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Database: PDB
Entry: 4WK2
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Original site: 4WK2 
HEADER    CELL ADHESION/IMMUNE SYSTEM             01-OCT-14   4WK2              
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;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: GLY-ARG-GLY-ASP-SER-PRO;                                   
COMPND  18 CHAIN: C;                                                            
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: 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;                                
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_COMMON: HUMAN;                                              
SOURCE  23 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL ADHESION-FIBRONECTIN RECEPTOR, CELL ADHESION-IMMUNE SYSTEM       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.XIA,T.A.SPRINGER                                                    
REVDAT   4   22-NOV-17 4WK2    1       COMPND SOURCE JRNL   REMARK              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   24-DEC-14 4WK2    1       JRNL                                     
REVDAT   2   17-DEC-14 4WK2    1       JRNL                                     
REVDAT   1   03-DEC-14 4WK2    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.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 42708                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.680                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1997                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.5787 -  6.0203    0.96     3040   150  0.1846 0.2418        
REMARK   3     2  6.0203 -  4.7806    0.97     2939   145  0.1681 0.1883        
REMARK   3     3  4.7806 -  4.1769    0.97     2904   142  0.1474 0.2027        
REMARK   3     4  4.1769 -  3.7952    0.96     2833   139  0.1715 0.2212        
REMARK   3     5  3.7952 -  3.5234    0.96     2868   140  0.2062 0.2660        
REMARK   3     6  3.5234 -  3.3157    0.97     2884   142  0.2245 0.2625        
REMARK   3     7  3.3157 -  3.1497    0.99     2896   142  0.2571 0.3145        
REMARK   3     8  3.1497 -  3.0126    0.99     2908   142  0.2750 0.3100        
REMARK   3     9  3.0126 -  2.8967    1.00     2909   143  0.2957 0.3099        
REMARK   3    10  2.8967 -  2.7968    0.99     2907   143  0.3096 0.3011        
REMARK   3    11  2.7968 -  2.7093    0.99     2914   143  0.3239 0.3823        
REMARK   3    12  2.7093 -  2.6319    0.99     2886   140  0.3485 0.3515        
REMARK   3    13  2.6319 -  2.5626    1.00     2906   143  0.3920 0.4119        
REMARK   3    14  2.5626 -  2.5000    0.99     2917   143  0.4072 0.4547        
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)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.500           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 99.46                          
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      :  0.006           7278                                  
REMARK   3   ANGLE     :  0.786           9842                                  
REMARK   3   CHIRALITY :  0.031           1133                                  
REMARK   3   PLANARITY :  0.002           1264                                  
REMARK   3   DIHEDRAL  : 12.885           2660                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 39 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1433 -18.4387 -25.5488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5454 T22:   0.6619                                     
REMARK   3      T33:   1.1226 T12:  -0.0543                                     
REMARK   3      T13:   0.3385 T23:   0.1075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9615 L22:   4.8292                                     
REMARK   3      L33:   3.3545 L12:  -0.9486                                     
REMARK   3      L13:   0.7576 L23:   2.1302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3479 S12:   0.0102 S13:  -0.6073                       
REMARK   3      S21:   0.0789 S22:   0.5516 S23:   1.3185                       
REMARK   3      S31:   0.2520 S32:  -0.5499 S33:  -0.1720                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 116 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7114  -1.3724 -14.4074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7476 T22:   0.6112                                     
REMARK   3      T33:   0.8581 T12:   0.1679                                     
REMARK   3      T13:   0.4420 T23:   0.1087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1148 L22:   1.1725                                     
REMARK   3      L33:   1.7615 L12:  -0.0018                                     
REMARK   3      L13:   0.2561 L23:  -0.4576                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1337 S12:  -0.3909 S13:  -0.1356                       
REMARK   3      S21:   0.6967 S22:   0.2078 S23:   0.9289                       
REMARK   3      S31:  -0.2135 S32:  -0.2195 S33:   0.1479                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 350 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6486  -8.9492 -19.5528              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4815 T22:   0.5458                                     
REMARK   3      T33:   0.5515 T12:   0.1116                                     
REMARK   3      T13:   0.1306 T23:   0.0641                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7565 L22:   2.9319                                     
REMARK   3      L33:   2.8516 L12:   0.2723                                     
REMARK   3      L13:  -0.8935 L23:  -0.3038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2166 S12:  -0.3719 S13:  -0.4148                       
REMARK   3      S21:   0.4854 S22:   0.0444 S23:  -0.1243                       
REMARK   3      S31:   0.1140 S32:   0.2857 S33:   0.2073                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 351 THROUGH 452 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7715 -21.7997 -33.9984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5186 T22:   0.5214                                     
REMARK   3      T33:   0.9999 T12:  -0.0371                                     
REMARK   3      T13:   0.2189 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8614 L22:   4.9554                                     
REMARK   3      L33:   4.3871 L12:   0.1867                                     
REMARK   3      L13:   0.0766 L23:  -1.5161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2477 S12:   0.1164 S13:  -0.7610                       
REMARK   3      S21:  -0.1823 S22:   0.2449 S23:   0.5758                       
REMARK   3      S31:   0.4801 S32:  -0.1831 S33:  -0.0326                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 65 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2411 -35.0828 -80.5156              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6971 T22:   1.0534                                     
REMARK   3      T33:   1.6924 T12:   0.0070                                     
REMARK   3      T13:  -0.0159 T23:  -0.4317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5548 L22:   5.1499                                     
REMARK   3      L33:   1.0069 L12:   1.4536                                     
REMARK   3      L13:   0.9111 L23:   2.0806                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6045 S12:   0.0712 S13:  -0.8897                       
REMARK   3      S21:   0.4958 S22:  -0.0369 S23:  -0.8987                       
REMARK   3      S31:   0.0649 S32:   0.6090 S33:  -0.6051                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 66 THROUGH 132 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1451   4.1851 -67.5089              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6324 T22:   0.5306                                     
REMARK   3      T33:   0.5338 T12:  -0.0806                                     
REMARK   3      T13:  -0.0216 T23:   0.0538                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6031 L22:   4.2526                                     
REMARK   3      L33:   4.9364 L12:   1.2095                                     
REMARK   3      L13:  -1.1296 L23:   1.5811                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2942 S12:   0.4571 S13:  -0.3293                       
REMARK   3      S21:  -1.0227 S22:   0.3153 S23:  -0.0810                       
REMARK   3      S31:  -0.1303 S32:  -0.0329 S33:  -0.1151                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 133 THROUGH 346 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3341  14.8675 -39.7983              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3952 T22:   0.3914                                     
REMARK   3      T33:   0.5427 T12:  -0.0614                                     
REMARK   3      T13:   0.0698 T23:  -0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0210 L22:   3.1796                                     
REMARK   3      L33:   3.3984 L12:  -0.0323                                     
REMARK   3      L13:  -1.2555 L23:  -0.7769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1636 S12:   0.0133 S13:   0.4960                       
REMARK   3      S21:   0.2449 S22:   0.0771 S23:   0.0596                       
REMARK   3      S31:  -0.5695 S32:   0.0865 S33:  -0.2416                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 347 THROUGH 444 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.1362  -3.9868 -63.1026              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7404 T22:   0.5320                                     
REMARK   3      T33:   0.7313 T12:  -0.0122                                     
REMARK   3      T13:   0.0401 T23:   0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1023 L22:   7.2886                                     
REMARK   3      L33:   6.1330 L12:   1.5878                                     
REMARK   3      L13:   1.5731 L23:   4.6763                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3352 S12:   0.1255 S13:  -0.6703                       
REMARK   3      S21:   0.0280 S22:   0.0329 S23:  -0.8177                       
REMARK   3      S31:   0.8194 S32:   0.1823 S33:  -0.3470                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 5000 THROUGH 5005 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  23.5417  13.7807 -22.0937              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2456 T22:   1.1053                                     
REMARK   3      T33:   1.5397 T12:  -0.3161                                     
REMARK   3      T13:  -0.1291 T23:  -0.2340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0522 L22:   2.9889                                     
REMARK   3      L33:   3.3512 L12:  -1.5508                                     
REMARK   3      L13:   2.8848 L23:  -2.6140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2362 S12:   0.3559 S13:   2.2045                       
REMARK   3      S21:   0.4329 S22:  -0.1188 S23:  -1.6825                       
REMARK   3      S31:  -1.3129 S32:   1.6541 S33:   0.1952                       
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 4WK2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203957.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-14                          
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   : 42741                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4600                             
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   (%): 60.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
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       30.49000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.14500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.19500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.14500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.49000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.19500            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    63                                                      
REMARK 465     PRO A    64                                                      
REMARK 465     THR A    65                                                      
REMARK 465     SER A    85                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLN B    35                                                      
REMARK 465     GLU B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     MET B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     THR B    40                                                      
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     GLU B   445                                                      
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  HD21  ASN A   266     C1   NAG A   518              0.63            
REMARK 500  HD21  ASN A   266     H1   NAG A   518              1.04            
REMARK 500  HD21  ASN A   266     O5   NAG A   518              1.47            
REMARK 500  HD21  ASN B   343     O5   NAG B   509              1.49            
REMARK 500  HD21  ASN B   343     C1   NAG B   509              1.51            
REMARK 500   OD2  ASP A    73     HZ3  LYS A    96              1.59            
REMARK 500   O6   MAN A   509     C2   MAN A   511              1.82            
REMARK 500   O4   NAG A   512     O5   NAG A   513              1.85            
REMARK 500   ND2  ASN B   249     O5   NAG B   504              2.04            
REMARK 500   O    SER B   134     O    HOH B   614              2.05            
REMARK 500   ND2  ASN B   343     O5   NAG B   509              2.05            
REMARK 500   OD2  ASP B   259     O    HOH B   614              2.08            
REMARK 500   ND2  ASN A   266     O5   NAG A   518              2.11            
REMARK 500   OD1  ASN B    30     OG1  THR B    32              2.15            
REMARK 500   O    HOH A   609     O    HOH A   657              2.18            
REMARK 500   O    HOH B   625     O    HOH B   646              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       74.38   -157.73                                   
REMARK 500    THR A  30      -32.94   -136.68                                   
REMARK 500    THR A 123      161.53     70.15                                   
REMARK 500    LYS A 125     -123.13   -116.44                                   
REMARK 500    TRP A 157      172.55     67.66                                   
REMARK 500    ASP A 243     -157.83   -120.90                                   
REMARK 500    ILE A 270       15.04     49.41                                   
REMARK 500    VAL A 321      -35.30   -130.82                                   
REMARK 500    PRO A 374      -18.18    -48.41                                   
REMARK 500    PHE B  33       53.66    -97.64                                   
REMARK 500    ASN B  72       61.87   -150.96                                   
REMARK 500    VAL B 168      -79.12   -137.20                                   
REMARK 500    THR B 171       48.44    -93.11                                   
REMARK 500    ASN B 192       53.85    -95.39                                   
REMARK 500    SER B 222     -152.35   -120.67                                   
REMARK 500    LEU B 225      -60.06   -105.19                                   
REMARK 500    SER B 341     -172.08    -68.34                                   
REMARK 500    LYS B 414     -145.58   -130.11                                   
REMARK 500    LYS B 417     -177.61     60.73                                   
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 A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 239   OE1                                                    
REMARK 620 2 GLU A 239   OE2  54.6                                              
REMARK 620 3 SER A 241   OG  127.9  73.5                                        
REMARK 620 4 ASP A 243   OD1  79.7  61.8  72.1                                  
REMARK 620 5 THR A 245   O    65.1 115.2 151.4  87.9                            
REMARK 620 6 ASP A 247   OD1 131.8 138.0  88.7 147.6  98.7                      
REMARK 620 7 ASP A 247   OD2  87.2  89.2  96.6 150.6 110.3  54.7                
REMARK 620 8 HOH A 621   O   131.6 130.9  78.8  71.5  75.5  79.4 134.1          
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  72.2                                              
REMARK 620 3 ASP A 297   OD1  69.7  82.1                                        
REMARK 620 4 LEU A 299   O    81.9 152.7  96.7                                  
REMARK 620 5 ASP A 301   OD1 137.3 110.3 152.0  83.3                            
REMARK 620 6 ASP A 301   OD2  91.7  70.4 150.7 103.0  53.4                      
REMARK 620 7 HOH A 601   O   146.4  92.3  79.0 114.4  75.7 111.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 360   OD1                                                    
REMARK 620 2 ASP A 362   OD1  92.9                                              
REMARK 620 3 ASP A 364   OD1  67.3  78.4                                        
REMARK 620 4 TYR A 366   O    67.2 157.5  83.8                                  
REMARK 620 5 ASP A 368   OD1 140.9 113.5 143.4  89.1                            
REMARK 620 6 ASP A 368   OD2 100.0  92.4 163.5 101.3  52.9                      
REMARK 620 7 HOH A 608   O   135.8 104.6  76.8  84.5  66.7 119.0                
REMARK 620 8 HOH A 623   O   148.0  58.6  91.0 136.2  69.9  95.8  52.2          
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 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 424   OD1                                                    
REMARK 620 2 ASP A 426   OD1  74.8                                              
REMARK 620 3 ASN A 428   OD1  79.3  78.8                                        
REMARK 620 4 TYR A 430   O    77.7 149.2  82.8                                  
REMARK 620 5 ASP A 432   OD1 133.7 120.2 143.3  89.0                            
REMARK 620 6 ASP A 432   OD2  89.4  82.9 160.5 110.5  54.0                      
REMARK 620 7 HOH A 610   O   153.1  87.8  77.3 112.0  72.8 108.8                
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 SER B 134   OG   96.3                                              
REMARK 620 3 GLU B 229   OE1  88.3 150.6                                        
REMARK 620 4 ASP C5003   OD1 115.4  93.2 111.0                                  
REMARK 620 5 HOH B 605   O    75.9  72.9  80.2 163.4                            
REMARK 620 6 HOH B 606   O   144.7  96.1  65.6  96.7  76.4                      
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 111.8                                              
REMARK 620 3 ASP B 138   OD1 114.2  73.9                                        
REMARK 620 4 HOH B 680   O   164.0  75.6  81.2                                  
REMARK 620 5 HOH B 614   O    50.3 152.7 129.9 116.9                            
REMARK 620 N                    1     2     3     4                             
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  98.1                                              
REMARK 620 3 ASP B 226   O   148.6  82.8                                        
REMARK 620 4 ASP B 226   OD1  84.1  79.8  65.0                                  
REMARK 620 5 PRO B 228   O    76.6 170.2  97.3  91.3                            
REMARK 620 6 GLU B 229   OE2 101.9  91.2 109.5 169.9  97.9                      
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 517 bound to ASN A 43                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 520 bound   
REMARK 800  to ASN A 141                                                        
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  512 through NAG A 513 bound to ASN A 256                            
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  518 through NAG A 519 bound to ASN A 266                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  505 through MAN A 508 bound to ASN A 275                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 510 bound   
REMARK 800  to ASN B 192                                                        
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  504 through NAG B 505 bound to ASN B 249                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 509 bound   
REMARK 800  to ASN B 343                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
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: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 508 bound   
REMARK 800  to ASN B 397                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues MAN A    
REMARK 800  509 through MAN A 511                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WJK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WK0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WK4   RELATED DB: PDB                                   
DBREF  4WK2 A    1   452  UNP    P08648   ITA5_HUMAN      42    493             
DBREF  4WK2 B    1   445  UNP    P05556   ITB1_HUMAN      21    465             
DBREF  4WK2 C 5000  5005  PDB    4WK2     4WK2          5000   5005             
SEQADV 4WK2 VAL A  451  UNP  P08648    ILE   492 ENGINEERED MUTATION            
SEQADV 4WK2 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                                                  
SEQRES   1 C    6  GLY ARG GLY ASP SER PRO                                      
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    MAN  A 511      21                                                       
HET    NAG  A 512      27                                                       
HET    NAG  A 513      28                                                       
HET    NAG  A 514      27                                                       
HET    NAG  A 515      27                                                       
HET    BMA  A 516      21                                                       
HET    MAN  A 517      21                                                       
HET    NAG  A 518      27                                                       
HET    NAG  A 519      27                                                       
HET    NAG  A 520      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      28                                                       
HET    NAG  B 509      28                                                       
HET    NAG  B 510      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   4   CA    6(CA 2+)                                                     
FORMUL   8  NAG    16(C8 H15 N O6)                                              
FORMUL   8  BMA    2(C6 H12 O6)                                                 
FORMUL   8  MAN    5(C6 H12 O6)                                                 
FORMUL  13   MG    MG 2+                                                        
FORMUL  21  HOH   *164(H2 O)                                                    
HELIX    1 AA1 GLY A  184  GLN A  189  1                                   6    
HELIX    2 AA2 THR A  196  SER A  203  1                                   8    
HELIX    3 AA3 SER A  223  ASP A  227  5                                   5    
HELIX    4 AA4 LYS A  254  TYR A  259  1                                   6    
HELIX    5 AA5 PHE A  438  VAL A  440  5                                   3    
HELIX    6 AA6 SER B   14  ALA B   21  1                                   8    
HELIX    7 AA7 LEU B   47  LYS B   52  1                                   6    
HELIX    8 AA8 LYS B   87  ILE B   91  5                                   5    
HELIX    9 AA9 SER B  132  SER B  134  5                                   3    
HELIX   10 AB1 MET B  135  VAL B  142  1                                   8    
HELIX   11 AB2 SER B  144  MET B  153  1                                  10    
HELIX   12 AB3 ARG B  154  ILE B  156  5                                   3    
HELIX   13 AB4 THR B  179  ASN B  185  1                                   7    
HELIX   14 AB5 LYS B  208  GLY B  217  1                                  10    
HELIX   15 AB6 GLY B  230  CYS B  241  1                                  12    
HELIX   16 AB7 GLY B  266  GLY B  272  5                                   7    
HELIX   17 AB8 SER B  298  ASN B  309  1                                  12    
HELIX   18 AB9 PHE B  321  ILE B  332  1                                  12    
HELIX   19 AC1 ASN B  346  SER B  360  1                                  15    
HELIX   20 AC2 LYS B  382  GLY B  384  5                                   3    
HELIX   21 AC3 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 423   O  ASP A 432           
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  ALA A  54   N  ALA A  39           
SHEET    4 AA2 4 THR A  68  ILE A  70 -1  O  ILE A  70   N  VAL A  55           
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  TYR A 148   N  CYS A 135           
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  VAL A 249   N  ALA A 236           
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  PHE A 276   N  VAL A 262           
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  LEU A 402   N  VAL A 384           
SHEET    1 AB2 2 CYS B  25  TRP B  27  0                                        
SHEET    2 AB2 2 CYS B  44  ASP B  46 -1  O  ASP B  45   N  GLY B  26           
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  GLN B 439   N  LEU B 103           
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  SER B 412 -1  O  VAL B 404   N  PHE B 115           
SHEET    4 AB4 5 VAL B 373  TYR B 380 -1  N  LYS B 378   O  GLU B 407           
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  SER B 166   O  LYS B 200           
SHEET    3 AB5 6 ILE B 123  ASP B 130  1  N  MET B 129   O  GLY B 165           
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  PHE B 256           
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  2.03  
SSBOND   2 CYS A  115    CYS A  135                          1555   1555  2.03  
SSBOND   3 CYS A  151    CYS A  164                          1555   1555  2.03  
SSBOND   4 CYS B    7    CYS B   25                          1555   1555  2.03  
SSBOND   5 CYS B   15    CYS B  444                          1555   1555  2.03  
SSBOND   6 CYS B   18    CYS B   44                          1555   1555  2.03  
SSBOND   7 CYS B   28    CYS B   55                          1555   1555  2.03  
SSBOND   8 CYS B  187    CYS B  193                          1555   1555  2.03  
SSBOND   9 CYS B  241    CYS B  281                          1555   1555  2.03  
SSBOND  10 CYS B  381    CYS B  395                          1555   1555  2.03  
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         ND2 ASN A 141                 C1  NAG A 520     1555   1555  1.37  
LINK         OE1 GLU A 239                CA    CA A 501     1555   1555  2.40  
LINK         OE2 GLU A 239                CA    CA A 501     1555   1555  2.39  
LINK         OG  SER A 241                CA    CA A 501     1555   1555  2.33  
LINK         OD1 ASP A 243                CA    CA A 501     1555   1555  2.39  
LINK         O   THR A 245                CA    CA A 501     1555   1555  2.32  
LINK         OD1 ASP A 247                CA    CA A 501     1555   1555  2.38  
LINK         OD2 ASP A 247                CA    CA A 501     1555   1555  2.39  
LINK         ND2 ASN A 256                 C1  NAG A 512     1555   1555  1.44  
LINK         ND2 ASN A 266                 C1  NAG A 518     1555   1555  1.30  
LINK         ND2 ASN A 275                 C1  NAG A 505     1555   1555  1.45  
LINK         OD1 ASP A 293                CA    CA A 502     1555   1555  2.41  
LINK         OD1 ASN A 295                CA    CA A 502     1555   1555  2.36  
LINK         OD1 ASP A 297                CA    CA A 502     1555   1555  2.44  
LINK         O   LEU A 299                CA    CA A 502     1555   1555  2.26  
LINK         OD1 ASP A 301                CA    CA A 502     1555   1555  2.43  
LINK         OD2 ASP A 301                CA    CA A 502     1555   1555  2.45  
LINK         OD1 ASP A 360                CA    CA A 503     1555   1555  2.42  
LINK         OD1 ASP A 362                CA    CA A 503     1555   1555  2.29  
LINK         OD1 ASP A 364                CA    CA A 503     1555   1555  2.44  
LINK         O   TYR A 366                CA    CA A 503     1555   1555  2.35  
LINK         OD1 ASP A 368                CA    CA A 503     1555   1555  2.46  
LINK         OD2 ASP A 368                CA    CA A 503     1555   1555  2.46  
LINK         OD1 ASP A 424                CA    CA A 504     1555   1555  2.32  
LINK         OD1 ASP A 426                CA    CA A 504     1555   1555  2.32  
LINK         OD1 ASN A 428                CA    CA A 504     1555   1555  2.41  
LINK         O   TYR A 430                CA    CA A 504     1555   1555  2.30  
LINK         OD1 ASP A 432                CA    CA A 504     1555   1555  2.40  
LINK         OD2 ASP A 432                CA    CA A 504     1555   1555  2.43  
LINK         OG  SER B 132                MG    MG B 501     1555   1555  2.07  
LINK         O   SER B 134                CA    CA B 502     1555   1555  2.39  
LINK         OG  SER B 134                MG    MG B 501     1555   1555  2.63  
LINK         OD1 ASP B 137                CA    CA B 502     1555   1555  2.38  
LINK         OD1 ASP B 138                CA    CA B 502     1555   1555  2.38  
LINK         OE1 GLU B 169                CA    CA B 503     1555   1555  2.33  
LINK         ND2 ASN B 192                 C1  NAG B 510     1555   1555  1.44  
LINK         OD1 ASN B 224                CA    CA B 503     1555   1555  2.25  
LINK         O   ASP B 226                CA    CA B 503     1555   1555  2.35  
LINK         OD1 ASP B 226                CA    CA B 503     1555   1555  2.29  
LINK         O   PRO B 228                CA    CA B 503     1555   1555  2.20  
LINK         OE1 GLU B 229                MG    MG B 501     1555   1555  2.11  
LINK         OE2 GLU B 229                CA    CA B 503     1555   1555  2.41  
LINK         ND2 ASN B 249                 C1  NAG B 504     1555   1555  1.37  
LINK         ND2 ASN B 343                 C1  NAG B 509     1555   1555  1.58  
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         OD1 ASP C5003                MG    MG B 501     1555   1555  2.03  
LINK        CA    CA A 501                 O   HOH A 621     1555   1555  2.46  
LINK        CA    CA A 502                 O   HOH A 601     1555   1555  2.46  
LINK        CA    CA A 503                 O   HOH A 608     1555   1555  2.47  
LINK        CA    CA A 503                 O   HOH A 623     1555   1555  3.05  
LINK        CA    CA A 504                 O   HOH A 610     1555   1555  2.55  
LINK         O4  NAG A 505                 C1  NAG A 506     1555   1555  1.44  
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         O3  MAN A 509                 C1  MAN A 510     1555   1555  1.44  
LINK         O6  MAN A 509                 C1  MAN A 511     1555   1555  1.35  
LINK         O4  NAG A 512                 C1  NAG A 513     1555   1555  1.31  
LINK         O4  NAG A 514                 C1  NAG A 515     1555   1555  1.44  
LINK         O4  NAG A 515                 C1  BMA A 516     1555   1555  1.44  
LINK         O6  BMA A 516                 C1  MAN A 517     1555   1555  1.44  
LINK         O4  NAG A 518                 C1  NAG A 519     1555   1555  1.44  
LINK        MG    MG B 501                 O   HOH B 605     1555   1555  2.08  
LINK        MG    MG B 501                 O   HOH B 606     1555   1555  2.07  
LINK        CA    CA B 502                 O   HOH B 680     1555   1555  2.51  
LINK        CA    CA B 502                 O   HOH B 614     1555   1555  2.44  
LINK         O4  NAG B 504                 C1  NAG B 505     1555   1555  1.44  
LINK         O4  NAG B 506                 C1  NAG B 507     1555   1555  1.44  
LINK         O6  BMA A 507                 C1  MAN A 509     1555   1555  1.75  
CISPEP   1 GLN B   95    PRO B   96          0        -0.48                     
CISPEP   2 MET B  173    PRO B  174          0         2.70                     
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 621                                          
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 601                                          
SITE     1 AC3  7 ASP A 360  ASP A 362  ASP A 364  TYR A 366                    
SITE     2 AC3  7 ASP A 368  HOH A 608  HOH A 623                               
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 610                                          
SITE     1 AC5  6 SER B 132  SER B 134  GLU B 229  HOH B 605                    
SITE     2 AC5  6 HOH B 606  ASP C5003                                          
SITE     1 AC6  5 SER B 134  ASP B 137  ASP B 138  HOH B 614                    
SITE     2 AC6  5 HOH B 680                                                     
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  6 PRO A  15  GLY A  16  LYS A  41  ASN A  43                    
SITE     2 AC8  6 LEU A  50  GLN A  51                                          
SITE     1 AC9  1 ASN A 141                                                     
SITE     1 AD1  3 ASN A 256  TYR A 259  SER A 277                               
SITE     1 AD2  3 SER A 241  ASN A 266  ASP A 269                               
SITE     1 AD3  9 ALA A 222  TYR A 226  TYR A 261  SER A 272                    
SITE     2 AD3  9 LEU A 273  ASN A 275  MAN A 509  HOH A 616                    
SITE     3 AD3  9 HOH A 671                                                     
SITE     1 AD4  3 ASN B 192  ARG B 220  HOH B 669                               
SITE     1 AD5  1 ASN B 249                                                     
SITE     1 AD6  2 ASP B 137  ASN B 343                                          
SITE     1 AD7  2 GLY B 384  ASN B 386                                          
SITE     1 AD8  3 LYS B 382  ASN B 383  ASN B 397                               
SITE     1 AD9  6 ARG A 220  GLN A 221  ALA A 222  SER A 223                    
SITE     2 AD9  6 BMA A 507  HOH A 674                                          
CRYST1   60.980  118.390  170.290  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      0.016399  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008447  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005872        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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