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Database: PDB
Entry: 4MMX
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HEADER    CELL ADHESION                           09-SEP-13   4MMX              
TITLE     INTEGRIN ALPHAVBETA3 ECTODOMAIN BOUND TO THE TENTH DOMAIN OF          
TITLE    2 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                                                      
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: FIBRONECTIN, FN, FN1;                                          
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  29 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    INTEGRIN, A DOMAIN, HYBRID DOMAIN, PSI, EGF REPEATS, BETA TA THIGH,   
KEYWDS   2 BETA PROPELLER, RGD MOTIF, FIBRONECTIN, VITRONECTIN, CELL ADHESION   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.VAN AGTHOVEN,J.XIONG,M.A.ARNAOUT                                    
REVDAT   4   15-NOV-17 4MMX    1       REMARK                                   
REVDAT   3   30-APR-14 4MMX    1       JRNL                                     
REVDAT   2   09-APR-14 4MMX    1       JRNL                                     
REVDAT   1   26-MAR-14 4MMX    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.    3.32 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) : 3.32                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 39586                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.910                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1942                            
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 42.5099 -  7.9853    0.99     3256   139  0.1941 0.2317        
REMARK   3     2  7.9853 -  6.3449    1.00     3125   168  0.2272 0.2866        
REMARK   3     3  6.3449 -  5.5449    1.00     3077   159  0.2188 0.2768        
REMARK   3     4  5.5449 -  5.0388    1.00     3037   184  0.1891 0.2432        
REMARK   3     5  5.0388 -  4.6781    1.00     3027   175  0.1677 0.2214        
REMARK   3     6  4.6781 -  4.4026    1.00     3029   173  0.1674 0.2187        
REMARK   3     7  4.4026 -  4.1823    1.00     3033   138  0.1915 0.2255        
REMARK   3     8  4.1823 -  4.0004    1.00     3046   152  0.2132 0.2318        
REMARK   3     9  4.0004 -  3.8465    0.47     1431    82  0.2311 0.3271        
REMARK   3    10  3.8465 -  3.7138    1.00     3018   127  0.2494 0.2879        
REMARK   3    11  3.7138 -  3.5978    0.40     1222    47  0.2532 0.3559        
REMARK   3    12  3.5978 -  3.4950    1.00     2984   166  0.2592 0.3379        
REMARK   3    13  3.4950 -  3.4030    0.46     1356    85  0.2925 0.3324        
REMARK   3    14  3.4030 -  3.3200    1.00     3003   147  0.2820 0.3442        
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)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.860           
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      :  0.010          14004                                  
REMARK   3   ANGLE     :  0.864          18917                                  
REMARK   3   CHIRALITY :  0.035           2172                                  
REMARK   3   PLANARITY :  0.004           2445                                  
REMARK   3   DIHEDRAL  : 12.476           5175                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 21                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 320 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6704  56.0227  22.3377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6904 T22:   0.3533                                     
REMARK   3      T33:   0.4231 T12:  -0.2076                                     
REMARK   3      T13:  -0.0271 T23:   0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3906 L22:   3.0593                                     
REMARK   3      L33:   2.1627 L12:   0.8884                                     
REMARK   3      L13:   0.6957 L23:  -0.5939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3552 S12:   0.2645 S13:   0.2765                       
REMARK   3      S21:  -0.2235 S22:   0.2243 S23:  -0.0609                       
REMARK   3      S31:  -0.4653 S32:   0.1520 S33:   0.1425                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 590 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.3462  48.1263   1.3003              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9959 T22:   0.7645                                     
REMARK   3      T33:   0.8212 T12:  -0.3319                                     
REMARK   3      T13:  -0.2124 T23:   0.1530                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2981 L22:  -0.2665                                     
REMARK   3      L33:   0.8940 L12:   0.1933                                     
REMARK   3      L13:   2.1397 L23:   0.0027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1531 S12:   0.7351 S13:   0.1780                       
REMARK   3      S21:  -0.2755 S22:   0.1111 S23:   0.2250                       
REMARK   3      S31:  -0.0398 S32:   0.0724 S33:   0.0594                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 591 THROUGH 729 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -51.8249  42.5084  21.8435              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7898 T22:   0.5470                                     
REMARK   3      T33:   0.7545 T12:  -0.0566                                     
REMARK   3      T13:  -0.1890 T23:   0.0677                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7018 L22:   3.2187                                     
REMARK   3      L33:   9.0208 L12:  -0.7638                                     
REMARK   3      L13:   1.2682 L23:  -1.3198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2405 S12:  -0.1566 S13:   0.0558                       
REMARK   3      S21:  -0.0511 S22:   0.1971 S23:   0.3381                       
REMARK   3      S31:   0.2684 S32:   0.4128 S33:  -0.0759                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 730 THROUGH 956 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.1579  36.5412  71.6901              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8593 T22:   0.4727                                     
REMARK   3      T33:   0.6140 T12:   0.2395                                     
REMARK   3      T13:   0.0473 T23:  -0.0590                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9222 L22:   3.2128                                     
REMARK   3      L33:   6.7644 L12:  -2.0789                                     
REMARK   3      L13:   3.2605 L23:  -2.1224                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1550 S12:  -0.4131 S13:  -0.0615                       
REMARK   3      S21:   0.4357 S22:   0.0949 S23:  -0.0331                       
REMARK   3      S31:   0.0388 S32:  -0.0316 S33:   0.0321                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 75 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -33.1360   2.3980  11.7970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3274 T22:   0.7164                                     
REMARK   3      T33:   1.2830 T12:  -0.3053                                     
REMARK   3      T13:  -0.1377 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1396 L22:   2.4857                                     
REMARK   3      L33:   6.1747 L12:  -2.3066                                     
REMARK   3      L13:   5.5588 L23:  -2.3752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2957 S12:   0.3559 S13:  -1.2890                       
REMARK   3      S21:  -0.5987 S22:   0.3098 S23:   0.3827                       
REMARK   3      S31:   0.4292 S32:  -0.5509 S33:  -0.5062                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 76 THROUGH 169 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7715  15.5187  34.8628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8462 T22:   0.3871                                     
REMARK   3      T33:   0.8027 T12:  -0.0059                                     
REMARK   3      T13:  -0.0195 T23:   0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9381 L22:   3.6621                                     
REMARK   3      L33:   0.9410 L12:   1.4970                                     
REMARK   3      L13:   0.2989 L23:  -0.9872                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2982 S12:  -0.2075 S13:  -1.2058                       
REMARK   3      S21:   0.5488 S22:  -0.2607 S23:  -1.0019                       
REMARK   3      S31:   0.3011 S32:   0.1458 S33:  -0.1428                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 170 THROUGH 278 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3917  27.1448  31.7473              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6910 T22:   0.4161                                     
REMARK   3      T33:   1.0625 T12:  -0.0766                                     
REMARK   3      T13:  -0.0120 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2874 L22:   4.6073                                     
REMARK   3      L33:   2.7900 L12:   0.2862                                     
REMARK   3      L13:  -0.5693 L23:  -1.5402                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0984 S12:   0.0834 S13:  -0.8833                       
REMARK   3      S21:  -0.1256 S22:   0.1570 S23:  -0.8196                       
REMARK   3      S31:   0.2755 S32:   0.4518 S33:  -0.2355                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 279 THROUGH 423 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8331  18.6510  33.7582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9226 T22:   0.3813                                     
REMARK   3      T33:   0.7074 T12:  -0.0438                                     
REMARK   3      T13:  -0.0131 T23:   0.0795                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8418 L22:   4.7899                                     
REMARK   3      L33:   0.0008 L12:   3.3952                                     
REMARK   3      L13:   0.0765 L23:   0.8594                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0753 S12:  -0.2195 S13:  -0.5022                       
REMARK   3      S21:   0.0282 S22:  -0.0898 S23:  -0.2800                       
REMARK   3      S31:   0.3084 S32:  -0.0967 S33:   0.1667                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 424 THROUGH 462 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.5690   7.8594  -2.3379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0135 T22:   2.0320                                     
REMARK   3      T33:   1.0894 T12:  -0.3861                                     
REMARK   3      T13:  -0.1296 T23:  -0.0713                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1800 L22:   3.2293                                     
REMARK   3      L33:   2.1099 L12:  -3.2691                                     
REMARK   3      L13:   1.6845 L23:  -2.7061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6809 S12:   2.6311 S13:  -0.2506                       
REMARK   3      S21:  -1.6997 S22:  -0.6401 S23:   0.4364                       
REMARK   3      S31:   1.3027 S32:   0.2625 S33:  -0.0145                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 463 THROUGH 588 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.5301  24.4071  15.2156              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2157 T22:   0.8646                                     
REMARK   3      T33:   1.3107 T12:  -0.2304                                     
REMARK   3      T13:  -0.2502 T23:   0.0657                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0040 L22:   2.6980                                     
REMARK   3      L33:   3.5831 L12:   0.2562                                     
REMARK   3      L13:   2.8339 L23:   2.0840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6597 S12:   0.7280 S13:   0.9211                       
REMARK   3      S21:  -0.9438 S22:  -0.1495 S23:   1.0887                       
REMARK   3      S31:  -0.1710 S32:  -0.0259 S33:   0.8049                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 589 THROUGH 630 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.5482  17.3280  58.9574              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9494 T22:   0.5691                                     
REMARK   3      T33:   1.0607 T12:  -0.0260                                     
REMARK   3      T13:   0.0384 T23:  -0.0382                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3504 L22:   2.2259                                     
REMARK   3      L33:   4.3707 L12:  -6.7994                                     
REMARK   3      L13:   4.5894 L23:  -6.5626                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1708 S12:  -0.3350 S13:  -0.0070                       
REMARK   3      S21:  -0.4141 S22:   0.2678 S23:  -1.3793                       
REMARK   3      S31:   0.1384 S32:  -0.4051 S33:  -0.1612                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 631 THROUGH 690 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5494  15.2362  68.4775              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3279 T22:   0.5809                                     
REMARK   3      T33:   1.2316 T12:   0.2755                                     
REMARK   3      T13:  -0.0487 T23:   0.0842                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2280 L22:   1.6969                                     
REMARK   3      L33:   5.7685 L12:   2.3051                                     
REMARK   3      L13:   0.8759 L23:   1.9466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0670 S12:   0.1901 S13:  -0.0700                       
REMARK   3      S21:   0.1472 S22:   0.1623 S23:  -0.7019                       
REMARK   3      S31:   0.0135 S32:   0.6996 S33:  -0.1742                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1417 THROUGH 1425 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  27.4369  47.1899  61.8913              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.0541 T22:   1.8254                                     
REMARK   3      T33:   2.1234 T12:   0.6199                                     
REMARK   3      T13:  -0.8702 T23:  -0.4401                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1995 L22:   1.1815                                     
REMARK   3      L33:   1.9972 L12:  -0.4275                                     
REMARK   3      L13:  -1.3764 L23:   3.5686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6349 S12:   0.4684 S13:   0.1802                       
REMARK   3      S21:   0.8019 S22:  -0.3390 S23:  -0.2921                       
REMARK   3      S31:  -0.2192 S32:   0.8305 S33:  -0.1297                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1426 THROUGH 1433 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9331  46.4354  78.4304              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   5.2685 T22:   4.1225                                     
REMARK   3      T33:   2.7309 T12:   1.3106                                     
REMARK   3      T13:  -0.8064 T23:  -1.6195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5514 L22:   2.0306                                     
REMARK   3      L33:   0.0502 L12:   1.0101                                     
REMARK   3      L13:  -0.1249 L23:  -0.3060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0147 S12:  -2.0355 S13:   1.3881                       
REMARK   3      S21:   1.3349 S22:  -1.5611 S23:   2.1458                       
REMARK   3      S31:  -1.5102 S32:   1.5451 S33:   1.2885                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1434 THROUGH 1452 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6445  46.6688  60.1587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3062 T22:   1.6258                                     
REMARK   3      T33:   1.0968 T12:  -0.0045                                     
REMARK   3      T13:  -0.0317 T23:  -0.1215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2787 L22:   2.0660                                     
REMARK   3      L33:   2.0855 L12:  -4.1987                                     
REMARK   3      L13:   8.9062 L23:  -6.5389                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2749 S12:  -1.8038 S13:   0.7175                       
REMARK   3      S21:   1.9619 S22:  -1.0808 S23:  -1.1184                       
REMARK   3      S31:   2.7997 S32:   0.8585 S33:   1.3704                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1453 THROUGH 1461 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  16.3178  28.8732  68.6822              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.8450 T22:   1.7921                                     
REMARK   3      T33:   2.3978 T12:   0.3147                                     
REMARK   3      T13:  -0.1910 T23:   0.2550                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0047 L22:   7.5850                                     
REMARK   3      L33:   9.3371 L12:  -1.5476                                     
REMARK   3      L13:   4.3422 L23:   4.4741                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8602 S12:   2.1821 S13:   3.7840                       
REMARK   3      S21:  -1.6325 S22:  -1.8395 S23:  -0.3513                       
REMARK   3      S31:  -2.6104 S32:   0.5692 S33:   2.5497                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1462 THROUGH 1473 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2785  48.2996  62.6235              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9604 T22:   1.4019                                     
REMARK   3      T33:   1.1627 T12:  -0.1782                                     
REMARK   3      T13:   0.4799 T23:  -0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6580 L22:   7.6071                                     
REMARK   3      L33:   8.5513 L12:  -6.7997                                     
REMARK   3      L13:  -1.6307 L23:   4.0153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5768 S12:  -1.3693 S13:  -0.6912                       
REMARK   3      S21:   2.2399 S22:  -1.6917 S23:   2.7145                       
REMARK   3      S31:   1.5124 S32:   1.7217 S33:   1.1122                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1474 THROUGH 1483 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5963  36.3368  76.4496              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1361 T22:   3.0573                                     
REMARK   3      T33:   1.9623 T12:   0.4741                                     
REMARK   3      T13:   0.3413 T23:   0.9116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8784 L22:   3.8529                                     
REMARK   3      L33:   9.0328 L12:   4.4080                                     
REMARK   3      L13:  -0.6743 L23:  -3.4556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4175 S12:  -0.4821 S13:  -0.0227                       
REMARK   3      S21:  -1.2215 S22:  -1.4617 S23:  -1.5183                       
REMARK   3      S31:   4.0437 S32:   2.9725 S33:   1.1077                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1484 THROUGH 1490 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  19.6309  40.1499  61.7817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.0997 T22:   2.5867                                     
REMARK   3      T33:   1.0750 T12:  -0.9451                                     
REMARK   3      T13:  -0.0637 T23:  -0.3614                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0018 L22:   1.6628                                     
REMARK   3      L33:   5.6361 L12:  -3.1645                                     
REMARK   3      L13:  -5.8047 L23:   3.0484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1676 S12:  -3.3730 S13:  -0.2199                       
REMARK   3      S21:   2.7305 S22:   0.6362 S23:  -1.0777                       
REMARK   3      S31:   2.9459 S32:   0.4031 S33:  -0.5229                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1491 THROUGH 1502 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  20.8235  41.5616  48.3461              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5795 T22:   0.7429                                     
REMARK   3      T33:   1.2194 T12:  -0.1504                                     
REMARK   3      T13:  -0.3793 T23:   0.1359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0362 L22:   4.7647                                     
REMARK   3      L33:   9.1199 L12:  -5.0136                                     
REMARK   3      L13:  -7.1467 L23:   6.5656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2013 S12:  -1.8619 S13:   1.1858                       
REMARK   3      S21:   2.0880 S22:  -0.4101 S23:  -2.7486                       
REMARK   3      S31:   3.6507 S32:   1.0801 S33:   0.4315                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1503 THROUGH 1509 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8692  38.8688  73.2168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.4879 T22:   3.6146                                     
REMARK   3      T33:   1.6814 T12:   0.1458                                     
REMARK   3      T13:   0.7988 T23:   0.6440                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0149 L22:  -0.0195                                     
REMARK   3      L33:  -0.0054 L12:  -0.0151                                     
REMARK   3      L13:  -0.0129 L23:  -0.0095                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.8068 S12:  -2.1859 S13:  -0.1172                       
REMARK   3      S21:   1.1708 S22:   0.3077 S23:   0.0987                       
REMARK   3      S31:  -5.3689 S32:   0.7216 S33:  -1.8447                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4MMX 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_1000082111.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-OCT-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) : 0.97921                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39593                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.320                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 75.490                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.300                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : 0.10900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.32                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.67600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85                     
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      203.88733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      101.94367            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      101.94367            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      203.88733            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 79550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 49.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     LEU A   838                                                      
REMARK 465     GLN A   839                                                      
REMARK 465     THR A   840                                                      
REMARK 465     THR A   841                                                      
REMARK 465     GLU A   842                                                      
REMARK 465     LYS A   843                                                      
REMARK 465     ASN A   844                                                      
REMARK 465     ASP A   845                                                      
REMARK 465     THR A   846                                                      
REMARK 465     VAL A   847                                                      
REMARK 465     ALA A   848                                                      
REMARK 465     GLY A   849                                                      
REMARK 465     GLN A   850                                                      
REMARK 465     GLY A   851                                                      
REMARK 465     GLU A   852                                                      
REMARK 465     ARG A   853                                                      
REMARK 465     ASP A   854                                                      
REMARK 465     HIS A   855                                                      
REMARK 465     LEU A   856                                                      
REMARK 465     ILE A   857                                                      
REMARK 465     THR A   858                                                      
REMARK 465     LYS A   859                                                      
REMARK 465     ARG A   860                                                      
REMARK 465     ASP A   861                                                      
REMARK 465     LEU A   862                                                      
REMARK 465     ALA A   863                                                      
REMARK 465     LEU A   864                                                      
REMARK 465     SER A   865                                                      
REMARK 465     GLU A   866                                                      
REMARK 465     GLY A   867                                                      
REMARK 465     PRO A   957                                                      
REMARK 465     ALA A   958                                                      
REMARK 465     PRO A   959                                                      
REMARK 465     PRO B   691                                                      
REMARK 465     ASP B   692                                                      
REMARK 465     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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 451   C   -  N   -  CD  ANGL. DEV. = -25.4 DEGREES          
REMARK 500    PRO B 163   C   -  N   -  CD  ANGL. DEV. = -18.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  64      -13.46     66.28                                   
REMARK 500    PHE A  72      -67.37   -107.54                                   
REMARK 500    ASP A  73      -65.35    -92.21                                   
REMARK 500    ALA A  74       -4.63     66.97                                   
REMARK 500    ASN A  77      -83.56    -90.67                                   
REMARK 500    ARG A  78      173.97    170.90                                   
REMARK 500    LYS A  82      -71.31    -47.68                                   
REMARK 500    ASP A  84       80.60   -151.67                                   
REMARK 500    GLN A 102     -119.36     55.70                                   
REMARK 500    ARG A 115      -10.56     85.53                                   
REMARK 500    THR A 116     -152.39     51.30                                   
REMARK 500    MET A 118      -74.54   -100.55                                   
REMARK 500    PRO A 124       68.85    -68.59                                   
REMARK 500    THR A 134      -66.80   -140.02                                   
REMARK 500    ASP A 148     -145.44     55.81                                   
REMARK 500    THR A 249       -3.83     74.57                                   
REMARK 500    ALA A 273       -3.65     66.47                                   
REMARK 500    ASP A 289       -3.82     72.74                                   
REMARK 500    PHE A 334      -62.99   -124.39                                   
REMARK 500    PHE A 337       -2.05     66.85                                   
REMARK 500    ARG A 339       71.07     57.08                                   
REMARK 500    VAL A 386      136.65    174.49                                   
REMARK 500    ARG A 398      -66.45    -95.85                                   
REMARK 500    SER A 399      -62.79   -108.34                                   
REMARK 500    TYR A 406      -18.27     74.39                                   
REMARK 500    VAL A 440       73.46     56.44                                   
REMARK 500    PRO A 451       62.35      9.37                                   
REMARK 500    THR A 466       75.81     65.30                                   
REMARK 500    LEU A 487      143.07   -177.23                                   
REMARK 500    GLN A 504       -5.52     74.19                                   
REMARK 500    SER A 528      -68.71   -131.84                                   
REMARK 500    ASP A 550     -143.60     55.66                                   
REMARK 500    LYS A 551      163.91    174.30                                   
REMARK 500    LEU A 563       71.92     62.13                                   
REMARK 500    ALA A 568       73.93     57.48                                   
REMARK 500    ASP A 570     -142.94     52.52                                   
REMARK 500    THR A 572     -113.39     52.00                                   
REMARK 500    ASP A 613     -117.69     55.75                                   
REMARK 500    LEU A 649     -118.33     53.19                                   
REMARK 500    ILE A 654      -64.82   -105.34                                   
REMARK 500    HIS A 702      -78.22   -106.61                                   
REMARK 500    GLN A 703      162.93    175.77                                   
REMARK 500    SER A 705     -127.78     50.50                                   
REMARK 500    THR A 709     -116.31     56.14                                   
REMARK 500    GLU A 767      -63.18   -126.42                                   
REMARK 500    VAL A 772      -64.85   -108.18                                   
REMARK 500    ASN A 785      -60.48   -107.07                                   
REMARK 500    PRO A 800       77.75    -69.88                                   
REMARK 500    ASN A 805       -3.78     71.06                                   
REMARK 500    LEU A 808      -73.68   -100.96                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     137 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1028  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 290   O                                                      
REMARK 620 2 ASP A 284   OD2  74.3                                              
REMARK 620 3 ASP A 292   OD1 101.7  89.9                                        
REMARK 620 4 ASN A 286   OD1 136.4  62.4  83.5                                  
REMARK 620 5 ASP A 292   OD2 102.7 149.4  60.5 116.7                            
REMARK 620 6 ASP A 288   OD1  92.1  62.3 144.3  64.4 147.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1030  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 419   O                                                      
REMARK 620 2 ASP A 413   OD1  77.1                                              
REMARK 620 3 ASP A 421   OD2 103.8  86.8                                        
REMARK 620 4 ASP A 421   OD1 113.6 147.1  60.7                                  
REMARK 620 5 ASP A 415   OD2 143.7  70.2  89.7 102.4                            
REMARK 620 6 ASN A 417   OD1  78.7  71.7 157.4 139.4  76.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 710  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   O                                                      
REMARK 620 2 ASP B 217   OD1  76.6                                              
REMARK 620 3 GLU B 220   OE2  92.7 163.6                                        
REMARK 620 4 ASP B 158   OD2 141.8  69.1 124.2                                  
REMARK 620 5 ASN B 215   OD1  88.8 110.0  81.8  87.5                            
REMARK 620 6 PRO B 219   O    93.0  58.5 110.6  83.3 167.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1027  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 232   OD1                                                    
REMARK 620 2 ASP A 234   OD1  75.2                                              
REMARK 620 3 ASP A 238   OD2  69.4 138.6                                        
REMARK 620 4 ASP A 238   OD1  90.5 141.4  60.7                                  
REMARK 620 5 ASP A 230   OD2  81.5  71.1  82.8 143.0                            
REMARK 620 6 ILE A 236   O   142.2  92.2 102.5 118.6  60.7                      
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 121.9                                              
REMARK 620 3 SER B 123   OG  149.1  79.2                                        
REMARK 620 4 SER B 121   OG  106.5  92.9  93.3                                  
REMARK 620 5 HOH B 802   O    94.7 142.1  63.2  84.9                            
REMARK 620 6 HOH B 801   O    78.5  96.7  76.7 164.6  80.1                      
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 126   OD1                                                    
REMARK 620 2 ASP B 127   OD1  89.0                                              
REMARK 620 3 ASP B 251   OD1 128.2 110.7                                        
REMARK 620 4 ASP B 251   OD2 148.5  61.4  61.3                                  
REMARK 620 5 ASP B 126   OD2  61.3  87.1 158.6 122.5                            
REMARK 620 6 SER B 123   O    63.2  88.7  69.6 103.0 124.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1031  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 599   OD1                                                    
REMARK 620 2 ASP A 599   OD2  61.2                                              
REMARK 620 3 GLU A 636   OE1 118.6 139.7                                        
REMARK 620 4 GLU A 636   OE2 132.5 152.8  61.0                                  
REMARK 620 5 CYS A 596   O    70.7 122.5  89.9  61.9                            
REMARK 620 6 VAL A 601   O    95.8  76.2 138.3  78.7  79.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1029  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 353   OD2                                                    
REMARK 620 2 ASP A 349   OD1 127.5                                              
REMARK 620 3 ASP A 357   OD1  95.6 134.2                                        
REMARK 620 4 ASP A 351   OD2  73.9  94.0 114.6                                  
REMARK 620 5 ASP A 353   OD1  60.9  70.7 134.1  97.0                            
REMARK 620 6 ASP A 357   OD2 145.7  84.0  60.8  92.8 153.4                      
REMARK 620 7 PHE A 355   O   104.1  67.9  89.4 156.0  63.0 100.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1027                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1028                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1029                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1030                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1031                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 708                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 709                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 710                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  44 RESIDUES 1001 TO 1004                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  260 RESIDUES 1005 TO 1006                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  266 RESIDUES 1007 TO 1012                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  458 RESIDUES 1013 TO 1016                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1017 BOUND   
REMARK 800  TO ASN A 524                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  585 RESIDUES 1018 TO 1019                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1020 BOUND   
REMARK 800  TO ASN A 674                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A1021 BOUND   
REMARK 800  TO ASN A 821                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  943 RESIDUES 1022 TO 1023                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  950 RESIDUES 1024 TO 1026                                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 701 BOUND   
REMARK 800  TO ASN B 99                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 702 BOUND   
REMARK 800  TO ASN B 320                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B   
REMARK 800  371 RESIDUES 703 TO 704                                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B   
REMARK 800  559 RESIDUES 705 TO 707                                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JV2   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHA-V COMPLEXED WITH A HIGH AFFINITY VARIANT OF FN10      
REMARK 900 RELATED ID: 1L5G   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHA-V COMPLEXED WITH A HIGH AFFINITY VARIANT OF FN10      
REMARK 900 RELATED ID: 3IJE   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHA-V COMPLEXED WITH A HIGH AFFINITY VARIANT OF FN10      
REMARK 900 RELATED ID: 4G1M   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHA-V COMPLEXED WITH A HIGH AFFINITY VARIANT OF FN10      
REMARK 900 RELATED ID: 4G1E   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHA-V COMPLEXED WITH A HIGH AFFINITY VARIANT OF FN10      
REMARK 900 RELATED ID: 4MMY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4MMZ   RELATED DB: PDB                                   
DBREF  4MMX A    1   959  UNP    P06756   ITAV_HUMAN      31    989             
DBREF  4MMX B    1   692  UNP    P05106   ITB3_HUMAN      27    718             
DBREF  4MMX C 1417  1509  UNP    P02751   FINC_HUMAN    1448   1540             
SEQADV 4MMX GLY C 1510  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMX LYS C 1511  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMX LYS C 1512  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMX GLY C 1513  UNP  P02751              EXPRESSION TAG                 
SEQADV 4MMX 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 GLY ARG GLY          
SEQRES   7 C   98  ASP SER PRO ALA SER SER LYS PRO ILE SER ILE ASN TYR          
SEQRES   8 C   98  ARG THR GLY LYS LYS GLY LYS                                  
MODRES 4MMX ASN A  266  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN A  943  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN A  260  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN A  585  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN A  458  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN A  950  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN B  559  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN A  821  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN A   44  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN A  524  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 4MMX ASN A  674  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1001      14                                                       
HET    NAG  A1002      14                                                       
HET    BMA  A1003      11                                                       
HET    MAN  A1004      11                                                       
HET    NAG  A1005      14                                                       
HET    NAG  A1006      14                                                       
HET    NAG  A1007      14                                                       
HET    NAG  A1008      14                                                       
HET    BMA  A1009      11                                                       
HET    MAN  A1010      11                                                       
HET    BMA  A1011      11                                                       
HET    MAN  A1012      11                                                       
HET    NAG  A1013      14                                                       
HET    NAG  A1014      14                                                       
HET    BMA  A1015      11                                                       
HET    MAN  A1016      11                                                       
HET    NAG  A1017      14                                                       
HET    NAG  A1018      14                                                       
HET    NAG  A1019      14                                                       
HET    NAG  A1020      14                                                       
HET    NAG  A1021      14                                                       
HET    NAG  A1022      14                                                       
HET    NAG  A1023      14                                                       
HET    NAG  A1024      14                                                       
HET    NAG  A1025      14                                                       
HET    BMA  A1026      11                                                       
HET     MN  A1027       1                                                       
HET     MN  A1028       1                                                       
HET     MN  A1029       1                                                       
HET     MN  A1030       1                                                       
HET     MN  A1031       1                                                       
HET    NAG  B 701      14                                                       
HET    NAG  B 702      14                                                       
HET    NAG  B 703      14                                                       
HET    NAG  B 704      14                                                       
HET    NAG  B 705      14                                                       
HET    NAG  B 706      14                                                       
HET    BMA  B 707      11                                                       
HET     MN  B 708       1                                                       
HET     MN  B 709       1                                                       
HET     MN  B 710       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   4  NAG    23(C8 H15 N O6)                                              
FORMUL   4  BMA    6(C6 H12 O6)                                                 
FORMUL   4  MAN    4(C6 H12 O6)                                                 
FORMUL  14   MN    8(MN 2+)                                                     
FORMUL  26  HOH   *2(H2 O)                                                      
HELIX    1   1 GLY A  175  GLN A  180  1                                   6    
HELIX    2   2 VAL A  188  LYS A  194  1                                   7    
HELIX    3   3 GLN A  214  ASP A  218  5                                   5    
HELIX    4   4 GLY A  366  LYS A  370  5                                   5    
HELIX    5   5 ASP A  544  PHE A  548  5                                   5    
HELIX    6   6 THR A  768  VAL A  772  5                                   5    
HELIX    7   7 ARG B    8  SER B   12  5                                   5    
HELIX    8   8 CYS B   13  ALA B   18  1                                   6    
HELIX    9   9 GLU B   42  ASP B   47  1                                   6    
HELIX   10  10 SER B  121  LYS B  125  5                                   5    
HELIX   11  11 ASP B  127  ILE B  131  5                                   5    
HELIX   12  12 LEU B  134  ARG B  143  1                                  10    
HELIX   13  13 PRO B  170  ASN B  175  1                                   6    
HELIX   14  14 TYR B  178  THR B  182  5                                   5    
HELIX   15  15 VAL B  200  LYS B  209  1                                  10    
HELIX   16  16 GLY B  222  CYS B  232  1                                  11    
HELIX   17  17 CYS B  232  GLY B  237  1                                   6    
HELIX   18  18 LEU B  258  LEU B  262  5                                   5    
HELIX   19  19 SER B  291  LYS B  302  1                                  12    
HELIX   20  20 VAL B  314  ILE B  325  1                                  12    
HELIX   21  21 SER B  338  ARG B  352  1                                  15    
HELIX   22  22 CYS B  435  ALA B  439  5                                   5    
HELIX   23  23 GLU B  534  GLY B  538  5                                   5    
HELIX   24  24 THR B  564  MET B  568  5                                   5    
HELIX   25  25 LEU B  573  GLY B  577  5                                   5    
HELIX   26  26 ALA B  607  LYS B  619  1                                  13    
HELIX   27  27 THR B  630  CYS B  635  1                                   6    
SHEET    1   A 4 LEU A   3  SER A  12  0                                        
SHEET    2   A 4 ARG A 431  ALA A 437 -1  O  ALA A 432   N  TYR A  11           
SHEET    3   A 4 ASP A 421  ALA A 426 -1  N  ALA A 426   O  ARG A 431           
SHEET    4   A 4 SER A 407  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  PHE A  35   N  PHE A  26           
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  ILE A  70 -1  O  GLN A  68   N  LYS A  58           
SHEET    1   C 2 ASP A  79  ALA A  81  0                                        
SHEET    2   C 2 ASP A  84  PRO A  85 -1  O  ASP A  84   N  TYR A  80           
SHEET    1   D 4 VAL A  98  LYS A 101  0                                        
SHEET    2   D 4 LYS A 104  ALA A 109 -1  O  LEU A 106   N  ARG A  99           
SHEET    3   D 4 THR A 127  ASP A 132 -1  O  THR A 127   N  ALA A 109           
SHEET    4   D 4 LYS A 135  TYR A 139 -1  O  VAL A 137   N  LEU A 130           
SHEET    1   E 4 SER A 160  PHE A 163  0                                        
SHEET    2   E 4 ARG A 168  GLY A 173 -1  O  LEU A 170   N  ASP A 162           
SHEET    3   E 4 GLN A 182  GLN A 187 -1  O  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 SER A 225  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  GLY A 348  0                                        
SHEET    2   I 4 ASP A 357  ALA A 362 -1  O  ASP A 357   N  GLY A 348           
SHEET    3   I 4 ILE A 372  PHE A 376 -1  O  TYR A 374   N  ILE A 360           
SHEET    4   I 4 GLN A 389  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 THR A 442  VAL A 449  0                                        
SHEET    2   K 4 SER A 471  ASP A 482 -1  O  ARG A 476   N  GLU A 448           
SHEET    3   K 4 GLN A 534  LEU A 542 -1  O  LEU A 542   N  SER A 471           
SHEET    4   K 4 ALA A 511  PHE A 513 -1  N  LEU A 512   O  TYR A 541           
SHEET    1   L 5 ILE A 453  LEU A 454  0                                        
SHEET    2   L 5 ASN A 585  ILE A 592  1  O  HIS A 591   N  LEU A 454           
SHEET    3   L 5 ILE A 555  TYR A 561 -1  N  ILE A 555   O  ALA A 590           
SHEET    4   L 5 LEU A 491  LEU A 498 -1  N  LEU A 498   O  PHE A 558           
SHEET    5   L 5 SER A 520  ILE A 527 -1  O  MET A 525   N  PHE A 493           
SHEET    1   M 4 LEU A 606  ASP A 611  0                                        
SHEET    2   M 4 ASN A 623  ASN A 633 -1  O  LYS A 630   N  SER A 609           
SHEET    3   M 4 THR A 691  VAL A 701 -1  O  PHE A 699   N  LEU A 625           
SHEET    4   M 4 ASP A 652  VAL A 656 -1  N  ILE A 654   O  ARG A 698           
SHEET    1   N 6 LYS A 616  TYR A 618  0                                        
SHEET    2   N 6 VAL A 730  ALA A 737  1  O  ALA A 737   N  ILE A 617           
SHEET    3   N 6 SER A 710  GLN A 718 -1  N  LEU A 715   O  VAL A 730           
SHEET    4   N 6 ALA A 641  SER A 646 -1  N  ILE A 644   O  GLN A 716           
SHEET    5   N 6 THR A 676  GLY A 684 -1  O  VAL A 679   N  VAL A 645           
SHEET    6   N 6 CYS A 668  GLU A 673 -1  N  ALA A 669   O  VAL A 680           
SHEET    1   O 4 VAL A 742  SER A 749  0                                        
SHEET    2   O 4 VAL A 775  ASN A 784 -1  O  GLU A 781   N  ARG A 745           
SHEET    3   O 4 SER A 894  LEU A 903 -1  O  ALA A 895   N  LEU A 782           
SHEET    4   O 4 LEU A 809  ASP A 817 -1  N  TYR A 810   O  LEU A 902           
SHEET    1   P 6 HIS A 752  LEU A 755  0                                        
SHEET    2   P 6 ILE A 941  TRP A 953  1  O  THR A 952   N  LEU A 755           
SHEET    3   P 6 SER A 917  GLU A 930 -1  N  LEU A 920   O  THR A 949           
SHEET    4   P 6 PHE A 790  TYR A 803 -1  N  HIS A 796   O  SER A 925           
SHEET    5   P 6 GLN A 878  LEU A 889 -1  O  CYS A 884   N  LEU A 795           
SHEET    6   P 6 MET A 820  SER A 824 -1  N  ASN A 821   O  GLN A 885           
SHEET    1   Q 4 ASN A 806  THR A 807  0                                        
SHEET    2   Q 4 PHE A 790  TYR A 803 -1  N  TYR A 803   O  ASN A 806           
SHEET    3   Q 4 SER A 917  GLU A 930 -1  O  SER A 925   N  HIS A 796           
SHEET    4   Q 4 ILE A 869  LEU A 872  1  N  HIS A 870   O  SER A 917           
SHEET    1   R 6 GLU B  60  GLU B  65  0                                        
SHEET    2   R 6 ARG B  87  LEU B  92 -1  O  ARG B  91   N  GLU B  60           
SHEET    3   R 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4   R 6 LYS B 412  PRO B 418 -1  N  ILE B 416   O  LEU B 425           
SHEET    5   R 6 VAL B 355  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6   R 6 SER B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1   S 4 VAL B  83  SER B  84  0                                        
SHEET    2   S 4 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3   S 4 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    4   S 4 LEU B 366  THR B 373 -1  N  THR B 373   O  SER B 396           
SHEET    1   T 6 LYS B 191  THR B 197  0                                        
SHEET    2   T 6 ARG B 150  PHE B 156 -1  N  ALA B 155   O  LYS B 191           
SHEET    3   T 6 VAL B 112  ASP B 119  1  N  TYR B 116   O  GLY B 154           
SHEET    4   T 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5   T 6 ILE B 304  THR B 311  1  O  ILE B 307   N  PHE B 248           
SHEET    6   T 6 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1   U 2 GLY B 540  SER B 543  0                                        
SHEET    2   U 2 ASP B 546  CYS B 549 -1  O  ASP B 546   N  SER B 543           
SHEET    1   V 2 TRP B 553  THR B 554  0                                        
SHEET    2   V 2 CYS B 560  THR B 561 -1  O  CYS B 560   N  THR B 554           
SHEET    1   W 2 GLY B 579  GLU B 582  0                                        
SHEET    2   W 2 SER B 585  CYS B 588 -1  O  VAL B 587   N  LYS B 580           
SHEET    1   X 4 ILE B 639  VAL B 642  0                                        
SHEET    2   X 4 LEU B 679  VAL B 682  1  O  LEU B 679   N  GLU B 640           
SHEET    3   X 4 VAL B 664  TYR B 670 -1  N  GLN B 668   O  TYR B 680           
SHEET    4   X 4 ALA B 652  LYS B 658 -1  N  TYR B 657   O  VAL B 665           
SHEET    1   Y 3 GLU C1424  VAL C1425  0                                        
SHEET    2   Y 3 LEU C1433  SER C1436 -1  O  SER C1436   N  GLU C1424           
SHEET    3   Y 3 THR C1471  ILE C1474 -1  O  ALA C1472   N  ILE C1435           
SHEET    1   Z 4 GLN C1461  PRO C1466  0                                        
SHEET    2   Z 4 TYR C1446  GLY C1452 -1  N  TYR C1447   O  VAL C1465           
SHEET    3   Z 4 TYR C1483  VAL C1490 -1  O  TYR C1488   N  ARG C1448           
SHEET    4   Z 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  2.03  
SSBOND   4 CYS A  461    CYS A  472                          1555   1555  2.03  
SSBOND   5 CYS A  478    CYS A  535                          1555   1555  2.03  
SSBOND   6 CYS A  596    CYS A  602                          1555   1555  2.03  
SSBOND   7 CYS A  668    CYS A  681                          1555   1555  2.03  
SSBOND   8 CYS A  822    CYS A  884                          1555   1555  2.03  
SSBOND   9 CYS A  874    CYS A  879                          1555   1555  2.03  
SSBOND  10 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND  11 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND  12 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND  13 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND  14 CYS B  177    CYS B  184                          1555   1555  2.03  
SSBOND  15 CYS B  232    CYS B  273                          1555   1555  2.03  
SSBOND  16 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  17 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  18 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  19 CYS B  448    CYS B  460                          1555   1555  2.03  
SSBOND  20 CYS B  462    CYS B  471                          1555   1555  2.03  
SSBOND  21 CYS B  473    CYS B  503                          1555   1555  2.03  
SSBOND  22 CYS B  486    CYS B  501                          1555   1555  2.04  
SSBOND  23 CYS B  495    CYS B  506                          1555   1555  2.03  
SSBOND  24 CYS B  508    CYS B  521                          1555   1555  2.04  
SSBOND  25 CYS B  523    CYS B  544                          1555   1555  2.03  
SSBOND  26 CYS B  528    CYS B  542                          1555   1555  2.03  
SSBOND  27 CYS B  536    CYS B  547                          1555   1555  2.03  
SSBOND  28 CYS B  549    CYS B  558                          1555   1555  2.03  
SSBOND  29 CYS B  560    CYS B  583                          1555   1555  2.03  
SSBOND  30 CYS B  567    CYS B  581                          1555   1555  2.03  
SSBOND  31 CYS B  575    CYS B  586                          1555   1555  2.03  
SSBOND  32 CYS B  588    CYS B  598                          1555   1555  2.03  
SSBOND  33 CYS B  601    CYS B  604                          1555   1555  2.03  
SSBOND  34 CYS B  608    CYS B  655                          1555   1555  2.03  
SSBOND  35 CYS B  614    CYS B  635                          1555   1555  2.03  
SSBOND  36 CYS B  617    CYS B  631                          1555   1555  2.03  
SSBOND  37 CYS B  663    CYS B  687                          1555   1555  2.03  
LINK         ND2 ASN A 266                 C1  NAG A1007     1555   1555  1.43  
LINK         ND2 ASN B 371                 C1  NAG B 703     1555   1555  1.44  
LINK         O4  NAG A1007                 C1  NAG A1008     1555   1555  1.44  
LINK         ND2 ASN A 943                 C1  NAG A1022     1555   1555  1.44  
LINK         O4  NAG A1001                 C1  NAG A1002     1555   1555  1.44  
LINK         ND2 ASN A 260                 C1  NAG A1005     1555   1555  1.44  
LINK         ND2 ASN A 585                 C1  NAG A1018     1555   1555  1.44  
LINK         O4  NAG A1002                 C1  BMA A1003     1555   1555  1.44  
LINK         ND2 ASN A 458                 C1  NAG A1013     1555   1555  1.44  
LINK         O4  NAG A1008                 C1  BMA A1009     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B 702     1555   1555  1.44  
LINK         O4  NAG A1013                 C1  NAG A1014     1555   1555  1.44  
LINK         O3  BMA A1009                 C1  MAN A1010     1555   1555  1.44  
LINK         O4  NAG B 703                 C1  NAG B 704     1555   1555  1.44  
LINK         ND2 ASN A 950                 C1  NAG A1024     1555   1555  1.44  
LINK         ND2 ASN B 559                 C1  NAG B 705     1555   1555  1.44  
LINK         O4  NAG A1024                 C1  NAG A1025     1555   1555  1.44  
LINK         O3  BMA A1015                 C1  MAN A1016     1555   1555  1.44  
LINK         ND2 ASN A 821                 C1  NAG A1021     1555   1555  1.44  
LINK         ND2 ASN A  44                 C1  NAG A1001     1555   1555  1.44  
LINK         O4  NAG A1005                 C1  NAG A1006     1555   1555  1.44  
LINK         O4  NAG A1014                 C1  BMA A1015     1555   1555  1.44  
LINK         ND2 ASN A 524                 C1  NAG A1017     1555   1555  1.44  
LINK         ND2 ASN B  99                 C1  NAG B 701     1555   1555  1.44  
LINK         O4  NAG A1018                 C1  NAG A1019     1555   1555  1.44  
LINK         O4  NAG A1025                 C1  BMA A1026     1555   1555  1.44  
LINK         O3  BMA A1003                 C1  MAN A1004     1555   1555  1.44  
LINK         O4  NAG A1022                 C1  NAG A1023     1555   1555  1.44  
LINK         O4  NAG B 706                 C1  BMA B 707     1555   1555  1.44  
LINK         O4  NAG B 705                 C1  NAG B 706     1555   1555  1.45  
LINK         ND2 ASN A 674                 C1  NAG A1020     1555   1555  1.45  
LINK         O6  BMA A1009                 C1  BMA A1011     1555   1555  1.45  
LINK         O4  BMA A1011                 C1  MAN A1012     1555   1555  1.45  
LINK         O   TYR A 290                MN    MN A1028     1555   1555  2.05  
LINK         O   TYR A 419                MN    MN A1030     1555   1555  2.08  
LINK         O   ASP B 217                MN    MN B 710     1555   1555  2.12  
LINK         OD1 ASN A 232                MN    MN A1027     1555   1555  2.13  
LINK         OD1 ASP B 217                MN    MN B 710     1555   1555  2.13  
LINK         OE1 GLU B 220                MN    MN B 708     1555   1555  2.13  
LINK         OD1 ASP C1495                MN    MN B 708     1555   1555  2.14  
LINK         OD1 ASP B 126                MN    MN B 709     1555   1555  2.14  
LINK         OD1 ASP B 127                MN    MN B 709     1555   1555  2.15  
LINK         OD1 ASP B 251                MN    MN B 709     1555   1555  2.15  
LINK         OD1 ASP A 413                MN    MN A1030     1555   1555  2.15  
LINK         OD2 ASP A 284                MN    MN A1028     1555   1555  2.15  
LINK         OD2 ASP B 251                MN    MN B 709     1555   1555  2.15  
LINK         OD1 ASP A 599                MN    MN A1031     1555   1555  2.16  
LINK         OD2 ASP A 353                MN    MN A1029     1555   1555  2.16  
LINK         OD1 ASP A 349                MN    MN A1029     1555   1555  2.16  
LINK         OD1 ASP A 234                MN    MN A1027     1555   1555  2.16  
LINK         OD2 ASP A 599                MN    MN A1031     1555   1555  2.16  
LINK         OE1 GLU A 636                MN    MN A1031     1555   1555  2.16  
LINK         OE2 GLU A 636                MN    MN A1031     1555   1555  2.16  
LINK         OD2 ASP B 126                MN    MN B 709     1555   1555  2.16  
LINK         OD1 ASP A 357                MN    MN A1029     1555   1555  2.16  
LINK         OD2 ASP A 351                MN    MN A1029     1555   1555  2.16  
LINK         OD1 ASP A 353                MN    MN A1029     1555   1555  2.16  
LINK         OD2 ASP A 238                MN    MN A1027     1555   1555  2.16  
LINK         OG  SER B 123                MN    MN B 708     1555   1555  2.16  
LINK         OD1 ASP A 238                MN    MN A1027     1555   1555  2.17  
LINK         OD2 ASP A 357                MN    MN A1029     1555   1555  2.17  
LINK         OD2 ASP A 421                MN    MN A1030     1555   1555  2.17  
LINK         OD1 ASP A 421                MN    MN A1030     1555   1555  2.17  
LINK         OD1 ASP A 292                MN    MN A1028     1555   1555  2.17  
LINK         OD1 ASN A 286                MN    MN A1028     1555   1555  2.17  
LINK         OE2 GLU B 220                MN    MN B 710     1555   1555  2.17  
LINK         OG  SER B 121                MN    MN B 708     1555   1555  2.17  
LINK         O   SER B 123                MN    MN B 709     1555   1555  2.17  
LINK         OD2 ASP A 292                MN    MN A1028     1555   1555  2.17  
LINK         OD2 ASP A 415                MN    MN A1030     1555   1555  2.18  
LINK         OD2 ASP B 158                MN    MN B 710     1555   1555  2.18  
LINK         OD1 ASN B 215                MN    MN B 710     1555   1555  2.18  
LINK         OD1 ASP A 288                MN    MN A1028     1555   1555  2.18  
LINK         OD2 ASP A 230                MN    MN A1027     1555   1555  2.18  
LINK         OD1 ASN A 417                MN    MN A1030     1555   1555  2.19  
LINK         O   CYS A 596                MN    MN A1031     1555   1555  2.20  
LINK         O   VAL A 601                MN    MN A1031     1555   1555  2.26  
LINK         O   ILE A 236                MN    MN A1027     1555   1555  2.29  
LINK         O   PHE A 355                MN    MN A1029     1555   1555  2.38  
LINK         O   PRO B 219                MN    MN B 710     1555   1555  2.41  
LINK        MN    MN B 708                 O   HOH B 802     1555   1555  2.19  
LINK        MN    MN B 708                 O   HOH B 801     1555   1555  2.20  
CISPEP   1 ASN A  685    PRO A  686          0        -0.21                     
CISPEP   2 SER A  749    PRO A  750          0        -0.98                     
CISPEP   3 LEU A  755    PRO A  756          0        -0.51                     
CISPEP   4 SER B   84    PRO B   85          0        -0.65                     
SITE     1 AC1  5 ASP A 230  ASN A 232  ASP A 234  ILE A 236                    
SITE     2 AC1  5 ASP A 238                                                     
SITE     1 AC2  5 ASP A 284  ASN A 286  ASP A 288  TYR A 290                    
SITE     2 AC2  5 ASP A 292                                                     
SITE     1 AC3  5 ASP A 349  ASP A 351  ASP A 353  PHE A 355                    
SITE     2 AC3  5 ASP A 357                                                     
SITE     1 AC4  5 ASP A 413  ASP A 415  ASN A 417  TYR A 419                    
SITE     2 AC4  5 ASP A 421                                                     
SITE     1 AC5  4 CYS A 596  ASP A 599  VAL A 601  GLU A 636                    
SITE     1 AC6  6 SER B 121  SER B 123  GLU B 220  HOH B 801                    
SITE     2 AC6  6 HOH B 802  ASP C1495                                          
SITE     1 AC7  4 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     1 AC8  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC8  5 GLU B 220                                                     
SITE     1 AC9  5 GLU A  15  GLY A  16  SER A  17  ASN A  44                    
SITE     2 AC9  5 GLU A  52                                                     
SITE     1 BC1  4 ASP A 257  LYS A 259  ASN A 260  SER A 262                    
SITE     1 BC2 11 ALA A 213  GLN A 214  PHE A 217  TYR A 254                    
SITE     2 BC2 11 SER A 263  LEU A 264  ASN A 266  ASN A 935                    
SITE     3 BC2 11 VAL C1444  ARG C1445  SER C1468                               
SITE     1 BC3  9 GLU A 448  TYR A 450  ASN A 458  THR A 460                    
SITE     2 BC3  9 CYS A 461  CYS A 472  ASN A 474  ARG A 476                    
SITE     3 BC3  9 ASN B  48                                                     
SITE     1 BC4  2 GLN A 494  ASN A 524                                          
SITE     1 BC5  3 PHE A 558  ALA A 584  ASN A 585                               
SITE     1 BC6  1 ASN A 674                                                     
SITE     1 BC7  2 PRO A 819  ASN A 821                                          
SITE     1 BC8  1 ASN A 943                                                     
SITE     1 BC9  3 ILE A 869  THR A 948  ASN A 950                               
SITE     1 CC1  2 ASN B  99  NAG B 703                                          
SITE     1 CC2  4 ARG A 248  ASN B 316  LEU B 317  ASN B 320                    
SITE     1 CC3  5 ASN B 371  SER B 398  ILE B 399  GLU B 400                    
SITE     2 CC3  5 NAG B 701                                                     
SITE     1 CC4  5 ASP A 621  PRO A 624  TYR B 531  TYR B 557                    
SITE     2 CC4  5 ASN B 559                                                     
CRYST1  129.859  129.859  305.831  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      0.007701  0.004446  0.000000        0.00000                         
SCALE2      0.000000  0.008892  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003270        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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