GenomeNet

Database: PDB
Entry: 4WJK
LinkDB: 4WJK
Original site: 4WJK 
HEADER    CELL ADHESION/IMMUNE SYSTEM             30-SEP-14   4WJK              
TITLE     METAL ION AND LIGAND BINDING OF INTEGRIN                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-5;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 42-493;                                       
COMPND   5 SYNONYM: CD49 ANTIGEN-LIKE FAMILY MEMBER E,FIBRONECTIN RECEPTOR      
COMPND   6 SUBUNIT ALPHA,INTEGRIN ALPHA-F,VLA-5;                                
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: INTEGRIN BETA-1;                                           
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 21-465;                                       
COMPND  13 SYNONYM: FIBRONECTIN RECEPTOR SUBUNIT BETA,GLYCOPROTEIN IIA,GPIIA,   
COMPND  14 VLA-4 SUBUNIT BETA;                                                  
COMPND  15 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: ITGA5, FNRA;                                                   
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: ITGB1, FNRB, MDF2, MSK12;                                      
SOURCE  15 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  16 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HEK 293                                 
KEYWDS    CELL ADHESION-IMMUNE SYSTEM COMPLEX                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.XIA,T.A.SPRINGER                                                    
REVDAT   4   22-NOV-17 4WJK    1       COMPND SOURCE JRNL   REMARK              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   24-DEC-14 4WJK    1       JRNL                                     
REVDAT   2   17-DEC-14 4WJK    1       JRNL                                     
REVDAT   1   03-DEC-14 4WJK    0                                                
JRNL        AUTH   W.XIA,T.A.SPRINGER                                           
JRNL        TITL   METAL ION AND LIGAND BINDING OF INTEGRIN ALPHA 5 BETA 1.     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111 17863 2014              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   25475857                                                     
JRNL        DOI    10.1073/PNAS.1420645111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1760)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.10                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 82685                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.420                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
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 47.1186 -  4.4574    0.96     5963   147  0.1459 0.1660        
REMARK   3     2  4.4574 -  3.5383    0.98     5835   145  0.1404 0.2135        
REMARK   3     3  3.5383 -  3.0912    0.98     5817   144  0.1752 0.2480        
REMARK   3     4  3.0912 -  2.8086    0.99     5833   145  0.1936 0.2448        
REMARK   3     5  2.8086 -  2.6073    0.99     5756   143  0.1975 0.2663        
REMARK   3     6  2.6073 -  2.4536    1.00     5842   144  0.1999 0.2307        
REMARK   3     7  2.4536 -  2.3307    1.00     5813   144  0.2090 0.2719        
REMARK   3     8  2.3307 -  2.2293    0.99     5776   143  0.2225 0.2259        
REMARK   3     9  2.2293 -  2.1434    1.00     5802   144  0.2338 0.2769        
REMARK   3    10  2.1434 -  2.0695    1.00     5766   142  0.2584 0.3228        
REMARK   3    11  2.0695 -  2.0048    1.00     5753   143  0.2893 0.3185        
REMARK   3    12  2.0048 -  1.9475    1.00     5783   143  0.3122 0.3348        
REMARK   3    13  1.9475 -  1.8962    0.98     5657   140  0.3748 0.4308        
REMARK   3    14  1.8962 -  1.8500    0.92     5291   131  0.3972 0.3963        
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)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.600           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           7292                                  
REMARK   3   ANGLE     :  1.063           9866                                  
REMARK   3   CHIRALITY :  0.040           1148                                  
REMARK   3   PLANARITY :  0.005           1258                                  
REMARK   3   DIHEDRAL  : 12.995           2686                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 66 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3827 -14.1925  22.4800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2120 T22:   0.4080                                     
REMARK   3      T33:   0.6312 T12:   0.0322                                     
REMARK   3      T13:   0.0357 T23:  -0.0480                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0704 L22:   1.8427                                     
REMARK   3      L33:   3.1591 L12:  -1.0834                                     
REMARK   3      L13:  -0.1988 L23:  -1.3253                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0296 S12:   0.0849 S13:  -0.4730                       
REMARK   3      S21:  -0.1728 S22:  -0.1011 S23:  -0.6874                       
REMARK   3      S31:   0.2499 S32:   0.3947 S33:   0.0964                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 108 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   9.1165   3.8130  10.1355              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3181 T22:   0.3623                                     
REMARK   3      T33:   0.4693 T12:  -0.0499                                     
REMARK   3      T13:   0.1388 T23:  -0.0215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6463 L22:   2.9297                                     
REMARK   3      L33:   4.4933 L12:  -0.1952                                     
REMARK   3      L13:   0.8563 L23:   0.0963                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0173 S12:   0.2888 S13:   0.4698                       
REMARK   3      S21:  -0.3792 S22:  -0.1043 S23:  -0.6837                       
REMARK   3      S31:  -0.6129 S32:   0.3413 S33:   0.2030                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 109 THROUGH 271 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2617  -5.1326   8.0789              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3418 T22:   0.3478                                     
REMARK   3      T33:   0.2133 T12:  -0.0317                                     
REMARK   3      T13:   0.0255 T23:  -0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2682 L22:   2.2206                                     
REMARK   3      L33:   1.8976 L12:  -0.0800                                     
REMARK   3      L13:  -0.6314 L23:   0.2207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0866 S12:   0.3926 S13:  -0.0464                       
REMARK   3      S21:  -0.5864 S22:   0.0540 S23:  -0.1575                       
REMARK   3      S31:  -0.0499 S32:  -0.0087 S33:   0.0325                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 272 THROUGH 350 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -17.4041 -17.0240  27.3224              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1878 T22:   0.2558                                     
REMARK   3      T33:   0.2905 T12:  -0.0410                                     
REMARK   3      T13:   0.0709 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5759 L22:   3.7525                                     
REMARK   3      L33:   1.8109 L12:   0.2029                                     
REMARK   3      L13:   0.5179 L23:   0.3896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1178 S12:  -0.0282 S13:  -0.3294                       
REMARK   3      S21:   0.1391 S22:   0.0169 S23:   0.1669                       
REMARK   3      S31:   0.2452 S32:  -0.1359 S33:   0.1585                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 351 THROUGH 397 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3113 -23.7523  30.5646              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2161 T22:   0.2529                                     
REMARK   3      T33:   0.3726 T12:   0.0333                                     
REMARK   3      T13:   0.0531 T23:   0.0392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3289 L22:   7.7692                                     
REMARK   3      L33:   3.7114 L12:   1.2640                                     
REMARK   3      L13:   0.8172 L23:   2.9521                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1448 S12:  -0.0633 S13:  -0.5080                       
REMARK   3      S21:   0.0985 S22:   0.1941 S23:  -0.5842                       
REMARK   3      S31:   0.3133 S32:   0.0778 S33:  -0.0947                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 398 THROUGH 431 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5549 -19.9826  30.9333              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1829 T22:   0.2821                                     
REMARK   3      T33:   0.4962 T12:   0.0276                                     
REMARK   3      T13:   0.0175 T23:   0.0696                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2281 L22:   5.3628                                     
REMARK   3      L33:   4.8294 L12:  -2.8424                                     
REMARK   3      L13:  -0.7433 L23:  -0.4801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2504 S12:  -0.0901 S13:  -0.4324                       
REMARK   3      S21:   0.0304 S22:   0.0993 S23:  -0.6110                       
REMARK   3      S31:   0.1517 S32:   0.2849 S33:   0.0156                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 432 THROUGH 452 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4400 -21.6296  29.7495              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3364 T22:   0.3339                                     
REMARK   3      T33:   0.6635 T12:   0.0447                                     
REMARK   3      T13:  -0.0314 T23:   0.0646                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2772 L22:   0.3343                                     
REMARK   3      L33:   1.4728 L12:  -0.2500                                     
REMARK   3      L13:   0.0049 L23:   0.5969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0826 S12:  -0.1840 S13:  -0.6659                       
REMARK   3      S21:   0.5541 S22:  -0.1183 S23:  -1.4234                       
REMARK   3      S31:   0.3683 S32:   0.2256 S33:  -0.0213                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 132 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -25.9844 -13.7106  66.3143              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7803 T22:   0.4797                                     
REMARK   3      T33:   0.4892 T12:   0.0249                                     
REMARK   3      T13:   0.0128 T23:   0.0645                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2174 L22:   4.0821                                     
REMARK   3      L33:   1.3841 L12:  -0.3011                                     
REMARK   3      L13:   0.2125 L23:  -2.2870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1002 S12:  -0.5153 S13:  -0.4268                       
REMARK   3      S21:   0.7899 S22:   0.3292 S23:   0.6737                       
REMARK   3      S31:  -0.0015 S32:  -0.0349 S33:  -0.3856                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 133 THROUGH 318 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7932  15.2374  34.8913              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2054 T22:   0.2094                                     
REMARK   3      T33:   0.2557 T12:  -0.0196                                     
REMARK   3      T13:  -0.0124 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8152 L22:   1.9447                                     
REMARK   3      L33:   1.4809 L12:  -0.4795                                     
REMARK   3      L13:  -0.8263 L23:   0.7966                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1073 S12:  -0.0186 S13:   0.3242                       
REMARK   3      S21:  -0.1441 S22:   0.0285 S23:  -0.0796                       
REMARK   3      S31:  -0.2317 S32:   0.0637 S33:  -0.1361                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 319 THROUGH 373 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -28.7476   5.7897  39.0388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1471 T22:   0.2461                                     
REMARK   3      T33:   0.2976 T12:  -0.0203                                     
REMARK   3      T13:  -0.0281 T23:  -0.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4270 L22:   3.7879                                     
REMARK   3      L33:   3.9964 L12:  -0.9127                                     
REMARK   3      L13:   0.0620 L23:  -1.5156                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0321 S12:   0.0250 S13:  -0.0704                       
REMARK   3      S21:   0.1525 S22:   0.0759 S23:   0.3725                       
REMARK   3      S31:   0.0486 S32:  -0.1690 S33:  -0.1408                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 374 THROUGH 411 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -36.2201  -4.9253  54.5319              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4741 T22:   0.3968                                     
REMARK   3      T33:   0.8496 T12:  -0.0442                                     
REMARK   3      T13:   0.1205 T23:   0.0862                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0752 L22:   5.4700                                     
REMARK   3      L33:   4.6897 L12:  -4.6878                                     
REMARK   3      L13:   3.0717 L23:  -3.1040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6323 S12:  -0.3243 S13:  -0.3421                       
REMARK   3      S21:  -0.0478 S22:   0.3342 S23:   1.4194                       
REMARK   3      S31:   0.4205 S32:  -0.4460 S33:  -0.7751                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 412 THROUGH 445 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.0387 -11.4574  62.4467              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6851 T22:   0.4348                                     
REMARK   3      T33:   0.4097 T12:   0.1004                                     
REMARK   3      T13:  -0.1069 T23:  -0.0365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4776 L22:   3.9206                                     
REMARK   3      L33:   5.9082 L12:   1.0104                                     
REMARK   3      L13:  -1.5348 L23:  -2.4177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1530 S12:  -0.3288 S13:  -0.7215                       
REMARK   3      S21:   0.6529 S22:  -0.2172 S23:  -0.7058                       
REMARK   3      S31:   0.3359 S32:   0.9689 S33:   0.0260                       
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 4WJK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203919.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82697                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.103                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5500                             
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES 7.2, 16% PEG 6000, PH 7.2,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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 -1.000000  0.000000  0.000000       26.06500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.74500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.37500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.74500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.06500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.37500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 9610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 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     GLN B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     SER B    31                                                      
REMARK 465     THR B    32                                                      
REMARK 465     PHE B    33                                                      
REMARK 465     LEU B    34                                                      
REMARK 465     GLN B    35                                                      
REMARK 465     GLU B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     LYS B    53                                                      
REMARK 465     GLY B    54                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     SER B    79                                                      
REMARK 465     LYS B    80                                                      
REMARK 465     GLY B    81                                                      
REMARK 465     THR B    82                                                      
REMARK 465     ALA B    83                                                      
REMARK 465     GLU B    84                                                      
REMARK 465     LYS B    85                                                      
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   700     O    HOH B   748              2.02            
REMARK 500   O    HOH A   753     O    HOH A   870              2.04            
REMARK 500   O    HOH B   707     O    HOH B   763              2.07            
REMARK 500   O    HOH B   694     O    HOH B   772              2.09            
REMARK 500   O    HOH B   712     O    HOH B   772              2.10            
REMARK 500   O    HOH B   734     O    HOH B   748              2.11            
REMARK 500   O    HOH A   605     O    HOH A   616              2.12            
REMARK 500   ND2  ASN B   343     O5   NAG B   512              2.12            
REMARK 500   O    HOH A   845     O    HOH A   860              2.14            
REMARK 500   O2   MAN B   511     O    HOH B   601              2.15            
REMARK 500   O    HOH B   700     O    HOH B   734              2.16            
REMARK 500   O    HOH A   707     O    HOH A   864              2.17            
REMARK 500   OE1  GLU B   308     O    HOH B   602              2.17            
REMARK 500   O    HOH A   728     O    HOH A   753              2.18            
REMARK 500   O    HOH A   824     O    HOH B   731              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   601     O    HOH B   610     1455     2.15            
REMARK 500   O    HOH A   622     O    HOH B   618     1655     2.19            
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    ALA A   7       58.54   -141.50                                   
REMARK 500    ARG A  27       82.80   -150.51                                   
REMARK 500    SER A  85     -116.76    -95.51                                   
REMARK 500    SER A  86     -111.24     57.85                                   
REMARK 500    SER A  87      -35.95   -176.48                                   
REMARK 500    THR A 123      161.70     69.10                                   
REMARK 500    LYS A 125     -120.73    -97.05                                   
REMARK 500    TRP A 157      175.52     66.67                                   
REMARK 500    ASN A 211       75.13   -107.47                                   
REMARK 500    ASP A 243     -157.87   -108.51                                   
REMARK 500    ILE A 270       15.52     49.44                                   
REMARK 500    VAL A 321      -37.93   -136.08                                   
REMARK 500    SER A 409     -168.84   -111.75                                   
REMARK 500    ASN B  62       75.95   -151.19                                   
REMARK 500    ASN B  72       48.68   -150.48                                   
REMARK 500    VAL B 168      -76.67   -128.49                                   
REMARK 500    THR B 171       52.52    -97.87                                   
REMARK 500    CYS B 187     -162.71   -100.28                                   
REMARK 500    ASN B 192       55.28   -110.25                                   
REMARK 500    SER B 222     -161.03   -127.15                                   
REMARK 500    LEU B 225      -60.71    -98.85                                   
REMARK 500    CYS B 415       93.02     62.10                                   
REMARK 500    LYS B 417      179.69     61.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 863        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH B 815        DISTANCE =  6.47 ANGSTROMS                       
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 A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 239   OE1                                                    
REMARK 620 2 GLU A 239   OE2  52.6                                              
REMARK 620 3 SER A 241   OG  129.6  77.1                                        
REMARK 620 4 ASP A 243   OD1  83.5  71.9  82.8                                  
REMARK 620 5 THR A 245   O    65.9 116.1 159.9  87.1                            
REMARK 620 6 ASP A 247   OD1 120.3 131.7  89.7 152.9  91.5                      
REMARK 620 7 ASP A 247   OD2  78.4  81.1  93.3 152.9 103.5  53.1                
REMARK 620 8 HOH A 650   O   146.5 140.7  75.3  77.5  85.6  75.5 127.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 293   OD1                                                    
REMARK 620 2 ASN A 295   OD1  73.8                                              
REMARK 620 3 ASP A 297   OD1  79.8  81.7                                        
REMARK 620 4 LEU A 299   O    82.6 156.3  95.6                                  
REMARK 620 5 ASP A 301   OD1 132.0 108.1 148.0  86.7                            
REMARK 620 6 ASP A 301   OD2  82.2  81.8 158.3  93.9  52.0                      
REMARK 620 7 HOH A 648   O   148.9  82.5  77.0 120.0  74.2 114.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 360   OD1                                                    
REMARK 620 2 ASP A 362   OD1  79.4                                              
REMARK 620 3 ASP A 364   OD1  72.4  88.1                                        
REMARK 620 4 TYR A 366   O    74.2 153.6  84.9                                  
REMARK 620 5 ASP A 368   OD1 135.1 108.7 148.9  89.7                            
REMARK 620 6 ASP A 368   OD2  87.4  80.4 158.3  97.3  52.8                      
REMARK 620 7 HOH A 649   O   149.4 104.4  77.4  98.8  73.3 123.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 424   OD1                                                    
REMARK 620 2 ASP A 426   OD1  78.1                                              
REMARK 620 3 ASN A 428   OD1  89.5  89.5                                        
REMARK 620 4 TYR A 430   O    78.2 156.1  86.8                                  
REMARK 620 5 ASP A 432   OD1 129.0 113.1 137.4  84.9                            
REMARK 620 6 ASP A 432   OD2  87.3  78.6 168.1 103.7  50.7                      
REMARK 620 7 HOH A 651   O   157.4  81.6  80.1 120.8  68.9  98.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 132   OG                                                     
REMARK 620 2 GLU B 229   OE1  86.5                                              
REMARK 620 3 HOH B 617   O    96.0 175.9                                        
REMARK 620 4 HOH B 664   O   169.5  89.4  88.7                                  
REMARK 620 5 HOH B 663   O    97.0  92.2  84.3  92.8                            
REMARK 620 6 HOH B 665   O    76.2  98.6  85.2  94.9 166.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 134   O                                                      
REMARK 620 2 ASP B 137   OD1  74.0                                              
REMARK 620 3 ASP B 137   OD2 119.4  50.8                                        
REMARK 620 4 ASP B 138   OD1  91.5  72.3  93.3                                  
REMARK 620 5 ALA B 342   O   165.7 118.8  74.9  87.0                            
REMARK 620 6 HOH B 648   O    82.3  96.8  81.7 168.7 101.4                      
REMARK 620 7 HOH B 661   O    85.3 157.5 151.6 100.2  80.9  88.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 169   OE1                                                    
REMARK 620 2 ASN B 224   OD1 104.3                                              
REMARK 620 3 ASP B 226   O   161.8  86.4                                        
REMARK 620 4 ASP B 226   OD1  88.3 101.7  75.0                                  
REMARK 620 5 PRO B 228   O    82.2 167.4  90.3  89.1                            
REMARK 620 6 GLU B 229   OE2 100.3  85.4  95.1 167.2  82.8                      
REMARK 620 N                    1     2     3     4     5                       
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  514 through MAN A 520 bound to ASN A 43                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  511 through BMA A 513 bound to ASN A 256                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  521 through NAG A 522 bound to ASN A 266                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  505 through MAN A 510 bound to ASN A 275                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  504 through NAG B 505 bound to ASN B 249                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 512 bound   
REMARK 800  to ASN B 343                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  506 through NAG B 507 bound to ASN B 386                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  508 through MAN B 511 bound to ASN B 397                            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WK0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WK2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WK4   RELATED DB: PDB                                   
DBREF  4WJK A    1   452  UNP    P08648   ITA5_HUMAN      42    493             
DBREF  4WJK B    1   445  UNP    P05556   ITB1_HUMAN      21    465             
SEQADV 4WJK VAL A  451  UNP  P08648    ILE   492 ENGINEERED MUTATION            
SEQADV 4WJK THR B  195  UNP  P05556    SER   215 CONFLICT                       
SEQRES   1 A  452  PHE ASN LEU ASP ALA GLU ALA PRO ALA VAL LEU SER GLY          
SEQRES   2 A  452  PRO PRO GLY SER PHE PHE GLY PHE SER VAL GLU PHE TYR          
SEQRES   3 A  452  ARG PRO GLY THR ASP GLY VAL SER VAL LEU VAL GLY ALA          
SEQRES   4 A  452  PRO LYS ALA ASN THR SER GLN PRO GLY VAL LEU GLN GLY          
SEQRES   5 A  452  GLY ALA VAL TYR LEU CYS PRO TRP GLY ALA SER PRO THR          
SEQRES   6 A  452  GLN CYS THR PRO ILE GLU PHE ASP SER LYS GLY SER ARG          
SEQRES   7 A  452  LEU LEU GLU SER SER LEU SER SER SER GLU GLY GLU GLU          
SEQRES   8 A  452  PRO VAL GLU TYR LYS SER LEU GLN TRP PHE GLY ALA THR          
SEQRES   9 A  452  VAL ARG ALA HIS GLY SER SER ILE LEU ALA CYS ALA PRO          
SEQRES  10 A  452  LEU TYR SER TRP ARG THR GLU LYS GLU PRO LEU SER ASP          
SEQRES  11 A  452  PRO VAL GLY THR CYS TYR LEU SER THR ASP ASN PHE THR          
SEQRES  12 A  452  ARG ILE LEU GLU TYR ALA PRO CYS ARG SER ASP PHE SER          
SEQRES  13 A  452  TRP ALA ALA GLY GLN GLY TYR CYS GLN GLY GLY PHE SER          
SEQRES  14 A  452  ALA GLU PHE THR LYS THR GLY ARG VAL VAL LEU GLY GLY          
SEQRES  15 A  452  PRO GLY SER TYR PHE TRP GLN GLY GLN ILE LEU SER ALA          
SEQRES  16 A  452  THR GLN GLU GLN ILE ALA GLU SER TYR TYR PRO GLU TYR          
SEQRES  17 A  452  LEU ILE ASN LEU VAL GLN GLY GLN LEU GLN THR ARG GLN          
SEQRES  18 A  452  ALA SER SER ILE TYR ASP ASP SER TYR LEU GLY TYR SER          
SEQRES  19 A  452  VAL ALA VAL GLY GLU PHE SER GLY ASP ASP THR GLU ASP          
SEQRES  20 A  452  PHE VAL ALA GLY VAL PRO LYS GLY ASN LEU THR TYR GLY          
SEQRES  21 A  452  TYR VAL THR ILE LEU ASN GLY SER ASP ILE ARG SER LEU          
SEQRES  22 A  452  TYR ASN PHE SER GLY GLU GLN MET ALA SER TYR PHE GLY          
SEQRES  23 A  452  TYR ALA VAL ALA ALA THR ASP VAL ASN GLY ASP GLY LEU          
SEQRES  24 A  452  ASP ASP LEU LEU VAL GLY ALA PRO LEU LEU MET ASP ARG          
SEQRES  25 A  452  THR PRO ASP GLY ARG PRO GLN GLU VAL GLY ARG VAL TYR          
SEQRES  26 A  452  VAL TYR LEU GLN HIS PRO ALA GLY ILE GLU PRO THR PRO          
SEQRES  27 A  452  THR LEU THR LEU THR GLY HIS ASP GLU PHE GLY ARG PHE          
SEQRES  28 A  452  GLY SER SER LEU THR PRO LEU GLY ASP LEU ASP GLN ASP          
SEQRES  29 A  452  GLY TYR ASN ASP VAL ALA ILE GLY ALA PRO PHE GLY GLY          
SEQRES  30 A  452  GLU THR GLN GLN GLY VAL VAL PHE VAL PHE PRO GLY GLY          
SEQRES  31 A  452  PRO GLY GLY LEU GLY SER LYS PRO SER GLN VAL LEU GLN          
SEQRES  32 A  452  PRO LEU TRP ALA ALA SER HIS THR PRO ASP PHE PHE GLY          
SEQRES  33 A  452  SER ALA LEU ARG GLY GLY ARG ASP LEU ASP GLY ASN GLY          
SEQRES  34 A  452  TYR PRO ASP LEU ILE VAL GLY SER PHE GLY VAL ASP LYS          
SEQRES  35 A  452  ALA VAL VAL TYR ARG GLY ARG PRO VAL VAL                      
SEQRES   1 B  445  GLN THR ASP GLU ASN ARG CYS LEU LYS ALA ASN ALA LYS          
SEQRES   2 B  445  SER CYS GLY GLU CYS ILE GLN ALA GLY PRO ASN CYS GLY          
SEQRES   3 B  445  TRP CYS THR ASN SER THR PHE LEU GLN GLU GLY MET PRO          
SEQRES   4 B  445  THR SER ALA ARG CYS ASP ASP LEU GLU ALA LEU LYS LYS          
SEQRES   5 B  445  LYS GLY CYS PRO PRO ASP ASP ILE GLU ASN PRO ARG GLY          
SEQRES   6 B  445  SER LYS ASP ILE LYS LYS ASN LYS ASN VAL THR ASN ARG          
SEQRES   7 B  445  SER LYS GLY THR ALA GLU LYS LEU LYS PRO GLU ASP ILE          
SEQRES   8 B  445  THR GLN ILE GLN PRO GLN GLN LEU VAL LEU ARG LEU ARG          
SEQRES   9 B  445  SER GLY GLU PRO GLN THR PHE THR LEU LYS PHE LYS ARG          
SEQRES  10 B  445  ALA GLU ASP TYR PRO ILE ASP LEU TYR TYR LEU MET ASP          
SEQRES  11 B  445  LEU SER TYR SER MET LYS ASP ASP LEU GLU ASN VAL LYS          
SEQRES  12 B  445  SER LEU GLY THR ASP LEU MET ASN GLU MET ARG ARG ILE          
SEQRES  13 B  445  THR SER ASP PHE ARG ILE GLY PHE GLY SER PHE VAL GLU          
SEQRES  14 B  445  LYS THR VAL MET PRO TYR ILE SER THR THR PRO ALA LYS          
SEQRES  15 B  445  LEU ARG ASN PRO CYS THR SER GLU GLN ASN CYS THR THR          
SEQRES  16 B  445  PRO PHE SER TYR LYS ASN VAL LEU SER LEU THR ASN LYS          
SEQRES  17 B  445  GLY GLU VAL PHE ASN GLU LEU VAL GLY LYS GLN ARG ILE          
SEQRES  18 B  445  SER GLY ASN LEU ASP SER PRO GLU GLY GLY PHE ASP ALA          
SEQRES  19 B  445  ILE MET GLN VAL ALA VAL CYS GLY SER LEU ILE GLY TRP          
SEQRES  20 B  445  ARG ASN VAL THR ARG LEU LEU VAL PHE SER THR ASP ALA          
SEQRES  21 B  445  GLY PHE HIS PHE ALA GLY ASP GLY LYS LEU GLY GLY ILE          
SEQRES  22 B  445  VAL LEU PRO ASN ASP GLY GLN CYS HIS LEU GLU ASN ASN          
SEQRES  23 B  445  MET TYR THR MET SER HIS TYR TYR ASP TYR PRO SER ILE          
SEQRES  24 B  445  ALA HIS LEU VAL GLN LYS LEU SER GLU ASN ASN ILE GLN          
SEQRES  25 B  445  THR ILE PHE ALA VAL THR GLU GLU PHE GLN PRO VAL TYR          
SEQRES  26 B  445  LYS GLU LEU LYS ASN LEU ILE PRO LYS SER ALA VAL GLY          
SEQRES  27 B  445  THR LEU SER ALA ASN SER SER ASN VAL ILE GLN LEU ILE          
SEQRES  28 B  445  ILE ASP ALA TYR ASN SER LEU SER SER GLU VAL ILE LEU          
SEQRES  29 B  445  GLU ASN GLY LYS LEU SER GLU GLY VAL THR ILE SER TYR          
SEQRES  30 B  445  LYS SER TYR CYS LYS ASN GLY VAL ASN GLY THR GLY GLU          
SEQRES  31 B  445  ASN GLY ARG LYS CYS SER ASN ILE SER ILE GLY ASP GLU          
SEQRES  32 B  445  VAL GLN PHE GLU ILE SER ILE THR SER ASN LYS CYS PRO          
SEQRES  33 B  445  LYS LYS ASP SER ASP SER PHE LYS ILE ARG PRO LEU GLY          
SEQRES  34 B  445  PHE THR GLU GLU VAL GLU VAL ILE LEU GLN TYR ILE CYS          
SEQRES  35 B  445  GLU CYS GLU                                                  
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HET    NAG  A 505      27                                                       
HET    NAG  A 506      27                                                       
HET    BMA  A 507      20                                                       
HET    MAN  A 508      21                                                       
HET    MAN  A 509      20                                                       
HET    MAN  A 510      21                                                       
HET    NAG  A 511      27                                                       
HET    NAG  A 512      27                                                       
HET    BMA  A 513      21                                                       
HET    NAG  A 514      27                                                       
HET    NAG  A 515      27                                                       
HET    BMA  A 516      20                                                       
HET    MAN  A 517      21                                                       
HET    MAN  A 518      20                                                       
HET    MAN  A 519      21                                                       
HET    MAN  A 520      21                                                       
HET    NAG  A 521      27                                                       
HET    NAG  A 522      28                                                       
HET     MG  B 501       1                                                       
HET     CA  B 502       1                                                       
HET     CA  B 503       1                                                       
HET    NAG  B 504      27                                                       
HET    NAG  B 505      28                                                       
HET    NAG  B 506      27                                                       
HET    NAG  B 507      28                                                       
HET    NAG  B 508      27                                                       
HET    NAG  B 509      27                                                       
HET    BMA  B 510      20                                                       
HET    MAN  B 511      21                                                       
HET    NAG  B 512      28                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3   CA    6(CA 2+)                                                     
FORMUL   7  NAG    15(C8 H15 N O6)                                              
FORMUL   7  BMA    4(C6 H12 O6)                                                 
FORMUL   7  MAN    8(C6 H12 O6)                                                 
FORMUL  11   MG    MG 2+                                                        
FORMUL  18  HOH   *560(H2 O)                                                    
HELIX    1 AA1 GLY A   29  GLY A   32  5                                   4    
HELIX    2 AA2 GLY A  184  GLN A  189  1                                   6    
HELIX    3 AA3 THR A  196  SER A  203  1                                   8    
HELIX    4 AA4 SER A  223  ASP A  227  5                                   5    
HELIX    5 AA5 PHE A  438  VAL A  440  5                                   3    
HELIX    6 AA6 ARG B    6  ALA B   10  1                                   5    
HELIX    7 AA7 SER B   14  GLN B   20  1                                   7    
HELIX    8 AA8 THR B   40  ALA B   42  5                                   3    
HELIX    9 AA9 LEU B   47  LYS B   52  1                                   6    
HELIX   10 AB1 LYS B   87  ILE B   91  5                                   5    
HELIX   11 AB2 SER B  132  SER B  134  5                                   3    
HELIX   12 AB3 MET B  135  LYS B  143  1                                   9    
HELIX   13 AB4 SER B  144  ARG B  154  1                                  11    
HELIX   14 AB5 THR B  179  ASN B  185  1                                   7    
HELIX   15 AB6 LYS B  208  GLY B  217  1                                  10    
HELIX   16 AB7 GLY B  230  CYS B  241  1                                  12    
HELIX   17 AB8 GLY B  266  GLY B  272  5                                   7    
HELIX   18 AB9 SER B  298  ASN B  309  1                                  12    
HELIX   19 AC1 PHE B  321  ILE B  332  1                                  12    
HELIX   20 AC2 ASN B  346  SER B  360  1                                  15    
HELIX   21 AC3 LYS B  382  GLY B  384  5                                   3    
HELIX   22 AC4 GLU B  390  GLY B  392  5                                   3    
SHEET    1 AA1 4 ALA A   9  SER A  12  0                                        
SHEET    2 AA1 4 LYS A 442  TYR A 446 -1  O  ALA A 443   N  LEU A  11           
SHEET    3 AA1 4 ASP A 432  SER A 437 -1  N  VAL A 435   O  VAL A 444           
SHEET    4 AA1 4 LEU A 419  ARG A 423 -1  N  ARG A 420   O  ILE A 434           
SHEET    1 AA2 4 VAL A  23  TYR A  26  0                                        
SHEET    2 AA2 4 SER A  34  ALA A  39 -1  O  LEU A  36   N  GLU A  24           
SHEET    3 AA2 4 ALA A  54  PRO A  59 -1  O  TYR A  56   N  VAL A  37           
SHEET    4 AA2 4 THR A  68  PRO A  69 -1  O  THR A  68   N  LEU A  57           
SHEET    1 AA3 2 GLU A  94  TYR A  95  0                                        
SHEET    2 AA3 2 SER A 120  TRP A 121 -1  O  SER A 120   N  TYR A  95           
SHEET    1 AA4 4 VAL A 105  HIS A 108  0                                        
SHEET    2 AA4 4 SER A 111  ALA A 116 -1  O  LEU A 113   N  ARG A 106           
SHEET    3 AA4 4 THR A 134  THR A 139 -1  O  THR A 134   N  ALA A 116           
SHEET    4 AA4 4 ARG A 144  TYR A 148 -1  O  LEU A 146   N  LEU A 137           
SHEET    1 AA5 4 SER A 169  PHE A 172  0                                        
SHEET    2 AA5 4 VAL A 178  GLY A 182 -1  O  GLY A 181   N  SER A 169           
SHEET    3 AA5 4 GLN A 191  ALA A 195 -1  O  LEU A 193   N  LEU A 180           
SHEET    4 AA5 4 LEU A 217  GLN A 218 -1  O  LEU A 217   N  SER A 194           
SHEET    1 AA6 4 VAL A 235  GLY A 238  0                                        
SHEET    2 AA6 4 ASP A 247  VAL A 252 -1  O  ASP A 247   N  GLY A 238           
SHEET    3 AA6 4 TYR A 261  LEU A 265 -1  O  LEU A 265   N  PHE A 248           
SHEET    4 AA6 4 SER A 272  SER A 277 -1  O  LEU A 273   N  ILE A 264           
SHEET    1 AA7 4 VAL A 289  THR A 292  0                                        
SHEET    2 AA7 4 ASP A 301  ALA A 306 -1  O  LEU A 303   N  ALA A 290           
SHEET    3 AA7 4 ARG A 323  TYR A 327 -1  O  TYR A 325   N  VAL A 304           
SHEET    4 AA7 4 LEU A 340  THR A 343 -1  O  LEU A 342   N  VAL A 324           
SHEET    1 AA8 2 MET A 310  ARG A 312  0                                        
SHEET    2 AA8 2 PRO A 318  GLU A 320 -1  O  GLN A 319   N  ASP A 311           
SHEET    1 AA9 2 GLN A 329  HIS A 330  0                                        
SHEET    2 AA9 2 GLY A 333  ILE A 334 -1  O  GLY A 333   N  HIS A 330           
SHEET    1 AB1 4 LEU A 355  GLY A 359  0                                        
SHEET    2 AB1 4 ASP A 368  ALA A 373 -1  O  ASP A 368   N  GLY A 359           
SHEET    3 AB1 4 VAL A 383  PHE A 387 -1  O  PHE A 387   N  VAL A 369           
SHEET    4 AB1 4 GLN A 400  LEU A 402 -1  O  GLN A 400   N  VAL A 386           
SHEET    1 AB2 3 CYS B  44  ASP B  46  0                                        
SHEET    2 AB2 3 CYS B  25  CYS B  28 -1  N  GLY B  26   O  ASP B  45           
SHEET    3 AB2 3 ILE B  60  GLU B  61 -1  O  GLU B  61   N  TRP B  27           
SHEET    1 AB3 6 SER B  66  LYS B  71  0                                        
SHEET    2 AB3 6 GLN B  98  ARG B 104 -1  O  VAL B 100   N  ASP B  68           
SHEET    3 AB3 6 VAL B 434  ILE B 441  1  O  ILE B 437   N  LEU B 101           
SHEET    4 AB3 6 ASP B 421  PRO B 427 -1  N  ILE B 425   O  VAL B 434           
SHEET    5 AB3 6 VAL B 362  ASN B 366 -1  N  GLU B 365   O  ARG B 426           
SHEET    6 AB3 6 LYS B 394  CYS B 395 -1  O  CYS B 395   N  VAL B 362           
SHEET    1 AB4 5 ILE B  94  GLN B  95  0                                        
SHEET    2 AB4 5 GLN B 109  LYS B 116 -1  O  LYS B 114   N  GLN B  95           
SHEET    3 AB4 5 GLU B 403  THR B 411 -1  O  PHE B 406   N  LEU B 113           
SHEET    4 AB4 5 THR B 374  TYR B 380 -1  N  TYR B 380   O  GLN B 405           
SHEET    5 AB4 5 ASN B 386  THR B 388 -1  O  GLY B 387   N  SER B 379           
SHEET    1 AB5 6 TYR B 199  THR B 206  0                                        
SHEET    2 AB5 6 PHE B 160  PHE B 167 -1  N  ILE B 162   O  THR B 206           
SHEET    3 AB5 6 ILE B 123  ASP B 130  1  N  LEU B 125   O  ARG B 161           
SHEET    4 AB5 6 THR B 251  THR B 258  1  O  LEU B 253   N  ASP B 124           
SHEET    5 AB5 6 ILE B 311  VAL B 317  1  O  ILE B 314   N  LEU B 254           
SHEET    6 AB5 6 SER B 335  THR B 339  1  O  ALA B 336   N  PHE B 315           
SHEET    1 AB6 2 LEU B 283  GLU B 284  0                                        
SHEET    2 AB6 2 MET B 287  TYR B 288 -1  O  MET B 287   N  GLU B 284           
SSBOND   1 CYS A   58    CYS A   67                          1555   1555  2.05  
SSBOND   2 CYS A  115    CYS A  135                          1555   1555  2.07  
SSBOND   3 CYS A  151    CYS A  164                          1555   1555  2.03  
SSBOND   4 CYS B    7    CYS B   25                          1555   1555  2.04  
SSBOND   5 CYS B   15    CYS B  444                          1555   1555  2.03  
SSBOND   6 CYS B   18    CYS B   44                          1555   1555  2.04  
SSBOND   7 CYS B   28    CYS B   55                          1555   1555  2.03  
SSBOND   8 CYS B  187    CYS B  193                          1555   1555  2.04  
SSBOND   9 CYS B  241    CYS B  281                          1555   1555  2.04  
SSBOND  10 CYS B  381    CYS B  395                          1555   1555  2.04  
SSBOND  11 CYS B  415    CYS B  442                          1555   1555  2.03  
LINK         ND2 ASN A  43                 C1  NAG A 514     1555   1555  1.44  
LINK         OE1 GLU A 239                CA    CA A 501     1555   1555  2.43  
LINK         OE2 GLU A 239                CA    CA A 501     1555   1555  2.53  
LINK         OG  SER A 241                CA    CA A 501     1555   1555  2.27  
LINK         OD1 ASP A 243                CA    CA A 501     1555   1555  2.37  
LINK         O   THR A 245                CA    CA A 501     1555   1555  2.33  
LINK         OD1 ASP A 247                CA    CA A 501     1555   1555  2.47  
LINK         OD2 ASP A 247                CA    CA A 501     1555   1555  2.46  
LINK         ND2 ASN A 256                 C1  NAG A 511     1555   1555  1.43  
LINK         ND2 ASN A 266                 C1  NAG A 521     1555   1555  1.44  
LINK         ND2 ASN A 275                 C1  NAG A 505     1555   1555  1.44  
LINK         OD1 ASP A 293                CA    CA A 502     1555   1555  2.46  
LINK         OD1 ASN A 295                CA    CA A 502     1555   1555  2.28  
LINK         OD1 ASP A 297                CA    CA A 502     1555   1555  2.47  
LINK         O   LEU A 299                CA    CA A 502     1555   1555  2.35  
LINK         OD1 ASP A 301                CA    CA A 502     1555   1555  2.51  
LINK         OD2 ASP A 301                CA    CA A 502     1555   1555  2.48  
LINK         OD1 ASP A 360                CA    CA A 503     1555   1555  2.53  
LINK         OD1 ASP A 362                CA    CA A 503     1555   1555  2.31  
LINK         OD1 ASP A 364                CA    CA A 503     1555   1555  2.42  
LINK         O   TYR A 366                CA    CA A 503     1555   1555  2.16  
LINK         OD1 ASP A 368                CA    CA A 503     1555   1555  2.45  
LINK         OD2 ASP A 368                CA    CA A 503     1555   1555  2.53  
LINK         OD1 ASP A 424                CA    CA A 504     1555   1555  2.27  
LINK         OD1 ASP A 426                CA    CA A 504     1555   1555  2.31  
LINK         OD1 ASN A 428                CA    CA A 504     1555   1555  2.37  
LINK         O   TYR A 430                CA    CA A 504     1555   1555  2.33  
LINK         OD1 ASP A 432                CA    CA A 504     1555   1555  2.54  
LINK         OD2 ASP A 432                CA    CA A 504     1555   1555  2.59  
LINK         OG  SER B 132                MG    MG B 501     1555   1555  2.28  
LINK         O   SER B 134                CA    CA B 502     1555   1555  2.53  
LINK         OD1 ASP B 137                CA    CA B 502     1555   1555  2.41  
LINK         OD2 ASP B 137                CA    CA B 502     1555   1555  2.65  
LINK         OD1 ASP B 138                CA    CA B 502     1555   1555  2.33  
LINK         OE1 GLU B 169                CA    CA B 503     1555   1555  2.30  
LINK         OD1 ASN B 224                CA    CA B 503     1555   1555  2.25  
LINK         O   ASP B 226                CA    CA B 503     1555   1555  2.29  
LINK         OD1 ASP B 226                CA    CA B 503     1555   1555  2.23  
LINK         O   PRO B 228                CA    CA B 503     1555   1555  2.29  
LINK         OE1 GLU B 229                MG    MG B 501     1555   1555  2.10  
LINK         OE2 GLU B 229                CA    CA B 503     1555   1555  2.33  
LINK         ND2 ASN B 249                 C1  NAG B 504     1555   1555  1.45  
LINK         O   ALA B 342                CA    CA B 502     1555   1555  2.20  
LINK         ND2 ASN B 343                 C1  NAG B 512     1555   1555  1.44  
LINK         ND2 ASN B 386                 C1  NAG B 506     1555   1555  1.44  
LINK         ND2 ASN B 397                 C1  NAG B 508     1555   1555  1.44  
LINK        CA    CA A 501                 O   HOH A 650     1555   1555  2.45  
LINK        CA    CA A 502                 O   HOH A 648     1555   1555  2.34  
LINK        CA    CA A 503                 O   HOH A 649     1555   1555  2.55  
LINK        CA    CA A 504                 O   HOH A 651     1555   1555  2.23  
LINK         O4  NAG A 505                 C1  NAG A 506     1555   1555  1.42  
LINK         O4  NAG A 506                 C1  BMA A 507     1555   1555  1.44  
LINK         O3  BMA A 507                 C1  MAN A 508     1555   1555  1.44  
LINK         O6  BMA A 507                 C1  MAN A 509     1555   1555  1.44  
LINK         O3  MAN A 509                 C1  MAN A 510     1555   1555  1.44  
LINK         O4  NAG A 511                 C1  NAG A 512     1555   1555  1.44  
LINK         O4  NAG A 512                 C1  BMA A 513     1555   1555  1.44  
LINK         O4  NAG A 514                 C1  NAG A 515     1555   1555  1.43  
LINK         O4  NAG A 515                 C1  BMA A 516     1555   1555  1.45  
LINK         O3  BMA A 516                 C1  MAN A 517     1555   1555  1.44  
LINK         O6  BMA A 516                 C1  MAN A 518     1555   1555  1.44  
LINK         O3  MAN A 518                 C1  MAN A 520     1555   1555  1.44  
LINK         O6  MAN A 518                 C1  MAN A 519     1555   1555  1.44  
LINK         O4  NAG A 521                 C1  NAG A 522     1555   1555  1.45  
LINK        MG    MG B 501                 O   HOH B 617     1555   1555  2.08  
LINK        MG    MG B 501                 O   HOH B 664     1555   1555  2.15  
LINK        MG    MG B 501                 O   HOH B 663     1555   1555  2.14  
LINK        MG    MG B 501                 O   HOH B 665     1555   1555  2.13  
LINK        CA    CA B 502                 O   HOH B 648     1555   1555  2.38  
LINK        CA    CA B 502                 O   HOH B 661     1555   1555  2.36  
LINK         O4  NAG B 504                 C1  NAG B 505     1555   1555  1.45  
LINK         O4  NAG B 506                 C1  NAG B 507     1555   1555  1.44  
LINK         O4  NAG B 508                 C1  NAG B 509     1555   1555  1.44  
LINK         O4  NAG B 509                 C1  BMA B 510     1555   1555  1.44  
LINK         O3  BMA B 510                 C1  MAN B 511     1555   1555  1.44  
CISPEP   1 GLN B   95    PRO B   96          0        -1.79                     
CISPEP   2 MET B  173    PRO B  174          0         3.42                     
SITE     1 AC1  6 GLU A 239  SER A 241  ASP A 243  THR A 245                    
SITE     2 AC1  6 ASP A 247  HOH A 650                                          
SITE     1 AC2  6 ASP A 293  ASN A 295  ASP A 297  LEU A 299                    
SITE     2 AC2  6 ASP A 301  HOH A 648                                          
SITE     1 AC3  6 ASP A 360  ASP A 362  ASP A 364  TYR A 366                    
SITE     2 AC3  6 ASP A 368  HOH A 649                                          
SITE     1 AC4  6 ASP A 424  ASP A 426  ASN A 428  TYR A 430                    
SITE     2 AC4  6 ASP A 432  HOH A 651                                          
SITE     1 AC5  6 SER B 132  GLU B 229  HOH B 617  HOH B 663                    
SITE     2 AC5  6 HOH B 664  HOH B 665                                          
SITE     1 AC6  6 SER B 134  ASP B 137  ASP B 138  ALA B 342                    
SITE     2 AC6  6 HOH B 648  HOH B 661                                          
SITE     1 AC7  5 GLU B 169  ASN B 224  ASP B 226  PRO B 228                    
SITE     2 AC7  5 GLU B 229                                                     
SITE     1 AC8 24 PRO A  15  GLY A  16  LYS A  41  ASN A  43                    
SITE     2 AC8 24 LEU A  50  GLN A  51  HOH A 601  HOH A 611                    
SITE     3 AC8 24 HOH A 613  HOH A 622  HOH A 623  HOH A 624                    
SITE     4 AC8 24 HOH A 865  HOH A 928  HOH A 933  GLU B 319                    
SITE     5 AC8 24 LYS B 326  THR B 339  SER B 341  ASP B 353                    
SITE     6 AC8 24 SER B 357  HOH B 608  HOH B 616  HOH B 624                    
SITE     1 AC9 12 PRO A  14  ASN A 256  LEU A 257  TYR A 259                    
SITE     2 AC9 12 SER A 277  GLU A 279  HOH A 602  HOH A 604                    
SITE     3 AC9 12 HOH A 617  HOH A 725  HOH A 795  GLU B 327                    
SITE     1 AD1  6 ASN A 266  SER A 268  ASP A 269  HOH A 702                    
SITE     2 AD1  6 HOH A 873  HOH A 929                                          
SITE     1 AD2 21 GLU A  71  SER A  74  ARG A 220  GLN A 221                    
SITE     2 AD2 21 ALA A 222  SER A 223  TYR A 226  TYR A 261                    
SITE     3 AD2 21 SER A 272  LEU A 273  ASN A 275  HOH A 705                    
SITE     4 AD2 21 HOH A 718  HOH A 745  HOH A 775  HOH A 808                    
SITE     5 AD2 21 HOH A 821  HOH A 826  HOH A 881  HOH A 922                    
SITE     6 AD2 21 HOH A 925                                                     
SITE     1 AD3  4 GLU B  89  ASN B 249  THR B 431  HOH B 795                    
SITE     1 AD4  3 ASN B 141  ASN B 343  SER B 345                               
SITE     1 AD5  3 TYR B 380  GLY B 384  ASN B 386                               
SITE     1 AD6  8 GLN B 280  LYS B 305  GLU B 308  LYS B 382                    
SITE     2 AD6  8 ASN B 383  ASN B 397  HOH B 601  HOH B 612                    
CRYST1   52.130  116.750  159.490  90.00  90.00  90.00 P 21 21 21    4          
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      0.019183  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008565  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006270        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system