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Database: PDB
Entry: 4G1M
LinkDB: 4G1M
Original site: 4G1M 
HEADER    PROTEIN BINDING                         10-JUL-12   4G1M              
TITLE     RE-REFINEMENT OF ALPHA V BETA 3 STRUCTURE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-V;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: VITRONECTIN RECEPTOR SUBUNIT ALPHA, INTEGRIN ALPHA-V HEAVY  
COMPND   5 CHAIN, INTEGRIN ALPHA-V LIGHT CHAIN;                                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITGAV, MSK8, VNRA;                                             
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ITGB3, GP3A;                                                   
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    PROTEIN BINDING                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.SPRINGER,L.MI,J.ZHU                                               
REVDAT   2   19-DEC-12 4G1M    1       REMARK                                   
REVDAT   1   12-DEC-12 4G1M    0                                                
JRNL        AUTH   X.DONG,L.Z.MI,J.ZHU,W.WANG,P.HU,B.H.LUO,T.A.SPRINGER         
JRNL        TITL   ALPHA V BETA 3 INTEGRIN CRYSTAL STRUCTURES AND THEIR         
JRNL        TITL 2 FUNCTIONAL IMPLICATIONS                                      
JRNL        REF    BIOCHEMISTRY                  V.  51  8814 2012              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   23106217                                                     
JRNL        DOI    10.1021/BI300734N                                            
REMARK   0                                                                      
REMARK   0 ORIGINAL DATA REFERENCE 1                                            
REMARK   0  AUTH   J.P.XIONG,B.MAHALINGHAM,J.L.ALONSO,L.A.BORRELLI,X.RUI,       
REMARK   0  AUTH 2 S.ANAND,B.T.HYMAN,T.RYSIOK,D.MULLER-POMPALLA,S.L.GOODMAN,    
REMARK   0  AUTH 3 M.A.ARNAOUT                                                  
REMARK   0  TITL   CRYSTAL STRUCTURE OF THE COMPLETE INTEGRIN ALPHAVBETA3       
REMARK   0  TITL 2 ECTODOMAIN PLUS AN ALPHA/BETA TRANSMEMBRANE FRAGMENT.        
REMARK   0  REF    J.CELL BIOL.                  V. 186   589 2009              
REMARK   0  REFN                   ISSN 0021-9525                               
REMARK   0  PMID   19704023                                                     
REMARK   0  DOI    10.1083/JCB.200905085                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 62216                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2924                            
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 64.9513 -  7.9965    0.99     3276   141  0.1908 0.2438        
REMARK   3     2  7.9965 -  6.3488    1.00     3132   168  0.1936 0.2934        
REMARK   3     3  6.3488 -  5.5468    1.00     3087   160  0.1803 0.2345        
REMARK   3     4  5.5468 -  5.0398    1.00     3037   185  0.1489 0.2157        
REMARK   3     5  5.0398 -  4.6787    1.00     3034   175  0.1301 0.1799        
REMARK   3     6  4.6787 -  4.4029    1.00     3031   173  0.1262 0.1817        
REMARK   3     7  4.4029 -  4.1825    1.00     3040   138  0.1368 0.1859        
REMARK   3     8  4.1825 -  4.0004    1.00     3048   153  0.1480 0.1886        
REMARK   3     9  4.0004 -  3.8465    1.00     3059   167  0.1578 0.2228        
REMARK   3    10  3.8465 -  3.7137    1.00     3015   130  0.1668 0.2001        
REMARK   3    11  3.7137 -  3.5976    1.00     3030   137  0.1814 0.2519        
REMARK   3    12  3.5976 -  3.4948    1.00     3007   169  0.1976 0.2709        
REMARK   3    13  3.4948 -  3.4028    1.00     2983   152  0.2154 0.2792        
REMARK   3    14  3.4028 -  3.3198    1.00     3034   147  0.2261 0.2746        
REMARK   3    15  3.3198 -  3.2443    1.00     2979   166  0.2370 0.2504        
REMARK   3    16  3.2443 -  3.1753    0.99     2960   175  0.2486 0.3066        
REMARK   3    17  3.1753 -  3.1118    0.95     2865   141  0.2580 0.3077        
REMARK   3    18  3.1118 -  3.0530    0.87     2651   115  0.2894 0.3325        
REMARK   3    19  3.0530 -  2.9985    0.72     2170    98  0.3009 0.3854        
REMARK   3    20  2.9985 -  2.9477    0.54     1646    31  0.3269 0.4037        
REMARK   3    21  2.9477 -  2.9001    0.38     1208     3  0.3396 0.1623        
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)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.270           
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) : -7.03910                                             
REMARK   3    B22 (A**2) : -7.03910                                             
REMARK   3    B33 (A**2) : 14.07820                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          13385                                  
REMARK   3   ANGLE     :  0.734          18165                                  
REMARK   3   CHIRALITY :  0.049           2064                                  
REMARK   3   PLANARITY :  0.003           2323                                  
REMARK   3   DIHEDRAL  : 20.238           5096                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A and (resi 1:439 or resi 2004:2007)             
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2556  54.1612  19.8051              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3727 T22:   0.1819                                     
REMARK   3      T33:   0.1802 T12:  -0.1923                                     
REMARK   3      T13:  -0.0693 T23:   0.0552                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9677 L22:   1.4607                                     
REMARK   3      L33:   0.7473 L12:   0.9744                                     
REMARK   3      L13:   0.4739 L23:  -0.0645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3022 S12:   0.0953 S13:   0.1305                       
REMARK   3      S21:  -0.0900 S22:   0.2343 S23:   0.2460                       
REMARK   3      S31:  -0.1548 S32:   0.0565 S33:  -0.0503                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain A and resi 440:594                               
REMARK   3    ORIGIN FOR THE GROUP (A): -41.8577  47.8429  -7.6488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8273 T22:   0.7790                                     
REMARK   3      T33:   0.8100 T12:  -0.2794                                     
REMARK   3      T13:  -0.3631 T23:   0.1592                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8969 L22:  -0.0131                                     
REMARK   3      L33:   0.9471 L12:  -0.0615                                     
REMARK   3      L13:   0.3055 L23:  -0.6248                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3863 S12:   0.3195 S13:   0.2871                       
REMARK   3      S21:  -0.3795 S22:   0.1913 S23:   0.1863                       
REMARK   3      S31:   0.0214 S32:   0.0228 S33:  -0.0015                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain A and (resi 595:737 or resi 2008)                
REMARK   3    ORIGIN FOR THE GROUP (A): -51.6777  42.7438  23.4808              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5619 T22:   0.6010                                     
REMARK   3      T33:   0.3048 T12:   0.0556                                     
REMARK   3      T13:  -0.3905 T23:   0.1754                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7545 L22:  -0.2150                                     
REMARK   3      L33:   1.2924 L12:   0.0159                                     
REMARK   3      L13:  -1.0089 L23:   0.3016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5843 S12:  -0.1774 S13:  -0.1977                       
REMARK   3      S21:  -0.1177 S22:   0.1273 S23:   0.3341                       
REMARK   3      S31:   0.0071 S32:   0.4588 S33:  -0.0745                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain A and resi 738:960                               
REMARK   3    ORIGIN FOR THE GROUP (A): -25.0579  35.5477  73.3583              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6859 T22:   0.4486                                     
REMARK   3      T33:   0.3979 T12:   0.2250                                     
REMARK   3      T13:  -0.0278 T23:   0.0352                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8568 L22:   1.7316                                     
REMARK   3      L33:   0.4549 L12:  -0.5441                                     
REMARK   3      L13:   0.0289 L23:  -0.1951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1244 S12:  -0.0559 S13:  -0.1064                       
REMARK   3      S21:   0.3673 S22:   0.0790 S23:  -0.0395                       
REMARK   3      S31:  -0.1041 S32:  -0.0134 S33:  -0.0005                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain B and resi 1:57                                  
REMARK   3    ORIGIN FOR THE GROUP (A): -41.9575   4.8879   7.5694              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2301 T22:   0.7690                                     
REMARK   3      T33:   0.9930 T12:  -0.0557                                     
REMARK   3      T13:  -0.4349 T23:  -0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0219 L22:  -0.0102                                     
REMARK   3      L33:   0.0260 L12:   0.0054                                     
REMARK   3      L13:   0.0007 L23:  -0.0494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0066 S12:  -0.3458 S13:  -0.4230                       
REMARK   3      S21:  -0.8240 S22:   0.0225 S23:   0.5839                       
REMARK   3      S31:  -0.1495 S32:  -0.1287 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain B and (resi 58:108 or resi 353:435)              
REMARK   3    ORIGIN FOR THE GROUP (A): -14.3551   7.7759  26.9618              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8026 T22:   0.3401                                     
REMARK   3      T33:   0.5312 T12:  -0.1140                                     
REMARK   3      T13:   0.0006 T23:   0.0829                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7014 L22:   0.9047                                     
REMARK   3      L33:   1.0664 L12:   0.4736                                     
REMARK   3      L13:   0.1637 L23:  -0.0979                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0797 S12:   0.1047 S13:   0.0045                       
REMARK   3      S21:   0.0419 S22:  -0.0134 S23:  -0.2420                       
REMARK   3      S31:  -0.0168 S32:   0.0012 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain B and (resi 109:352 or resi 2001:2002)           
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5615  25.1941  35.4464              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4611 T22:   0.2733                                     
REMARK   3      T33:   0.5565 T12:  -0.1125                                     
REMARK   3      T13:  -0.1150 T23:   0.1038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8427 L22:   1.9372                                     
REMARK   3      L33:   1.2979 L12:   0.2304                                     
REMARK   3      L13:   0.2207 L23:  -0.5290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1205 S12:  -0.0160 S13:  -0.2796                       
REMARK   3      S21:   0.0747 S22:  -0.0298 S23:  -0.3445                       
REMARK   3      S31:   0.0364 S32:   0.0613 S33:   0.0024                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain B and resi 436:472                               
REMARK   3    ORIGIN FOR THE GROUP (A): -39.7084  10.1072  -8.9695              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6739 T22:   1.4797                                     
REMARK   3      T33:   1.2310 T12:  -0.3153                                     
REMARK   3      T13:  -0.3971 T23:   0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0385 L22:   0.0243                                     
REMARK   3      L33:   0.0096 L12:   0.0037                                     
REMARK   3      L13:  -0.0576 L23:   0.0416                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4180 S12:   0.4195 S13:  -0.4726                       
REMARK   3      S21:  -0.2731 S22:   0.4877 S23:  -0.1747                       
REMARK   3      S31:   0.3454 S32:   0.1078 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain B and resi 473:522                               
REMARK   3    ORIGIN FOR THE GROUP (A): -51.3768  23.3811   1.7905              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5395 T22:   0.9664                                     
REMARK   3      T33:   1.4454 T12:  -0.0457                                     
REMARK   3      T13:  -0.5299 T23:  -0.1002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0046 L22:  -0.0991                                     
REMARK   3      L33:   0.0460 L12:  -0.1010                                     
REMARK   3      L13:  -0.0753 L23:   0.0887                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3927 S12:   0.2653 S13:  -0.2074                       
REMARK   3      S21:  -0.4261 S22:  -0.3110 S23:   0.2576                       
REMARK   3      S31:   0.1006 S32:   0.1742 S33:   0.0001                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain B and resi 523:559                               
REMARK   3    ORIGIN FOR THE GROUP (A): -33.2651  28.2810  21.4200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7278 T22:   0.6561                                     
REMARK   3      T33:   1.3257 T12:  -0.0164                                     
REMARK   3      T13:  -0.2772 T23:  -0.0661                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0609 L22:   0.0600                                     
REMARK   3      L33:   0.0577 L12:   0.0317                                     
REMARK   3      L13:  -0.0414 L23:   0.0452                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7148 S12:  -0.3203 S13:   0.5304                       
REMARK   3      S21:   0.0148 S22:   0.0453 S23:   0.9259                       
REMARK   3      S31:  -0.1819 S32:   0.0590 S33:  -0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain B and resi 560:605                               
REMARK   3    ORIGIN FOR THE GROUP (A): -21.5381  26.2823  46.3162              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8134 T22:   0.6464                                     
REMARK   3      T33:   0.5495 T12:   0.0489                                     
REMARK   3      T13:   0.1262 T23:  -0.1365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1156 L22:   0.0045                                     
REMARK   3      L33:   0.1093 L12:  -0.0353                                     
REMARK   3      L13:   0.0215 L23:  -0.0441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2117 S12:   0.3263 S13:   0.2533                       
REMARK   3      S21:   0.3473 S22:   0.0221 S23:  -0.0343                       
REMARK   3      S31:   0.8403 S32:   0.1273 S33:  -0.0001                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain B and resi 606:695                               
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0673  13.4276  67.0664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7921 T22:   0.4919                                     
REMARK   3      T33:   0.8593 T12:   0.1571                                     
REMARK   3      T13:   0.0643 T23:   0.1167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1737 L22:   0.5426                                     
REMARK   3      L33:   0.2488 L12:   0.4308                                     
REMARK   3      L13:   0.3235 L23:   0.0110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0016 S12:   0.1602 S13:   0.2702                       
REMARK   3      S21:   0.0202 S22:   0.2580 S23:  -0.1413                       
REMARK   3      S31:   0.1675 S32:   0.0513 S33:  -0.0000                       
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 4G1M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073623.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSE                   
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66702                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG3350, 0.1M NA ACETATE, 0.8M       
REMARK 280  NACL, 2.5MM CACL2, PH 4.8, EVAPORATION, TEMPERATURE 298K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      203.93333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      101.96667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      101.96667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      203.93333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15500 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 75470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 57.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 837    C    O    CB   OG                                   
REMARK 470     ASP A 868    CG   OD1  OD2                                       
REMARK 470     PRO A 959    C    O    CB   CG   CD                              
REMARK 470     ASP B 692    C    O    CB   CG   OD1  OD2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  1007     O    HOH B  1040              2.10            
REMARK 500   ND2  ASN A   585     C2   NAG A  3585              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  63     -112.82     59.20                                   
REMARK 500    ALA A  81     -168.59   -161.77                                   
REMARK 500    GLN A 102     -119.75     59.86                                   
REMARK 500    THR A 116      165.31     66.69                                   
REMARK 500    ALA A 140       65.47   -152.24                                   
REMARK 500    ASP A 148      178.05     68.39                                   
REMARK 500    ALA A 166       35.08    -87.46                                   
REMARK 500    ASN A 206       49.51    -88.56                                   
REMARK 500    LEU A 264      -70.79   -115.88                                   
REMARK 500    ALA A 273       -0.63     66.92                                   
REMARK 500    ASP A 413       92.85    -66.56                                   
REMARK 500    ASN A 458       66.13   -101.76                                   
REMARK 500    THR A 460      -62.57    -99.86                                   
REMARK 500    GLN A 504     -155.88   -135.93                                   
REMARK 500    LYS A 551       25.82   -144.02                                   
REMARK 500    ASP A 570     -169.31    -75.72                                   
REMARK 500    PRO A 576     -176.64    -64.57                                   
REMARK 500    GLN A 634       37.20    -92.75                                   
REMARK 500    ASN A 674     -154.72     56.22                                   
REMARK 500    GLN A 703     -126.28   -122.82                                   
REMARK 500    GLU A 706     -145.82     60.50                                   
REMARK 500    MET A 707      109.18    -59.30                                   
REMARK 500    GLU A 767      -38.63   -135.71                                   
REMARK 500    LEU A 808     -105.75     53.91                                   
REMARK 500    SER A 836       28.90   -165.79                                   
REMARK 500    ASN A 910       54.79    -98.77                                   
REMARK 500    GLU A 912      -63.03     57.82                                   
REMARK 500    GLN A 914      -86.11    -82.48                                   
REMARK 500    ASN A 935       38.11    -93.51                                   
REMARK 500    SER B  77      -77.77    -66.13                                   
REMARK 500    PRO B  85     -166.37    -75.34                                   
REMARK 500    LYS B  98      114.74   -164.07                                   
REMARK 500    VAL B 157      -85.65   -132.05                                   
REMARK 500    PRO B 160       62.86    -69.51                                   
REMARK 500    THR B 182     -168.17   -163.94                                   
REMARK 500    SER B 213     -158.28   -125.03                                   
REMARK 500    LEU B 258      -12.96     80.90                                   
REMARK 500    HIS B 274       25.70   -144.64                                   
REMARK 500    TYR B 281       99.77    -69.94                                   
REMARK 500    PRO B 363      150.53    -49.32                                   
REMARK 500    ASN B 376     -112.53     51.53                                   
REMARK 500    LYS B 410      -78.62    -86.43                                   
REMARK 500    GLN B 440       41.14    -94.55                                   
REMARK 500    SER B 445     -139.18     46.36                                   
REMARK 500    HIS B 446      -98.13     54.05                                   
REMARK 500    ASN B 449     -160.31     54.16                                   
REMARK 500    CYS B 462     -176.38    -66.00                                   
REMARK 500    GLN B 470       59.81   -142.17                                   
REMARK 500    CYS B 471       67.40     61.98                                   
REMARK 500    GLU B 472      -92.50    -98.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      70 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 236   O                                                      
REMARK 620 2 ASN A 232   OD1 154.9                                              
REMARK 620 3 ASP A 234   OD1 111.0  81.2                                        
REMARK 620 4 ASP A 238   OD1  89.1  97.9 133.8                                  
REMARK 620 5 HOH A4001   O   122.5  82.1  68.2  66.0                            
REMARK 620 6 ASP A 230   OD2  81.1  74.8 101.6 122.9 156.0                      
REMARK 620 7 ASP A 238   OD2 103.7  65.7 145.2  47.3  95.6  80.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 290   O                                                      
REMARK 620 2 ASN A 286   OD1 176.5                                              
REMARK 620 3 HOH A4002   O    97.8  79.1                                        
REMARK 620 4 ASP A 284   OD2  95.7  87.8 146.1                                  
REMARK 620 5 ASP A 292   OD2  93.9  86.2 116.4  93.5                            
REMARK 620 6 ASP A 288   OD1 100.8  79.6  69.5  77.5 163.4                      
REMARK 620 7 ASP A 292   OD1  74.9 102.6  72.3 141.5  51.3 140.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 419   O                                                      
REMARK 620 2 ASP A 415   OD1 158.3                                              
REMARK 620 3 ASP A 413   OD1  78.4  81.0                                        
REMARK 620 4 ASN A 417   OD1  82.0  85.1  72.2                                  
REMARK 620 5 HOH A4004   O   123.4  71.2 142.6  80.7                            
REMARK 620 6 ASP A 421   OD2  81.8 119.6 144.9 133.0  72.4                      
REMARK 620 7 ASP A 421   OD1 109.2  83.8 108.1 168.7  93.6  52.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2008  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A 601   O                                                      
REMARK 620 2 ASP A 599   OD1  94.6                                              
REMARK 620 3 CYS A 596   O    76.3  80.7                                        
REMARK 620 4 GLU A 636   OE2 106.6 142.9  75.6                                  
REMARK 620 5 HOH A4006   O   161.0 104.4 106.2  57.2                            
REMARK 620 6 HOH A4005   O   110.6 109.0 167.0  91.7  63.6                      
REMARK 620 7 GLU A 636   OE1  71.6 163.4 104.1  52.8  89.7  69.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 127   OD1                                                    
REMARK 620 2 SER B 123   O    99.9                                              
REMARK 620 3 HOH B1033   O   147.2  87.4                                        
REMARK 620 4 MET B 335   O    77.6 169.6  89.5                                  
REMARK 620 5 ASP B 126   OD1  71.4  74.0  80.2  95.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 355   O                                                      
REMARK 620 2 ASP A 351   OD1 166.6                                              
REMARK 620 3 ASP A 353   OD1  79.2  92.3                                        
REMARK 620 4 ASP A 349   OD2  74.5  93.5  75.7                                  
REMARK 620 5 HOH A4003   O    83.3 104.6  74.8 145.8                            
REMARK 620 6 ASP A 357   OD2  88.7 104.5 138.2 139.1  64.0                      
REMARK 620 7 ASP A 357   OD1 106.4  80.2 168.0  95.3 116.0  53.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A3000  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 705   O                                                      
REMARK 620 2 MET A 707   O   133.6                                              
REMARK 620 3 ASP A 708   OD1 107.4  85.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 121   OG                                                     
REMARK 620 2 SER B 123   OG   83.9                                              
REMARK 620 3 ASP B 251   OD1 109.4  86.8                                        
REMARK 620 4 GLU B 220   OE2  67.9 151.5 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3044                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3045                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 3046                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3047                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3048                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3260                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3261                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3266                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3267                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 3268                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3269                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3270                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3271                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3272                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3458                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3459                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3524                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3525                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3585                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3586                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3674                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3805                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3821                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3822                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3943                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3944                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3950                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3951                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3099                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3321                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3452                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3559                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3560                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 3561                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3IJE   RELATED DB: PDB                                   
REMARK 900 RE-REFINEMENT OF ALPHA V BETA 3 STRUCTURE                            
REMARK 900 RELATED ID: 4G1E   RELATED DB: PDB                                   
REMARK 900 RELATED IN THE SAME PAPER                                            
DBREF  4G1M A    1   959  UNP    P06756   ITAV_HUMAN      31    989             
DBREF  4G1M B    1   692  UNP    P05106   ITB3_HUMAN      27    718             
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                                                  
MODRES 4G1M ASN A  943  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN A  260  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN A  266  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN A  950  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN A  674  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN A  524  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN A  821  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN A  585  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN A  458  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN B  559  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN A   44  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN A  805  ASN  GLYCOSYLATION SITE                                 
MODRES 4G1M ASN B  452  ASN  GLYCOSYLATION SITE                                 
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET     CA  A2008       1                                                       
HET    NAG  A3044      14                                                       
HET    NAG  A3045      14                                                       
HET    BMA  A3046      11                                                       
HET    MAN  A3047      11                                                       
HET    MAN  A3048      11                                                       
HET    NAG  A3260      14                                                       
HET    NAG  A3261      14                                                       
HET    NAG  A3266      14                                                       
HET    NAG  A3267      14                                                       
HET    BMA  A3268      11                                                       
HET    MAN  A3269      11                                                       
HET    MAN  A3270      11                                                       
HET    MAN  A3271      11                                                       
HET    MAN  A3272      11                                                       
HET    NAG  A3458      14                                                       
HET    NAG  A3459      14                                                       
HET    NAG  A3524      14                                                       
HET    NAG  A3525      14                                                       
HET    NAG  A3585      14                                                       
HET    NAG  A3586      14                                                       
HET    NAG  A3674      14                                                       
HET    NAG  A3805      14                                                       
HET    NAG  A3821      14                                                       
HET    NAG  A3822      14                                                       
HET    NAG  A3943      14                                                       
HET    NAG  A3944      14                                                       
HET    NAG  A3950      14                                                       
HET    NAG  A3951      14                                                       
HET     CA  B2001       1                                                       
HET     NA  A3000       1                                                       
HET     CA  B2002       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    NAG  B3452      14                                                       
HET    NAG  B3559      14                                                       
HET    NAG  B3560      14                                                       
HET    BMA  B3561      11                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      NA SODIUM ION                                                       
FORMUL   3   CA    7(CA 2+)                                                     
FORMUL   8  NAG    28(C8 H15 N O6)                                              
FORMUL   8  BMA    3(C6 H12 O6)                                                 
FORMUL   8  MAN    6(C6 H12 O6)                                                 
FORMUL  20   NA    NA 1+                                                        
FORMUL  27  HOH   *106(H2 O)                                                    
HELIX    1   1 GLY A  175  GLN A  180  1                                   6    
HELIX    2   2 VAL A  188  LYS A  194  1                                   7    
HELIX    3   3 GLN A  214  ASP A  218  5                                   5    
HELIX    4   4 ARG A  245  LEU A  250  1                                   6    
HELIX    5   5 GLY A  366  LYS A  370  5                                   5    
HELIX    6   6 PHE A  427  VAL A  429  5                                   3    
HELIX    7   7 THR A  768  GLY A  773  1                                   6    
HELIX    8   8 TRP A  904  ASN A  910  1                                   7    
HELIX    9   9 ILE B    4  GLY B    9  1                                   6    
HELIX   10  10 SER B   12  SER B   20  1                                   9    
HELIX   11  11 LYS B   41  ASP B   47  1                                   7    
HELIX   12  12 ALA B   50  GLU B   52  5                                   3    
HELIX   13  13 SER B  121  SER B  123  5                                   3    
HELIX   14  14 MET B  124  ILE B  131  1                                   8    
HELIX   15  15 ASN B  133  LYS B  144  1                                  12    
HELIX   16  16 PRO B  169  ASN B  175  1                                   7    
HELIX   17  17 VAL B  200  GLN B  210  1                                  11    
HELIX   18  18 GLY B  221  CYS B  232  1                                  12    
HELIX   19  19 CYS B  232  GLY B  237  1                                   6    
HELIX   20  20 LEU B  258  GLY B  264  5                                   7    
HELIX   21  21 TYR B  281  THR B  286  5                                   6    
HELIX   22  22 SER B  291  LYS B  302  1                                  12    
HELIX   23  23 VAL B  314  GLU B  323  1                                  10    
HELIX   24  24 ASN B  339  ARG B  352  1                                  14    
HELIX   25  25 CYS B  435  ALA B  439  5                                   5    
HELIX   26  26 PRO B  493  GLN B  497  5                                   5    
HELIX   27  27 GLU B  534  GLY B  538  5                                   5    
HELIX   28  28 THR B  564  MET B  568  5                                   5    
HELIX   29  29 ALA B  607  ASP B  621  1                                  15    
HELIX   30  30 GLY B  623  GLU B  628  1                                   6    
HELIX   31  31 THR B  630  CYS B  635  1                                   6    
SHEET    1   A 4 ALA A   9  SER A  12  0                                        
SHEET    2   A 4 ARG A 431  TYR A 435 -1  O  ALA A 432   N  TYR A  11           
SHEET    3   A 4 ASP A 421  ALA A 426 -1  N  ALA A 426   O  ARG A 431           
SHEET    4   A 4 SER A 407  THR A 412 -1  N  LYS A 409   O  ILE A 423           
SHEET    1   B 4 VAL A  23  PHE A  26  0                                        
SHEET    2   B 4 PHE A  35  ALA A  40 -1  O  LEU A  37   N  ASP A  24           
SHEET    3   B 4 GLN A  55  CYS A  59 -1  O  CYS A  59   N  LEU A  36           
SHEET    4   B 4 CYS A  67  PRO A  69 -1  O  GLN A  68   N  LYS A  58           
SHEET    1   C 2 ASP A  79  ALA A  81  0                                        
SHEET    2   C 2 ASP A  84  PRO A  85 -1  O  ASP A  84   N  TYR A  80           
SHEET    1   D 2 GLU A  87  PHE A  88  0                                        
SHEET    2   D 2 HIS A 113  TRP A 114 -1  O  HIS A 113   N  PHE A  88           
SHEET    1   E 4 VAL A  98  LYS A 101  0                                        
SHEET    2   E 4 LYS A 104  ALA A 109 -1  O  LEU A 106   N  ARG A  99           
SHEET    3   E 4 THR A 127  ASP A 132 -1  O  THR A 127   N  ALA A 109           
SHEET    4   E 4 LYS A 135  TYR A 139 -1  O  TYR A 139   N  CYS A 128           
SHEET    1   F 4 ILE A 161  PHE A 163  0                                        
SHEET    2   F 4 ARG A 168  GLY A 173 -1  O  LEU A 170   N  ASP A 162           
SHEET    3   F 4 GLN A 182  GLN A 187 -1  O  GLN A 182   N  GLY A 173           
SHEET    4   F 4 LEU A 208  ALA A 209 -1  O  LEU A 208   N  SER A 185           
SHEET    1   G 4 VAL A 226  GLY A 229  0                                        
SHEET    2   G 4 ASP A 238  VAL A 243 -1  O  ASP A 238   N  GLY A 229           
SHEET    3   G 4 MET A 252  TYR A 256 -1  O  MET A 252   N  VAL A 243           
SHEET    4   G 4 SER A 263  THR A 268 -1  O  LEU A 264   N  ILE A 255           
SHEET    1   H 4 VAL A 280  THR A 283  0                                        
SHEET    2   H 4 ASP A 292  ALA A 297 -1  O  PHE A 294   N  ALA A 281           
SHEET    3   H 4 GLN A 314  GLN A 320 -1  O  SER A 318   N  VAL A 293           
SHEET    4   H 4 PHE A 326  ASN A 332 -1  O  LEU A 331   N  VAL A 315           
SHEET    1   I 2 MET A 301  ARG A 303  0                                        
SHEET    2   I 2 LEU A 309  GLU A 311 -1  O  GLN A 310   N  ASP A 302           
SHEET    1   J 4 ILE A 344  GLY A 348  0                                        
SHEET    2   J 4 ASP A 357  ALA A 362 -1  O  ASP A 357   N  GLY A 348           
SHEET    3   J 4 ILE A 372  ARG A 379 -1  O  TYR A 374   N  ILE A 360           
SHEET    4   J 4 GLY A 382  LEU A 383 -1  O  GLY A 382   N  ARG A 379           
SHEET    1   K 4 ILE A 344  GLY A 348  0                                        
SHEET    2   K 4 ASP A 357  ALA A 362 -1  O  ASP A 357   N  GLY A 348           
SHEET    3   K 4 ILE A 372  ARG A 379 -1  O  TYR A 374   N  ILE A 360           
SHEET    4   K 4 GLN A 389  GLU A 392 -1  O  GLN A 389   N  ILE A 375           
SHEET    1   L 5 ALA A 511  PHE A 513  0                                        
SHEET    2   L 5 GLN A 534  LEU A 542 -1  O  TYR A 541   N  LEU A 512           
SHEET    3   L 5 PHE A 473  ASP A 482 -1  N  VAL A 475   O  LEU A 538           
SHEET    4   L 5 VAL A 440  TYR A 450 -1  N  TYR A 450   O  ASN A 474           
SHEET    5   L 5 ILE A 577  LEU A 578  1  O  ILE A 577   N  ILE A 441           
SHEET    1   M 5 ILE A 453  LEU A 454  0                                        
SHEET    2   M 5 ASN A 585  ILE A 592  1  O  HIS A 591   N  LEU A 454           
SHEET    3   M 5 ILE A 555  TYR A 561 -1  N  ILE A 555   O  ALA A 590           
SHEET    4   M 5 LYS A 490  LEU A 499 -1  N  LEU A 498   O  PHE A 558           
SHEET    5   M 5 SER A 520  SER A 528 -1  O  MET A 525   N  PHE A 493           
SHEET    1   N 4 LEU A 606  VAL A 610  0                                        
SHEET    2   N 4 ASP A 622  ASN A 633 -1  O  LYS A 630   N  SER A 609           
SHEET    3   N 4 GLN A 692  HIS A 702 -1  O  LEU A 697   N  LEU A 627           
SHEET    4   N 4 ALA A 651  VAL A 656 -1  N  GLY A 655   O  ARG A 698           
SHEET    1   O 6 ILE A 617  TYR A 618  0                                        
SHEET    2   O 6 VAL A 730  ALA A 737  1  O  ASP A 735   N  ILE A 617           
SHEET    3   O 6 SER A 710  GLN A 718 -1  N  LEU A 715   O  VAL A 730           
SHEET    4   O 6 ALA A 641  SER A 646 -1  N  SER A 646   O  ASP A 714           
SHEET    5   O 6 GLN A 678  GLY A 684 -1  O  VAL A 679   N  VAL A 645           
SHEET    6   O 6 SER A 667  LYS A 671 -1  N  ALA A 669   O  VAL A 680           
SHEET    1   P 4 VAL A 742  SER A 749  0                                        
SHEET    2   P 4 VAL A 775  ASN A 784 -1  O  GLU A 781   N  ARG A 745           
SHEET    3   P 4 LYS A 893  LEU A 903 -1  O  SER A 901   N  VAL A 776           
SHEET    4   P 4 LEU A 809  ASP A 817 -1  N  TYR A 810   O  LEU A 902           
SHEET    1   Q 6 HIS A 752  LEU A 755  0                                        
SHEET    2   Q 6 ILE A 941  TRP A 953  1  O  ASN A 950   N  VAL A 753           
SHEET    3   Q 6 SER A 917  GLU A 930 -1  N  SER A 922   O  VAL A 947           
SHEET    4   Q 6 LYS A 792  LYS A 802 -1  N  GLN A 798   O  SER A 923           
SHEET    5   Q 6 GLN A 878  VAL A 886 -1  O  VAL A 886   N  ALA A 793           
SHEET    6   Q 6 MET A 820  SER A 824 -1  N  THR A 823   O  VAL A 883           
SHEET    1   R 4 HIS A 752  LEU A 755  0                                        
SHEET    2   R 4 ILE A 941  TRP A 953  1  O  ASN A 950   N  VAL A 753           
SHEET    3   R 4 SER A 917  GLU A 930 -1  N  SER A 922   O  VAL A 947           
SHEET    4   R 4 ILE A 869  LEU A 872  1  N  HIS A 870   O  SER A 917           
SHEET    1   S 3 CYS B  38  LEU B  40  0                                        
SHEET    2   S 3 CYS B  23  CYS B  26 -1  N  ALA B  24   O  ASP B  39           
SHEET    3   S 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1   T 6 GLU B  60  GLU B  65  0                                        
SHEET    2   T 6 ARG B  87  LEU B  92 -1  O  ARG B  87   N  LEU B  64           
SHEET    3   T 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4   T 6 LYS B 412  PRO B 418 -1  N  PHE B 414   O  VAL B 427           
SHEET    5   T 6 VAL B 355  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6   T 6 SER B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1   U 5 VAL B  83  SER B  84  0                                        
SHEET    2   U 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3   U 5 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    4   U 5 LEU B 366  THR B 373 -1  N  THR B 373   O  SER B 396           
SHEET    5   U 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1   V 6 TYR B 190  THR B 197  0                                        
SHEET    2   V 6 LEU B 149  PHE B 156 -1  N  ILE B 151   O  THR B 197           
SHEET    3   V 6 VAL B 112  ASP B 119  1  N  MET B 118   O  GLY B 154           
SHEET    4   V 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5   V 6 ILE B 304  THR B 311  1  O  ALA B 309   N  PHE B 248           
SHEET    6   V 6 THR B 329  LEU B 333  1  O  LEU B 333   N  VAL B 310           
SHEET    1   W 2 PHE B 455  GLU B 456  0                                        
SHEET    2   W 2 VAL B 459  CYS B 460 -1  O  VAL B 459   N  GLU B 456           
SHEET    1   X 2 GLY B 499  CYS B 501  0                                        
SHEET    2   X 2 CYS B 506  CYS B 508 -1  O  VAL B 507   N  GLU B 500           
SHEET    1   Y 2 ILE B 516  THR B 517  0                                        
SHEET    2   Y 2 CYS B 523  ASP B 524 -1  O  CYS B 523   N  THR B 517           
SHEET    1   Z 2 GLY B 540  CYS B 542  0                                        
SHEET    2   Z 2 CYS B 547  CYS B 549 -1  O  LEU B 548   N  GLN B 541           
SHEET    1  AA 2 TRP B 553  THR B 554  0                                        
SHEET    2  AA 2 CYS B 560  THR B 561 -1  O  CYS B 560   N  THR B 554           
SHEET    1  AB 2 GLY B 579  GLU B 582  0                                        
SHEET    2  AB 2 SER B 585  CYS B 588 -1  O  VAL B 587   N  LYS B 580           
SHEET    1  AC 4 GLU B 638  VAL B 642  0                                        
SHEET    2  AC 4 ILE B 678  VAL B 682  1  O  VAL B 681   N  VAL B 642           
SHEET    3  AC 4 VAL B 664  TYR B 669 -1  N  GLN B 668   O  TYR B 680           
SHEET    4  AC 4 VAL B 653  LYS B 658 -1  N  CYS B 655   O  PHE B 667           
SSBOND   1 CYS A   59    CYS A   67                          1555   1555  2.04  
SSBOND   2 CYS A  108    CYS A  128                          1555   1555  2.04  
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  2.04  
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  2.04  
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  2.04  
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  2.03  
SSBOND  23 CYS B  495    CYS B  506                          1555   1555  2.03  
SSBOND  24 CYS B  508    CYS B  521                          1555   1555  2.03  
SSBOND  25 CYS B  523    CYS B  544                          1555   1555  2.04  
SSBOND  26 CYS B  528    CYS B  542                          1555   1555  2.03  
SSBOND  27 CYS B  536    CYS B  547                          1555   1555  2.04  
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  2.04  
SSBOND  33 CYS B  601    CYS B  604                          1555   1555  2.02  
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 943                 C1  NAG A3943     1555   1555  1.44  
LINK         O4  NAG A3044                 C1  NAG A3045     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         O4  NAG A3266                 C1  NAG A3267     1555   1555  1.44  
LINK         O4  NAG B3560                 C1  BMA B3561     1555   1555  1.44  
LINK         O4  NAG A3045                 C1  BMA A3046     1555   1555  1.44  
LINK         ND2 ASN A 260                 C1  NAG A3260     1555   1555  1.44  
LINK         ND2 ASN A 266                 C1  NAG A3266     1555   1555  1.44  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         ND2 ASN A 950                 C1  NAG A3950     1555   1555  1.44  
LINK         O4  NAG B3559                 C1  NAG B3560     1555   1555  1.44  
LINK         O6  BMA A3046                 C1  MAN A3047     1555   1555  1.44  
LINK         ND2 ASN A 674                 C1  NAG A3674     1555   1555  1.44  
LINK         O4  NAG A3585                 C1  NAG A3586     1555   1555  1.44  
LINK         ND2 ASN A 524                 C1  NAG A3524     1555   1555  1.44  
LINK         O4  NAG A3260                 C1  NAG A3261     1555   1555  1.44  
LINK         O3  BMA A3268                 C1  MAN A3269     1555   1555  1.44  
LINK         ND2 ASN A 821                 C1  NAG A3821     1555   1555  1.44  
LINK         O4  NAG A3267                 C1  BMA A3268     1555   1555  1.44  
LINK         O4  NAG A3950                 C1  NAG A3951     1555   1555  1.44  
LINK         ND2 ASN A 585                 C1  NAG A3585     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK         O3  MAN A3270                 C1  MAN A3271     1555   1555  1.44  
LINK         ND2 ASN A 458                 C1  NAG A3458     1555   1555  1.44  
LINK         O4  NAG A3524                 C1  NAG A3525     1555   1555  1.44  
LINK         O4  NAG A3943                 C1  NAG A3944     1555   1555  1.44  
LINK         O6  BMA A3268                 C1  MAN A3270     1555   1555  1.44  
LINK         ND2 ASN B 559                 C1  NAG B3559     1555   1555  1.44  
LINK         O4  NAG A3821                 C1  NAG A3822     1555   1555  1.44  
LINK         ND2 ASN A  44                 C1  NAG A3044     1555   1555  1.45  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.45  
LINK         ND2 ASN A 805                 C1  NAG A3805     1555   1555  1.45  
LINK         O4  NAG A3458                 C1  NAG A3459     1555   1555  1.45  
LINK         ND2 ASN B 452                 C1  NAG B3452     1555   1555  1.45  
LINK         O3  BMA A3046                 C1  MAN A3048     1555   1555  1.45  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.45  
LINK         O2  MAN A3269                 C1  MAN A3272     1555   1555  1.46  
LINK         O   ILE A 236                CA    CA A2004     1555   1555  2.14  
LINK         O   TYR A 290                CA    CA A2005     1555   1555  2.18  
LINK         O   TYR A 419                CA    CA A2007     1555   1555  2.19  
LINK         O   VAL A 601                CA    CA A2008     1555   1555  2.23  
LINK         OD1 ASP B 127                CA    CA B2002     1555   1555  2.25  
LINK         OD1 ASP A 415                CA    CA A2007     1555   1555  2.26  
LINK         O   PHE A 355                CA    CA A2006     1555   1555  2.28  
LINK         OD1 ASN A 286                CA    CA A2005     1555   1555  2.29  
LINK         OD1 ASP A 351                CA    CA A2006     1555   1555  2.30  
LINK         O   SER A 705                NA    NA A3000     1555   1555  2.31  
LINK         OD1 ASN A 232                CA    CA A2004     1555   1555  2.32  
LINK        CA    CA A2005                 O   HOH A4002     1555   1555  2.32  
LINK         OD1 ASP A 599                CA    CA A2008     1555   1555  2.32  
LINK         O   SER B 123                CA    CA B2002     1555   1555  2.34  
LINK         OD1 ASP A 353                CA    CA A2006     1555   1555  2.35  
LINK         OD1 ASP A 413                CA    CA A2007     1555   1555  2.35  
LINK         OD1 ASP A 234                CA    CA A2004     1555   1555  2.36  
LINK         OD2 ASP A 349                CA    CA A2006     1555   1555  2.36  
LINK         OG  SER B 121                CA    CA B2001     1555   1555  2.37  
LINK         OD1 ASN A 417                CA    CA A2007     1555   1555  2.37  
LINK         OD1 ASP A 238                CA    CA A2004     1555   1555  2.37  
LINK        CA    CA A2007                 O   HOH A4004     1555   1555  2.37  
LINK         O   CYS A 596                CA    CA A2008     1555   1555  2.39  
LINK         OD2 ASP A 284                CA    CA A2005     1555   1555  2.39  
LINK         OE2 GLU A 636                CA    CA A2008     1555   1555  2.39  
LINK        CA    CA B2002                 O   HOH B1033     1555   1555  2.39  
LINK         OD2 ASP A 292                CA    CA A2005     1555   1555  2.39  
LINK        CA    CA A2004                 O   HOH A4001     1555   1555  2.40  
LINK        CA    CA A2006                 O   HOH A4003     1555   1555  2.40  
LINK         OG  SER B 123                CA    CA B2001     1555   1555  2.40  
LINK        CA    CA A2008                 O   HOH A4006     1555   1555  2.40  
LINK         OD2 ASP A 421                CA    CA A2007     1555   1555  2.41  
LINK         OD2 ASP A 357                CA    CA A2006     1555   1555  2.42  
LINK        CA    CA A2008                 O   HOH A4005     1555   1555  2.42  
LINK         OD1 ASP A 288                CA    CA A2005     1555   1555  2.42  
LINK         OD1 ASP B 251                CA    CA B2001     1555   1555  2.44  
LINK         OD1 ASP A 357                CA    CA A2006     1555   1555  2.45  
LINK         O   MET B 335                CA    CA B2002     1555   1555  2.46  
LINK         OD1 ASP B 126                CA    CA B2002     1555   1555  2.46  
LINK         OD2 ASP A 230                CA    CA A2004     1555   1555  2.46  
LINK         OE1 GLU A 636                CA    CA A2008     1555   1555  2.54  
LINK         OD1 ASP A 421                CA    CA A2007     1555   1555  2.54  
LINK         O   MET A 707                NA    NA A3000     1555   1555  2.62  
LINK         OD1 ASP A 292                CA    CA A2005     1555   1555  2.65  
LINK         OD1 ASP A 708                NA    NA A3000     1555   1555  2.67  
LINK         OD2 ASP A 238                CA    CA A2004     1555   1555  2.94  
LINK         OE2 GLU B 220                CA    CA B2001     1555   1555  3.02  
CISPEP   1 TYR A  450    PRO A  451          0        -5.77                     
CISPEP   2 ASN A  685    PRO A  686          0         4.55                     
CISPEP   3 SER A  749    PRO A  750          0        -0.61                     
CISPEP   4 LEU A  755    PRO A  756          0        -0.78                     
CISPEP   5 SER B   84    PRO B   85          0        -1.08                     
CISPEP   6 SER B  162    PRO B  163          0         3.01                     
CISPEP   7 SER B  168    PRO B  169          0        -0.30                     
SITE     1 AC1  6 ASP A 230  ASN A 232  ASP A 234  ILE A 236                    
SITE     2 AC1  6 ASP A 238  HOH A4001                                          
SITE     1 AC2  6 ASP A 284  ASN A 286  ASP A 288  TYR A 290                    
SITE     2 AC2  6 ASP A 292  HOH A4002                                          
SITE     1 AC3  6 ASP A 349  ASP A 351  ASP A 353  PHE A 355                    
SITE     2 AC3  6 ASP A 357  HOH A4003                                          
SITE     1 AC4  6 ASP A 413  ASP A 415  ASN A 417  TYR A 419                    
SITE     2 AC4  6 ASP A 421  HOH A4004                                          
SITE     1 AC5  6 CYS A 596  ASP A 599  VAL A 601  GLU A 636                    
SITE     2 AC5  6 HOH A4005  HOH A4006                                          
SITE     1 AC6  6 GLU A  15  GLY A  16  LYS A  42  ASN A  44                    
SITE     2 AC6  6 GLU A  52  NAG A3045                                          
SITE     1 AC7  3 NAG A3044  BMA A3046  MAN A3047                               
SITE     1 AC8  3 NAG A3045  MAN A3047  MAN A3048                               
SITE     1 AC9  2 NAG A3045  BMA A3046                                          
SITE     1 BC1  1 BMA A3046                                                     
SITE     1 BC2  4 ASP A 257  LYS A 259  ASN A 260  NAG A3261                    
SITE     1 BC3  1 NAG A3260                                                     
SITE     1 BC4  6 PHE A 217  TYR A 254  SER A 263  LEU A 264                    
SITE     2 BC4  6 ASN A 266  NAG A3267                                          
SITE     1 BC5  5 ALA A 213  GLN A 214  PHE A 217  NAG A3266                    
SITE     2 BC5  5 BMA A3268                                                     
SITE     1 BC6  4 GLN A 214  NAG A3267  MAN A3269  MAN A3270                    
SITE     1 BC7  2 BMA A3268  MAN A3272                                          
SITE     1 BC8  2 BMA A3268  MAN A3271                                          
SITE     1 BC9  1 MAN A3270                                                     
SITE     1 CC1  1 MAN A3269                                                     
SITE     1 CC2  4 ASN A 458  THR A 460  CYS A 472  NAG A3459                    
SITE     1 CC3  1 NAG A3458                                                     
SITE     1 CC4  2 ASN A 524  NAG A3525                                          
SITE     1 CC5  1 NAG A3524                                                     
SITE     1 CC6  3 GLU A 560  ASN A 585  NAG A3586                               
SITE     1 CC7  1 NAG A3585                                                     
SITE     1 CC8  1 ASN A 674                                                     
SITE     1 CC9  2 ASN A 804  ASN A 805                                          
SITE     1 DC1  3 ASN A 821  GLY A 887  NAG A3822                               
SITE     1 DC2  1 NAG A3821                                                     
SITE     1 DC3  3 THR A 942  ASN A 943  NAG A3944                               
SITE     1 DC4  1 NAG A3943                                                     
SITE     1 DC5  4 ASP A 751  ILE A 869  ASN A 950  NAG A3951                    
SITE     1 DC6  1 NAG A3950                                                     
SITE     1 DC7  4 SER A 705  GLU A 706  MET A 707  ASP A 708                    
SITE     1 DC8  5 ASP B 119  SER B 121  SER B 123  GLU B 220                    
SITE     2 DC8  5 ASP B 251                                                     
SITE     1 DC9  5 SER B 123  ASP B 126  ASP B 127  MET B 335                    
SITE     2 DC9  5 HOH B1033                                                     
SITE     1 EC1  3 ASN B  99  NAG B3371  NAG B3372                               
SITE     1 EC2  6 ARG A 248  ASN B 316  LEU B 317  ASN B 320                    
SITE     2 EC2  6 HOH B1090  NAG B3321                                          
SITE     1 EC3  2 ARG A 248  NAG B3320                                          
SITE     1 EC4  5 ASN B 371  SER B 398  GLU B 400  NAG B3099                    
SITE     2 EC4  5 NAG B3372                                                     
SITE     1 EC5  2 NAG B3099  NAG B3371                                          
SITE     1 EC6  1 ASN B 452                                                     
SITE     1 EC7  4 TYR B 531  TYR B 557  ASN B 559  NAG B3560                    
SITE     1 EC8  4 PRO A 624  TYR B 557  NAG B3559  BMA B3561                    
SITE     1 EC9  1 NAG B3560                                                     
CRYST1  129.870  129.870  305.900  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007700  0.004446  0.000000        0.00000                         
SCALE2      0.000000  0.008891  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003269        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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