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Entry: 4MMY
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HEADER    CELL ADHESION                           09-SEP-13   4MMY              
TITLE     INTEGRIN ALPHAVBETA3 ECTODOMAIN BOUND TO THE TENTH DOMAIN OF          
TITLE    2 FIBRONECTIN WITH THE IAKGDWND MOTIF                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-V;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN (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: EXTRACELLULAR DOMAIN (UNP RESIDUES 27-718);                
COMPND  12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: FIBRONECTIN;                                               
COMPND  16 CHAIN: C;                                                            
COMPND  17 FRAGMENT: FIBRONECTIN TYPE-III DOMAIN 10 (UNP RESIDUES 1448-1540);   
COMPND  18 SYNONYM: FN, COLD-INSOLUBLE GLOBULIN, CIG;                           
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MUTATION: 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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: HI5;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: ITGB3, GP3A;                                                   
SOURCE  16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: HI5;                                       
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: FN1, FN;                                                       
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  29 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    INTEGRIN, A DOMAIN, HYBRID DOMAIN, PSI, EGF REPEATS, BETA TA THIGH,   
KEYWDS   2 BETA PROPELLER, RGD MOTIF, FIBRONECTIN, VITRONECTIN, CELL ADHESION   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.VAN AGTHOVEN,J.XIONG,M.A.ARNAOUT                                    
REVDAT   4   15-NOV-17 4MMY    1       REMARK                                   
REVDAT   3   30-APR-14 4MMY    1       JRNL                                     
REVDAT   2   09-APR-14 4MMY    1       JRNL                                     
REVDAT   1   26-MAR-14 4MMY    0                                                
JRNL        AUTH   J.F.VAN AGTHOVEN,J.P.XIONG,J.L.ALONSO,X.RUI,B.D.ADAIR,       
JRNL        AUTH 2 S.L.GOODMAN,M.A.ARNAOUT                                      
JRNL        TITL   STRUCTURAL BASIS FOR PURE ANTAGONISM OF INTEGRIN ALPHA V     
JRNL        TITL 2 BETA 3 BY A HIGH-AFFINITY FORM OF FIBRONECTIN.               
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  21   383 2014              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   24658351                                                     
JRNL        DOI    10.1038/NSMB.2797                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.18 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.18                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.02                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 51144                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2535                            
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 41.0246 -  8.3196    0.97     2895   120  0.1984 0.2336        
REMARK   3     2  8.3196 -  6.6125    1.00     2774   155  0.2242 0.2601        
REMARK   3     3  6.6125 -  5.7792    1.00     2753   147  0.2282 0.2903        
REMARK   3     4  5.7792 -  5.2520    1.00     2742   148  0.2084 0.2319        
REMARK   3     5  5.2520 -  4.8762    1.00     2700   165  0.1808 0.2326        
REMARK   3     6  4.8762 -  4.5891    1.00     2704   149  0.1713 0.2200        
REMARK   3     7  4.5891 -  4.3596    1.00     2701   149  0.1799 0.2033        
REMARK   3     8  4.3596 -  4.1700    1.00     2711   130  0.1927 0.2236        
REMARK   3     9  4.1700 -  4.0096    1.00     2707   137  0.2021 0.2270        
REMARK   3    10  4.0096 -  3.8713    1.00     2682   141  0.2160 0.2802        
REMARK   3    11  3.8713 -  3.7504    1.00     2695   115  0.2241 0.2529        
REMARK   3    12  3.7504 -  3.6432    1.00     2684   133  0.2199 0.2581        
REMARK   3    13  3.6432 -  3.5474    1.00     2660   133  0.2346 0.2928        
REMARK   3    14  3.5474 -  3.4609    1.00     2696   154  0.2460 0.3198        
REMARK   3    15  3.4609 -  3.3822    1.00     2678   123  0.2614 0.3027        
REMARK   3    16  3.3822 -  3.3103    1.00     2649   133  0.2703 0.2941        
REMARK   3    17  3.3103 -  3.2441    1.00     2651   148  0.2819 0.3479        
REMARK   3    18  3.2441 -  3.1829    0.95     2527   155  0.3069 0.3341        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.090           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007          13359                                  
REMARK   3   ANGLE     :  0.996          18031                                  
REMARK   3   CHIRALITY :  0.039           2064                                  
REMARK   3   PLANARITY :  0.005           2332                                  
REMARK   3   DIHEDRAL  : 13.730           4942                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 421 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   3.4461  54.0378  21.0785              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8556 T22:   0.4284                                     
REMARK   3      T33:   0.6111 T12:  -0.2561                                     
REMARK   3      T13:  -0.0618 T23:   0.0553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1006 L22:   2.1819                                     
REMARK   3      L33:   2.0999 L12:   0.7562                                     
REMARK   3      L13:   0.8758 L23:  -0.6107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4137 S12:   0.3676 S13:   0.3743                       
REMARK   3      S21:  -0.4862 S22:   0.3263 S23:   0.2311                       
REMARK   3      S31:  -0.2305 S32:   0.0354 S33:   0.0694                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 422 THROUGH 633 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.4919  47.0121  -0.5515              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2144 T22:   0.8907                                     
REMARK   3      T33:   1.0916 T12:  -0.2904                                     
REMARK   3      T13:  -0.3816 T23:   0.2270                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0147 L22:   0.3841                                     
REMARK   3      L33:   0.3307 L12:   0.1507                                     
REMARK   3      L13:   0.8565 L23:  -0.0572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4184 S12:   1.2202 S13:   0.7077                       
REMARK   3      S21:  -0.4571 S22:   0.3235 S23:   0.3711                       
REMARK   3      S31:  -0.2641 S32:   0.0738 S33:   0.0928                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 634 THROUGH 737 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -50.1378  43.0450  22.8554              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0342 T22:   0.9815                                     
REMARK   3      T33:   0.9535 T12:  -0.1020                                     
REMARK   3      T13:  -0.1911 T23:   0.2071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8081 L22:   2.9092                                     
REMARK   3      L33:   2.1086 L12:  -1.4457                                     
REMARK   3      L13:   1.8088 L23:   0.4630                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4217 S12:   0.1941 S13:  -0.0316                       
REMARK   3      S21:  -0.1480 S22:   0.3559 S23:   0.6634                       
REMARK   3      S31:  -0.1369 S32:   1.0327 S33:   0.1278                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 738 THROUGH 956 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.4010  36.2757  73.2419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9144 T22:   0.5255                                     
REMARK   3      T33:   0.7861 T12:   0.2798                                     
REMARK   3      T13:   0.0084 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0923 L22:   3.7039                                     
REMARK   3      L33:   6.1554 L12:  -0.5549                                     
REMARK   3      L13:   1.3561 L23:  -0.6591                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2209 S12:  -0.5872 S13:  -0.2364                       
REMARK   3      S21:   0.6500 S22:   0.0797 S23:  -0.1693                       
REMARK   3      S31:   0.1068 S32:   0.1869 S33:   0.1319                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 59 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -41.0860   4.4011   7.4339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6242 T22:   1.2968                                     
REMARK   3      T33:   1.4471 T12:  -0.1405                                     
REMARK   3      T13:  -0.4571 T23:   0.1298                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7703 L22:   6.7475                                     
REMARK   3      L33:   5.0062 L12:   7.5125                                     
REMARK   3      L13:   6.5614 L23:   5.8039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0883 S12:   0.3319 S13:  -0.6041                       
REMARK   3      S21:  -1.2881 S22:  -0.0319 S23:   0.5210                       
REMARK   3      S31:   0.1529 S32:  -1.3848 S33:   0.1176                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 60 THROUGH 169 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4249  13.0033  34.4407              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1617 T22:   0.5429                                     
REMARK   3      T33:   1.0336 T12:  -0.0817                                     
REMARK   3      T13:  -0.0436 T23:   0.1608                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3677 L22:   5.5251                                     
REMARK   3      L33:   0.9965 L12:   2.9972                                     
REMARK   3      L13:  -0.2154 L23:  -0.4963                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4520 S12:  -0.5558 S13:  -1.5020                       
REMARK   3      S21:   0.6903 S22:  -0.4534 S23:  -1.3764                       
REMARK   3      S31:   0.6007 S32:   0.0194 S33:  -0.0229                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 170 THROUGH 291 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7740  27.5064  31.4178              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6986 T22:   0.5756                                     
REMARK   3      T33:   1.2418 T12:  -0.0749                                     
REMARK   3      T13:  -0.0180 T23:   0.1148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2078 L22:   8.7177                                     
REMARK   3      L33:   5.1829 L12:   1.0351                                     
REMARK   3      L13:  -0.7365 L23:  -2.1201                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1368 S12:  -0.2111 S13:  -1.2283                       
REMARK   3      S21:  -0.0750 S22:   0.0047 S23:  -1.1922                       
REMARK   3      S31:   0.5740 S32:   0.6383 S33:  -0.1416                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 292 THROUGH 342 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.5267  25.4391  40.9380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0984 T22:   0.7285                                     
REMARK   3      T33:   1.0282 T12:  -0.2034                                     
REMARK   3      T13:  -0.1231 T23:   0.3713                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0102 L22:   4.5466                                     
REMARK   3      L33:   4.5983 L12:   3.2035                                     
REMARK   3      L13:  -0.5580 L23:   1.7224                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0063 S12:  -1.4254 S13:  -1.3363                       
REMARK   3      S21:   0.9355 S22:   0.0514 S23:  -0.1604                       
REMARK   3      S31:   1.5170 S32:  -1.0085 S33:  -1.0437                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 343 THROUGH 423 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7125  12.3477  31.6404              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3095 T22:   0.4542                                     
REMARK   3      T33:   0.9112 T12:  -0.0876                                     
REMARK   3      T13:  -0.0121 T23:   0.0922                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4282 L22:   4.1863                                     
REMARK   3      L33:   3.0913 L12:   2.4244                                     
REMARK   3      L13:   2.0979 L23:   2.0976                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5339 S12:   0.1383 S13:   0.1251                       
REMARK   3      S21:  -0.3079 S22:   0.0762 S23:  -0.3560                       
REMARK   3      S31:  -1.1057 S32:   0.0974 S33:   0.4643                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 424 THROUGH 462 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.0764   7.9994  -2.2448              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0399 T22:   1.5723                                     
REMARK   3      T33:   1.4870 T12:  -0.3400                                     
REMARK   3      T13:  -0.3721 T23:  -0.1613                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6833 L22:   1.4943                                     
REMARK   3      L33:   3.2985 L12:   0.9235                                     
REMARK   3      L13:  -0.0134 L23:   2.0820                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3582 S12:   1.8108 S13:  -0.1143                       
REMARK   3      S21:  -1.1775 S22:  -0.7827 S23:   0.7315                       
REMARK   3      S31:   1.5333 S32:  -1.1896 S33:   0.4356                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 463 THROUGH 502 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -52.3490  20.3744  -2.4562              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9505 T22:   1.5018                                     
REMARK   3      T33:   2.1137 T12:  -0.1292                                     
REMARK   3      T13:  -0.7949 T23:   0.1574                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7700 L22:   3.3176                                     
REMARK   3      L33:   1.9638 L12:  -2.4305                                     
REMARK   3      L13:  -1.8526 L23:   2.5539                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1153 S12:   1.2887 S13:   0.0806                       
REMARK   3      S21:  -0.7514 S22:  -0.7162 S23:   0.4595                       
REMARK   3      S31:  -1.2477 S32:  -0.8099 S33:   0.8490                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 503 THROUGH 549 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.7892  27.4267  12.6184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5104 T22:   1.2192                                     
REMARK   3      T33:   1.5142 T12:  -0.1578                                     
REMARK   3      T13:  -0.4571 T23:   0.1576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8785 L22:   6.2424                                     
REMARK   3      L33:   2.0157 L12:   5.9002                                     
REMARK   3      L13:   8.4614 L23:   3.9868                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1871 S12:   0.9943 S13:   1.9490                       
REMARK   3      S21:  -1.4792 S22:  -0.1668 S23:   0.9876                       
REMARK   3      S31:  -1.3670 S32:   0.0431 S33:   1.3881                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 550 THROUGH 630 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0985  20.8275  49.0150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7680 T22:   0.7624                                     
REMARK   3      T33:   1.0796 T12:   0.0584                                     
REMARK   3      T13:   0.0884 T23:  -0.0376                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3918 L22:   4.6654                                     
REMARK   3      L33:   4.7499 L12:  -1.3394                                     
REMARK   3      L13:   1.3127 L23:  -4.5916                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1289 S12:  -0.0118 S13:  -0.1924                       
REMARK   3      S21:  -0.0571 S22:   0.1867 S23:  -0.2727                       
REMARK   3      S31:   0.4116 S32:  -0.1288 S33:  -0.0563                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 631 THROUGH 690 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.9635  15.3585  68.8222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2685 T22:   0.6311                                     
REMARK   3      T33:   1.4314 T12:   0.3112                                     
REMARK   3      T13:  -0.1556 T23:   0.0874                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3554 L22:   2.1196                                     
REMARK   3      L33:   8.9222 L12:   1.7477                                     
REMARK   3      L13:  -1.0502 L23:   3.1036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2945 S12:   0.0567 S13:   0.8464                       
REMARK   3      S21:   0.3458 S22:   0.0444 S23:  -0.5591                       
REMARK   3      S31:  -0.8531 S32:   0.5260 S33:   0.2575                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1492 THROUGH 1497 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3706  42.2829  44.1906              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5850 T22:   0.9243                                     
REMARK   3      T33:   1.2104 T12:  -0.2546                                     
REMARK   3      T13:  -0.1467 T23:   0.3680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9686 L22:   2.0000                                     
REMARK   3      L33:   3.9348 L12:   1.9989                                     
REMARK   3      L13:   5.9633 L23:  -5.1421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3923 S12:  -1.7517 S13:  -0.9299                       
REMARK   3      S21:   2.7280 S22:   1.0869 S23:   0.4328                       
REMARK   3      S31:   0.2911 S32:   0.1667 S33:  -0.6747                       
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 4MMY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082112.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97921                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51260                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.180                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 14.300                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.18                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.89400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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   (%): 68.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG3350, 0.8 M SODIUM CHLORIDE,      
REMARK 280  0.1 M SODIUM ACETATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 277.15K                                                 
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      205.46867            
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      102.73433            
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      102.73433            
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      205.46867            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15920 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 75180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 52.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     LEU A   838                                                      
REMARK 465     GLN A   839                                                      
REMARK 465     THR A   840                                                      
REMARK 465     THR A   841                                                      
REMARK 465     GLU A   842                                                      
REMARK 465     LYS A   843                                                      
REMARK 465     ASN A   844                                                      
REMARK 465     ASP A   845                                                      
REMARK 465     THR A   846                                                      
REMARK 465     VAL A   847                                                      
REMARK 465     ALA A   848                                                      
REMARK 465     GLY A   849                                                      
REMARK 465     GLN A   850                                                      
REMARK 465     GLY A   851                                                      
REMARK 465     GLU A   852                                                      
REMARK 465     ARG A   853                                                      
REMARK 465     ASP A   854                                                      
REMARK 465     HIS A   855                                                      
REMARK 465     LEU A   856                                                      
REMARK 465     ILE A   857                                                      
REMARK 465     THR A   858                                                      
REMARK 465     LYS A   859                                                      
REMARK 465     ARG A   860                                                      
REMARK 465     ASP A   861                                                      
REMARK 465     LEU A   862                                                      
REMARK 465     ALA A   863                                                      
REMARK 465     LEU A   864                                                      
REMARK 465     SER A   865                                                      
REMARK 465     GLU A   866                                                      
REMARK 465     GLY A   867                                                      
REMARK 465     PRO A   957                                                      
REMARK 465     ALA A   958                                                      
REMARK 465     PRO A   959                                                      
REMARK 465     PRO B   691                                                      
REMARK 465     ASP B   692                                                      
REMARK 465     SER C  1417                                                      
REMARK 465     ASP C  1418                                                      
REMARK 465     VAL C  1419                                                      
REMARK 465     PRO C  1420                                                      
REMARK 465     ARG C  1421                                                      
REMARK 465     ASP C  1422                                                      
REMARK 465     LEU C  1423                                                      
REMARK 465     GLU C  1424                                                      
REMARK 465     VAL C  1425                                                      
REMARK 465     VAL C  1426                                                      
REMARK 465     ALA C  1427                                                      
REMARK 465     ALA C  1428                                                      
REMARK 465     THR C  1429                                                      
REMARK 465     PRO C  1430                                                      
REMARK 465     THR C  1431                                                      
REMARK 465     SER C  1432                                                      
REMARK 465     LEU C  1433                                                      
REMARK 465     LEU C  1434                                                      
REMARK 465     ILE C  1435                                                      
REMARK 465     SER C  1436                                                      
REMARK 465     TRP C  1437                                                      
REMARK 465     ASP C  1438                                                      
REMARK 465     ALA C  1439                                                      
REMARK 465     PRO C  1440                                                      
REMARK 465     ALA C  1441                                                      
REMARK 465     VAL C  1442                                                      
REMARK 465     THR C  1443                                                      
REMARK 465     VAL C  1444                                                      
REMARK 465     ARG C  1445                                                      
REMARK 465     TYR C  1446                                                      
REMARK 465     TYR C  1447                                                      
REMARK 465     ARG C  1448                                                      
REMARK 465     ILE C  1449                                                      
REMARK 465     THR C  1450                                                      
REMARK 465     TYR C  1451                                                      
REMARK 465     GLY C  1452                                                      
REMARK 465     GLU C  1453                                                      
REMARK 465     THR C  1454                                                      
REMARK 465     GLY C  1455                                                      
REMARK 465     GLY C  1456                                                      
REMARK 465     ASN C  1457                                                      
REMARK 465     SER C  1458                                                      
REMARK 465     PRO C  1459                                                      
REMARK 465     VAL C  1460                                                      
REMARK 465     GLN C  1461                                                      
REMARK 465     GLU C  1462                                                      
REMARK 465     PHE C  1463                                                      
REMARK 465     THR C  1464                                                      
REMARK 465     VAL C  1465                                                      
REMARK 465     PRO C  1466                                                      
REMARK 465     GLY C  1467                                                      
REMARK 465     SER C  1468                                                      
REMARK 465     LYS C  1469                                                      
REMARK 465     SER C  1470                                                      
REMARK 465     THR C  1471                                                      
REMARK 465     ALA C  1472                                                      
REMARK 465     THR C  1473                                                      
REMARK 465     ILE C  1474                                                      
REMARK 465     SER C  1475                                                      
REMARK 465     GLY C  1476                                                      
REMARK 465     LEU C  1477                                                      
REMARK 465     LYS C  1478                                                      
REMARK 465     PRO C  1479                                                      
REMARK 465     GLY C  1480                                                      
REMARK 465     VAL C  1481                                                      
REMARK 465     ASP C  1482                                                      
REMARK 465     TYR C  1483                                                      
REMARK 465     THR C  1484                                                      
REMARK 465     ILE C  1485                                                      
REMARK 465     THR C  1486                                                      
REMARK 465     VAL C  1487                                                      
REMARK 465     TYR C  1488                                                      
REMARK 465     ALA C  1489                                                      
REMARK 465     ASP C  1498                                                      
REMARK 465     GLY C  1499                                                      
REMARK 465     SER C  1500                                                      
REMARK 465     LYS C  1501                                                      
REMARK 465     PRO C  1502                                                      
REMARK 465     ILE C  1503                                                      
REMARK 465     SER C  1504                                                      
REMARK 465     ILE C  1505                                                      
REMARK 465     ASN C  1506                                                      
REMARK 465     TYR C  1507                                                      
REMARK 465     ARG C  1508                                                      
REMARK 465     THR C  1509                                                      
REMARK 465     GLY C  1510                                                      
REMARK 465     LYS C  1511                                                      
REMARK 465     LYS C  1512                                                      
REMARK 465     GLY C  1513                                                      
REMARK 465     LYS C  1514                                                      
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    THR A  64       -7.90     65.09                                   
REMARK 500    ASP A  73      -65.95   -123.50                                   
REMARK 500    ALA A  74       -3.20     67.29                                   
REMARK 500    LYS A  82      -72.07    -48.86                                   
REMARK 500    ASP A  84       80.08   -153.29                                   
REMARK 500    GLN A 102     -118.16     55.00                                   
REMARK 500    TRP A 114      -74.93   -120.53                                   
REMARK 500    ARG A 115       -7.67     90.17                                   
REMARK 500    THR A 116     -149.13     54.40                                   
REMARK 500    MET A 118      -74.67   -108.60                                   
REMARK 500    PRO A 124       74.31    -68.78                                   
REMARK 500    THR A 134      -67.71   -139.50                                   
REMARK 500    ASP A 148     -144.56     56.86                                   
REMARK 500    ASP A 234     -178.80    -67.54                                   
REMARK 500    THR A 249       -3.24     74.77                                   
REMARK 500    LEU A 264      -67.28   -122.17                                   
REMARK 500    ALA A 273       -3.25     67.11                                   
REMARK 500    ASP A 289       -4.08     70.74                                   
REMARK 500    VAL A 312      -57.92   -127.05                                   
REMARK 500    PHE A 334      -65.95   -122.79                                   
REMARK 500    ARG A 339       70.25     56.25                                   
REMARK 500    ARG A 398      -74.99   -113.51                                   
REMARK 500    TYR A 406      -18.30     73.87                                   
REMARK 500    THR A 466       70.60     59.67                                   
REMARK 500    LEU A 487      145.52   -176.63                                   
REMARK 500    LEU A 532       74.17     57.81                                   
REMARK 500    LEU A 552      -62.26    -91.91                                   
REMARK 500    LEU A 563       72.83     62.00                                   
REMARK 500    ALA A 568      -61.06   -127.59                                   
REMARK 500    ASP A 570       -3.73     63.37                                   
REMARK 500    THR A 572     -111.66     45.67                                   
REMARK 500    THR A 582      134.87   -177.62                                   
REMARK 500    ASP A 613     -116.07     55.82                                   
REMARK 500    LEU A 649     -115.77     55.04                                   
REMARK 500    HIS A 702      -77.33   -102.22                                   
REMARK 500    GLN A 703      161.61    176.97                                   
REMARK 500    SER A 705     -129.78     48.51                                   
REMARK 500    THR A 709     -118.76     52.99                                   
REMARK 500    VAL A 772      -65.06   -102.68                                   
REMARK 500    ASN A 785      -60.07   -103.21                                   
REMARK 500    ASN A 805       -3.94     66.36                                   
REMARK 500    LEU A 808      -73.73   -102.44                                   
REMARK 500    ARG A 832     -147.92     52.65                                   
REMARK 500    ILE A 833      167.80    171.71                                   
REMARK 500    LYS A 834      -76.28   -122.86                                   
REMARK 500    ARG A 888       70.89     44.01                                   
REMARK 500    MET A 909     -132.85     64.75                                   
REMARK 500    ASN A 910     -140.34     51.95                                   
REMARK 500    GLU A 912        2.68    -63.91                                   
REMARK 500    ASN A 913       -3.44     91.31                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     122 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                              MN B 709  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 251   OD1                                                    
REMARK 620 2 ASP B 127   OD1 115.3                                              
REMARK 620 3 ASP B 126   OD2 147.5  96.6                                        
REMARK 620 4 ASP B 126   OD1 132.7  72.3  61.0                                  
REMARK 620 5 SER B 123   O    68.7  93.3 117.6  64.2                            
REMARK 620 6 ASP B 251   OD2  62.0  64.9 134.5 135.3 105.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1028  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 290   O                                                      
REMARK 620 2 ASP A 284   OD2  75.6                                              
REMARK 620 3 ASP A 292   OD2  96.7 144.4                                        
REMARK 620 4 ASP A 288   OD1  90.4  64.8 150.8                                  
REMARK 620 5 ASP A 292   OD1 100.5  86.3  60.6 145.6                            
REMARK 620 6 ASN A 286   OD1 148.5  74.4 113.4  68.2  87.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1030  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 419   O                                                      
REMARK 620 2 ASP A 413   OD1  69.3                                              
REMARK 620 3 ASP A 421   OD2  90.2  82.7                                        
REMARK 620 4 ASP A 421   OD1 121.1 140.2  60.4                                  
REMARK 620 5 ASN A 417   OD1  82.1  70.6 153.2 144.2                            
REMARK 620 6 ASP A 415   OD1 132.0  63.6  75.7  91.5  90.5                      
REMARK 620 7 ASP A 415   OD2 155.5 107.9 113.9  77.4  74.3  55.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1027  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 230   OD2                                                    
REMARK 620 2 ASP A 238   OD1 145.5                                              
REMARK 620 3 ASP A 234   OD1  65.2 149.0                                        
REMARK 620 4 ASP A 238   OD2  89.6  60.7 137.6                                  
REMARK 620 5 ASN A 232   OD1  68.4 112.4  68.4  70.8                            
REMARK 620 6 ILE A 236   O    77.9  97.3  94.7 113.5 146.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 710  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   OD1                                                    
REMARK 620 2 GLU B 220   OE2 146.7                                              
REMARK 620 3 ASP B 217   O    72.8  84.4                                        
REMARK 620 4 ASP B 158   OD2  95.4 107.9 167.7                                  
REMARK 620 5 ASN B 215   OD1  82.2  70.3  81.1 101.2                            
REMARK 620 6 PRO B 219   O   102.8 103.9  97.2  81.7 174.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 708  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 220   OE1                                                    
REMARK 620 2 SER B 123   OG  145.0                                              
REMARK 620 3 SER B 121   OG  106.8  97.9                                        
REMARK 620 4 HOH B 802   O    89.7  64.6  92.1                                  
REMARK 620 5 HOH B 801   O    76.2  74.7 167.7  75.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1031  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 636   OE2                                                    
REMARK 620 2 ASP A 599   OD1 151.4                                              
REMARK 620 3 ASP A 599   OD2 128.7  61.2                                        
REMARK 620 4 GLU A 636   OE1  61.2 129.5 145.0                                  
REMARK 620 5 CYS A 596   O   100.3  66.8 127.6  70.4                            
REMARK 620 6 VAL A 601   O    80.9  71.2  93.9 120.9  74.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1029  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 353   OD2                                                    
REMARK 620 2 ASP A 353   OD1  61.0                                              
REMARK 620 3 ASP A 357   OD1 100.2 136.4                                        
REMARK 620 4 ASP A 351   OD2  79.0  94.4 121.9                                  
REMARK 620 5 ASP A 357   OD2 133.8 160.0  60.8  78.3                            
REMARK 620 6 ASP A 349   OD1 137.3  77.3 117.1  96.7  85.1                      
REMARK 620 7 PHE A 355   O    99.7  64.7  82.5 155.5 116.9  67.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1027                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1028                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1029                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1030                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1031                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 708                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 709                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 710                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  44 RESIDUES 1001 TO 1004                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  260 RESIDUES 1005 TO 1006                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  266 RESIDUES 1007 TO 1012                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  458 RESIDUES 1013 TO 1016                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1017 BOUND   
REMARK 800  TO ASN A 524                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  585 RESIDUES 1018 TO 1019                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1020 BOUND   
REMARK 800  TO ASN A 674                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1021 BOUND   
REMARK 800  TO ASN A 821                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  943 RESIDUES 1022 TO 1023                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  950 RESIDUES 1024 TO 1026                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 701 BOUND   
REMARK 800  TO ASN B 99                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 702 BOUND   
REMARK 800  TO ASN B 320                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B   
REMARK 800  371 RESIDUES 703 TO 704                                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B   
REMARK 800  559 RESIDUES 705 TO 707                                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JV2   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHA-V COMPLEXED WITH A HIGH AFFINITY VARIANT OF FN10      
REMARK 900 RELATED ID: 1L5G   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHA-V COMPLEXED WITH A HIGH AFFINITY VARIANT OF FN10      
REMARK 900 RELATED ID: 3IJE   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHA-V COMPLEXED WITH A HIGH AFFINITY VARIANT OF FN10      
REMARK 900 RELATED ID: 4G1M   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHA-V COMPLEXED WITH A HIGH AFFINITY VARIANT OF FN10      
REMARK 900 RELATED ID: 4G1E   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHA-V COMPLEXED WITH A HIGH AFFINITY VARIANT OF FN10      
REMARK 900 RELATED ID: 4MMX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4MMZ   RELATED DB: PDB                                   
DBREF  4MMY A    1   959  UNP    P06756   ITAV_HUMAN      31    989             
DBREF  4MMY B    1   692  UNP    P05106   ITB3_HUMAN      27    718             
DBREF  4MMY C 1417  1509  UNP    P02751   FINC_HUMAN    1448   1540             
SEQADV 4MMY ILE C 1491  UNP  P02751    THR  1522 ENGINEERED MUTATION            
SEQADV 4MMY ALA C 1492  UNP  P02751    GLY  1523 ENGINEERED MUTATION            
SEQADV 4MMY TRP C 1496  UNP  P02751    SER  1527 ENGINEERED MUTATION            
SEQADV 4MMY ASN C 1497  UNP  P02751    PRO  1528 ENGINEERED MUTATION            
SEQADV 4MMY ASP C 1498  UNP  P02751    ALA  1529 ENGINEERED MUTATION            
SEQADV 4MMY GLY C 1499  UNP  P02751    SER  1530 ENGINEERED MUTATION            
SEQADV 4MMY GLY C 1510  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMY LYS C 1511  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMY LYS C 1512  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMY GLY C 1513  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMY LYS C 1514  UNP  P02751              EXPRESSION TAG                 
SEQRES   1 A  959  PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY          
SEQRES   2 A  959  PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE          
SEQRES   3 A  959  VAL PRO SER ALA SER SER ARG MET PHE LEU LEU VAL GLY          
SEQRES   4 A  959  ALA PRO LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU          
SEQRES   5 A  959  GLY GLY GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG          
SEQRES   6 A  959  ARG CYS GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG          
SEQRES   7 A  959  ASP TYR ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS          
SEQRES   8 A  959  GLN TRP PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS          
SEQRES   9 A  959  ILE LEU ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU          
SEQRES  10 A  959  MET LYS GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU          
SEQRES  11 A  959  GLN ASP GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG          
SEQRES  12 A  959  SER GLN ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN          
SEQRES  13 A  959  GLY GLY PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL          
SEQRES  14 A  959  LEU LEU GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN          
SEQRES  15 A  959  LEU ILE SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR          
SEQRES  16 A  959  ASP PRO ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU          
SEQRES  17 A  959  ALA THR ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR          
SEQRES  18 A  959  LEU GLY TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP          
SEQRES  19 A  959  GLY ILE ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA          
SEQRES  20 A  959  ARG THR LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN          
SEQRES  21 A  959  MET SER SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA          
SEQRES  22 A  959  ALA TYR PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN          
SEQRES  23 A  959  GLY ASP ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU          
SEQRES  24 A  959  PHE MET ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL          
SEQRES  25 A  959  GLY GLN VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP          
SEQRES  26 A  959  PHE GLN THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA          
SEQRES  27 A  959  ARG PHE GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP          
SEQRES  28 A  959  GLN ASP GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR          
SEQRES  29 A  959  GLY GLY GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN          
SEQRES  30 A  959  GLY ARG SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE          
SEQRES  31 A  959  LEU GLU GLY GLN TRP ALA ALA ARG SER MET PRO PRO SER          
SEQRES  32 A  959  PHE GLY TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS          
SEQRES  33 A  959  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL          
SEQRES  34 A  959  ASP ARG ALA ILE LEU TYR ARG ALA ARG PRO VAL ILE THR          
SEQRES  35 A  959  VAL ASN ALA GLY LEU GLU VAL TYR PRO SER ILE LEU ASN          
SEQRES  36 A  959  GLN ASP ASN LYS THR CYS SER LEU PRO GLY THR ALA LEU          
SEQRES  37 A  959  LYS VAL SER CYS PHE ASN VAL ARG PHE CYS LEU LYS ALA          
SEQRES  38 A  959  ASP GLY LYS GLY VAL LEU PRO ARG LYS LEU ASN PHE GLN          
SEQRES  39 A  959  VAL GLU LEU LEU LEU ASP LYS LEU LYS GLN LYS GLY ALA          
SEQRES  40 A  959  ILE ARG ARG ALA LEU PHE LEU TYR SER ARG SER PRO SER          
SEQRES  41 A  959  HIS SER LYS ASN MET THR ILE SER ARG GLY GLY LEU MET          
SEQRES  42 A  959  GLN CYS GLU GLU LEU ILE ALA TYR LEU ARG ASP GLU SER          
SEQRES  43 A  959  GLU PHE ARG ASP LYS LEU THR PRO ILE THR ILE PHE MET          
SEQRES  44 A  959  GLU TYR ARG LEU ASP TYR ARG THR ALA ALA ASP THR THR          
SEQRES  45 A  959  GLY LEU GLN PRO ILE LEU ASN GLN PHE THR PRO ALA ASN          
SEQRES  46 A  959  ILE SER ARG GLN ALA HIS ILE LEU LEU ASP CYS GLY GLU          
SEQRES  47 A  959  ASP ASN VAL CYS LYS PRO LYS LEU GLU VAL SER VAL ASP          
SEQRES  48 A  959  SER ASP GLN LYS LYS ILE TYR ILE GLY ASP ASP ASN PRO          
SEQRES  49 A  959  LEU THR LEU ILE VAL LYS ALA GLN ASN GLN GLY GLU GLY          
SEQRES  50 A  959  ALA TYR GLU ALA GLU LEU ILE VAL SER ILE PRO LEU GLN          
SEQRES  51 A  959  ALA ASP PHE ILE GLY VAL VAL ARG ASN ASN GLU ALA LEU          
SEQRES  52 A  959  ALA ARG LEU SER CYS ALA PHE LYS THR GLU ASN GLN THR          
SEQRES  53 A  959  ARG GLN VAL VAL CYS ASP LEU GLY ASN PRO MET LYS ALA          
SEQRES  54 A  959  GLY THR GLN LEU LEU ALA GLY LEU ARG PHE SER VAL HIS          
SEQRES  55 A  959  GLN GLN SER GLU MET ASP THR SER VAL LYS PHE ASP LEU          
SEQRES  56 A  959  GLN ILE GLN SER SER ASN LEU PHE ASP LYS VAL SER PRO          
SEQRES  57 A  959  VAL VAL SER HIS LYS VAL ASP LEU ALA VAL LEU ALA ALA          
SEQRES  58 A  959  VAL GLU ILE ARG GLY VAL SER SER PRO ASP HIS VAL PHE          
SEQRES  59 A  959  LEU PRO ILE PRO ASN TRP GLU HIS LYS GLU ASN PRO GLU          
SEQRES  60 A  959  THR GLU GLU ASP VAL GLY PRO VAL VAL GLN HIS ILE TYR          
SEQRES  61 A  959  GLU LEU ARG ASN ASN GLY PRO SER SER PHE SER LYS ALA          
SEQRES  62 A  959  MET LEU HIS LEU GLN TRP PRO TYR LYS TYR ASN ASN ASN          
SEQRES  63 A  959  THR LEU LEU TYR ILE LEU HIS TYR ASP ILE ASP GLY PRO          
SEQRES  64 A  959  MET ASN CYS THR SER ASP MET GLU ILE ASN PRO LEU ARG          
SEQRES  65 A  959  ILE LYS ILE SER SER LEU GLN THR THR GLU LYS ASN ASP          
SEQRES  66 A  959  THR VAL ALA GLY GLN GLY GLU ARG ASP HIS LEU ILE THR          
SEQRES  67 A  959  LYS ARG ASP LEU ALA LEU SER GLU GLY ASP ILE HIS THR          
SEQRES  68 A  959  LEU GLY CYS GLY VAL ALA GLN CYS LEU LYS ILE VAL CYS          
SEQRES  69 A  959  GLN VAL GLY ARG LEU ASP ARG GLY LYS SER ALA ILE LEU          
SEQRES  70 A  959  TYR VAL LYS SER LEU LEU TRP THR GLU THR PHE MET ASN          
SEQRES  71 A  959  LYS GLU ASN GLN ASN HIS SER TYR SER LEU LYS SER SER          
SEQRES  72 A  959  ALA SER PHE ASN VAL ILE GLU PHE PRO TYR LYS ASN LEU          
SEQRES  73 A  959  PRO ILE GLU ASP ILE THR ASN SER THR LEU VAL THR THR          
SEQRES  74 A  959  ASN VAL THR TRP GLY ILE GLN PRO ALA PRO                      
SEQRES   1 B  692  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  692  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  692  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  692  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  692  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  692  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  692  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  692  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  692  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  692  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  692  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  692  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  692  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  692  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  692  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  692  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  692  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  692  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  692  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  692  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  692  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  692  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  692  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  692  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  692  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  692  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  692  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  692  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  692  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  692  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  692  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  692  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  692  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  692  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  692  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  692  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  692  SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG PRO SER          
SEQRES  38 B  692  GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN PRO VAL          
SEQRES  39 B  692  CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL          
SEQRES  40 B  692  CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY LYS TYR          
SEQRES  41 B  692  CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR LYS GLY          
SEQRES  42 B  692  GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS GLY ASP          
SEQRES  43 B  692  CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR CYS ASN          
SEQRES  44 B  692  CYS THR THR ARG THR ASP THR CYS MET SER SER ASN GLY          
SEQRES  45 B  692  LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS GLY SER          
SEQRES  46 B  692  CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP THR CYS          
SEQRES  47 B  692  GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR PHE LYS          
SEQRES  48 B  692  LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG GLY ALA          
SEQRES  49 B  692  LEU HIS ASP GLU ASN THR CYS ASN ARG TYR CYS ARG ASP          
SEQRES  50 B  692  GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR GLY LYS          
SEQRES  51 B  692  ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP ASP CYS          
SEQRES  52 B  692  VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER GLY LYS          
SEQRES  53 B  692  SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS PRO LYS          
SEQRES  54 B  692  GLY PRO ASP                                                  
SEQRES   1 C   98  SER ASP VAL PRO ARG ASP LEU GLU VAL VAL ALA ALA THR          
SEQRES   2 C   98  PRO THR SER LEU LEU ILE SER TRP ASP ALA PRO ALA VAL          
SEQRES   3 C   98  THR VAL ARG TYR TYR ARG ILE THR TYR GLY GLU THR GLY          
SEQRES   4 C   98  GLY ASN SER PRO VAL GLN GLU PHE THR VAL PRO GLY SER          
SEQRES   5 C   98  LYS SER THR ALA THR ILE SER GLY LEU LYS PRO GLY VAL          
SEQRES   6 C   98  ASP TYR THR ILE THR VAL TYR ALA VAL ILE ALA ARG GLY          
SEQRES   7 C   98  ASP TRP ASN ASP GLY SER LYS PRO ILE SER ILE ASN TYR          
SEQRES   8 C   98  ARG THR GLY LYS LYS GLY LYS                                  
MODRES 4MMY ASN A  821  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN A  524  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN A  458  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN B  559  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN A   44  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN A  585  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN A  266  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN A  950  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN A  943  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN A  674  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMY ASN A  260  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1001      14                                                       
HET    NAG  A1002      14                                                       
HET    BMA  A1003      11                                                       
HET    MAN  A1004      11                                                       
HET    NAG  A1005      14                                                       
HET    NAG  A1006      14                                                       
HET    NAG  A1007      14                                                       
HET    NAG  A1008      14                                                       
HET    BMA  A1009      11                                                       
HET    MAN  A1010      11                                                       
HET    BMA  A1011      11                                                       
HET    MAN  A1012      11                                                       
HET    NAG  A1013      14                                                       
HET    NAG  A1014      14                                                       
HET    BMA  A1015      11                                                       
HET    MAN  A1016      11                                                       
HET    NAG  A1017      14                                                       
HET    NAG  A1018      14                                                       
HET    NAG  A1019      14                                                       
HET    NAG  A1020      14                                                       
HET    NAG  A1021      14                                                       
HET    NAG  A1022      14                                                       
HET    NAG  A1023      14                                                       
HET    NAG  A1024      14                                                       
HET    NAG  A1025      14                                                       
HET    BMA  A1026      11                                                       
HET     MN  A1027       1                                                       
HET     MN  A1028       1                                                       
HET     MN  A1029       1                                                       
HET     MN  A1030       1                                                       
HET     MN  A1031       1                                                       
HET    NAG  B 701      14                                                       
HET    NAG  B 702      14                                                       
HET    NAG  B 703      14                                                       
HET    NAG  B 704      14                                                       
HET    NAG  B 705      14                                                       
HET    NAG  B 706      14                                                       
HET    BMA  B 707      11                                                       
HET     MN  B 708       1                                                       
HET     MN  B 709       1                                                       
HET     MN  B 710       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   4  NAG    23(C8 H15 N O6)                                              
FORMUL   4  BMA    6(C6 H12 O6)                                                 
FORMUL   4  MAN    4(C6 H12 O6)                                                 
FORMUL  14   MN    8(MN 2+)                                                     
FORMUL  26  HOH   *5(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 GLY A  366  LYS A  370  5                                   5    
HELIX    5   5 THR A  768  VAL A  772  5                                   5    
HELIX    6   6 ASN B    3  GLY B    9  1                                   7    
HELIX    7   7 SER B   12  ALA B   18  1                                   7    
HELIX    8   8 LEU B   40  LYS B   46  5                                   7    
HELIX    9   9 SER B  121  LYS B  125  5                                   5    
HELIX   10  10 ASP B  127  GLN B  132  5                                   6    
HELIX   11  11 LEU B  134  ARG B  143  1                                  10    
HELIX   12  12 PRO B  169  LEU B  173  5                                   5    
HELIX   13  13 GLN B  199  LYS B  208  1                                  10    
HELIX   14  14 GLY B  222  CYS B  232  1                                  11    
HELIX   15  15 CYS B  232  GLY B  237  1                                   6    
HELIX   16  16 LEU B  258  GLY B  264  5                                   7    
HELIX   17  17 SER B  291  LYS B  302  1                                  12    
HELIX   18  18 VAL B  314  GLU B  323  1                                  10    
HELIX   19  19 SER B  338  ARG B  352  1                                  15    
HELIX   20  20 GLU B  534  GLY B  538  5                                   5    
HELIX   21  21 THR B  564  MET B  568  5                                   5    
HELIX   22  22 LEU B  573  GLY B  577  5                                   5    
HELIX   23  23 ALA B  607  LYS B  619  1                                  13    
HELIX   24  24 THR B  630  CYS B  635  1                                   6    
SHEET    1   A 4 LEU A   3  SER A  12  0                                        
SHEET    2   A 4 ARG A 431  ALA A 437 -1  O  ALA A 432   N  TYR A  11           
SHEET    3   A 4 ASP A 421  ALA A 426 -1  N  ALA A 426   O  ARG A 431           
SHEET    4   A 4 PHE A 404  THR A 412 -1  N  THR A 412   O  ASP A 421           
SHEET    1   B 4 VAL A  23  PHE A  26  0                                        
SHEET    2   B 4 PHE A  35  ALA A  40 -1  O  LEU A  37   N  ASP A  24           
SHEET    3   B 4 GLN A  55  ASP A  60 -1  O  GLN A  55   N  ALA A  40           
SHEET    4   B 4 CYS A  67  PRO A  69 -1  O  GLN A  68   N  LYS A  58           
SHEET    1   C 2 ASP A  79  ALA A  81  0                                        
SHEET    2   C 2 ASP A  84  PRO A  85 -1  O  ASP A  84   N  TYR A  80           
SHEET    1   D 4 VAL A  98  LYS A 101  0                                        
SHEET    2   D 4 LYS A 104  ALA A 109 -1  O  LEU A 106   N  ARG A  99           
SHEET    3   D 4 THR A 127  ASP A 132 -1  O  THR A 127   N  ALA A 109           
SHEET    4   D 4 LYS A 135  TYR A 139 -1  O  VAL A 137   N  LEU A 130           
SHEET    1   E 4 SER A 160  PHE A 163  0                                        
SHEET    2   E 4 ARG A 168  GLY A 173 -1  O  LEU A 170   N  ASP A 162           
SHEET    3   E 4 GLN A 182  GLN A 187 -1  O  ASP A 186   N  VAL A 169           
SHEET    4   E 4 LEU A 208  ALA A 209 -1  O  LEU A 208   N  SER A 185           
SHEET    1   F 4 VAL A 226  GLY A 229  0                                        
SHEET    2   F 4 ASP A 238  VAL A 243 -1  O  VAL A 240   N  ALA A 227           
SHEET    3   F 4 MET A 252  TYR A 256 -1  O  TYR A 256   N  PHE A 239           
SHEET    4   F 4 SER A 263  THR A 268 -1  O  LEU A 264   N  ILE A 255           
SHEET    1   G 4 VAL A 280  THR A 283  0                                        
SHEET    2   G 4 ASP A 292  ALA A 297 -1  O  ASP A 292   N  THR A 283           
SHEET    3   G 4 GLN A 314  GLN A 320 -1  O  SER A 318   N  VAL A 293           
SHEET    4   G 4 PHE A 326  ASN A 332 -1  O  GLN A 327   N  LEU A 319           
SHEET    1   H 2 MET A 301  ARG A 303  0                                        
SHEET    2   H 2 LEU A 309  GLU A 311 -1  O  GLN A 310   N  ASP A 302           
SHEET    1   I 4 ALA A 343  GLY A 348  0                                        
SHEET    2   I 4 ASP A 357  ALA A 362 -1  O  ALA A 359   N  ALA A 345           
SHEET    3   I 4 ILE A 372  PHE A 376 -1  O  TYR A 374   N  ILE A 360           
SHEET    4   I 4 GLN A 389  LEU A 391 -1  O  LEU A 391   N  VAL A 373           
SHEET    1   J 2 GLY A 378  ARG A 379  0                                        
SHEET    2   J 2 GLY A 382  LEU A 383 -1  O  GLY A 382   N  ARG A 379           
SHEET    1   K 5 ALA A 511  PHE A 513  0                                        
SHEET    2   K 5 GLN A 534  LEU A 542 -1  O  TYR A 541   N  LEU A 512           
SHEET    3   K 5 SER A 471  GLY A 483 -1  N  VAL A 475   O  LEU A 538           
SHEET    4   K 5 VAL A 440  TYR A 450 -1  N  THR A 442   O  ASP A 482           
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  LEU A 454  0                                        
SHEET    2   L 5 ASN A 585  ILE A 592  1  O  HIS A 591   N  LEU A 454           
SHEET    3   L 5 ILE A 555  TYR A 561 -1  N  ILE A 555   O  ALA A 590           
SHEET    4   L 5 GLN A 494  LEU A 498 -1  N  GLU A 496   O  GLU A 560           
SHEET    5   L 5 SER A 520  ASN A 524 -1  O  HIS A 521   N  LEU A 497           
SHEET    1   M 4 LEU A 606  VAL A 610  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  PHE A 699   N  LEU A 625           
SHEET    4   M 4 ASP A 652  VAL A 656 -1  N  ILE A 654   O  ARG A 698           
SHEET    1   N 6 LYS A 616  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 ALA A 641  SER A 646 -1  N  ILE A 644   O  GLN A 716           
SHEET    5   N 6 THR A 676  GLY A 684 -1  O  CYS A 681   N  LEU A 643           
SHEET    6   N 6 CYS A 668  GLU A 673 -1  N  LYS A 671   O  GLN A 678           
SHEET    1   O 4 VAL A 742  SER A 749  0                                        
SHEET    2   O 4 VAL A 775  ASN A 784 -1  O  GLN A 777   N  SER A 749           
SHEET    3   O 4 SER A 894  LEU A 903 -1  O  LEU A 897   N  TYR A 780           
SHEET    4   O 4 LEU A 809  ASP A 817 -1  N  ASP A 817   O  ILE A 896           
SHEET    1   P 6 HIS A 752  LEU A 755  0                                        
SHEET    2   P 6 ILE A 941  TRP A 953  1  O  THR A 952   N  LEU A 755           
SHEET    3   P 6 SER A 917  GLU A 930 -1  N  SER A 922   O  VAL A 947           
SHEET    4   P 6 PHE A 790  TYR A 803 -1  N  GLN A 798   O  SER A 923           
SHEET    5   P 6 GLN A 878  LEU A 889 -1  O  VAL A 886   N  ALA A 793           
SHEET    6   P 6 MET A 820  SER A 824 -1  N  ASN A 821   O  GLN A 885           
SHEET    1   Q 4 ASN A 806  THR A 807  0                                        
SHEET    2   Q 4 PHE A 790  TYR A 803 -1  N  TYR A 803   O  ASN A 806           
SHEET    3   Q 4 SER A 917  GLU A 930 -1  O  SER A 923   N  GLN A 798           
SHEET    4   Q 4 ILE A 869  LEU A 872  1  N  HIS A 870   O  SER A 917           
SHEET    1   R 2 TRP B  25  CYS B  26  0                                        
SHEET    2   R 2 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 4 VAL B  83  SER B  84  0                                        
SHEET    2   T 4 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3   T 4 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    4   T 4 LEU B 366  THR B 373 -1  N  SER B 367   O  LYS B 402           
SHEET    1   U 6 TYR B 190  THR B 197  0                                        
SHEET    2   U 6 ARG B 150  PHE B 156 -1  N  ALA B 155   O  LYS B 191           
SHEET    3   U 6 VAL B 112  ASP B 119  1  N  ILE B 114   O  ARG B 150           
SHEET    4   U 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5   U 6 ILE B 304  THR B 311  1  O  ILE B 307   N  PHE B 248           
SHEET    6   U 6 THR B 329  LEU B 333  1  O  LEU B 333   N  VAL B 310           
SHEET    1   V 2 GLY B 540  SER B 543  0                                        
SHEET    2   V 2 ASP B 546  CYS B 549 -1  O  LEU B 548   N  GLN B 541           
SHEET    1   W 2 TRP B 553  THR B 554  0                                        
SHEET    2   W 2 CYS B 560  THR B 561 -1  O  CYS B 560   N  THR B 554           
SHEET    1   X 2 GLY B 579  GLU B 582  0                                        
SHEET    2   X 2 SER B 585  CYS B 588 -1  O  VAL B 587   N  LYS B 580           
SHEET    1   Y 4 ILE B 639  VAL B 642  0                                        
SHEET    2   Y 4 LEU B 679  VAL B 682  1  O  VAL B 681   N  VAL B 642           
SHEET    3   Y 4 VAL B 664  TYR B 670 -1  N  GLN B 668   O  TYR B 680           
SHEET    4   Y 4 ALA B 652  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 B    5    CYS B   23                          1555   1555  2.03  
SSBOND  11 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND  12 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND  13 CYS B   26    CYS B   49                          1555   1555  2.04  
SSBOND  14 CYS B  177    CYS B  184                          1555   1555  2.03  
SSBOND  15 CYS B  232    CYS B  273                          1555   1555  2.03  
SSBOND  16 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  17 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  18 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  19 CYS B  448    CYS B  460                          1555   1555  2.03  
SSBOND  20 CYS B  462    CYS B  471                          1555   1555  2.03  
SSBOND  21 CYS B  473    CYS B  503                          1555   1555  2.03  
SSBOND  22 CYS B  486    CYS B  501                          1555   1555  2.04  
SSBOND  23 CYS B  495    CYS B  506                          1555   1555  2.04  
SSBOND  24 CYS B  508    CYS B  521                          1555   1555  2.03  
SSBOND  25 CYS B  523    CYS B  544                          1555   1555  2.03  
SSBOND  26 CYS B  528    CYS B  542                          1555   1555  2.03  
SSBOND  27 CYS B  536    CYS B  547                          1555   1555  2.03  
SSBOND  28 CYS B  549    CYS B  558                          1555   1555  2.03  
SSBOND  29 CYS B  560    CYS B  583                          1555   1555  2.03  
SSBOND  30 CYS B  567    CYS B  581                          1555   1555  2.03  
SSBOND  31 CYS B  575    CYS B  586                          1555   1555  2.03  
SSBOND  32 CYS B  588    CYS B  598                          1555   1555  2.03  
SSBOND  33 CYS B  601    CYS B  604                          1555   1555  2.03  
SSBOND  34 CYS B  608    CYS B  655                          1555   1555  2.03  
SSBOND  35 CYS B  614    CYS B  635                          1555   1555  2.03  
SSBOND  36 CYS B  617    CYS B  631                          1555   1555  2.03  
SSBOND  37 CYS B  663    CYS B  687                          1555   1555  2.03  
LINK         ND2 ASN A 821                 C1  NAG A1021     1555   1555  1.44  
LINK         ND2 ASN A 524                 C1  NAG A1017     1555   1555  1.44  
LINK         ND2 ASN A 458                 C1  NAG A1013     1555   1555  1.44  
LINK         ND2 ASN B 559                 C1  NAG B 705     1555   1555  1.44  
LINK         ND2 ASN A  44                 C1  NAG A1001     1555   1555  1.44  
LINK         O4  NAG A1007                 C1  NAG A1008     1555   1555  1.44  
LINK         O4  NAG A1013                 C1  NAG A1014     1555   1555  1.44  
LINK         O4  NAG A1005                 C1  NAG A1006     1555   1555  1.44  
LINK         ND2 ASN B  99                 C1  NAG B 701     1555   1555  1.44  
LINK         ND2 ASN A 585                 C1  NAG A1018     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B 702     1555   1555  1.44  
LINK         ND2 ASN A 266                 C1  NAG A1007     1555   1555  1.44  
LINK         ND2 ASN A 950                 C1  NAG A1024     1555   1555  1.44  
LINK         O4  NAG A1001                 C1  NAG A1002     1555   1555  1.44  
LINK         O4  NAG A1002                 C1  BMA A1003     1555   1555  1.44  
LINK         ND2 ASN A 943                 C1  NAG A1022     1555   1555  1.44  
LINK         O3  BMA A1003                 C1  MAN A1004     1555   1555  1.44  
LINK         O4  BMA A1011                 C1  MAN A1012     1555   1555  1.44  
LINK         O6  BMA A1009                 C1  BMA A1011     1555   1555  1.44  
LINK         O3  BMA A1009                 C1  MAN A1010     1555   1555  1.44  
LINK         O4  NAG A1008                 C1  BMA A1009     1555   1555  1.44  
LINK         O4  NAG A1025                 C1  BMA A1026     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B 703     1555   1555  1.44  
LINK         ND2 ASN A 674                 C1  NAG A1020     1555   1555  1.44  
LINK         ND2 ASN A 260                 C1  NAG A1005     1555   1555  1.44  
LINK         O4  NAG A1018                 C1  NAG A1019     1555   1555  1.44  
LINK         O3  BMA A1015                 C1  MAN A1016     1555   1555  1.44  
LINK         O4  NAG B 706                 C1  BMA B 707     1555   1555  1.44  
LINK         O4  NAG A1014                 C1  BMA A1015     1555   1555  1.44  
LINK         O4  NAG A1022                 C1  NAG A1023     1555   1555  1.44  
LINK         O4  NAG A1024                 C1  NAG A1025     1555   1555  1.45  
LINK         O4  NAG B 703                 C1  NAG B 704     1555   1555  1.45  
LINK         O4  NAG B 705                 C1  NAG B 706     1555   1555  1.45  
LINK         OD1 ASP B 251                MN    MN B 709     1555   1555  2.05  
LINK         O   TYR A 290                MN    MN A1028     1555   1555  2.07  
LINK         O   TYR A 419                MN    MN A1030     1555   1555  2.07  
LINK         OD2 ASP A 230                MN    MN A1027     1555   1555  2.14  
LINK         OD1 ASP A 413                MN    MN A1030     1555   1555  2.15  
LINK         OD1 ASP B 217                MN    MN B 710     1555   1555  2.15  
LINK         OE1 GLU B 220                MN    MN B 708     1555   1555  2.15  
LINK         OE2 GLU A 636                MN    MN A1031     1555   1555  2.15  
LINK         OD1 ASP A 238                MN    MN A1027     1555   1555  2.15  
LINK         OD2 ASP A 284                MN    MN A1028     1555   1555  2.15  
LINK         OD1 ASP A 599                MN    MN A1031     1555   1555  2.15  
LINK         OD1 ASP B 127                MN    MN B 709     1555   1555  2.15  
LINK         OD2 ASP A 599                MN    MN A1031     1555   1555  2.16  
LINK         OD2 ASP A 353                MN    MN A1029     1555   1555  2.16  
LINK         OD2 ASP B 126                MN    MN B 709     1555   1555  2.16  
LINK         OD1 ASP A 353                MN    MN A1029     1555   1555  2.16  
LINK         OE1 GLU A 636                MN    MN A1031     1555   1555  2.16  
LINK         OD1 ASP B 126                MN    MN B 709     1555   1555  2.16  
LINK         OE2 GLU B 220                MN    MN B 710     1555   1555  2.16  
LINK         OD1 ASP A 357                MN    MN A1029     1555   1555  2.16  
LINK         O   ASP B 217                MN    MN B 710     1555   1555  2.16  
LINK         OD2 ASP B 158                MN    MN B 710     1555   1555  2.16  
LINK         OD2 ASP A 292                MN    MN A1028     1555   1555  2.17  
LINK         OG  SER B 123                MN    MN B 708     1555   1555  2.17  
LINK         OD2 ASP A 351                MN    MN A1029     1555   1555  2.17  
LINK         OD1 ASP A 288                MN    MN A1028     1555   1555  2.17  
LINK         OD2 ASP A 357                MN    MN A1029     1555   1555  2.17  
LINK         O   SER B 123                MN    MN B 709     1555   1555  2.17  
LINK         OD1 ASP A 292                MN    MN A1028     1555   1555  2.17  
LINK         OG  SER B 121                MN    MN B 708     1555   1555  2.17  
LINK         OD2 ASP A 421                MN    MN A1030     1555   1555  2.17  
LINK         OD1 ASP A 234                MN    MN A1027     1555   1555  2.18  
LINK         OD1 ASP A 421                MN    MN A1030     1555   1555  2.18  
LINK         OD1 ASN B 215                MN    MN B 710     1555   1555  2.18  
LINK         OD1 ASN A 286                MN    MN A1028     1555   1555  2.18  
LINK         OD2 ASP A 238                MN    MN A1027     1555   1555  2.19  
LINK         OD1 ASN A 417                MN    MN A1030     1555   1555  2.19  
LINK         O   CYS A 596                MN    MN A1031     1555   1555  2.19  
LINK         OD2 ASP B 251                MN    MN B 709     1555   1555  2.20  
LINK         O   PRO B 219                MN    MN B 710     1555   1555  2.22  
LINK         OD1 ASP A 415                MN    MN A1030     1555   1555  2.24  
LINK         OD1 ASN A 232                MN    MN A1027     1555   1555  2.27  
LINK         O   VAL A 601                MN    MN A1031     1555   1555  2.29  
LINK         O   ILE A 236                MN    MN A1027     1555   1555  2.37  
LINK         OD1 ASP A 349                MN    MN A1029     1555   1555  2.37  
LINK         O   PHE A 355                MN    MN A1029     1555   1555  2.42  
LINK         OD2 ASP A 415                MN    MN A1030     1555   1555  2.43  
LINK        MN    MN B 708                 O   HOH B 802     1555   1555  2.19  
LINK        MN    MN B 708                 O   HOH B 801     1555   1555  2.20  
CISPEP   1 TYR A  450    PRO A  451          0       -16.75                     
CISPEP   2 ASN A  685    PRO A  686          0         1.50                     
CISPEP   3 SER A  749    PRO A  750          0        -5.52                     
CISPEP   4 LEU A  755    PRO A  756          0        -2.24                     
CISPEP   5 SER B   84    PRO B   85          0        -4.33                     
CISPEP   6 SER B  162    PRO B  163          0       -11.22                     
CISPEP   7 SER B  510    SER B  511          0        -9.56                     
SITE     1 AC1  5 ASP A 230  ASN A 232  ASP A 234  ILE A 236                    
SITE     2 AC1  5 ASP A 238                                                     
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  5 ASP A 349  ASP A 351  ASP A 353  PHE A 355                    
SITE     2 AC3  5 ASP A 357                                                     
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  4 CYS A 596  ASP A 599  VAL A 601  GLU A 636                    
SITE     1 AC6  6 SER B 121  SER B 123  GLU B 220  HOH B 801                    
SITE     2 AC6  6 HOH B 802  ASP C1495                                          
SITE     1 AC7  5 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 AC7  5 ASN C1497                                                     
SITE     1 AC8  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC8  5 GLU B 220                                                     
SITE     1 AC9  5 GLU A  15  GLY A  16  LYS A  42  ASN A  44                    
SITE     2 AC9  5 GLU A  52                                                     
SITE     1 BC1  3 ASP A 257  ASN A 260  SER A 262                               
SITE     1 BC2  6 GLN A 214  PHE A 217  TYR A 254  SER A 263                    
SITE     2 BC2  6 LEU A 264  ASN A 266                                          
SITE     1 BC3  5 TYR A 450  ASN A 458  THR A 460  CYS A 472                    
SITE     2 BC3  5 ASN B  48                                                     
SITE     1 BC4  1 ASN A 524                                                     
SITE     1 BC5  2 PHE A 558  ASN A 585                                          
SITE     1 BC6  1 ASN A 674                                                     
SITE     1 BC7  2 ASN A 821  GLN A 885                                          
SITE     1 BC8  1 ASN A 943                                                     
SITE     1 BC9  3 ASP A 751  ILE A 869  ASN A 950                               
SITE     1 CC1  2 LYS B  98  ASN B  99                                          
SITE     1 CC2  2 ARG A 248  ASN B 320                                          
SITE     1 CC3  3 ASN B 371  SER B 398  GLU B 400                               
SITE     1 CC4  5 ASP A 621  PRO A 624  TYR B 531  TYR B 557                    
SITE     2 CC4  5 ASN B 559                                                     
CRYST1  130.018  130.018  308.203  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      0.007691  0.004441  0.000000        0.00000                         
SCALE2      0.000000  0.008881  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003245        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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