0.0320 T23:  -0.0603                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4729 L22:   2.6715                                     
REMARK   3      L33:   5.8279 L12:  -1.2086                                     
REMARK   3      L13:   1.9182 L23:  -2.5967                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1629 S12:  -0.2374 S13:   0.3360                       
REMARK   3      S21:   0.4175 S22:   0.2042 S23:   0.0981                       
REMARK   3      S31:  -0.6806 S32:  -0.0849 S33:  -0.3529                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain B and resseq 706:729                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7858 -49.0538 -51.4583              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3176 T22:   1.4352                                     
REMARK   3      T33:   0.9984 T12:   0.0117                                     
REMARK   3      T13:  -0.0311 T23:  -0.3137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7224 L22:   9.3248                                     
REMARK   3      L33:   6.8463 L12:   0.0107                                     
REMARK   3      L13:  -0.3141 L23:  -7.2509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7347 S12:   0.3509 S13:   0.6440                       
REMARK   3      S21:   1.3228 S22:  -0.2041 S23:   0.9494                       
REMARK   3      S31:  -0.5087 S32:   1.2375 S33:  -0.5820                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4G1E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073615.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79656                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULFATE, 80MM SODIUM       
REMARK 280  CACODYLATE, 6MM MAGNESIUM CHLORIDE, 2MM CALCIUM CHLORIDE, PH 5.8,   
REMARK 280  EVAPORATION, TEMPERATURE 293K                                       
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      235.23933            
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      117.61967            
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      117.61967            
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      235.23933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 23260 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 78310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 11430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 74140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 51640 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 151500 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     GLY A   620                                                      
REMARK 465     GLN A   839                                                      
REMARK 465     THR A   840                                                      
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     MET A   960                                                      
REMARK 465     GLY A   961                                                      
REMARK 465     SER A   962                                                      
REMARK 465     GLY A   963                                                      
REMARK 465     GLY A   964                                                      
REMARK 465     GLU A   965                                                      
REMARK 465     ASN A   966                                                      
REMARK 465     ALA A   967                                                      
REMARK 465     GLN A   968                                                      
REMARK 465     GLN A   995                                                      
REMARK 465     ALA A   996                                                      
REMARK 465     LEU A   997                                                      
REMARK 465     CYS A   998                                                      
REMARK 465     GLY B    34                                                      
REMARK 465     SER B    35                                                      
REMARK 465     ARG B   479                                                      
REMARK 465     PRO B   480                                                      
REMARK 465     SER B   481                                                      
REMARK 465     GLN B   482                                                      
REMARK 465     GLU B   692                                                      
REMARK 465     SER B   693                                                      
REMARK 465     MET B   694                                                      
REMARK 465     GLU B   695                                                      
REMARK 465     ASN B   696                                                      
REMARK 465     LEU B   697                                                      
REMARK 465     TYR B   698                                                      
REMARK 465     PHE B   699                                                      
REMARK 465     GLN B   700                                                      
REMARK 465     SER B   701                                                      
REMARK 465     GLY B   702                                                      
REMARK 465     GLY B   703                                                      
REMARK 465     LYS B   704                                                      
REMARK 465     ASN B   705                                                      
REMARK 465     CYS B   730                                                      
REMARK 465     THR B   731                                                      
REMARK 465     GLY B   732                                                      
REMARK 465     HIS B   733                                                      
REMARK 465     HIS B   734                                                      
REMARK 465     HIS B   735                                                      
REMARK 465     HIS B   736                                                      
REMARK 465     HIS B   737                                                      
REMARK 465     HIS B   738                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A   950     C2   NAG A  2039              2.17            
REMARK 500   ND2  ASN A   585     C2   NAG A  2026              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    ALA A   958     NH1  ARG B    62     4555     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  29     -156.79     69.10                                   
REMARK 500    SER A  31       74.89     40.95                                   
REMARK 500    ARG A  33      139.93    -23.40                                   
REMARK 500    SER A  63     -121.13     58.46                                   
REMARK 500    GLN A 102     -133.92     52.60                                   
REMARK 500    THR A 116      -18.09     78.94                                   
REMARK 500    MET A 118      -61.39   -135.32                                   
REMARK 500    ASP A 148     -172.15     62.52                                   
REMARK 500    ASP A 234      153.59    -48.87                                   
REMARK 500    ALA A 247       70.93     58.20                                   
REMARK 500    LYS A 259      -68.61    -93.22                                   
REMARK 500    ALA A 273       -2.30     70.28                                   
REMARK 500    ASP A 289       -0.69     67.34                                   
REMARK 500    SER A 399      -62.06   -136.48                                   
REMARK 500    THR A 460      -74.58    -86.22                                   
REMARK 500    PRO A 519       40.29    -84.81                                   
REMARK 500    GLN A 534      -66.76    -92.84                                   
REMARK 500    CYS A 535       88.75     66.72                                   
REMARK 500    ASP A 570      -59.76   -121.47                                   
REMARK 500    THR A 571      -77.02   -124.58                                   
REMARK 500    PRO A 576     -176.69    -68.90                                   
REMARK 500    LYS A 605       73.82     52.43                                   
REMARK 500    GLN A 614       -7.76     73.08                                   
REMARK 500    ASN A 674     -126.31     50.87                                   
REMARK 500    GLN A 704      -61.07   -102.69                                   
REMARK 500    GLU A 767      -57.45   -131.96                                   
REMARK 500    VAL A 772      -70.33    -80.77                                   
REMARK 500    PRO A 800       77.92    -68.41                                   
REMARK 500    LEU A 808     -109.68     52.65                                   
REMARK 500    SER A 836      -70.71   -130.30                                   
REMARK 500    LYS A 843     -119.82     76.01                                   
REMARK 500    ASP A 868     -142.84     48.82                                   
REMARK 500    LYS A 911     -130.59     61.89                                   
REMARK 500    GLN A 914      -62.93   -142.34                                   
REMARK 500    PRO A 937       92.09    -68.35                                   
REMARK 500    GLN A 956       44.23   -142.17                                   
REMARK 500    SER B  20      149.32   -171.18                                   
REMARK 500    GLU B  29     -156.08     60.55                                   
REMARK 500    ALA B  30      118.77   -161.91                                   
REMARK 500    VAL B 157      -70.69   -124.93                                   
REMARK 500    ASP B 158      160.99    177.40                                   
REMARK 500    PRO B 160       69.85    -66.67                                   
REMARK 500    THR B 182     -140.81     52.68                                   
REMARK 500    PRO B 186     -174.54    -60.55                                   
REMARK 500    ASP B 217      107.20     66.55                                   
REMARK 500    LYS B 253     -175.73    -64.94                                   
REMARK 500    LEU B 258       -4.85     79.44                                   
REMARK 500    CYS B 374      -71.05    -96.26                                   
REMARK 500    ASN B 376     -127.11     57.56                                   
REMARK 500    GLU B 476     -168.44   -103.29                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 236   O                                                      
REMARK 620 2 ASN A 232   OD1 142.1                                              
REMARK 620 3 ASP A 234   OD1  94.2  79.4                                        
REMARK 620 4 ASP A 238   OD1 117.1  90.5 137.2                                  
REMARK 620 5 ASP A 230   OD1  74.0  68.3  84.9 129.7                            
REMARK 620 6 HOH A2133   O   120.6  92.3  69.6  69.4 150.7                      
REMARK 620 7 ASP A 238   OD2  97.8  76.3 153.0  55.0  75.4 122.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO B 219   O                                                      
REMARK 620 2 ASP B 217   OD1 102.6                                              
REMARK 620 3 ASP B 217   O    92.2  67.1                                        
REMARK 620 4 ASP B 158   OD2  83.0  98.8 163.8                                  
REMARK 620 5 ASN B 215   OD1 140.2 114.2  88.7 104.9                            
REMARK 620 6 GLU B 220   OE1  77.2 164.6  97.6  96.4  63.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 419   O                                                      
REMARK 620 2 ASP A 415   OD1 138.5                                              
REMARK 620 3 ASP A 421   OD1 104.0 117.3                                        
REMARK 620 4 ASN A 417   OD1  73.7  76.8 141.2                                  
REMARK 620 5 ASP A 413   OD1  74.2  66.5 155.8  62.4                            
REMARK 620 6 ASP A 421   OD2 128.5  76.7  55.5 153.5 106.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 355   O                                                      
REMARK 620 2 ASP A 351   OD1 161.1                                              
REMARK 620 3 ASP A 349   OD1  99.4  91.5                                        
REMARK 620 4 ASP A 353   OD1  85.7  81.6  77.9                                  
REMARK 620 5 HOH A2140   O    77.0  85.3 145.8  68.0                            
REMARK 620 6 ASP A 357   OD2 105.2  86.6 104.4 168.1 109.3                      
REMARK 620 7 ASP A 357   OD1  81.9  93.8 157.7 124.3  56.3  54.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 288   OD1                                                    
REMARK 620 2 TYR A 290   O    77.9                                              
REMARK 620 3 ASP A 292   OD1 168.5 100.0                                        
REMARK 620 4 ASN A 286   OD1  83.3 144.7 103.9                                  
REMARK 620 5 ASP A 292   OD2 135.5  88.7  55.1  84.2                            
REMARK 620 6 ASP A 288   OD2  55.8 117.9 117.4  72.7 153.3                      
REMARK 620 7 ASP A 284   OD1  58.0  77.0 132.8  67.7  77.7 104.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A 601   O                                                      
REMARK 620 2 ASP A 599   OD2  68.2                                              
REMARK 620 3 GLU A 636   OE2  96.6 132.2                                        
REMARK 620 4 GLU A 636   OE1  96.4 162.5  55.1                                  
REMARK 620 5 ASP A 599   OD1 108.3  55.0 153.6 127.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2024                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2025                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2026                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2027                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2028                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2029                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2030                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2031                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2032                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2033                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2034                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2035                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2036                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2037                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2038                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2039                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2040                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2041                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2042                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2044                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2045                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 2047                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 2008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 2009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 2012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 2015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 2016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2020                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2021                 
DBREF  4G1E A    1   959  UNP    P06756   ITAV_HUMAN      31    989             
DBREF  4G1E B    1   691  UNP    P05106   ITB3_HUMAN      27    717             
SEQADV 4G1E MET A  960  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLY A  961  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E SER A  962  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLY A  963  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLY A  964  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLU A  965  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E ASN A  966  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E ALA A  967  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLN A  968  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E CYS A  969  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLU A  970  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E LYS A  971  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLU A  972  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E LEU A  973  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLN A  974  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E ALA A  975  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E LEU A  976  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLU A  977  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E LYS A  978  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLU A  979  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E ASN A  980  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E ALA A  981  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLN A  982  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E LEU A  983  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLU A  984  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E TRP A  985  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLU A  986  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E LEU A  987  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLN A  988  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E ALA A  989  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E LEU A  990  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLU A  991  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E LYS A  992  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLU A  993  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E LEU A  994  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLN A  995  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E ALA A  996  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E LEU A  997  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E CYS A  998  UNP  P06756              EXPRESSION TAG                 
SEQADV 4G1E GLU B  692  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E SER B  693  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E MET B  694  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E GLU B  695  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E ASN B  696  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LEU B  697  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E TYR B  698  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E PHE B  699  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E GLN B  700  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E SER B  701  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E GLY B  702  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E GLY B  703  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LYS B  704  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E ASN B  705  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E ALA B  706  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E GLN B  707  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E CYS B  708  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LYS B  709  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LYS B  710  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LYS B  711  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LEU B  712  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E GLN B  713  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E ALA B  714  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LEU B  715  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LYS B  716  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LYS B  717  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LYS B  718  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E ASN B  719  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E ALA B  720  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E GLN B  721  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LEU B  722  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LYS B  723  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E TRP B  724  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LYS B  725  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LEU B  726  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E GLN B  727  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E ALA B  728  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E LEU B  729  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E CYS B  730  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E THR B  731  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E GLY B  732  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E HIS B  733  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E HIS B  734  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E HIS B  735  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E HIS B  736  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E HIS B  737  UNP  P05106              EXPRESSION TAG                 
SEQADV 4G1E HIS B  738  UNP  P05106              EXPRESSION TAG                 
SEQRES   1 A  998  PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY          
SEQRES   2 A  998  PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE          
SEQRES   3 A  998  VAL PRO SER ALA SER SER ARG MET PHE LEU LEU VAL GLY          
SEQRES   4 A  998  ALA PRO LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU          
SEQRES   5 A  998  GLY GLY GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG          
SEQRES   6 A  998  ARG CYS GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG          
SEQRES   7 A  998  ASP TYR ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS          
SEQRES   8 A  998  GLN TRP PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS          
SEQRES   9 A  998  ILE LEU ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU          
SEQRES  10 A  998  MET LYS GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU          
SEQRES  11 A  998  GLN ASP GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG          
SEQRES  12 A  998  SER GLN ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN          
SEQRES  13 A  998  GLY GLY PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL          
SEQRES  14 A  998  LEU LEU GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN          
SEQRES  15 A  998  LEU ILE SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR          
SEQRES  16 A  998  ASP PRO ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU          
SEQRES  17 A  998  ALA THR ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR          
SEQRES  18 A  998  LEU GLY TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP          
SEQRES  19 A  998  GLY ILE ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA          
SEQRES  20 A  998  ARG THR LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN          
SEQRES  21 A  998  MET SER SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA          
SEQRES  22 A  998  ALA TYR PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN          
SEQRES  23 A  998  GLY ASP ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU          
SEQRES  24 A  998  PHE MET ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL          
SEQRES  25 A  998  GLY GLN VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP          
SEQRES  26 A  998  PHE GLN THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA          
SEQRES  27 A  998  ARG PHE GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP          
SEQRES  28 A  998  GLN ASP GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR          
SEQRES  29 A  998  GLY GLY GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN          
SEQRES  30 A  998  GLY ARG SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE          
SEQRES  31 A  998  LEU GLU GLY GLN TRP ALA ALA ARG SER MET PRO PRO SER          
SEQRES  32 A  998  PHE GLY TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS          
SEQRES  33 A  998  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL          
SEQRES  34 A  998  ASP ARG ALA ILE LEU TYR ARG ALA ARG PRO VAL ILE THR          
SEQRES  35 A  998  VAL ASN ALA GLY LEU GLU VAL TYR PRO SER ILE LEU ASN          
SEQRES  36 A  998  GLN ASP ASN LYS THR CYS SER LEU PRO GLY THR ALA LEU          
SEQRES  37 A  998  LYS VAL SER CYS PHE ASN VAL ARG PHE CYS LEU LYS ALA          
SEQRES  38 A  998  ASP GLY LYS GLY VAL LEU PRO ARG LYS LEU ASN PHE GLN          
SEQRES  39 A  998  VAL GLU LEU LEU LEU ASP LYS LEU LYS GLN LYS GLY ALA          
SEQRES  40 A  998  ILE ARG ARG ALA LEU PHE LEU TYR SER ARG SER PRO SER          
SEQRES  41 A  998  HIS SER LYS ASN MET THR ILE SER ARG GLY GLY LEU MET          
SEQRES  42 A  998  GLN CYS GLU GLU LEU ILE ALA TYR LEU ARG ASP GLU SER          
SEQRES  43 A  998  GLU PHE ARG ASP LYS LEU THR PRO ILE THR ILE PHE MET          
SEQRES  44 A  998  GLU TYR ARG LEU ASP TYR ARG THR ALA ALA ASP THR THR          
SEQRES  45 A  998  GLY LEU GLN PRO ILE LEU ASN GLN PHE THR PRO ALA ASN          
SEQRES  46 A  998  ILE SER ARG GLN ALA HIS ILE LEU LEU ASP CYS GLY GLU          
SEQRES  47 A  998  ASP ASN VAL CYS LYS PRO LYS LEU GLU VAL SER VAL ASP          
SEQRES  48 A  998  SER ASP GLN LYS LYS ILE TYR ILE GLY ASP ASP ASN PRO          
SEQRES  49 A  998  LEU THR LEU ILE VAL LYS ALA GLN ASN GLN GLY GLU GLY          
SEQRES  50 A  998  ALA TYR GLU ALA GLU LEU ILE VAL SER ILE PRO LEU GLN          
SEQRES  51 A  998  ALA ASP PHE ILE GLY VAL VAL ARG ASN ASN GLU ALA LEU          
SEQRES  52 A  998  ALA ARG LEU SER CYS ALA PHE LYS THR GLU ASN GLN THR          
SEQRES  53 A  998  ARG GLN VAL VAL CYS ASP LEU GLY ASN PRO MET LYS ALA          
SEQRES  54 A  998  GLY THR GLN LEU LEU ALA GLY LEU ARG PHE SER VAL HIS          
SEQRES  55 A  998  GLN GLN SER GLU MET ASP THR SER VAL LYS PHE ASP LEU          
SEQRES  56 A  998  GLN ILE GLN SER SER ASN LEU PHE ASP LYS VAL SER PRO          
SEQRES  57 A  998  VAL VAL SER HIS LYS VAL ASP LEU ALA VAL LEU ALA ALA          
SEQRES  58 A  998  VAL GLU ILE ARG GLY VAL SER SER PRO ASP HIS VAL PHE          
SEQRES  59 A  998  LEU PRO ILE PRO ASN TRP GLU HIS LYS GLU ASN PRO GLU          
SEQRES  60 A  998  THR GLU GLU ASP VAL GLY PRO VAL VAL GLN HIS ILE TYR          
SEQRES  61 A  998  GLU LEU ARG ASN ASN GLY PRO SER SER PHE SER LYS ALA          
SEQRES  62 A  998  MET LEU HIS LEU GLN TRP PRO TYR LYS TYR ASN ASN ASN          
SEQRES  63 A  998  THR LEU LEU TYR ILE LEU HIS TYR ASP ILE ASP GLY PRO          
SEQRES  64 A  998  MET ASN CYS THR SER ASP MET GLU ILE ASN PRO LEU ARG          
SEQRES  65 A  998  ILE LYS ILE SER SER LEU GLN THR THR GLU LYS ASN ASP          
SEQRES  66 A  998  THR VAL ALA GLY GLN GLY GLU ARG ASP HIS LEU ILE THR          
SEQRES  67 A  998  LYS ARG ASP LEU ALA LEU SER GLU GLY ASP ILE HIS THR          
SEQRES  68 A  998  LEU GLY CYS GLY VAL ALA GLN CYS LEU LYS ILE VAL CYS          
SEQRES  69 A  998  GLN VAL GLY ARG LEU ASP ARG GLY LYS SER ALA ILE LEU          
SEQRES  70 A  998  TYR VAL LYS SER LEU LEU TRP THR GLU THR PHE MET ASN          
SEQRES  71 A  998  LYS GLU ASN GLN ASN HIS SER TYR SER LEU LYS SER SER          
SEQRES  72 A  998  ALA SER PHE ASN VAL ILE GLU PHE PRO TYR LYS ASN LEU          
SEQRES  73 A  998  PRO ILE GLU ASP ILE THR ASN SER THR LEU VAL THR THR          
SEQRES  74 A  998  ASN VAL THR TRP GLY ILE GLN PRO ALA PRO MET GLY SER          
SEQRES  75 A  998  GLY GLY GLU ASN ALA GLN CYS GLU LYS GLU LEU GLN ALA          
SEQRES  76 A  998  LEU GLU LYS GLU ASN ALA GLN LEU GLU TRP GLU LEU GLN          
SEQRES  77 A  998  ALA LEU GLU LYS GLU LEU GLN ALA LEU CYS                      
SEQRES   1 B  738  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  738  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  738  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  738  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  738  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  738  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  738  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  738  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  738  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  738  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  738  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  738  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  738  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  738  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  738  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  738  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  738  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  738  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  738  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  738  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  738  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  738  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  738  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  738  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  738  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  738  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  738  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  738  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  738  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  738  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  738  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  738  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  738  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  738  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  738  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  738  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  738  SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG PRO SER          
SEQRES  38 B  738  GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN PRO VAL          
SEQRES  39 B  738  CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL          
SEQRES  40 B  738  CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY LYS TYR          
SEQRES  41 B  738  CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR LYS GLY          
SEQRES  42 B  738  GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS GLY ASP          
SEQRES  43 B  738  CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR CYS ASN          
SEQRES  44 B  738  CYS THR THR ARG THR ASP THR CYS MET SER SER ASN GLY          
SEQRES  45 B  738  LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS GLY SER          
SEQRES  46 B  738  CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP THR CYS          
SEQRES  47 B  738  GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR PHE LYS          
SEQRES  48 B  738  LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG GLY ALA          
SEQRES  49 B  738  LEU HIS ASP GLU ASN THR CYS ASN ARG TYR CYS ARG ASP          
SEQRES  50 B  738  GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR GLY LYS          
SEQRES  51 B  738  ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP ASP CYS          
SEQRES  52 B  738  VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER GLY LYS          
SEQRES  53 B  738  SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS PRO LYS          
SEQRES  54 B  738  GLY PRO GLU SER MET GLU ASN LEU TYR PHE GLN SER GLY          
SEQRES  55 B  738  GLY LYS ASN ALA GLN CYS LYS LYS LYS LEU GLN ALA LEU          
SEQRES  56 B  738  LYS LYS LYS ASN ALA GLN LEU LYS TRP LYS LEU GLN ALA          
SEQRES  57 B  738  LEU CYS THR GLY HIS HIS HIS HIS HIS HIS                      
MODRES 4G1E ASN A  524  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN A  266  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN A  844  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN A  950  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN A  585  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN A  458  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN A  260  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN B  559  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN B  654  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN A  821  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN A   44  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1E ASN A  943  ASN  GLYCOSYLATION SITE                                 
HET     CA  A2001       1                                                       
HET     CA  A2002       1                                                       
HET     CA  A2003       1                                                       
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET    NAG  A2006      14                                                       
HET    NAG  A2007      14                                                       
HET    BMA  A2008      11                                                       
HET    MAN  A2009      11                                                       
HET    NAG  A2010      14                                                       
HET    NAG  A2011      14                                                       
HET    BMA  A2012      11                                                       
HET    NAG  A2013      14                                                       
HET    NAG  A2014      14                                                       
HET    BMA  A2015      11                                                       
HET    MAN  A2016      11                                                       
HET    MAN  A2017      11                                                       
HET    MAN  A2018      11                                                       
HET    MAN  A2019      11                                                       
HET    MAN  A2020      11                                                       
HET    NAG  A2021      14                                                       
HET    NAG  A2022      14                                                       
HET    BMA  A2023      11                                                       
HET    MAN  A2024      11                                                       
HET    NAG  A2025      14                                                       
HET    NAG  A2026      14                                                       
HET    NAG  A2027      14                                                       
HET    NAG  A2028      14                                                       
HET    NAG  A2029      14                                                       
HET    BMA  A2030      11                                                       
HET    NAG  A2031      14                                                       
HET    NAG  A2032      14                                                       
HET    BMA  A2033      11                                                       
HET    MAN  A2034      11                                                       
HET    MAN  A2035      11                                                       
HET    MAN  A2036      11                                                       
HET    NAG  A2037      14                                                       
HET    NAG  A2038      14                                                       
HET    NAG  A2039      14                                                       
HET    SO4  A2040       5                                                       
HET    SO4  A2041       5                                                       
HET    SO4  A2042       5                                                       
HET     CL  A2043       1                                                       
HET     CL  A2044       1                                                       
HET     CL  A2045       1                                                       
HET     CL  A2046       1                                                       
HET     NI  A2047       1                                                       
HET     CA  B2001       1                                                       
HET    NAG  B2002      14                                                       
HET    NAG  B2003      14                                                       
HET    NAG  B2004      14                                                       
HET    NAG  B2005      14                                                       
HET    NAG  B2006      14                                                       
HET    NAG  B2007      14                                                       
HET    BMA  B2008      11                                                       
HET    MAN  B2009      11                                                       
HET    NAG  B2010      14                                                       
HET    NAG  B2011      14                                                       
HET    BMA  B2012      11                                                       
HET    NAG  B2013      14                                                       
HET    NAG  B2014      14                                                       
HET    BMA  B2015      11                                                       
HET    MAN  B2016      11                                                       
HET    SO4  B2017       5                                                       
HET    SO4  B2018       5                                                       
HET    SO4  B2019       5                                                       
HET     CL  B2020       1                                                       
HET     CL  B2021       1                                                       
HET     CL  B2022       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   3   CA    6(CA 2+)                                                     
FORMUL   8  NAG    28(C8 H15 N O6)                                              
FORMUL   8  BMA    9(C6 H12 O6)                                                 
FORMUL   8  MAN    12(C6 H12 O6)                                                
FORMUL  18  SO4    6(O4 S 2-)                                                   
FORMUL  21   CL    7(CL 1-)                                                     
FORMUL  25   NI    NI 2+                                                        
FORMUL  38  HOH   *99(H2 O)                                                     
HELIX    1   1 GLY A  175  GLN A  180  1                                   6    
HELIX    2   2 VAL A  188  LYS A  194  1                                   7    
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 GLY A  366  LYS A  370  5                                   5    
HELIX    6   6 ASP A  544  PHE A  548  5                                   5    
HELIX    7   7 THR A  768  GLY A  773  1                                   6    
HELIX    8   8 TRP A  904  ASN A  910  1                                   7    
HELIX    9   9 GLU A  970  GLU A  993  1                                  24    
HELIX   10  10 ASN B    3  GLY B    9  1                                   7    
HELIX   11  11 SER B   12  SER B   20  1                                   9    
HELIX   12  12 LYS B   41  ASP B   47  1                                   7    
HELIX   13  13 ALA B   50  GLU B   52  5                                   3    
HELIX   14  14 SER B  121  SER B  123  5                                   3    
HELIX   15  15 MET B  124  ILE B  131  1                                   8    
HELIX   16  16 ASN B  133  MET B  142  1                                  10    
HELIX   17  17 PRO B  169  ASN B  175  1                                   7    
HELIX   18  18 VAL B  200  GLN B  210  1                                  11    
HELIX   19  19 GLY B  221  CYS B  232  1                                  12    
HELIX   20  20 CYS B  232  GLY B  237  1                                   6    
HELIX   21  21 LEU B  258  GLY B  264  5                                   7    
HELIX   22  22 TYR B  281  THR B  285  5                                   5    
HELIX   23  23 SER B  291  LYS B  302  1                                  12    
HELIX   24  24 THR B  311  ILE B  325  1                                  15    
HELIX   25  25 ASN B  339  ARG B  352  1                                  14    
HELIX   26  26 GLY B  468  GLU B  472  5                                   5    
HELIX   27  27 VAL B  494  ARG B  498  5                                   5    
HELIX   28  28 GLU B  534  GLY B  538  5                                   5    
HELIX   29  29 THR B  564  MET B  568  5                                   5    
HELIX   30  30 LEU B  573  GLY B  577  5                                   5    
HELIX   31  31 ASP B  606  LYS B  619  1                                  14    
HELIX   32  32 GLY B  623  GLU B  628  1                                   6    
HELIX   33  33 THR B  630  CYS B  635  1                                   6    
HELIX   34  34 GLN B  707  LYS B  725  1                                  19    
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  VAL A 424   O  ILE A 433           
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  LEU A  57   N  VAL A  38           
SHEET    4   B 4 ARG A  66  ILE A  70 -1  O  ILE A  70   N  VAL A  56           
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 SER A 160  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  ILE A 184   N  LEU A 171           
SHEET    4   F 4 GLN A 207  ALA A 209 -1  O  LEU A 208   N  SER A 185           
SHEET    1   G 4 VAL A 226  GLY A 229  0                                        
SHEET    2   G 4 ASP A 238  VAL A 243 -1  O  ASP A 238   N  GLY A 229           
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  ASP A 292   N  THR A 283           
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  THR A 329   N  VAL A 317           
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 ILE A 344  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  PHE A 376 -1  O  ILE A 372   N  ALA A 362           
SHEET    4   J 4 GLN A 389  GLU A 392 -1  O  LEU A 391   N  VAL A 373           
SHEET    1   K 5 ALA A 511  PHE A 513  0                                        
SHEET    2   K 5 GLU A 536  LEU A 542 -1  O  TYR A 541   N  LEU A 512           
SHEET    3   K 5 CYS A 472  GLY A 483 -1  N  VAL A 475   O  LEU A 538           
SHEET    4   K 5 VAL A 440  TYR A 450 -1  N  ASN A 444   O  LYS A 480           
SHEET    5   K 5 ILE A 577  LEU A 578  1  O  ILE A 577   N  ILE A 441           
SHEET    1   L 5 ILE A 453  ASN A 455  0                                        
SHEET    2   L 5 ASN A 585  LEU A 593  1  O  HIS A 591   N  LEU A 454           
SHEET    3   L 5 ILE A 555  LEU A 563 -1  N  ILE A 555   O  ALA A 590           
SHEET    4   L 5 LYS A 490  LEU A 498 -1  N  LEU A 498   O  PHE A 558           
SHEET    5   L 5 SER A 520  SER A 528 -1  O  ILE A 527   N  LEU A 491           
SHEET    1   M 4 LEU A 606  ASP A 611  0                                        
SHEET    2   M 4 ASN A 623  ASN A 633 -1  O  LYS A 630   N  SER A 609           
SHEET    3   M 4 GLN A 692  VAL A 701 -1  O  LEU A 693   N  ALA A 631           
SHEET    4   M 4 ALA A 651  VAL A 656 -1  N  GLY A 655   O  ARG A 698           
SHEET    1   N 6 ILE A 617  TYR A 618  0                                        
SHEET    2   N 6 VAL A 730  ALA A 737  1  O  ALA A 737   N  ILE A 617           
SHEET    3   N 6 SER A 710  GLN A 718 -1  N  LEU A 715   O  VAL A 730           
SHEET    4   N 6 GLU A 642  SER A 646 -1  N  SER A 646   O  ASP A 714           
SHEET    5   N 6 GLN A 678  ASP A 682 -1  O  CYS A 681   N  LEU A 643           
SHEET    6   N 6 CYS A 668  LYS A 671 -1  N  ALA A 669   O  VAL A 680           
SHEET    1   O 4 VAL A 742  SER A 749  0                                        
SHEET    2   O 4 VAL A 775  ASN A 784 -1  O  GLU A 781   N  ARG A 745           
SHEET    3   O 4 LYS A 893  LEU A 903 -1  O  ALA A 895   N  LEU A 782           
SHEET    4   O 4 LEU A 809  ASP A 817 -1  N  TYR A 810   O  LEU A 902           
SHEET    1   P 6 HIS A 752  LEU A 755  0                                        
SHEET    2   P 6 THR A 942  TRP A 953  1  O  THR A 952   N  VAL A 753           
SHEET    3   P 6 TYR A 918  GLU A 930 -1  N  ALA A 924   O  THR A 945           
SHEET    4   P 6 LYS A 792  LYS A 802 -1  N  GLN A 798   O  SER A 923           
SHEET    5   P 6 GLN A 878  VAL A 886 -1  O  VAL A 886   N  ALA A 793           
SHEET    6   P 6 ASN A 821  SER A 824 -1  N  ASN A 821   O  GLN A 885           
SHEET    1   Q 4 HIS A 752  LEU A 755  0                                        
SHEET    2   Q 4 THR A 942  TRP A 953  1  O  THR A 952   N  VAL A 753           
SHEET    3   Q 4 TYR A 918  GLU A 930 -1  N  ALA A 924   O  THR A 945           
SHEET    4   Q 4 HIS A 870  LEU A 872  1  N  LEU A 872   O  SER A 919           
SHEET    1   R 3 CYS B  38  LEU B  40  0                                        
SHEET    2   R 3 CYS B  23  CYS B  26 -1  N  ALA B  24   O  ASP B  39           
SHEET    3   R 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1   S 6 GLU B  60  GLU B  65  0                                        
SHEET    2   S 6 ARG B  87  LEU B  92 -1  O  ARG B  91   N  GLU B  60           
SHEET    3   S 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4   S 6 GLU B 411  PRO B 418 -1  N  ILE B 416   O  LEU B 425           
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 5 VAL B  83  SER B  84  0                                        
SHEET    2   T 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3   T 5 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    4   T 5 LEU B 366  THR B 373 -1  N  THR B 373   O  SER B 396           
SHEET    5   T 5 VAL B 379  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 ASN B 305  VAL B 310  1  O  ASN B 305   N  HIS B 244           
SHEET    6   U 6 THR B 328  VAL B 332  1  O  GLY B 331   N  PHE B 308           
SHEET    1   V 2 GLY B 453  GLU B 456  0                                        
SHEET    2   V 2 VAL B 459  CYS B 462 -1  O  ARG B 461   N  THR B 454           
SHEET    1   W 2 GLY B 540  SER B 543  0                                        
SHEET    2   W 2 ASP B 546  CYS B 549 -1  O  LEU B 548   N  GLN B 541           
SHEET    1   X 2 TRP B 553  THR B 554  0                                        
SHEET    2   X 2 CYS B 560  THR B 561 -1  O  CYS B 560   N  THR B 554           
SHEET    1   Y 2 GLY B 579  GLU B 582  0                                        
SHEET    2   Y 2 SER B 585  CYS B 588 -1  O  VAL B 587   N  LYS B 580           
SHEET    1   Z 4 GLU B 638  VAL B 642  0                                        
SHEET    2   Z 4 ILE B 678  VAL B 682  1  O  LEU B 679   N  GLU B 638           
SHEET    3   Z 4 VAL B 664  TYR B 670 -1  N  ARG B 666   O  VAL B 682           
SHEET    4   Z 4 VAL B 653  LYS B 658 -1  N  CYS B 655   O  PHE B 667           
SSBOND   1 CYS A   59    CYS A   67                          1555   1555  2.03  
SSBOND   2 CYS A  108    CYS A  128                          1555   1555  2.03  
SSBOND   3 CYS A  142    CYS A  155                          1555   1555  2.03  
SSBOND   4 CYS A  461    CYS A  472                          1555   1555  2.03  
SSBOND   5 CYS A  478    CYS A  535                          1555   1555  2.03  
SSBOND   6 CYS A  596    CYS A  602                          1555   1555  2.03  
SSBOND   7 CYS A  668    CYS A  681                          1555   1555  2.03  
SSBOND   8 CYS A  822    CYS A  884                          1555   1555  2.03  
SSBOND   9 CYS A  874    CYS A  879                          1555   1555  2.03  
SSBOND  10 CYS A  969    CYS B  708                          1555   1555  2.03  
SSBOND  11 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND  12 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND  13 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND  14 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND  15 CYS B  177    CYS B  184                          1555   1555  2.03  
SSBOND  16 CYS B  232    CYS B  273                          1555   1555  2.03  
SSBOND  17 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  18 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  19 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  20 CYS B  448    CYS B  460                          1555   1555  2.03  
SSBOND  21 CYS B  462    CYS B  471                          1555   1555  2.03  
SSBOND  22 CYS B  473    CYS B  503                          1555   1555  2.03  
SSBOND  23 CYS B  486    CYS B  501                          1555   1555  2.03  
SSBOND  24 CYS B  495    CYS B  506                          1555   1555  2.03  
SSBOND  25 CYS B  508    CYS B  521                          1555   1555  2.03  
SSBOND  26 CYS B  523    CYS B  544                          1555   1555  2.03  
SSBOND  27 CYS B  528    CYS B  542                          1555   1555  2.03  
SSBOND  28 CYS B  536    CYS B  547                          1555   1555  2.03  
SSBOND  29 CYS B  549    CYS B  558                          1555   1555  2.03  
SSBOND  30 CYS B  560    CYS B  583                          1555   1555  2.03  
SSBOND  31 CYS B  567    CYS B  581                          1555   1555  2.03  
SSBOND  32 CYS B  575    CYS B  586                          1555   1555  2.03  
SSBOND  33 CYS B  588    CYS B  598                          1555   1555  2.03  
SSBOND  34 CYS B  601    CYS B  604                          1555   1555  2.03  
SSBOND  35 CYS B  608    CYS B  655                          1555   1555  2.03  
SSBOND  36 CYS B  614    CYS B  635                          1555   1555  2.03  
SSBOND  37 CYS B  617    CYS B  631                          1555   1555  2.03  
SSBOND  38 CYS B  663    CYS B  687                          1555   1555  2.03  
LINK         O4  NAG A2022                 C1  BMA A2023     1555   1555  1.43  
LINK         ND2 ASN A 524                 C1  NAG A2025     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B2004     1555   1555  1.44  
LINK         O3  MAN A2016                 C1  MAN A2019     1555   1555  1.44  
LINK         O4  NAG A2032                 C1  BMA A2033     1555   1555  1.44  
LINK         O6  BMA B2015                 C1  MAN B2016     1555   1555  1.44  
LINK         ND2 ASN A 266                 C1  NAG A2013     1555   1555  1.44  
LINK         O3  MAN A2017                 C1  MAN A2018     1555   1555  1.44  
LINK         O4  NAG A2021                 C1  NAG A2022     1555   1555  1.44  
LINK         O3  BMA A2015                 C1  MAN A2016     1555   1555  1.44  
LINK         O4  NAG B2004                 C1  NAG B2005     1555   1555  1.44  
LINK         ND2 ASN A 844                 C1  NAG A2031     1555   1555  1.44  
LINK         ND2 ASN A 950                 C1  NAG A2039     1555   1555  1.44  
LINK         ND2 ASN A 585                 C1  NAG A2026     1555   1555  1.44  
LINK         O4  NAG B2011                 C1  BMA B2012     1555   1555  1.44  
LINK         ND2 ASN B  99                 C1  NAG B2002     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B2006     1555   1555  1.44  
LINK         ND2 ASN A 458                 C1  NAG A2021     1555   1555  1.44  
LINK         O6  BMA B2008                 C1  MAN B2009     1555   1555  1.44  
LINK         ND2 ASN A 260                 C1  NAG A2010     1555   1555  1.44  
LINK         O4  NAG A2007                 C1  BMA A2008     1555   1555  1.44  
LINK         O4  NAG A2014                 C1  BMA A2015     1555   1555  1.44  
LINK         O3  MAN A2035                 C1  MAN A2036     1555   1555  1.44  
LINK         O4  NAG A2011                 C1  BMA A2012     1555   1555  1.44  
LINK         O4  NAG B2007                 C1  BMA B2008     1555   1555  1.44  
LINK         O4  NAG A2029                 C1  BMA A2030     1555   1555  1.44  
LINK         ND2 ASN B 559                 C1  NAG B2010     1555   1555  1.44  
LINK         ND2 ASN B 654                 C1  NAG B2013     1555   1555  1.44  
LINK         O4  NAG B2014                 C1  BMA B2015     1555   1555  1.44  
LINK         O4  NAG A2031                 C1  NAG A2032     1555   1555  1.44  
LINK         O4  NAG B2010                 C1  NAG B2011     1555   1555  1.44  
LINK         O4  NAG A2013                 C1  NAG A2014     1555   1555  1.44  
LINK         O2  MAN A2018                 C1  MAN A2020     1555   1555  1.44  
LINK         O4  NAG A2026                 C1  NAG A2027     1555   1555  1.44  
LINK         O4  NAG B2002                 C1  NAG B2003     1555   1555  1.44  
LINK         O4  NAG A2006                 C1  NAG A2007     1555   1555  1.44  
LINK         O3  BMA A2033                 C1  MAN A2034     1555   1555  1.44  
LINK         O4  NAG A2010                 C1  NAG A2011     1555   1555  1.44  
LINK         O4  NAG A2028                 C1  NAG A2029     1555   1555  1.44  
LINK         O6  BMA A2008                 C1  MAN A2009     1555   1555  1.44  
LINK         ND2 ASN A 821                 C1  NAG A2028     1555   1555  1.44  
LINK         O4  NAG B2006                 C1  NAG B2007     1555   1555  1.44  
LINK         ND2 ASN A  44                 C1  NAG A2006     1555   1555  1.44  
LINK         O6  BMA A2015                 C1  MAN A2017     1555   1555  1.44  
LINK         ND2 ASN A 943                 C1  NAG A2037     1555   1555  1.44  
LINK         O4  NAG A2037                 C1  NAG A2038     1555   1555  1.44  
LINK         O4  NAG B2013                 C1  NAG B2014     1555   1555  1.44  
LINK         O3  BMA A2023                 C1  MAN A2024     1555   1555  1.45  
LINK         O6  BMA A2033                 C1  MAN A2035     1555   1555  1.45  
LINK         O   ILE A 236                CA    CA A2001     1555   1555  2.12  
LINK         O   PRO B 219                CA    CA B2001     1555   1555  2.12  
LINK         O   TYR A 419                CA    CA A2004     1555   1555  2.17  
LINK         O   PHE A 355                CA    CA A2003     1555   1555  2.22  
LINK         OD1 ASP A 288                CA    CA A2002     1555   1555  2.27  
LINK         O   VAL A 601                CA    CA A2005     1555   1555  2.28  
LINK         OD1 ASN A 232                CA    CA A2001     1555   1555  2.29  
LINK         OD1 ASP A 351                CA    CA A2003     1555   1555  2.29  
LINK         OD1 ASP A 415                CA    CA A2004     1555   1555  2.30  
LINK         O   TYR A 290                CA    CA A2002     1555   1555  2.31  
LINK         OD1 ASP A 421                CA    CA A2004     1555   1555  2.33  
LINK         OD1 ASP B 217                CA    CA B2001     1555   1555  2.33  
LINK         OD2 ASP A 599                CA    CA A2005     1555   1555  2.33  
LINK         OD1 ASP A 349                CA    CA A2003     1555   1555  2.34  
LINK         OD1 ASP A 292                CA    CA A2002     1555   1555  2.34  
LINK         OE2 GLU A 636                CA    CA A2005     1555   1555  2.34  
LINK         OD1 ASP A 234                CA    CA A2001     1555   1555  2.34  
LINK         OD1 ASP A 353                CA    CA A2003     1555   1555  2.35  
LINK         OD1 ASN A 286                CA    CA A2002     1555   1555  2.36  
LINK         OD1 ASN A 417                CA    CA A2004     1555   1555  2.36  
LINK         OD1 ASP A 238                CA    CA A2001     1555   1555  2.36  
LINK         OD1 ASP A 230                CA    CA A2001     1555   1555  2.37  
LINK        CA    CA A2001                 O   HOH A2133     1555   1555  2.37  
LINK        CA    CA A2003                 O   HOH A2140     1555   1555  2.38  
LINK         O   ASP B 217                CA    CA B2001     1555   1555  2.38  
LINK         OD2 ASP A 357                CA    CA A2003     1555   1555  2.38  
LINK         OD1 ASP A 413                CA    CA A2004     1555   1555  2.38  
LINK         OD2 ASP A 421                CA    CA A2004     1555   1555  2.38  
LINK         OD2 ASP A 238                CA    CA A2001     1555   1555  2.39  
LINK         OE1 GLU A 636                CA    CA A2005     1555   1555  2.40  
LINK         OD2 ASP A 292                CA    CA A2002     1555   1555  2.41  
LINK         OD2 ASP B 158                CA    CA B2001     1555   1555  2.41  
LINK         OD2 ASP A 288                CA    CA A2002     1555   1555  2.41  
LINK         OD1 ASP A 357                CA    CA A2003     1555   1555  2.41  
LINK         OD1 ASP A 284                CA    CA A2002     1555   1555  2.42  
LINK         OD1 ASP A 599                CA    CA A2005     1555   1555  2.42  
LINK         OD1 ASN B 215                CA    CA B2001     1555   1555  2.44  
LINK         OE1 GLU B 220                CA    CA B2001     1555   1555  2.45  
CISPEP   1 TYR A  450    PRO A  451          0        -1.75                     
CISPEP   2 ASN A  685    PRO A  686          0         0.58                     
CISPEP   3 SER A  749    PRO A  750          0        -2.03                     
CISPEP   4 LEU A  755    PRO A  756          0        -1.64                     
CISPEP   5 SER B   84    PRO B   85          0        -2.68                     
CISPEP   6 SER B  162    PRO B  163          0        -1.50                     
CISPEP   7 SER B  168    PRO B  169          0         0.22                     
SITE     1 AC1  6 ASP A 230  ASN A 232  ASP A 234  ILE A 236                    
SITE     2 AC1  6 ASP A 238  HOH A2133                                          
SITE     1 AC2  5 ASP A 284  ASN A 286  ASP A 288  TYR A 290                    
SITE     2 AC2  5 ASP A 292                                                     
SITE     1 AC3  7 ASP A 349  LEU A 350  ASP A 351  ASP A 353                    
SITE     2 AC3  7 PHE A 355  ASP A 357  HOH A2140                               
SITE     1 AC4  5 ASP A 413  ASP A 415  ASN A 417  TYR A 419                    
SITE     2 AC4  5 ASP A 421                                                     
SITE     1 AC5  3 ASP A 599  VAL A 601  GLU A 636                               
SITE     1 AC6  5 GLY A  16  LYS A  42  ASN A  44  GLU A  52                    
SITE     2 AC6  5 NAG A2007                                                     
SITE     1 AC7  2 NAG A2006  BMA A2008                                          
SITE     1 AC8  2 NAG A2007  MAN A2009                                          
SITE     1 AC9  1 BMA A2008                                                     
SITE     1 BC1  4 ASP A 257  LYS A 259  ASN A 260  NAG A2011                    
SITE     1 BC2  2 NAG A2010  BMA A2012                                          
SITE     1 BC3  1 NAG A2011                                                     
SITE     1 BC4  5 TYR A 254  SER A 263  LEU A 264  ASN A 266                    
SITE     2 BC4  5 NAG A2014                                                     
SITE     1 BC5  5 ALA A 213  GLN A 214  PHE A 217  NAG A2013                    
SITE     2 BC5  5 BMA A2015                                                     
SITE     1 BC6  4 GLN A 214  NAG A2014  MAN A2016  MAN A2017                    
SITE     1 BC7  2 BMA A2015  MAN A2019                                          
SITE     1 BC8  4 ARG A 211  BMA A2015  MAN A2018  MAN A2020                    
SITE     1 BC9  2 MAN A2017  MAN A2020                                          
SITE     1 CC1  1 MAN A2016                                                     
SITE     1 CC2  4 GLN A 214  ALA A 215  MAN A2017  MAN A2018                    
SITE     1 CC3  5 ASN A 458  THR A 460  CYS A 472  PHE A 473                    
SITE     2 CC3  5 NAG A2022                                                     
SITE     1 CC4  4 TYR A 450  ASN A 474  NAG A2021  BMA A2023                    
SITE     1 CC5  3 TYR A 450  NAG A2022  MAN A2024                               
SITE     1 CC6  1 BMA A2023                                                     
SITE     1 CC7  2 GLN A 494  ASN A 524                                          
SITE     1 CC8  3 GLU A 560  ASN A 585  NAG A2027                               
SITE     1 CC9  1 NAG A2026                                                     
SITE     1 DC1  6 TYR A  80  MET A 118  ASN A 821  THR A 823                    
SITE     2 DC1  6 GLN A 885  NAG A2029                                          
SITE     1 DC2  3 GLN A 120  NAG A2028  BMA A2030                               
SITE     1 DC3  3 GLN A 120  NAG A2029  GLU B 171                               
SITE     1 DC4  8 LYS A 843  ASN A 844  THR A 846  VAL A 847                    
SITE     2 DC4  8 NAG A2032  ASN B 571  TYR B 669  GLU B 671                    
SITE     1 DC5  5 NAG A2031  BMA A2033  ASN B 571  ARG B 636                    
SITE     2 DC5  5 ASP B 637                                                     
SITE     1 DC6  5 NAG A2032  MAN A2034  MAN A2035  SER B 353                    
SITE     2 DC6  5 MET B 387                                                     
SITE     1 DC7  4 BMA A2033  THR B 328  THR B 329  LYS B 354                    
SITE     1 DC8  4 BMA A2033  MAN A2036  SER B 353  ARG B 636                    
SITE     1 DC9  4 MAN A2035  ARG B 636  GLU B 638  SER B 677                    
SITE     1 EC1  2 ASN A 943  NAG A2038                                          
SITE     1 EC2  1 NAG A2037                                                     
SITE     1 EC3  3 HIS A 752  ILE A 869  ASN A 950                               
SITE     1 EC4  5 SER A 516  SER A 520  HIS A 521  SER A 522                    
SITE     2 EC4  5 TRP B 724                                                     
SITE     1 EC5  7 GLY A  49  ASN A  77  PHE A  88  LYS A  89                    
SITE     2 EC5  7 SER A  90  ARG A 122  HOH A2121                               
SITE     1 EC6  3 GLY A 304  SER A 305  GLN A 310                               
SITE     1 EC7  1 LYS A 330                                                     
SITE     1 EC8  2 ARG A  99  SER A 100                                          
SITE     1 EC9  3 GLU A 117  TYR A 200  HIS A 796                               
SITE     1 FC1  6 ASP B 158  ASN B 215  ARG B 216  ASP B 217                    
SITE     2 FC1  6 PRO B 219  GLU B 220                                          
SITE     1 FC2  2 ASN B  99  NAG B2003                                          
SITE     1 FC3  1 NAG B2002                                                     
SITE     1 FC4  6 ARG A 248  ASN B 316  GLN B 319  ASN B 320                    
SITE     2 FC4  6 GLU B 323  NAG B2005                                          
SITE     1 FC5  2 ASN B 316  NAG B2004                                          
SITE     1 FC6  5 ASN B 371  SER B 398  ILE B 399  GLU B 400                    
SITE     2 FC6  5 NAG B2007                                                     
SITE     1 FC7  2 NAG B2006  BMA B2008                                          
SITE     1 FC8  3 NAG B2007  MAN B2009  HOH B2128                               
SITE     1 FC9  1 BMA B2008                                                     
SITE     1 GC1  6 ILE A 654  TYR B 531  TYR B 557  ASN B 559                    
SITE     2 GC1  6 CYS B 583  NAG B2011                                          
SITE     1 GC2  3 PRO A 624  NAG B2010  BMA B2012                               
SITE     1 GC3  2 NAG B2011  HOH B2104                                          
SITE     1 GC4  6 LEU B 645  ASP B 647  GLY B 649  ALA B 652                    
SITE     2 GC4  6 ASN B 654  NAG B2014                                          
SITE     1 GC5  5 ASN A 759  GLU B 644  ASP B 647  NAG B2013                    
SITE     2 GC5  5 BMA B2015                                                     
SITE     1 GC6  3 NAG B2014  MAN B2016  HOH B2132                               
SITE     1 GC7  1 BMA B2015                                                     
SITE     1 GC8  6 SER B  70  ASP B  71  LYS B  72  LYS B 619                    
SITE     2 GC8  6 GLU B 640  SER B 641                                          
SITE     1 GC9  5 ARG A 665  ILE B   4  THR B   7  ARG B   8                    
SITE     2 GC9  5 GLU B 522                                                     
SITE     1 HC1  3 VAL B 359  ARG B 360  ASP B 361                               
SITE     1 HC2  2 MET B 535  HOH B2123                                          
SITE     1 HC3  1 TYR B 556                                                     
CRYST1  128.558  128.558  352.859  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      0.007779  0.004491  0.000000        0.00000                         
SCALE2      0.000000  0.008982  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002834        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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