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Database: PDB
Entry: 4MMZ
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Original site: 4MMZ 
HEADER    CELL ADHESION                           09-SEP-13   4MMZ              
TITLE     INTEGRIN ALPHAVBETA3 ECTODOMAIN BOUND TO AN ANTAGONISTIC TENTH DOMAIN 
TITLE    2 OF FIBRONECTIN                                                       
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: ALPHAV, 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: GP3A, ITGB3;                                                   
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: 511693;                                     
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    INTEGRIN, A DOMAIN, HYBRID DOMAIN, PSI, EGF REPEATS, BETA TAIL, CALF, 
KEYWDS   2 THIGH, BETA PROPELLER, RGD MOTIF, FIBRONECTIN, VITRONECTIN, CELL     
KEYWDS   3 ADHESION                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.VAN AGTHOVEN,J.XIONG,M.A.ARNAOUT                                    
REVDAT   4   15-NOV-17 4MMZ    1       REMARK                                   
REVDAT   3   30-APR-14 4MMZ    1       JRNL                                     
REVDAT   2   09-APR-14 4MMZ    1       JRNL                                     
REVDAT   1   26-MAR-14 4MMZ    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.    3.10 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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 55185                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2706                            
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 42.4884 -  8.2588    0.98     2952   123  0.1782 0.2431        
REMARK   3     2  8.2588 -  6.5631    1.00     2840   156  0.2101 0.2499        
REMARK   3     3  6.5631 -  5.7357    1.00     2824   147  0.2092 0.2704        
REMARK   3     4  5.7357 -  5.2123    1.00     2752   157  0.1897 0.2204        
REMARK   3     5  5.2123 -  4.8393    1.00     2758   164  0.1684 0.2484        
REMARK   3     6  4.8393 -  4.5543    1.00     2779   155  0.1614 0.1996        
REMARK   3     7  4.5543 -  4.3265    1.00     2722   140  0.1724 0.2345        
REMARK   3     8  4.3265 -  4.1383    1.00     2783   140  0.1961 0.2358        
REMARK   3     9  4.1383 -  3.9791    1.00     2764   133  0.2049 0.2534        
REMARK   3    10  3.9791 -  3.8419    1.00     2732   150  0.2226 0.2448        
REMARK   3    11  3.8419 -  3.7218    1.00     2744   120  0.2245 0.2941        
REMARK   3    12  3.7218 -  3.6155    1.00     2752   127  0.2265 0.2944        
REMARK   3    13  3.6155 -  3.5204    1.00     2700   143  0.2383 0.3297        
REMARK   3    14  3.5204 -  3.4345    1.00     2752   149  0.2525 0.2904        
REMARK   3    15  3.4345 -  3.3565    1.00     2738   133  0.2756 0.3165        
REMARK   3    16  3.3565 -  3.2851    1.00     2745   151  0.2657 0.3369        
REMARK   3    17  3.2851 -  3.2194    1.00     2693   129  0.2706 0.3085        
REMARK   3    18  3.2194 -  3.1587    1.00     2689   175  0.2727 0.2990        
REMARK   3    19  3.1587 -  3.1023    1.00     2760   114  0.2778 0.3188        
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) : 25.360           
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          13864                                  
REMARK   3   ANGLE     :  0.904          18703                                  
REMARK   3   CHIRALITY :  0.035           2118                                  
REMARK   3   PLANARITY :  0.004           2434                                  
REMARK   3   DIHEDRAL  : 13.016           5097                                  
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 342 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9361  54.9650  23.0087              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9032 T22:   0.3867                                     
REMARK   3      T33:   0.6384 T12:  -0.2360                                     
REMARK   3      T13:  -0.0663 T23:   0.0306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4039 L22:   3.3991                                     
REMARK   3      L33:   1.8917 L12:   1.2493                                     
REMARK   3      L13:   0.3367 L23:  -0.2429                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2103 S12:   0.1497 S13:   0.3250                       
REMARK   3      S21:  -0.0678 S22:   0.1581 S23:   0.2350                       
REMARK   3      S31:  -0.2280 S32:   0.0061 S33:   0.0465                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 343 THROUGH 598 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.0330  47.6911  -1.0324              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0543 T22:   0.8600                                     
REMARK   3      T33:   1.0424 T12:  -0.3840                                     
REMARK   3      T13:  -0.2154 T23:   0.1496                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2294 L22:   0.1651                                     
REMARK   3      L33:   1.6332 L12:   0.9412                                     
REMARK   3      L13:   3.6584 L23:   0.2101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2528 S12:   1.1745 S13:   0.3171                       
REMARK   3      S21:  -0.3495 S22:   0.1632 S23:   0.2744                       
REMARK   3      S31:  -0.1425 S32:   0.2098 S33:   0.0793                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 599 THROUGH 764 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -46.2994  40.2253  32.1507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0067 T22:   0.9424                                     
REMARK   3      T33:   0.9532 T12:   0.1417                                     
REMARK   3      T13:  -0.0567 T23:   0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3943 L22:   1.2775                                     
REMARK   3      L33:   2.0962 L12:  -1.0335                                     
REMARK   3      L13:   6.2627 L23:  -2.1352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5364 S12:   0.1314 S13:   0.0030                       
REMARK   3      S21:  -0.0160 S22:   0.3229 S23:   0.1578                       
REMARK   3      S31:  -0.0698 S32:   0.4330 S33:   0.2441                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 765 THROUGH 954 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.5433  38.1154  72.6980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7948 T22:   0.3909                                     
REMARK   3      T33:   0.7571 T12:   0.2088                                     
REMARK   3      T13:   0.0716 T23:  -0.0638                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4173 L22:   7.4691                                     
REMARK   3      L33:   9.7268 L12:  -3.3485                                     
REMARK   3      L13:   4.6699 L23:  -4.0745                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1940 S12:  -0.4610 S13:   0.1057                       
REMARK   3      S21:   0.6832 S22:   0.1767 S23:  -0.1089                       
REMARK   3      S31:  -0.2419 S32:  -0.0371 S33:   0.0137                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 445 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.2408  16.4092  28.8328              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1142 T22:   0.4112                                     
REMARK   3      T33:   0.8758 T12:  -0.1409                                     
REMARK   3      T13:   0.0202 T23:   0.0309                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0075 L22:   2.8476                                     
REMARK   3      L33:   1.1096 L12:   1.4753                                     
REMARK   3      L13:   0.4265 L23:   0.2578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1739 S12:  -0.0064 S13:  -0.7187                       
REMARK   3      S21:   0.3978 S22:  -0.0397 S23:  -0.2968                       
REMARK   3      S31:   0.2635 S32:  -0.0933 S33:  -0.1334                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 446 THROUGH 606 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -37.5583  23.0103  17.3090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2437 T22:   0.9998                                     
REMARK   3      T33:   1.2807 T12:  -0.2329                                     
REMARK   3      T13:  -0.0902 T23:   0.1339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4038 L22:   4.4471                                     
REMARK   3      L33:   6.5570 L12:   2.8889                                     
REMARK   3      L13:   3.8530 L23:   5.3107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9108 S12:   1.0631 S13:   0.6323                       
REMARK   3      S21:  -1.0498 S22:   0.3825 S23:   1.0178                       
REMARK   3      S31:  -0.6057 S32:   0.7911 S33:   0.5277                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 607 THROUGH 690 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2860  14.0472  66.8141              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1781 T22:   0.6523                                     
REMARK   3      T33:   1.6100 T12:   0.3420                                     
REMARK   3      T13:  -0.0614 T23:   0.0759                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5428 L22:   1.3913                                     
REMARK   3      L33:   5.2053 L12:   1.5631                                     
REMARK   3      L13:  -0.7818 L23:   0.9840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1355 S12:   0.3131 S13:   0.9065                       
REMARK   3      S21:   0.1143 S22:   0.3313 S23:  -0.3557                       
REMARK   3      S31:  -0.2785 S32:   0.0452 S33:  -0.4648                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1417 THROUGH 1421 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9548  50.2673  56.8835              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5798 T22:   2.2110                                     
REMARK   3      T33:   2.6981 T12:  -0.7070                                     
REMARK   3      T13:  -0.1116 T23:  -0.8229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0000 L22:   5.7287                                     
REMARK   3      L33:   2.0000 L12:  -6.0184                                     
REMARK   3      L13:   4.2069 L23:   3.5282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6966 S12:   3.4896 S13:  -0.0052                       
REMARK   3      S21:   3.8705 S22:   1.4597 S23:   0.6597                       
REMARK   3      S31:   1.4407 S32:   4.1719 S33:  -2.1560                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1422 THROUGH 1431 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9844  37.0235  67.1646              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5315 T22:   2.5887                                     
REMARK   3      T33:   2.1525 T12:  -0.5726                                     
REMARK   3      T13:  -0.8025 T23:   0.9854                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0885 L22:   6.5054                                     
REMARK   3      L33:   9.5827 L12:   6.2329                                     
REMARK   3      L13:  -1.6829 L23:  -2.7888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0494 S12:  -1.4343 S13:  -2.2800                       
REMARK   3      S21:   6.3087 S22:  -1.4479 S23:  -3.8570                       
REMARK   3      S31:  -1.1339 S32:  -0.0847 S33:   1.4970                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1432 THROUGH 1443 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4411  41.4329  61.3633              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6751 T22:   1.1880                                     
REMARK   3      T33:   1.3055 T12:  -0.2345                                     
REMARK   3      T13:  -0.4745 T23:   0.1536                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0004 L22:   6.7362                                     
REMARK   3      L33:   2.0002 L12:  -4.1836                                     
REMARK   3      L13:   7.8561 L23:  -6.5809                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1365 S12:  -0.7191 S13:   0.2373                       
REMARK   3      S21:   3.2975 S22:  -1.0419 S23:  -1.1710                       
REMARK   3      S31:  -1.5351 S32:   0.1284 S33:   2.1768                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1444 THROUGH 1453 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9315  37.0120  52.6908              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7494 T22:   1.1313                                     
REMARK   3      T33:   1.4198 T12:  -0.4677                                     
REMARK   3      T13:  -0.7099 T23:   0.4928                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0001 L22:   2.0004                                     
REMARK   3      L33:   2.0005 L12:   0.3278                                     
REMARK   3      L13:   2.9486 L23:   1.3996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3431 S12:  -1.2828 S13:  -0.4983                       
REMARK   3      S21:   1.6237 S22:  -0.4708 S23:  -1.7683                       
REMARK   3      S31:  -0.3990 S32:   1.2388 S33:   0.8136                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1454 THROUGH 1470 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7624  33.9459  53.2167              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6927 T22:   1.1859                                     
REMARK   3      T33:   1.6216 T12:  -0.3604                                     
REMARK   3      T13:  -0.4268 T23:   0.3079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8757 L22:   9.0172                                     
REMARK   3      L33:   5.5359 L12:  -2.9606                                     
REMARK   3      L13:  -0.1336 L23:   2.6219                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1804 S12:   0.2445 S13:   0.5158                       
REMARK   3      S21:   1.0254 S22:   0.2808 S23:  -1.6808                       
REMARK   3      S31:   0.3212 S32:   0.5983 S33:  -0.0998                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1471 THROUGH 1482 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7149  30.3575  61.8406              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.4554 T22:   1.4459                                     
REMARK   3      T33:   2.0378 T12:   0.0655                                     
REMARK   3      T13:  -0.9032 T23:   0.4779                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0000 L22:   0.6981                                     
REMARK   3      L33:   1.3081 L12:  -2.4862                                     
REMARK   3      L13:  -3.6345 L23:   0.9515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7898 S12:  -1.3752 S13:  -0.7782                       
REMARK   3      S21:   1.8803 S22:   1.4064 S23:   0.1091                       
REMARK   3      S31:   0.6017 S32:   0.0675 S33:  -0.6159                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1483 THROUGH 1491 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7753  39.9769  53.3488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9349 T22:   1.2896                                     
REMARK   3      T33:   1.9154 T12:  -0.5568                                     
REMARK   3      T13:  -0.9316 T23:   0.2395                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2994 L22:   7.5297                                     
REMARK   3      L33:   5.0513 L12:   5.5757                                     
REMARK   3      L13:  -2.2573 L23:   0.2331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3394 S12:  -0.4987 S13:  -1.1404                       
REMARK   3      S21:   1.8570 S22:  -1.7231 S23:  -1.5573                       
REMARK   3      S31:  -0.3596 S32:   0.5666 S33:   1.3814                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1492 THROUGH 1507 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6498  43.4839  50.4637              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6790 T22:   0.9664                                     
REMARK   3      T33:   1.4787 T12:  -0.2635                                     
REMARK   3      T13:  -0.5514 T23:   0.0494                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1836 L22:   0.9602                                     
REMARK   3      L33:   8.9261 L12:  -2.6135                                     
REMARK   3      L13:   6.6047 L23:  -2.2361                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1053 S12:  -0.5733 S13:   0.9591                       
REMARK   3      S21:   1.1894 S22:  -0.4838 S23:  -2.0933                       
REMARK   3      S31:  -1.8782 S32:   0.9110 S33:   0.5917                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RAMACHANDRAN RESTRAINTS APPLIED           
REMARK   4                                                                      
REMARK   4 4MMZ 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_1000082113.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-AUG-12                          
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) : 0.97934                            
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   : 55243                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.400                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.73900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3IJE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.87                     
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      205.11733            
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      102.55867            
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      102.55867            
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      205.11733            
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 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     ASP A   868                                                      
REMARK 465     ILE A   869                                                      
REMARK 465     ILE A   955                                                      
REMARK 465     GLN A   956                                                      
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     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    SER A  63       -3.24     83.34                                   
REMARK 500    ASP A  73      -63.46    -95.56                                   
REMARK 500    ALA A  74       -2.17     67.96                                   
REMARK 500    LYS A  89      -13.64     71.49                                   
REMARK 500    GLN A 102     -118.18     54.56                                   
REMARK 500    THR A 116      -11.25     69.82                                   
REMARK 500    GLU A 117       -4.04     66.89                                   
REMARK 500    MET A 118      -74.66   -105.38                                   
REMARK 500    PRO A 124       74.06    -67.13                                   
REMARK 500    ILE A 147      -71.31   -101.12                                   
REMARK 500    LYS A 259      -71.40   -109.22                                   
REMARK 500    ALA A 273       -3.73     65.90                                   
REMARK 500    PHE A 334      -62.68   -128.68                                   
REMARK 500    ARG A 398     -135.63     60.21                                   
REMARK 500    ALA A 411       -3.12     74.32                                   
REMARK 500    PHE A 427      -17.48     73.02                                   
REMARK 500    THR A 460      -66.32   -128.41                                   
REMARK 500    LYS A 505     -133.29     44.76                                   
REMARK 500    ALA A 507      176.02    174.39                                   
REMARK 500    ARG A 510      -16.32     73.47                                   
REMARK 500    ARG A 529     -136.01     44.85                                   
REMARK 500    ALA A 540       72.79     34.85                                   
REMARK 500    PHE A 548      -58.44   -121.51                                   
REMARK 500    ARG A 549       -7.18     87.26                                   
REMARK 500    LYS A 551     -158.21    -98.50                                   
REMARK 500    LEU A 552      -93.80     62.83                                   
REMARK 500    THR A 553      126.35    -38.42                                   
REMARK 500    TYR A 565      -74.87    -55.76                                   
REMARK 500    ARG A 566     -110.41     46.71                                   
REMARK 500    THR A 572       73.40     62.30                                   
REMARK 500    THR A 582      137.94   -177.21                                   
REMARK 500    ASN A 623      144.76   -175.41                                   
REMARK 500    ALA A 651      -70.73    -57.15                                   
REMARK 500    ASP A 652       70.43     56.64                                   
REMARK 500    ARG A 665     -147.89     42.96                                   
REMARK 500    LEU A 666      174.04    169.92                                   
REMARK 500    GLU A 673      -71.65   -115.75                                   
REMARK 500    GLN A 675       -7.75     62.89                                   
REMARK 500    GLN A 703     -143.98     49.47                                   
REMARK 500    GLN A 704      178.22    175.89                                   
REMARK 500    SER A 705     -101.04     58.58                                   
REMARK 500    GLU A 706       -7.38     94.04                                   
REMARK 500    THR A 768      -60.26   -140.89                                   
REMARK 500    GLU A 769      -16.00     85.95                                   
REMARK 500    ASN A 805       -2.57     74.62                                   
REMARK 500    LEU A 808      -74.34   -100.94                                   
REMARK 500    MET A 909       -2.77     67.65                                   
REMARK 500    ASN A 910      -78.42    -99.29                                   
REMARK 500    LYS A 911      -69.41   -133.79                                   
REMARK 500    GLN A 914      -77.48   -119.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     136 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE A  539     ALA A  540                  123.54                    
REMARK 500 GLU B  476     ASP B  477                 -135.33                    
REMARK 500 SER B  481     GLN B  482                 -146.93                    
REMARK 500 ASN B  632     ARG B  633                  149.44                    
REMARK 500 TYR C 1451     GLY C 1452                  149.44                    
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 710  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO B 219   O                                                      
REMARK 620 2 ASP B 217   OD1 111.4                                              
REMARK 620 3 GLU B 220   OE2 100.4 147.4                                        
REMARK 620 4 ASP B 158   OD2  83.4 101.0  89.6                                  
REMARK 620 5 ASP B 217   O    99.2  70.1  98.3 171.0                            
REMARK 620 6 ASN B 215   OD1 166.3  82.3  66.0  94.5  85.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1018  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 238   OD1                                                    
REMARK 620 2 ASP A 234   OD1 162.3                                              
REMARK 620 3 ASP A 234   OD2 130.0  61.9                                        
REMARK 620 4 ASN A 232   OD1  83.1  88.6  75.6                                  
REMARK 620 5 ASP A 230   OD1  99.2  64.4 122.9  85.4                            
REMARK 620 6 ASP A 238   OD2  61.3 134.9  97.7 127.1 134.8                      
REMARK 620 7 ILE A 236   O    98.9  84.6 114.4 162.8  77.4  67.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1021  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 419   O                                                      
REMARK 620 2 ASP A 415   OD1 147.1                                              
REMARK 620 3 ASP A 421   OD1 106.6 101.6                                        
REMARK 620 4 ASP A 421   OD2  94.1  85.5  59.8                                  
REMARK 620 5 ASN A 417   OD1  85.3  77.5 152.0 146.3                            
REMARK 620 6 ASP A 413   OD1  69.5  78.3 137.8  78.2  70.0                      
REMARK 620 7 ASN A 417   ND2 109.6  83.8  95.7 150.5  56.3 125.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1019  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 290   O                                                      
REMARK 620 2 ASP A 284   OD1  78.9                                              
REMARK 620 3 ASP A 292   OD1  79.9 145.7                                        
REMARK 620 4 ASP A 292   OD2 107.6 101.1  60.7                                  
REMARK 620 5 ASN A 286   OD1 157.3  78.4 120.2  77.2                            
REMARK 620 6 ASP A 288   OD1 110.5  71.9 141.5 138.7  61.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1022  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 599   OD1                                                    
REMARK 620 2 GLU A 636   OE1 121.9                                              
REMARK 620 3 GLU A 636   OE2 127.1  61.3                                        
REMARK 620 4 ASP A 599   OD2  61.4 171.7 124.0                                  
REMARK 620 5 VAL A 601   O    76.3  68.9 130.0 105.9                            
REMARK 620 6 CYS A 596   O    68.4  58.5  76.2 127.5  74.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1020  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 349   OD1                                                    
REMARK 620 2 ASP A 353   OD1  81.9                                              
REMARK 620 3 ASP A 357   OD1 136.0 141.3                                        
REMARK 620 4 ASP A 351   OD1  84.5  65.8 116.6                                  
REMARK 620 5 ASP A 357   OD2  82.7 152.3  60.7  90.0                            
REMARK 620 6 PHE A 355   O    60.1  91.3 101.2 140.9 100.6                      
REMARK 620 N                    1     2     3     4     5                       
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 127   OD1                                                    
REMARK 620 2 ASP B 126   OD1  61.8                                              
REMARK 620 3 ASP B 126   OD2  90.2  60.8                                        
REMARK 620 4 SER B 123   O    98.4  72.3 120.4                                  
REMARK 620 5 MET B 335   O    76.1 105.5  61.3 174.4                            
REMARK 620 6 HOH C1702   O   165.3 116.6  77.2  94.6  90.9                      
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 ASP C1495   OD1  84.8                                              
REMARK 620 3 SER B 121   OG  112.1  91.5                                        
REMARK 620 4 HOH B 801   O   133.0 139.7  86.1                                  
REMARK 620 5 HOH B 802   O   104.4  90.4 143.5  69.6                            
REMARK 620 6 HOH C1701   O   150.3  68.0  81.7  71.9  65.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1023  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 546   O                                                      
REMARK 620 2 ASP A 544   OD1 116.3                                              
REMARK 620 N                    1                                               
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 1018                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1019                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1020                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1021                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1022                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1023                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1024                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 708                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 709                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 710                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 711                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 712                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 713                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1601                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
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 1002                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1003 BOUND   
REMARK 800  TO ASN A 260                                                        
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  266 RESIDUES 1004 TO 1009                                           
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  458 RESIDUES 1010 TO 1011                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1012 BOUND   
REMARK 800  TO ASN A 585                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1013 BOUND   
REMARK 800  TO ASN A 805                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  821 RESIDUES 1014 TO 1015                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1016 BOUND   
REMARK 800  TO ASN A 943                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1017 BOUND   
REMARK 800  TO ASN A 950                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
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: CC7                                                 
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: CC8                                                 
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: CC9                                                 
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: 4MMY   RELATED DB: PDB                                   
DBREF  4MMZ A    1   959  UNP    P06756   ITAV_HUMAN      31    989             
DBREF  4MMZ B    1   692  UNP    P05106   ITB3_HUMAN      27    718             
DBREF  4MMZ C 1417  1509  UNP    P02751   FINC_HUMAN    1448   1540             
SEQADV 4MMZ PRO C 1492  UNP  P02751    GLY  1523 ENGINEERED MUTATION            
SEQADV 4MMZ TRP C 1496  UNP  P02751    SER  1527 ENGINEERED MUTATION            
SEQADV 4MMZ ASN C 1497  UNP  P02751    PRO  1528 ENGINEERED MUTATION            
SEQADV 4MMZ GLU C 1498  UNP  P02751    ALA  1529 ENGINEERED MUTATION            
SEQADV 4MMZ GLY C 1499  UNP  P02751    SER  1530 ENGINEERED MUTATION            
SEQADV 4MMZ GLY C 1510  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMZ LYS C 1511  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMZ LYS C 1512  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMZ GLY C 1513  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMZ 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 THR PRO ARG GLY          
SEQRES   7 C   98  ASP TRP ASN GLU GLY SER LYS PRO ILE SER ILE ASN TYR          
SEQRES   8 C   98  ARG THR GLY LYS LYS GLY LYS                                  
MODRES 4MMZ ASN A  458  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN A  266  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN A  821  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN B  559  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN A  585  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN A  943  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN A  805  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN A  950  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN A   44  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN A  260  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMZ ASN B   99  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1001      14                                                       
HET    NAG  A1002      14                                                       
HET    NAG  A1003      14                                                       
HET    NAG  A1004      14                                                       
HET    NAG  A1005      14                                                       
HET    BMA  A1006      11                                                       
HET    MAN  A1007      11                                                       
HET    BMA  A1008      11                                                       
HET    MAN  A1009      11                                                       
HET    NAG  A1010      14                                                       
HET    NAG  A1011      14                                                       
HET    NAG  A1012      14                                                       
HET    NAG  A1013      14                                                       
HET    NAG  A1014      14                                                       
HET    NAG  A1015      14                                                       
HET    NAG  A1016      14                                                       
HET    NAG  A1017      14                                                       
HET     MN  A1018       1                                                       
HET     MN  A1019       1                                                       
HET     MN  A1020       1                                                       
HET     MN  A1021       1                                                       
HET     MN  A1022       1                                                       
HET     NA  A1023       1                                                       
HET    GOL  A1024       6                                                       
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                                                       
HET     NA  B 711       1                                                       
HET     CL  B 712       1                                                       
HET     CL  B 713       1                                                       
HET    GOL  C1601       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MN MANGANESE (II) ION                                               
HETNAM      NA SODIUM ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4  NAG    19(C8 H15 N O6)                                              
FORMUL   6  BMA    3(C6 H12 O6)                                                 
FORMUL   6  MAN    2(C6 H12 O6)                                                 
FORMUL  13   MN    8(MN 2+)                                                     
FORMUL  18   NA    2(NA 1+)                                                     
FORMUL  19  GOL    2(C3 H8 O3)                                                  
FORMUL  28   CL    2(CL 1-)                                                     
FORMUL  31  HOH   *9(H2 O)                                                      
HELIX    1   1 GLY A  175  GLN A  180  1                                   6    
HELIX    2   2 VAL A  188  LYS A  194  1                                   7    
HELIX    3   3 GLN A  214  ASP A  218  5                                   5    
HELIX    4   4 ARG A  245  LEU A  250  1                                   6    
HELIX    5   5 GLY A  366  LYS A  370  5                                   5    
HELIX    6   6 SER B   12  ALA B   18  1                                   7    
HELIX    7   7 LEU B   40  ASP B   47  1                                   8    
HELIX    8   8 SER B  121  SER B  123  5                                   3    
HELIX    9   9 MET B  124  ILE B  131  1                                   8    
HELIX   10  10 ASN B  133  THR B  146  1                                  14    
HELIX   11  11 VAL B  200  VAL B  207  1                                   8    
HELIX   12  12 GLY B  222  CYS B  232  1                                  11    
HELIX   13  13 CYS B  232  GLY B  237  1                                   6    
HELIX   14  14 LEU B  258  LEU B  262  5                                   5    
HELIX   15  15 TYR B  281  THR B  285  5                                   5    
HELIX   16  16 SER B  291  LYS B  302  1                                  12    
HELIX   17  17 VAL B  314  GLU B  323  1                                  10    
HELIX   18  18 ASN B  339  ARG B  352  1                                  14    
HELIX   19  19 ALA B  436  ALA B  441  5                                   6    
HELIX   20  20 SER B  445  ASN B  449  5                                   5    
HELIX   21  21 PRO B  493  GLN B  497  5                                   5    
HELIX   22  22 GLU B  534  GLY B  538  5                                   5    
HELIX   23  23 THR B  564  MET B  568  5                                   5    
HELIX   24  24 LEU B  573  GLY B  577  5                                   5    
HELIX   25  25 ASP B  606  LYS B  611  1                                   6    
HELIX   26  26 LYS B  611  PHE B  620  1                                  10    
SHEET    1   A 4 ALA A   9  SER A  12  0                                        
SHEET    2   A 4 ARG A 431  TYR A 435 -1  O  ALA A 432   N  TYR A  11           
SHEET    3   A 4 ASP A 421  GLY A 425 -1  N  VAL A 424   O  ILE A 433           
SHEET    4   A 4 MET A 408  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  CYS A  59   N  LEU A  36           
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 ILE A 161  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  ILE A 184   N  LEU A 171           
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  ASP A 238   N  GLY A 229           
SHEET    3   F 4 MET A 252  TYR A 256 -1  O  MET A 252   N  VAL A 243           
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  LEU A 319 -1  O  SER A 316   N  ILE A 295           
SHEET    4   G 4 GLN A 327  ASN A 332 -1  O  THR A 329   N  VAL A 317           
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  LEU A 347  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  PHE A 376   N  ILE A 358           
SHEET    4   I 4 GLN A 389  GLU A 392 -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 4 GLN A 534  LEU A 538  0                                        
SHEET    2   K 4 ASN A 474  ASP A 482 -1  N  LEU A 479   O  GLN A 534           
SHEET    3   K 4 VAL A 440  TYR A 450 -1  N  TYR A 450   O  ASN A 474           
SHEET    4   K 4 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  LEU A 563 -1  N  ILE A 555   O  ALA A 590           
SHEET    4   L 5 LYS A 490  LEU A 498 -1  N  LEU A 498   O  PHE A 558           
SHEET    5   L 5 SER A 520  SER A 528 -1  O  ILE A 527   N  LEU A 491           
SHEET    1   M 2 CYS A 461  SER A 462  0                                        
SHEET    2   M 2 LYS A 469  VAL A 470 -1  O  VAL A 470   N  CYS A 461           
SHEET    1   N 2 ALA A 511  LEU A 512  0                                        
SHEET    2   N 2 TYR A 541  LEU A 542 -1  O  TYR A 541   N  LEU A 512           
SHEET    1   O 4 LEU A 606  ASP A 611  0                                        
SHEET    2   O 4 PRO A 624  ASN A 633 -1  O  LYS A 630   N  SER A 609           
SHEET    3   O 4 GLN A 692  SER A 700 -1  O  PHE A 699   N  LEU A 625           
SHEET    4   O 4 PHE A 653  ILE A 654 -1  N  ILE A 654   O  ARG A 698           
SHEET    1   P 6 LYS A 616  TYR A 618  0                                        
SHEET    2   P 6 VAL A 730  ALA A 737  1  O  ALA A 737   N  ILE A 617           
SHEET    3   P 6 SER A 710  GLN A 718 -1  N  LEU A 715   O  VAL A 730           
SHEET    4   P 6 ALA A 641  SER A 646 -1  N  ILE A 644   O  GLN A 716           
SHEET    5   P 6 ARG A 677  GLY A 684 -1  O  CYS A 681   N  LEU A 643           
SHEET    6   P 6 SER A 667  THR A 672 -1  N  SER A 667   O  ASP A 682           
SHEET    1   Q 4 VAL A 742  SER A 749  0                                        
SHEET    2   Q 4 VAL A 775  ASN A 784 -1  O  GLN A 777   N  SER A 749           
SHEET    3   Q 4 SER A 894  LEU A 903 -1  O  ALA A 895   N  LEU A 782           
SHEET    4   Q 4 LEU A 809  ASP A 817 -1  N  TYR A 810   O  LEU A 902           
SHEET    1   R 6 HIS A 752  PHE A 754  0                                        
SHEET    2   R 6 ILE A 941  THR A 952  1  O  ASN A 950   N  VAL A 753           
SHEET    3   R 6 TYR A 918  GLU A 930 -1  N  SER A 922   O  VAL A 947           
SHEET    4   R 6 LYS A 792  TYR A 803 -1  N  GLN A 798   O  SER A 923           
SHEET    5   R 6 GLN A 878  VAL A 886 -1  O  VAL A 886   N  ALA A 793           
SHEET    6   R 6 MET A 820  SER A 824 -1  N  THR A 823   O  VAL A 883           
SHEET    1   S 4 ASN A 806  THR A 807  0                                        
SHEET    2   S 4 LYS A 792  TYR A 803 -1  N  TYR A 803   O  ASN A 806           
SHEET    3   S 4 TYR A 918  GLU A 930 -1  O  SER A 923   N  GLN A 798           
SHEET    4   S 4 THR A 871  LEU A 872  1  N  LEU A 872   O  LYS A 921           
SHEET    1   T 6 VAL B  63  GLU B  65  0                                        
SHEET    2   T 6 ARG B  87  LEU B  92 -1  O  ARG B  87   N  LEU B  64           
SHEET    3   T 6 LEU B 425  PHE B 431  1  O  THR B 430   N  LEU B  92           
SHEET    4   T 6 PHE B 414  PRO B 418 -1  N  ILE B 416   O  LEU B 425           
SHEET    5   T 6 VAL B 355  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6   T 6 SER B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1   U 4 VAL B  83  SER B  84  0                                        
SHEET    2   U 4 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3   U 4 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    4   U 4 LEU B 366  THR B 373 -1  N  THR B 373   O  SER B 396           
SHEET    1   V 6 TYR B 190  THR B 197  0                                        
SHEET    2   V 6 LEU B 149  PHE B 156 -1  N  ALA B 155   O  LYS B 191           
SHEET    3   V 6 VAL B 112  ASP B 119  1  N  TYR B 116   O  GLY B 152           
SHEET    4   V 6 SER B 243  THR B 250  1  O  VAL B 247   N  LEU B 117           
SHEET    5   V 6 ILE B 304  VAL B 310  1  O  ALA B 309   N  PHE B 248           
SHEET    6   V 6 THR B 329  VAL B 332  1  O  THR B 329   N  PHE B 308           
SHEET    1   W 2 ILE B 516  THR B 517  0                                        
SHEET    2   W 2 CYS B 523  ASP B 524 -1  O  CYS B 523   N  THR B 517           
SHEET    1   X 2 GLY B 540  SER B 543  0                                        
SHEET    2   X 2 ASP B 546  CYS B 549 -1  O  LEU B 548   N  GLN B 541           
SHEET    1   Y 2 TRP B 553  THR B 554  0                                        
SHEET    2   Y 2 CYS B 560  THR B 561 -1  O  CYS B 560   N  THR B 554           
SHEET    1   Z 2 GLY B 579  GLU B 582  0                                        
SHEET    2   Z 2 SER B 585  CYS B 588 -1  O  VAL B 587   N  LYS B 580           
SHEET    1  AA 4 GLU B 638  VAL B 642  0                                        
SHEET    2  AA 4 SER B 677  VAL B 682  1  O  LEU B 679   N  GLU B 638           
SHEET    3  AA 4 VAL B 664  GLU B 671 -1  N  TYR B 670   O  ILE B 678           
SHEET    4  AA 4 ALA B 652  LYS B 658 -1  N  CYS B 655   O  PHE B 667           
SHEET    1  AB 3 ARG C1421  VAL C1425  0                                        
SHEET    2  AB 3 ILE C1435  ASP C1438 -1  O  SER C1436   N  GLU C1424           
SHEET    3  AB 3 THR C1471  ALA C1472 -1  O  ALA C1472   N  ILE C1435           
SHEET    1  AC 4 GLU C1462  PRO C1466  0                                        
SHEET    2  AC 4 TYR C1446  TYR C1451 -1  N  TYR C1447   O  VAL C1465           
SHEET    3  AC 4 TYR C1483  THR C1491 -1  O  TYR C1488   N  ARG C1448           
SHEET    4  AC 4 ASN C1497  GLU C1498 -1  O  ASN C1497   N  THR C1491           
SHEET    1  AD 4 GLU C1462  PRO C1466  0                                        
SHEET    2  AD 4 TYR C1446  TYR C1451 -1  N  TYR C1447   O  VAL C1465           
SHEET    3  AD 4 TYR C1483  THR C1491 -1  O  TYR C1488   N  ARG C1448           
SHEET    4  AD 4 ILE C1503  TYR C1507 -1  O  TYR C1507   N  TYR C1483           
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  2.04  
SSBOND   4 CYS A  478    CYS A  535                          1555   1555  2.03  
SSBOND   5 CYS A  596    CYS A  602                          1555   1555  2.03  
SSBOND   6 CYS A  668    CYS A  681                          1555   1555  2.03  
SSBOND   7 CYS A  822    CYS A  884                          1555   1555  2.03  
SSBOND   8 CYS A  874    CYS A  879                          1555   1555  2.03  
SSBOND   9 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND  10 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND  11 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND  12 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND  13 CYS B  177    CYS B  184                          1555   1555  2.03  
SSBOND  14 CYS B  232    CYS B  273                          1555   1555  2.03  
SSBOND  15 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  16 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  17 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  18 CYS B  448    CYS B  460                          1555   1555  2.03  
SSBOND  19 CYS B  462    CYS B  471                          1555   1555  2.03  
SSBOND  20 CYS B  473    CYS B  503                          1555   1555  2.03  
SSBOND  21 CYS B  486    CYS B  501                          1555   1555  2.03  
SSBOND  22 CYS B  495    CYS B  506                          1555   1555  2.03  
SSBOND  23 CYS B  508    CYS B  521                          1555   1555  2.03  
SSBOND  24 CYS B  523    CYS B  544                          1555   1555  2.03  
SSBOND  25 CYS B  528    CYS B  542                          1555   1555  2.03  
SSBOND  26 CYS B  536    CYS B  547                          1555   1555  2.03  
SSBOND  27 CYS B  549    CYS B  558                          1555   1555  2.03  
SSBOND  28 CYS B  560    CYS B  583                          1555   1555  2.03  
SSBOND  29 CYS B  567    CYS B  581                          1555   1555  2.04  
SSBOND  30 CYS B  575    CYS B  586                          1555   1555  2.03  
SSBOND  31 CYS B  588    CYS B  598                          1555   1555  2.04  
SSBOND  32 CYS B  601    CYS B  604                          1555   1555  2.03  
SSBOND  33 CYS B  608    CYS B  655                          1555   1555  2.03  
SSBOND  34 CYS B  614    CYS B  635                          1555   1555  2.03  
SSBOND  35 CYS B  617    CYS B  631                          1555   1555  2.04  
SSBOND  36 CYS B  663    CYS B  687                          1555   1555  2.04  
LINK         ND2 ASN A 458                 C1  NAG A1010     1555   1555  1.43  
LINK         ND2 ASN A 266                 C1  NAG A1004     1555   1555  1.43  
LINK         O4  NAG A1004                 C1  NAG A1005     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B 702     1555   1555  1.44  
LINK         ND2 ASN A 821                 C1  NAG A1014     1555   1555  1.44  
LINK         O4  NAG B 705                 C1  NAG B 706     1555   1555  1.44  
LINK         O4  NAG A1005                 C1  BMA A1006     1555   1555  1.44  
LINK         ND2 ASN B 559                 C1  NAG B 705     1555   1555  1.44  
LINK         O4  NAG A1010                 C1  NAG A1011     1555   1555  1.44  
LINK         O3  BMA A1006                 C1  MAN A1007     1555   1555  1.44  
LINK         O4  NAG A1001                 C1  NAG A1002     1555   1555  1.44  
LINK         ND2 ASN A 585                 C1  NAG A1012     1555   1555  1.44  
LINK         ND2 ASN A 943                 C1  NAG A1016     1555   1555  1.44  
LINK         ND2 ASN A 805                 C1  NAG A1013     1555   1555  1.44  
LINK         O4  BMA A1008                 C1  MAN A1009     1555   1555  1.44  
LINK         ND2 ASN A 950                 C1  NAG A1017     1555   1555  1.44  
LINK         ND2 ASN A  44                 C1  NAG A1001     1555   1555  1.44  
LINK         O4  NAG B 706                 C1  BMA B 707     1555   1555  1.44  
LINK         ND2 ASN A 260                 C1  NAG A1003     1555   1555  1.44  
LINK         O6  BMA A1006                 C1  BMA A1008     1555   1555  1.45  
LINK         ND2 ASN B 371                 C1  NAG B 703     1555   1555  1.45  
LINK         ND2 ASN B  99                 C1  NAG B 701     1555   1555  1.45  
LINK         O4  NAG A1014                 C1  NAG A1015     1555   1555  1.45  
LINK         O4  NAG B 703                 C1  NAG B 704     1555   1555  1.45  
LINK         O   PRO B 219                MN    MN B 710     1555   1555  2.07  
LINK         OD1 ASP A 238                MN    MN A1018     1555   1555  2.07  
LINK         O   TYR A 419                MN    MN A1021     1555   1555  2.08  
LINK         O   TYR A 290                MN    MN A1019     1555   1555  2.09  
LINK         OD1 ASP A 284                MN    MN A1019     1555   1555  2.10  
LINK         OD1 ASP A 234                MN    MN A1018     1555   1555  2.13  
LINK         OD2 ASP A 234                MN    MN A1018     1555   1555  2.14  
LINK         OD1 ASP A 599                MN    MN A1022     1555   1555  2.14  
LINK         OD1 ASP A 349                MN    MN A1020     1555   1555  2.14  
LINK         OD1 ASP B 127                MN    MN B 709     1555   1555  2.14  
LINK         OD1 ASP B 126                MN    MN B 709     1555   1555  2.15  
LINK         OE1 GLU A 636                MN    MN A1022     1555   1555  2.15  
LINK         OD1 ASP A 353                MN    MN A1020     1555   1555  2.15  
LINK         OE1 GLU B 220                MN    MN B 708     1555   1555  2.15  
LINK         OE2 GLU A 636                MN    MN A1022     1555   1555  2.15  
LINK         OD1 ASP B 217                MN    MN B 710     1555   1555  2.15  
LINK         OD1 ASP A 357                MN    MN A1020     1555   1555  2.16  
LINK         OD2 ASP A 599                MN    MN A1022     1555   1555  2.16  
LINK         OE2 GLU B 220                MN    MN B 710     1555   1555  2.16  
LINK         OD1 ASN A 232                MN    MN A1018     1555   1555  2.16  
LINK         OD1 ASP A 292                MN    MN A1019     1555   1555  2.16  
LINK         OD1 ASP A 351                MN    MN A1020     1555   1555  2.16  
LINK         OD1 ASP C1495                MN    MN B 708     1555   1555  2.16  
LINK         OD2 ASP A 292                MN    MN A1019     1555   1555  2.17  
LINK         OD1 ASP A 415                MN    MN A1021     1555   1555  2.17  
LINK         OD2 ASP A 357                MN    MN A1020     1555   1555  2.17  
LINK         OD2 ASP B 158                MN    MN B 710     1555   1555  2.18  
LINK         OD1 ASP A 421                MN    MN A1021     1555   1555  2.19  
LINK         OG  SER B 121                MN    MN B 708     1555   1555  2.19  
LINK         OD2 ASP A 421                MN    MN A1021     1555   1555  2.19  
LINK         OD2 ASP B 126                MN    MN B 709     1555   1555  2.19  
LINK         O   ASP B 217                MN    MN B 710     1555   1555  2.20  
LINK         O   SER B 123                MN    MN B 709     1555   1555  2.20  
LINK         OD1 ASN A 286                MN    MN A1019     1555   1555  2.20  
LINK         OD1 ASP A 230                MN    MN A1018     1555   1555  2.20  
LINK         OD1 ASN B 215                MN    MN B 710     1555   1555  2.21  
LINK         OD1 ASN A 417                MN    MN A1021     1555   1555  2.21  
LINK         OD2 ASP A 238                MN    MN A1018     1555   1555  2.22  
LINK         OD1 ASP A 288                MN    MN A1019     1555   1555  2.22  
LINK         O   VAL A 601                MN    MN A1022     1555   1555  2.24  
LINK         OD1 ASP A 413                MN    MN A1021     1555   1555  2.28  
LINK         O   PHE A 355                MN    MN A1020     1555   1555  2.30  
LINK         O   SER A 546                NA    NA A1023     1555   1555  2.42  
LINK         OD1 ASP A 544                NA    NA A1023     1555   1555  2.42  
LINK         OD1 ASN B 654                NA    NA B 711     1555   1555  2.44  
LINK         O   CYS A 596                MN    MN A1022     1555   1555  2.45  
LINK         ND2 ASN A 417                MN    MN A1021     1555   1555  2.51  
LINK         O   ILE A 236                MN    MN A1018     1555   1555  2.54  
LINK         O   MET B 335                MN    MN B 709     1555   1555  2.58  
LINK        MN    MN B 708                 O   HOH B 801     1555   1555  2.18  
LINK        MN    MN B 708                 O   HOH B 802     1555   1555  2.18  
LINK        MN    MN B 708                 O   HOH C1701     1555   1555  2.19  
LINK        MN    MN B 709                 O   HOH C1702     1555   1555  2.20  
CISPEP   1 TYR A  450    PRO A  451          0       -10.49                     
CISPEP   2 ASN A  685    PRO A  686          0         2.44                     
CISPEP   3 SER A  749    PRO A  750          0         3.33                     
CISPEP   4 LEU A  755    PRO A  756          0         1.43                     
CISPEP   5 SER B   84    PRO B   85          0        -1.16                     
CISPEP   6 SER B  162    PRO B  163          0        -0.21                     
CISPEP   7 SER B  168    PRO B  169          0         2.53                     
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  4 ASP A 544  GLU A 545  SER A 546  GLU A 547                    
SITE     1 AC7  3 ASP A 148  ASP A 150  GLU A 930                               
SITE     1 AC8  6 SER B 121  GLU B 220  HOH B 801  HOH B 802                    
SITE     2 AC8  6 ASP C1495  HOH C1701                                          
SITE     1 AC9  6 SER B 123  MET B 124  ASP B 126  ASP B 127                    
SITE     2 AC9  6 MET B 335  HOH C1702                                          
SITE     1 BC1  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 BC1  5 GLU B 220                                                     
SITE     1 BC2  4 ASP B 647  ASN B 654   CL B 712   CL B 713                    
SITE     1 BC3  3 LEU B 645  ASP B 647   NA B 711                               
SITE     1 BC4  3 ASP B 647  ASN B 654   NA B 711                               
SITE     1 BC5  3 THR C1491  ASN C1497  GLU C1498                               
SITE     1 BC6  4 GLU A  15  LYS A  42  ASN A  44  GLU A  52                    
SITE     1 BC7  4 ASP A 257  LYS A 259  ASN A 260  SER A 262                    
SITE     1 BC8  6 GLN A 214  PHE A 217  TYR A 254  SER A 263                    
SITE     2 BC8  6 LEU A 264  ASN A 266                                          
SITE     1 BC9  6 TYR A 450  PRO A 451  ASN A 458  THR A 460                    
SITE     2 BC9  6 CYS A 472  ASN A 474                                          
SITE     1 CC1  3 LYS A 501  ASN A 585  ASP B 512                               
SITE     1 CC2  1 ASN A 805                                                     
SITE     1 CC3  2 ASN A 821  GLY A 887                                          
SITE     1 CC4  2 THR A 942  ASN A 943                                          
SITE     1 CC5  3 ASP A 751  HIS A 752  ASN A 950                               
SITE     1 CC6  2 ASN B  99  NAG B 703                                          
SITE     1 CC7  5 ARG A 248  MET A 272  ASN B 316  LEU B 317                    
SITE     2 CC7  5 ASN B 320                                                     
SITE     1 CC8  4 ASN B 371  SER B 398  GLU B 400  NAG B 701                    
SITE     1 CC9  4 ASP A 621  TYR B 531  TYR B 557  ASN B 559                    
CRYST1  129.790  129.790  307.676  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      0.007705  0.004448  0.000000        0.00000                         
SCALE2      0.000000  0.008897  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003250        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system