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Database: PDB
Entry: 3K72
LinkDB: 3K72
Original site: 3K72 
HEADER    CELL ADHESION                           11-OCT-09   3K72              
TITLE     STRUCTURE OF INTEGRIN ALPHAX BETA2                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-X;                                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 20-1103;                                          
COMPND   5 SYNONYM: LEUKOCYTE ADHESION GLYCOPROTEIN P150,95 ALPHA               
COMPND   6 CHAIN, LEUKOCYTE ADHESION RECEPTOR P150,95, LEU M5, CD11             
COMPND   7 ANTIGEN-LIKE FAMILY MEMBER C;                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: INTEGRIN BETA-2;                                           
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: RESIDUES 23-700;                                           
COMPND  13 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA-                    
COMPND  14 1/CR3/P150,95 SUBUNIT BETA, COMPLEMENT RECEPTOR C3 SUBUNIT           
COMPND  15 BETA;                                                                
COMPND  16 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: CD11C, ITGAX;                                                  
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: CHO LEC 3.2.8.1;                           
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1;                                 
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: CD18, ITGB2, MFI7;                                             
SOURCE  17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  18 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: CHO LEC 3.2.8.1;                           
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PEF1/PURO                                 
KEYWDS    INTEGRIN, CELL ADHESION, CELL RECEPTOR, PYRROLIDONE                   
KEYWDS   2 CARBOXYLIC ACID                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.XIE,J.ZHU,X.CHEN,L.MI,N.NISHIDA,T.A.SPRINGER                        
REVDAT   2   02-MAR-10 3K72    1       JRNL                                     
REVDAT   1   12-JAN-10 3K72    0                                                
JRNL        AUTH   C.XIE,J.ZHU,X.CHEN,L.MI,N.NISHIDA,T.A.SPRINGER               
JRNL        TITL   STRUCTURE OF AN INTEGRIN WITH AN ALPHAI DOMAIN,              
JRNL        TITL 2 COMPLEMENT RECEPTOR TYPE 4.                                  
JRNL        REF    EMBO J.                       V.  29   666 2010              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   20033057                                                     
JRNL        DOI    10.1038/EMBOJ.2009.367                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 76217                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.315                           
REMARK   3   R VALUE            (WORKING SET) : 0.315                           
REMARK   3   FREE R VALUE                     : 0.335                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 843                             
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 48.4792 -  6.7184    0.99    12927   146  0.2750 0.2882        
REMARK   3     2  6.7184 -  5.3348    1.00    12585   167  0.2970 0.3611        
REMARK   3     3  5.3348 -  4.6610    0.99    12548   144  0.2645 0.2442        
REMARK   3     4  4.6610 -  4.2351    0.99    12449   128  0.2991 0.3708        
REMARK   3     5  4.2351 -  3.9317    0.99    12463   119  0.3637 0.3928        
REMARK   3     6  3.9317 -  3.7000    0.99    12402   139  0.4126 0.4249        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 150.00                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.690            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 124.30                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.093          48556                                  
REMARK   3   ANGLE     :  1.179          87257                                  
REMARK   3   CHIRALITY :  0.055           3798                                  
REMARK   3   PLANARITY :  0.006           7656                                  
REMARK   3   DIHEDRAL  : 19.718          12299                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN D AND RESSEQ 600-676                             
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1254   2.7088 121.6270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5731 T22:   0.9883                                     
REMARK   3      T33:   0.5809 T12:  -0.0630                                     
REMARK   3      T13:   0.0873 T23:  -0.1817                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -2.2257 L22:  -0.6547                                     
REMARK   3      L33:  -2.9061 L12:   0.8561                                     
REMARK   3      L13:  -1.3039 L23:   0.9459                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3667 S12:   0.3662 S13:  -0.1024                       
REMARK   3      S21:  -0.3536 S22:  -0.3367 S23:   0.1040                       
REMARK   3      S31:  -0.0890 S32:  -0.0513 S33:   0.0680                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 14                                          
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 1:126 or resseq         
REMARK   3                          330:595 or resseq 2005-2007)                
REMARK   3     SELECTION          : chain C and (resseq 1:126 or resseq         
REMARK   3                          330:595 or resseq 2005-2007)                
REMARK   3     ATOM PAIRS NUMBER  : 5796                                        
REMARK   3     RMSD               : 0.298                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 600:617 or resseq       
REMARK   3                          627:750 )                                   
REMARK   3     SELECTION          : chain C and (resseq 600:617 or resseq       
REMARK   3                          627:750 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 2275                                        
REMARK   3     RMSD               : 0.053                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 760:902 )               
REMARK   3     SELECTION          : chain C and (resseq 760:902 )               
REMARK   3     ATOM PAIRS NUMBER  : 2158                                        
REMARK   3     RMSD               : 0.625                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 903:986 or resseq       
REMARK   3                          995:1081 )                                  
REMARK   3     SELECTION          : chain C and (resseq 903:986 or resseq       
REMARK   3                          995:1081 )                                  
REMARK   3     ATOM PAIRS NUMBER  : 2709                                        
REMARK   3     RMSD               : 0.160                                       
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 1:56 )                  
REMARK   3     SELECTION          : chain D and (resseq 1:56 )                  
REMARK   3     ATOM PAIRS NUMBER  : 826                                         
REMARK   3     RMSD               : 0.005                                       
REMARK   3   NCS GROUP : 6                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 60:67 or resseq         
REMARK   3                          73:99 or resseq 348:423 )                   
REMARK   3     SELECTION          : chain D and (resseq 60:67 or resseq         
REMARK   3                          73:99 or resseq 348:423 )                   
REMARK   3     ATOM PAIRS NUMBER  : 1720                                        
REMARK   3     RMSD               : 0.096                                       
REMARK   3   NCS GROUP : 7                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 436:461 )               
REMARK   3     SELECTION          : chain D and (resseq 436:461 )               
REMARK   3     ATOM PAIRS NUMBER  : 366                                         
REMARK   3     RMSD               : 0.121                                       
REMARK   3   NCS GROUP : 8                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 102:342 or resid        
REMARK   3                          2002 )                                      
REMARK   3     SELECTION          : chain D and (resseq 102:342 or resid        
REMARK   3                          2002 )                                      
REMARK   3     ATOM PAIRS NUMBER  : 3752                                        
REMARK   3     RMSD               : 0.064                                       
REMARK   3   NCS GROUP : 9                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 463:473 )               
REMARK   3     SELECTION          : chain D and (resseq 463:473 )               
REMARK   3     ATOM PAIRS NUMBER  : 157                                         
REMARK   3     RMSD               : 0.590                                       
REMARK   3   NCS GROUP : 10                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 475:512 )               
REMARK   3     SELECTION          : chain D and (resseq 475:512 )               
REMARK   3     ATOM PAIRS NUMBER  : 534                                         
REMARK   3     RMSD               : 0.301                                       
REMARK   3   NCS GROUP : 11                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 516:550 )               
REMARK   3     SELECTION          : chain D and (resseq 516:550 )               
REMARK   3     ATOM PAIRS NUMBER  : 479                                         
REMARK   3     RMSD               : 0.009                                       
REMARK   3   NCS GROUP : 12                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 555:592 )               
REMARK   3     SELECTION          : chain D and (resseq 555:592 )               
REMARK   3     ATOM PAIRS NUMBER  : 568                                         
REMARK   3     RMSD               : 0.014                                       
REMARK   3   NCS GROUP : 13                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 593:597 )               
REMARK   3     SELECTION          : chain D and (resseq 593:597 )               
REMARK   3     ATOM PAIRS NUMBER  : 57                                          
REMARK   3     RMSD               : 0.520                                       
REMARK   3   NCS GROUP : 14                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 600:673 )               
REMARK   3     SELECTION          : chain D and (resseq 600:673 )               
REMARK   3     ATOM PAIRS NUMBER  : 1114                                        
REMARK   3     RMSD               : 0.021                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MLHL                                      
REMARK   4                                                                      
REMARK   4 3K72 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055627.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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) : 0.97928                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                   AND K-B PAIR OF BIOMORPH           
REMARK 200                                   MIRRORS FOR VERTICAL AND           
REMARK 200                                   HORIZONTAL FOCUSING                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76217                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : 0.10400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.35500                            
REMARK 200  R SYM FOR SHELL            (I) : 1.35500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.915M SODIUM/POTASSIUM PHOSPHATE,       
REMARK 280  PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
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       80.48100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      268.08900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       82.77450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      268.08900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       80.48100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       82.77450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       80.48100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       82.77450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      268.08900            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       82.77450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       80.48100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      268.08900            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 6380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 75600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 6330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 75320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 40540 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 286720 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       82.77450            
REMARK 350   BIOMT3   2  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     ARG A   128                                                      
REMARK 465     GLN A   129                                                      
REMARK 465     GLU A   130                                                      
REMARK 465     GLN A   131                                                      
REMARK 465     ASP A   132                                                      
REMARK 465     ILE A   133                                                      
REMARK 465     VAL A   134                                                      
REMARK 465     PHE A   135                                                      
REMARK 465     LEU A   136                                                      
REMARK 465     ILE A   137                                                      
REMARK 465     ASP A   138                                                      
REMARK 465     GLY A   139                                                      
REMARK 465     SER A   140                                                      
REMARK 465     GLY A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     ILE A   143                                                      
REMARK 465     SER A   144                                                      
REMARK 465     SER A   145                                                      
REMARK 465     ARG A   146                                                      
REMARK 465     ASN A   147                                                      
REMARK 465     PHE A   148                                                      
REMARK 465     ALA A   149                                                      
REMARK 465     THR A   150                                                      
REMARK 465     MET A   151                                                      
REMARK 465     MET A   152                                                      
REMARK 465     ASN A   153                                                      
REMARK 465     PHE A   154                                                      
REMARK 465     VAL A   155                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     ALA A   157                                                      
REMARK 465     VAL A   158                                                      
REMARK 465     ILE A   159                                                      
REMARK 465     SER A   160                                                      
REMARK 465     GLN A   161                                                      
REMARK 465     PHE A   162                                                      
REMARK 465     GLN A   163                                                      
REMARK 465     ARG A   164                                                      
REMARK 465     PRO A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     THR A   167                                                      
REMARK 465     GLN A   168                                                      
REMARK 465     PHE A   169                                                      
REMARK 465     SER A   170                                                      
REMARK 465     LEU A   171                                                      
REMARK 465     MET A   172                                                      
REMARK 465     GLN A   173                                                      
REMARK 465     PHE A   174                                                      
REMARK 465     SER A   175                                                      
REMARK 465     ASN A   176                                                      
REMARK 465     LYS A   177                                                      
REMARK 465     PHE A   178                                                      
REMARK 465     GLN A   179                                                      
REMARK 465     THR A   180                                                      
REMARK 465     HIS A   181                                                      
REMARK 465     PHE A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     PHE A   184                                                      
REMARK 465     GLU A   185                                                      
REMARK 465     GLU A   186                                                      
REMARK 465     PHE A   187                                                      
REMARK 465     ARG A   188                                                      
REMARK 465     ARG A   189                                                      
REMARK 465     SER A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     ASN A   192                                                      
REMARK 465     PRO A   193                                                      
REMARK 465     LEU A   194                                                      
REMARK 465     SER A   195                                                      
REMARK 465     LEU A   196                                                      
REMARK 465     LEU A   197                                                      
REMARK 465     ALA A   198                                                      
REMARK 465     SER A   199                                                      
REMARK 465     VAL A   200                                                      
REMARK 465     HIS A   201                                                      
REMARK 465     GLN A   202                                                      
REMARK 465     LEU A   203                                                      
REMARK 465     GLN A   204                                                      
REMARK 465     GLY A   205                                                      
REMARK 465     PHE A   206                                                      
REMARK 465     THR A   207                                                      
REMARK 465     TYR A   208                                                      
REMARK 465     THR A   209                                                      
REMARK 465     ALA A   210                                                      
REMARK 465     THR A   211                                                      
REMARK 465     ALA A   212                                                      
REMARK 465     ILE A   213                                                      
REMARK 465     GLN A   214                                                      
REMARK 465     ASN A   215                                                      
REMARK 465     VAL A   216                                                      
REMARK 465     VAL A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     ARG A   219                                                      
REMARK 465     LEU A   220                                                      
REMARK 465     PHE A   221                                                      
REMARK 465     HIS A   222                                                      
REMARK 465     ALA A   223                                                      
REMARK 465     SER A   224                                                      
REMARK 465     TYR A   225                                                      
REMARK 465     GLY A   226                                                      
REMARK 465     ALA A   227                                                      
REMARK 465     ARG A   228                                                      
REMARK 465     ARG A   229                                                      
REMARK 465     ASP A   230                                                      
REMARK 465     ALA A   231                                                      
REMARK 465     ALA A   232                                                      
REMARK 465     LYS A   233                                                      
REMARK 465     ILE A   234                                                      
REMARK 465     LEU A   235                                                      
REMARK 465     ILE A   236                                                      
REMARK 465     VAL A   237                                                      
REMARK 465     ILE A   238                                                      
REMARK 465     THR A   239                                                      
REMARK 465     ASP A   240                                                      
REMARK 465     GLY A   241                                                      
REMARK 465     LYS A   242                                                      
REMARK 465     LYS A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     GLY A   245                                                      
REMARK 465     ASP A   246                                                      
REMARK 465     SER A   247                                                      
REMARK 465     LEU A   248                                                      
REMARK 465     ASP A   249                                                      
REMARK 465     TYR A   250                                                      
REMARK 465     LYS A   251                                                      
REMARK 465     ASP A   252                                                      
REMARK 465     VAL A   253                                                      
REMARK 465     ILE A   254                                                      
REMARK 465     PRO A   255                                                      
REMARK 465     MET A   256                                                      
REMARK 465     ALA A   257                                                      
REMARK 465     ASP A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     ALA A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ILE A   262                                                      
REMARK 465     ILE A   263                                                      
REMARK 465     ARG A   264                                                      
REMARK 465     TYR A   265                                                      
REMARK 465     ALA A   266                                                      
REMARK 465     ILE A   267                                                      
REMARK 465     GLY A   268                                                      
REMARK 465     VAL A   269                                                      
REMARK 465     GLY A   270                                                      
REMARK 465     LEU A   271                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     PHE A   273                                                      
REMARK 465     GLN A   274                                                      
REMARK 465     ASN A   275                                                      
REMARK 465     ARG A   276                                                      
REMARK 465     ASN A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     TRP A   279                                                      
REMARK 465     LYS A   280                                                      
REMARK 465     GLU A   281                                                      
REMARK 465     LEU A   282                                                      
REMARK 465     ASN A   283                                                      
REMARK 465     ASP A   284                                                      
REMARK 465     ILE A   285                                                      
REMARK 465     ALA A   286                                                      
REMARK 465     SER A   287                                                      
REMARK 465     LYS A   288                                                      
REMARK 465     PRO A   289                                                      
REMARK 465     SER A   290                                                      
REMARK 465     GLN A   291                                                      
REMARK 465     GLU A   292                                                      
REMARK 465     HIS A   293                                                      
REMARK 465     ILE A   294                                                      
REMARK 465     PHE A   295                                                      
REMARK 465     LYS A   296                                                      
REMARK 465     VAL A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     ASP A   299                                                      
REMARK 465     PHE A   300                                                      
REMARK 465     ASP A   301                                                      
REMARK 465     ALA A   302                                                      
REMARK 465     LEU A   303                                                      
REMARK 465     LYS A   304                                                      
REMARK 465     ASP A   305                                                      
REMARK 465     ILE A   306                                                      
REMARK 465     GLN A   307                                                      
REMARK 465     ASN A   308                                                      
REMARK 465     GLN A   309                                                      
REMARK 465     LEU A   310                                                      
REMARK 465     LYS A   311                                                      
REMARK 465     GLU A   312                                                      
REMARK 465     LYS A   313                                                      
REMARK 465     ILE A   314                                                      
REMARK 465     PHE A   315                                                      
REMARK 465     ALA A   316                                                      
REMARK 465     ILE A   317                                                      
REMARK 465     GLU A   318                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     THR A   320                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     THR A   322                                                      
REMARK 465     THR A   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     SER A   325                                                      
REMARK 465     VAL A  1083                                                      
REMARK 465     HIS A  1084                                                      
REMARK 465     GLY A  1085                                                      
REMARK 465     CYS A  1086                                                      
REMARK 465     GLY A  1087                                                      
REMARK 465     GLY A  1088                                                      
REMARK 465     LEU A  1089                                                      
REMARK 465     GLU A  1090                                                      
REMARK 465     ASN A  1091                                                      
REMARK 465     LEU A  1092                                                      
REMARK 465     TYR A  1093                                                      
REMARK 465     PHE A  1094                                                      
REMARK 465     GLN A  1095                                                      
REMARK 465     VAL B   674                                                      
REMARK 465     ALA B   675                                                      
REMARK 465     GLY B   676                                                      
REMARK 465     PRO B   677                                                      
REMARK 465     ASP B   678                                                      
REMARK 465     GLY B   679                                                      
REMARK 465     CYS B   680                                                      
REMARK 465     GLY B   681                                                      
REMARK 465     GLU B   682                                                      
REMARK 465     ASN B   683                                                      
REMARK 465     LEU B   684                                                      
REMARK 465     TYR B   685                                                      
REMARK 465     PHE B   686                                                      
REMARK 465     GLN B   687                                                      
REMARK 465     ARG C   128                                                      
REMARK 465     GLN C   129                                                      
REMARK 465     GLU C   130                                                      
REMARK 465     GLN C   131                                                      
REMARK 465     ASP C   132                                                      
REMARK 465     ILE C   133                                                      
REMARK 465     VAL C   134                                                      
REMARK 465     PHE C   135                                                      
REMARK 465     LEU C   136                                                      
REMARK 465     ILE C   137                                                      
REMARK 465     ASP C   138                                                      
REMARK 465     GLY C   139                                                      
REMARK 465     SER C   140                                                      
REMARK 465     GLY C   141                                                      
REMARK 465     SER C   142                                                      
REMARK 465     ILE C   143                                                      
REMARK 465     SER C   144                                                      
REMARK 465     SER C   145                                                      
REMARK 465     ARG C   146                                                      
REMARK 465     ASN C   147                                                      
REMARK 465     PHE C   148                                                      
REMARK 465     ALA C   149                                                      
REMARK 465     THR C   150                                                      
REMARK 465     MET C   151                                                      
REMARK 465     MET C   152                                                      
REMARK 465     ASN C   153                                                      
REMARK 465     PHE C   154                                                      
REMARK 465     VAL C   155                                                      
REMARK 465     ARG C   156                                                      
REMARK 465     ALA C   157                                                      
REMARK 465     VAL C   158                                                      
REMARK 465     ILE C   159                                                      
REMARK 465     SER C   160                                                      
REMARK 465     GLN C   161                                                      
REMARK 465     PHE C   162                                                      
REMARK 465     GLN C   163                                                      
REMARK 465     ARG C   164                                                      
REMARK 465     PRO C   165                                                      
REMARK 465     SER C   166                                                      
REMARK 465     THR C   167                                                      
REMARK 465     GLN C   168                                                      
REMARK 465     PHE C   169                                                      
REMARK 465     SER C   170                                                      
REMARK 465     LEU C   171                                                      
REMARK 465     MET C   172                                                      
REMARK 465     GLN C   173                                                      
REMARK 465     PHE C   174                                                      
REMARK 465     SER C   175                                                      
REMARK 465     ASN C   176                                                      
REMARK 465     LYS C   177                                                      
REMARK 465     PHE C   178                                                      
REMARK 465     GLN C   179                                                      
REMARK 465     THR C   180                                                      
REMARK 465     HIS C   181                                                      
REMARK 465     PHE C   182                                                      
REMARK 465     THR C   183                                                      
REMARK 465     PHE C   184                                                      
REMARK 465     GLU C   185                                                      
REMARK 465     GLU C   186                                                      
REMARK 465     PHE C   187                                                      
REMARK 465     ARG C   188                                                      
REMARK 465     ARG C   189                                                      
REMARK 465     SER C   190                                                      
REMARK 465     SER C   191                                                      
REMARK 465     ASN C   192                                                      
REMARK 465     PRO C   193                                                      
REMARK 465     LEU C   194                                                      
REMARK 465     SER C   195                                                      
REMARK 465     LEU C   196                                                      
REMARK 465     LEU C   197                                                      
REMARK 465     ALA C   198                                                      
REMARK 465     SER C   199                                                      
REMARK 465     VAL C   200                                                      
REMARK 465     HIS C   201                                                      
REMARK 465     GLN C   202                                                      
REMARK 465     LEU C   203                                                      
REMARK 465     GLN C   204                                                      
REMARK 465     GLY C   205                                                      
REMARK 465     PHE C   206                                                      
REMARK 465     THR C   207                                                      
REMARK 465     TYR C   208                                                      
REMARK 465     THR C   209                                                      
REMARK 465     ALA C   210                                                      
REMARK 465     THR C   211                                                      
REMARK 465     ALA C   212                                                      
REMARK 465     ILE C   213                                                      
REMARK 465     GLN C   214                                                      
REMARK 465     ASN C   215                                                      
REMARK 465     VAL C   216                                                      
REMARK 465     VAL C   217                                                      
REMARK 465     HIS C   218                                                      
REMARK 465     ARG C   219                                                      
REMARK 465     LEU C   220                                                      
REMARK 465     PHE C   221                                                      
REMARK 465     HIS C   222                                                      
REMARK 465     ALA C   223                                                      
REMARK 465     SER C   224                                                      
REMARK 465     TYR C   225                                                      
REMARK 465     GLY C   226                                                      
REMARK 465     ALA C   227                                                      
REMARK 465     ARG C   228                                                      
REMARK 465     ARG C   229                                                      
REMARK 465     ASP C   230                                                      
REMARK 465     ALA C   231                                                      
REMARK 465     ALA C   232                                                      
REMARK 465     LYS C   233                                                      
REMARK 465     ILE C   234                                                      
REMARK 465     LEU C   235                                                      
REMARK 465     ILE C   236                                                      
REMARK 465     VAL C   237                                                      
REMARK 465     ILE C   238                                                      
REMARK 465     THR C   239                                                      
REMARK 465     ASP C   240                                                      
REMARK 465     GLY C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     LYS C   243                                                      
REMARK 465     GLU C   244                                                      
REMARK 465     GLY C   245                                                      
REMARK 465     ASP C   246                                                      
REMARK 465     SER C   247                                                      
REMARK 465     LEU C   248                                                      
REMARK 465     ASP C   249                                                      
REMARK 465     TYR C   250                                                      
REMARK 465     LYS C   251                                                      
REMARK 465     ASP C   252                                                      
REMARK 465     VAL C   253                                                      
REMARK 465     ILE C   254                                                      
REMARK 465     PRO C   255                                                      
REMARK 465     MET C   256                                                      
REMARK 465     ALA C   257                                                      
REMARK 465     ASP C   258                                                      
REMARK 465     ALA C   259                                                      
REMARK 465     ALA C   260                                                      
REMARK 465     GLY C   261                                                      
REMARK 465     ILE C   262                                                      
REMARK 465     ILE C   263                                                      
REMARK 465     ARG C   264                                                      
REMARK 465     TYR C   265                                                      
REMARK 465     ALA C   266                                                      
REMARK 465     ILE C   267                                                      
REMARK 465     GLY C   268                                                      
REMARK 465     VAL C   269                                                      
REMARK 465     GLY C   270                                                      
REMARK 465     LEU C   271                                                      
REMARK 465     ALA C   272                                                      
REMARK 465     PHE C   273                                                      
REMARK 465     GLN C   274                                                      
REMARK 465     ASN C   275                                                      
REMARK 465     ARG C   276                                                      
REMARK 465     ASN C   277                                                      
REMARK 465     SER C   278                                                      
REMARK 465     TRP C   279                                                      
REMARK 465     LYS C   280                                                      
REMARK 465     GLU C   281                                                      
REMARK 465     LEU C   282                                                      
REMARK 465     ASN C   283                                                      
REMARK 465     ASP C   284                                                      
REMARK 465     ILE C   285                                                      
REMARK 465     ALA C   286                                                      
REMARK 465     SER C   287                                                      
REMARK 465     LYS C   288                                                      
REMARK 465     PRO C   289                                                      
REMARK 465     SER C   290                                                      
REMARK 465     GLN C   291                                                      
REMARK 465     GLU C   292                                                      
REMARK 465     HIS C   293                                                      
REMARK 465     ILE C   294                                                      
REMARK 465     PHE C   295                                                      
REMARK 465     LYS C   296                                                      
REMARK 465     VAL C   297                                                      
REMARK 465     GLU C   298                                                      
REMARK 465     ASP C   299                                                      
REMARK 465     PHE C   300                                                      
REMARK 465     ASP C   301                                                      
REMARK 465     ALA C   302                                                      
REMARK 465     LEU C   303                                                      
REMARK 465     LYS C   304                                                      
REMARK 465     ASP C   305                                                      
REMARK 465     ILE C   306                                                      
REMARK 465     GLN C   307                                                      
REMARK 465     ASN C   308                                                      
REMARK 465     GLN C   309                                                      
REMARK 465     LEU C   310                                                      
REMARK 465     LYS C   311                                                      
REMARK 465     GLU C   312                                                      
REMARK 465     LYS C   313                                                      
REMARK 465     ILE C   314                                                      
REMARK 465     PHE C   315                                                      
REMARK 465     ALA C   316                                                      
REMARK 465     ILE C   317                                                      
REMARK 465     GLU C   318                                                      
REMARK 465     GLY C   319                                                      
REMARK 465     THR C   320                                                      
REMARK 465     GLU C   321                                                      
REMARK 465     THR C   322                                                      
REMARK 465     THR C   323                                                      
REMARK 465     SER C   324                                                      
REMARK 465     SER C   325                                                      
REMARK 465     SER C   326                                                      
REMARK 465     SER C   327                                                      
REMARK 465     VAL C  1083                                                      
REMARK 465     HIS C  1084                                                      
REMARK 465     GLY C  1085                                                      
REMARK 465     CYS C  1086                                                      
REMARK 465     GLY C  1087                                                      
REMARK 465     GLY C  1088                                                      
REMARK 465     LEU C  1089                                                      
REMARK 465     GLU C  1090                                                      
REMARK 465     ASN C  1091                                                      
REMARK 465     LEU C  1092                                                      
REMARK 465     TYR C  1093                                                      
REMARK 465     PHE C  1094                                                      
REMARK 465     GLN C  1095                                                      
REMARK 465     VAL D   674                                                      
REMARK 465     ALA D   675                                                      
REMARK 465     GLY D   676                                                      
REMARK 465     PRO D   677                                                      
REMARK 465     ASP D   678                                                      
REMARK 465     GLY D   679                                                      
REMARK 465     CYS D   680                                                      
REMARK 465     GLY D   681                                                      
REMARK 465     GLU D   682                                                      
REMARK 465     ASN D   683                                                      
REMARK 465     LEU D   684                                                      
REMARK 465     TYR D   685                                                      
REMARK 465     PHE D   686                                                      
REMARK 465     GLN D   687                                                      
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   ND2  ASN A   678     C2   NAG A  3678              1.70            
REMARK 500   ND2  ASN C   678     C2   NAG C  3678              1.70            
REMARK 500   CG   ASN B   479     C1   NAG B  3479              1.85            
REMARK 500   ND2  ASN C   880     C2   NAG C  3880              1.91            
REMARK 500   ND2  ASN D   479     C2   NAG D  3479              2.03            
REMARK 500   O4   NAG A  3717     O5   MAN A  3718              2.10            
REMARK 500   OD1  ASN B   479     O5   NAG B  3479              2.12            
REMARK 500   ND2  ASN D    94     C2   NAG D  3094              2.17            
REMARK 500   OD2  ASP C   659     C8   NAG C  3716              2.18            
REMARK 500   SG   CYS B   437     CB   CYS B   448              2.19            
REMARK 500   CG   ASN B    94     C1   NAG B  3094              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER A 326   CA    SER A 326   CB      0.096                       
REMARK 500    SER A 326   CB    SER A 326   OG      0.088                       
REMARK 500    SER A 327   CA    SER A 327   CB      0.099                       
REMARK 500    ASN B 479   CB    ASN B 479   CG      0.159                       
REMARK 500    ASN D 479   CB    ASN D 479   CG      0.169                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 478   CA  -  CB  -  CG  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    LEU C 478   CA  -  CB  -  CG  ANGL. DEV. =  19.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   2       54.90   -119.06                                   
REMARK 500    GLU A   6      -67.46   -150.27                                   
REMARK 500    ARG A  12       72.52   -104.29                                   
REMARK 500    ALA A  16     -109.58     67.19                                   
REMARK 500    ALA A  26      137.37    -30.70                                   
REMARK 500    GLN A  36       32.35    -97.68                                   
REMARK 500    ALA A  40     -142.24     63.30                                   
REMARK 500    ASN A  42       56.06     35.06                                   
REMARK 500    GLN A  43     -133.15   -110.51                                   
REMARK 500    THR A  44     -167.79    -76.98                                   
REMARK 500    ASN A  70       39.66     36.12                                   
REMARK 500    SER A  72       71.41     38.31                                   
REMARK 500    ALA A  78      140.21   -172.96                                   
REMARK 500    SER A  82      -72.70    -67.52                                   
REMARK 500    THR A  92       43.00   -147.70                                   
REMARK 500    LEU A 110     -162.56   -108.43                                   
REMARK 500    PRO A 112       47.17    -76.27                                   
REMARK 500    THR A 113     -139.80   -148.55                                   
REMARK 500    VAL A 121       11.30     58.96                                   
REMARK 500    GLN A 124       95.10    -67.36                                   
REMARK 500    SER A 327      -35.99   -163.18                                   
REMARK 500    GLU A 329      -82.22   -120.28                                   
REMARK 500    LEU A 330       57.02   -148.61                                   
REMARK 500    GLN A 334       45.33     38.54                                   
REMARK 500    THR A 342      148.65    176.91                                   
REMARK 500    ASP A 344       57.90   -107.31                                   
REMARK 500    PRO A 346      176.69    -58.49                                   
REMARK 500    PHE A 354     -112.98     74.76                                   
REMARK 500    THR A 355       43.10    -84.37                                   
REMARK 500    PRO A 364     -169.71    -75.82                                   
REMARK 500    ASN A 366      -11.38     72.50                                   
REMARK 500    THR A 370     -168.44   -109.08                                   
REMARK 500    ASN A 373     -155.66    -95.14                                   
REMARK 500    SER A 375     -179.01     58.99                                   
REMARK 500    ASP A 380     -164.09    -75.92                                   
REMARK 500    ASP A 383       69.41     60.08                                   
REMARK 500    LEU A 386      109.43    -50.91                                   
REMARK 500    ALA A 393       50.54   -155.54                                   
REMARK 500    LEU A 394      155.22    -46.30                                   
REMARK 500    ALA A 405       79.50   -117.17                                   
REMARK 500    THR A 411      -61.01   -106.49                                   
REMARK 500    GLN A 423      -72.49   -146.29                                   
REMARK 500    TYR A 438       40.79     74.27                                   
REMARK 500    ALA A 441      -71.11    -41.31                                   
REMARK 500    ASP A 449     -130.82   -106.60                                   
REMARK 500    SER A 450       25.92   -151.00                                   
REMARK 500    ALA A 461       58.96   -165.57                                   
REMARK 500    HIS A 463       63.07   -110.09                                   
REMARK 500    TYR A 465     -176.25   -179.26                                   
REMARK 500    GLU A 466      -38.06   -151.40                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     463 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A   82     PRO A   83                  129.23                    
REMARK 500 ARG A  118     LEU A  119                  148.43                    
REMARK 500 SER A  326     SER A  327                 -136.85                    
REMARK 500 SER A  327     PHE A  328                 -139.29                    
REMARK 500 VAL A  490     LEU A  491                 -141.42                    
REMARK 500 LEU A  558     SER A  559                  149.91                    
REMARK 500 VAL A  624     VAL A  625                 -144.06                    
REMARK 500 VAL A  625     SER A  626                  136.92                    
REMARK 500 GLY A  816     GLN A  817                 -124.61                    
REMARK 500 GLN A  821     LEU A  822                 -136.24                    
REMARK 500 SER A  824     LEU A  825                 -132.22                    
REMARK 500 ARG A  889     THR A  890                 -141.54                    
REMARK 500 LEU A 1063     PRO A 1064                 -149.66                    
REMARK 500 ALA B  100     LYS B  101                 -149.04                    
REMARK 500 CYS B  425     ARG B  426                 -148.59                    
REMARK 500 SER C   82     PRO C   83                  129.91                    
REMARK 500 ARG C  118     LEU C  119                  147.81                    
REMARK 500 VAL C  490     LEU C  491                 -141.46                    
REMARK 500 LEU C  558     SER C  559                  149.90                    
REMARK 500 GLU C  622     GLN C  623                  148.95                    
REMARK 500 VAL C  624     VAL C  625                 -144.36                    
REMARK 500 VAL C  625     SER C  626                  142.95                    
REMARK 500 GLY C  816     GLN C  817                 -104.12                    
REMARK 500 GLN C  817     LYS C  818                  122.94                    
REMARK 500 GLN C  819     GLY C  820                  143.59                    
REMARK 500 GLY C  820     GLN C  821                  142.15                    
REMARK 500 GLN C  821     LEU C  822                 -139.24                    
REMARK 500 SER C  824     LEU C  825                 -133.98                    
REMARK 500 ARG C  889     THR C  890                 -141.44                    
REMARK 500 LEU C 1063     PRO C 1064                 -149.36                    
REMARK 500 CYS D  427     ARG D  428                 -133.18                    
REMARK 500 GLN D  430     SER D  431                 -136.11                    
REMARK 500 SER D  431     ARG D  432                  144.36                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MAN C 3378                                                       
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 A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 447   OD1                                                    
REMARK 620 2 ASP A 449   OD1  54.0                                              
REMARK 620 3 SER A 453   O   119.6 118.3                                        
REMARK 620 4 ASP A 455   OD2 119.4  75.7 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 574   OD1                                                    
REMARK 620 2 ASP A 578   O    65.5                                              
REMARK 620 3 ASP A 578   OD1 106.8  52.7                                        
REMARK 620 4 LEU A 580   O   101.5  83.6 106.1                                  
REMARK 620 5 ASP A 582   OD1 146.7 147.8 100.3  88.9                            
REMARK 620 6 ASP A 582   OD2 102.2 153.8 115.8 122.3  47.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 116   O                                                      
REMARK 620 2 ASP B 119   OD1 115.8                                              
REMARK 620 3 ASP B 120   OD1 142.1  71.9                                        
REMARK 620 4 GLU B 325   O   155.6  81.5  57.3                                  
REMARK 620 5 GLU B 325   OE2  78.9 150.7 113.0  78.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 447   OD1                                                    
REMARK 620 2 ASP C 449   OD1  54.7                                              
REMARK 620 3 SER C 453   O   119.8 118.1                                        
REMARK 620 4 ASP C 455   OD2 120.1  76.1 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 574   OD1                                                    
REMARK 620 2 ASP C 578   O    65.4                                              
REMARK 620 3 ASP C 578   OD1 107.6  53.0                                        
REMARK 620 4 LEU C 580   O    99.5  82.5 105.8                                  
REMARK 620 5 ASP C 582   OD1 146.9 147.7 100.4  89.3                            
REMARK 620 6 ASP C 582   OD2 102.8 155.3 117.1 121.8  47.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D 116   O                                                      
REMARK 620 2 ASP D 119   OD1 115.8                                              
REMARK 620 3 ASP D 120   OD1 142.5  71.8                                        
REMARK 620 4 GLU D 325   O   155.9  81.4  56.5                                  
REMARK 620 5 GLU D 325   OE2  79.2 150.2 113.0  78.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3042                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3043                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3373                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3374                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3375                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3376                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3377                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3678                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3716                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3717                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3718                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3880                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3881                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3882                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3094                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3479                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3042                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3043                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3373                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3374                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 3375                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 3376                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 3377                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 3378                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3678                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3716                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3717                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 3718                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3880                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3094                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3479                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3K6S   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AN INTEGRIN WITH AN I DOMAIN, COMPLEMENT                
REMARK 900 RECEPTOR TYPE 4                                                      
REMARK 900 RELATED ID: 3K71   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF INTEGRIN ALPHAX BETA2 ECTODOMAIN                        
DBREF  3K72 A    1  1084  UNP    P20702   ITAX_HUMAN      20   1103             
DBREF  3K72 B    1   683  UNP    P05107   ITB2_HUMAN      23    700             
DBREF  3K72 C    1  1084  UNP    P20702   ITAX_HUMAN      20   1103             
DBREF  3K72 D    1   683  UNP    P05107   ITB2_HUMAN      23    700             
SEQADV 3K72 GLY A 1085  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 CYS A 1086  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 GLY A 1087  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 GLY A 1088  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 LEU A 1089  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 GLU A 1090  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 ASN A 1091  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 LEU A 1092  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 TYR A 1093  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 PHE A 1094  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 GLN A 1095  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 ASP B  678  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 GLY B  679  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 CYS B  680  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 GLY B  681  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 GLU B  682  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 LEU B  684  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 TYR B  685  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 PHE B  686  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 GLN B  687  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 GLY C 1085  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 CYS C 1086  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 GLY C 1087  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 GLY C 1088  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 LEU C 1089  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 GLU C 1090  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 ASN C 1091  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 LEU C 1092  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 TYR C 1093  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 PHE C 1094  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 GLN C 1095  UNP  P20702              EXPRESSION TAG                 
SEQADV 3K72 ASP D  678  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 GLY D  679  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 CYS D  680  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 GLY D  681  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 GLU D  682  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 LEU D  684  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 TYR D  685  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 PHE D  686  UNP  P05107              EXPRESSION TAG                 
SEQADV 3K72 GLN D  687  UNP  P05107              EXPRESSION TAG                 
SEQRES   1 A 1095  PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL          
SEQRES   2 A 1095  ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA          
SEQRES   3 A 1095  ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR          
SEQRES   4 A 1095  ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR          
SEQRES   5 A 1095  SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO          
SEQRES   6 A 1095  PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA          
SEQRES   7 A 1095  SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO          
SEQRES   8 A 1095  THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR          
SEQRES   9 A 1095  GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN          
SEQRES  10 A 1095  ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU          
SEQRES  11 A 1095  GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE          
SEQRES  12 A 1095  SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG          
SEQRES  13 A 1095  ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE          
SEQRES  14 A 1095  SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE          
SEQRES  15 A 1095  THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER          
SEQRES  16 A 1095  LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR          
SEQRES  17 A 1095  THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE          
SEQRES  18 A 1095  HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE          
SEQRES  19 A 1095  LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER          
SEQRES  20 A 1095  LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA          
SEQRES  21 A 1095  GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE          
SEQRES  22 A 1095  GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA          
SEQRES  23 A 1095  SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP          
SEQRES  24 A 1095  PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU          
SEQRES  25 A 1095  LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER          
SEQRES  26 A 1095  SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER          
SEQRES  27 A 1095  ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL          
SEQRES  28 A 1095  GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO          
SEQRES  29 A 1095  PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU          
SEQRES  30 A 1095  ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR          
SEQRES  31 A 1095  GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU          
SEQRES  32 A 1095  GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE          
SEQRES  33 A 1095  PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU          
SEQRES  34 A 1095  VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER          
SEQRES  35 A 1095  LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP          
SEQRES  36 A 1095  LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR          
SEQRES  37 A 1095  ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY          
SEQRES  38 A 1095  TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU          
SEQRES  39 A 1095  GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR          
SEQRES  40 A 1095  VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL          
SEQRES  41 A 1095  VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA          
SEQRES  42 A 1095  VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER          
SEQRES  43 A 1095  PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER          
SEQRES  44 A 1095  SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY          
SEQRES  45 A 1095  GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL          
SEQRES  46 A 1095  GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO          
SEQRES  47 A 1095  VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA          
SEQRES  48 A 1095  GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL          
SEQRES  49 A 1095  VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU          
SEQRES  50 A 1095  TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG          
SEQRES  51 A 1095  ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP          
SEQRES  52 A 1095  PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR          
SEQRES  53 A 1095  LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU          
SEQRES  54 A 1095  LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER          
SEQRES  55 A 1095  CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU          
SEQRES  56 A 1095  ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG          
SEQRES  57 A 1095  ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR          
SEQRES  58 A 1095  PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA          
SEQRES  59 A 1095  ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER          
SEQRES  60 A 1095  PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU          
SEQRES  61 A 1095  GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU          
SEQRES  62 A 1095  ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA          
SEQRES  63 A 1095  GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN          
SEQRES  64 A 1095  GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA          
SEQRES  65 A 1095  PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG          
SEQRES  66 A 1095  ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR          
SEQRES  67 A 1095  PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU          
SEQRES  68 A 1095  GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU          
SEQRES  69 A 1095  ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU          
SEQRES  70 A 1095  GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER          
SEQRES  71 A 1095  SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU          
SEQRES  72 A 1095  SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR          
SEQRES  73 A 1095  GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER          
SEQRES  74 A 1095  ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA          
SEQRES  75 A 1095  VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO          
SEQRES  76 A 1095  SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA          
SEQRES  77 A 1095  SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU          
SEQRES  78 A 1095  ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP          
SEQRES  79 A 1095  VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR          
SEQRES  80 A 1095  LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE          
SEQRES  81 A 1095  LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE          
SEQRES  82 A 1095  THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN          
SEQRES  83 A 1095  GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU          
SEQRES  84 A 1095  LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU          
SEQRES  85 A 1095  TYR PHE GLN                                                  
SEQRES   1 B  687  GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU          
SEQRES   2 B  687  CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS          
SEQRES   3 B  687  LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG          
SEQRES   4 B  687  CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA          
SEQRES   5 B  687  ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR          
SEQRES   6 B  687  GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO          
SEQRES   7 B  687  GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA          
SEQRES   8 B  687  ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO          
SEQRES   9 B  687  ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET          
SEQRES  10 B  687  LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP          
SEQRES  11 B  687  LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG          
SEQRES  12 B  687  ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO          
SEQRES  13 B  687  PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS          
SEQRES  14 B  687  PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE          
SEQRES  15 B  687  ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE          
SEQRES  16 B  687  GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU          
SEQRES  17 B  687  ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL          
SEQRES  18 B  687  ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR          
SEQRES  19 B  687  ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE          
SEQRES  20 B  687  ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN          
SEQRES  21 B  687  ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG          
SEQRES  22 B  687  SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA          
SEQRES  23 B  687  HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA          
SEQRES  24 B  687  VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR          
SEQRES  25 B  687  GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU          
SEQRES  26 B  687  ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR          
SEQRES  27 B  687  ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA          
SEQRES  28 B  687  LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS          
SEQRES  29 B  687  SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP          
SEQRES  30 B  687  CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN          
SEQRES  31 B  687  VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER          
SEQRES  32 B  687  PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR          
SEQRES  33 B  687  VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP          
SEQRES  34 B  687  GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE          
SEQRES  35 B  687  LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE          
SEQRES  36 B  687  GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER          
SEQRES  37 B  687  GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER          
SEQRES  38 B  687  ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN          
SEQRES  39 B  687  CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE          
SEQRES  40 B  687  TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU          
SEQRES  41 B  687  ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY          
SEQRES  42 B  687  LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE          
SEQRES  43 B  687  GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY          
SEQRES  44 B  687  CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY          
SEQRES  45 B  687  ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR          
SEQRES  46 B  687  GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER          
SEQRES  47 B  687  PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS          
SEQRES  48 B  687  PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA          
SEQRES  49 B  687  CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY          
SEQRES  50 B  687  ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL          
SEQRES  51 B  687  ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR          
SEQRES  52 B  687  LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ALA GLY          
SEQRES  53 B  687  PRO ASP GLY CYS GLY GLU ASN LEU TYR PHE GLN                  
SEQRES   1 C 1095  PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL          
SEQRES   2 C 1095  ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA          
SEQRES   3 C 1095  ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR          
SEQRES   4 C 1095  ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR          
SEQRES   5 C 1095  SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO          
SEQRES   6 C 1095  PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA          
SEQRES   7 C 1095  SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO          
SEQRES   8 C 1095  THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR          
SEQRES   9 C 1095  GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN          
SEQRES  10 C 1095  ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU          
SEQRES  11 C 1095  GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE          
SEQRES  12 C 1095  SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG          
SEQRES  13 C 1095  ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE          
SEQRES  14 C 1095  SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE          
SEQRES  15 C 1095  THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER          
SEQRES  16 C 1095  LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR          
SEQRES  17 C 1095  THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE          
SEQRES  18 C 1095  HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE          
SEQRES  19 C 1095  LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER          
SEQRES  20 C 1095  LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA          
SEQRES  21 C 1095  GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE          
SEQRES  22 C 1095  GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA          
SEQRES  23 C 1095  SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP          
SEQRES  24 C 1095  PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU          
SEQRES  25 C 1095  LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER          
SEQRES  26 C 1095  SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER          
SEQRES  27 C 1095  ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL          
SEQRES  28 C 1095  GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO          
SEQRES  29 C 1095  PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU          
SEQRES  30 C 1095  ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR          
SEQRES  31 C 1095  GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU          
SEQRES  32 C 1095  GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE          
SEQRES  33 C 1095  PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU          
SEQRES  34 C 1095  VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER          
SEQRES  35 C 1095  LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP          
SEQRES  36 C 1095  LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR          
SEQRES  37 C 1095  ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY          
SEQRES  38 C 1095  TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU          
SEQRES  39 C 1095  GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR          
SEQRES  40 C 1095  VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL          
SEQRES  41 C 1095  VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA          
SEQRES  42 C 1095  VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER          
SEQRES  43 C 1095  PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER          
SEQRES  44 C 1095  SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY          
SEQRES  45 C 1095  GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL          
SEQRES  46 C 1095  GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO          
SEQRES  47 C 1095  VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA          
SEQRES  48 C 1095  GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL          
SEQRES  49 C 1095  VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU          
SEQRES  50 C 1095  TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG          
SEQRES  51 C 1095  ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP          
SEQRES  52 C 1095  PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR          
SEQRES  53 C 1095  LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU          
SEQRES  54 C 1095  LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER          
SEQRES  55 C 1095  CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU          
SEQRES  56 C 1095  ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG          
SEQRES  57 C 1095  ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR          
SEQRES  58 C 1095  PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA          
SEQRES  59 C 1095  ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER          
SEQRES  60 C 1095  PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU          
SEQRES  61 C 1095  GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU          
SEQRES  62 C 1095  ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA          
SEQRES  63 C 1095  GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN          
SEQRES  64 C 1095  GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA          
SEQRES  65 C 1095  PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG          
SEQRES  66 C 1095  ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR          
SEQRES  67 C 1095  PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU          
SEQRES  68 C 1095  GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU          
SEQRES  69 C 1095  ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU          
SEQRES  70 C 1095  GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER          
SEQRES  71 C 1095  SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU          
SEQRES  72 C 1095  SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR          
SEQRES  73 C 1095  GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER          
SEQRES  74 C 1095  ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA          
SEQRES  75 C 1095  VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO          
SEQRES  76 C 1095  SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA          
SEQRES  77 C 1095  SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU          
SEQRES  78 C 1095  ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP          
SEQRES  79 C 1095  VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR          
SEQRES  80 C 1095  LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE          
SEQRES  81 C 1095  LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE          
SEQRES  82 C 1095  THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN          
SEQRES  83 C 1095  GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU          
SEQRES  84 C 1095  LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU          
SEQRES  85 C 1095  TYR PHE GLN                                                  
SEQRES   1 D  687  GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU          
SEQRES   2 D  687  CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS          
SEQRES   3 D  687  LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG          
SEQRES   4 D  687  CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA          
SEQRES   5 D  687  ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR          
SEQRES   6 D  687  GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO          
SEQRES   7 D  687  GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA          
SEQRES   8 D  687  ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO          
SEQRES   9 D  687  ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET          
SEQRES  10 D  687  LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP          
SEQRES  11 D  687  LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG          
SEQRES  12 D  687  ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO          
SEQRES  13 D  687  PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS          
SEQRES  14 D  687  PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE          
SEQRES  15 D  687  ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE          
SEQRES  16 D  687  GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU          
SEQRES  17 D  687  ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL          
SEQRES  18 D  687  ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR          
SEQRES  19 D  687  ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE          
SEQRES  20 D  687  ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN          
SEQRES  21 D  687  ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG          
SEQRES  22 D  687  SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA          
SEQRES  23 D  687  HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA          
SEQRES  24 D  687  VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR          
SEQRES  25 D  687  GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU          
SEQRES  26 D  687  ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR          
SEQRES  27 D  687  ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA          
SEQRES  28 D  687  LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS          
SEQRES  29 D  687  SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP          
SEQRES  30 D  687  CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN          
SEQRES  31 D  687  VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER          
SEQRES  32 D  687  PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR          
SEQRES  33 D  687  VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP          
SEQRES  34 D  687  GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE          
SEQRES  35 D  687  LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE          
SEQRES  36 D  687  GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER          
SEQRES  37 D  687  GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER          
SEQRES  38 D  687  ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN          
SEQRES  39 D  687  CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE          
SEQRES  40 D  687  TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU          
SEQRES  41 D  687  ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY          
SEQRES  42 D  687  LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE          
SEQRES  43 D  687  GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY          
SEQRES  44 D  687  CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY          
SEQRES  45 D  687  ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR          
SEQRES  46 D  687  GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER          
SEQRES  47 D  687  PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS          
SEQRES  48 D  687  PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA          
SEQRES  49 D  687  CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY          
SEQRES  50 D  687  ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL          
SEQRES  51 D  687  ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR          
SEQRES  52 D  687  LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ALA GLY          
SEQRES  53 D  687  PRO ASP GLY CYS GLY GLU ASN LEU TYR PHE GLN                  
MODRES 3K72 ASN A   42  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN A  373  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN A  678  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN A  716  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN A  880  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN B   94  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN B  479  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN C   42  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN C  373  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN C  678  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN C  716  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN C  880  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN D   94  ASN  GLYCOSYLATION SITE                                 
MODRES 3K72 ASN D  479  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A3042      14                                                       
HET    NAG  A3043      14                                                       
HET    NAG  A3373      14                                                       
HET    NAG  A3374      14                                                       
HET    MAN  A3375      11                                                       
HET    MAN  A3376      11                                                       
HET    MAN  A3377      11                                                       
HET    NAG  A3678      14                                                       
HET    NAG  A3716      14                                                       
HET    NAG  A3717      14                                                       
HET    MAN  A3718      11                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    NAG  A3880      14                                                       
HET    NAG  A3881      14                                                       
HET    MAN  A3882      11                                                       
HET    NAG  B3094      14                                                       
HET     CA  B2002       1                                                       
HET    NAG  B3479      14                                                       
HET    NAG  C3042      14                                                       
HET    NAG  C3043      14                                                       
HET    NAG  C3373      14                                                       
HET    NAG  C3374      14                                                       
HET    MAN  C3375      11                                                       
HET    MAN  C3376      11                                                       
HET    MAN  C3377      11                                                       
HET    MAN  C3378      11                                                       
HET    NAG  C3678      14                                                       
HET    NAG  C3716      14                                                       
HET    NAG  C3717      14                                                       
HET    MAN  C3718      11                                                       
HET    NAG  C3880      14                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET    NAG  D3094      14                                                       
HET     CA  D2002       1                                                       
HET    NAG  D3479      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      CA CALCIUM ION                                                      
FORMUL   5  NAG    21(C8 H15 N O6)                                              
FORMUL   6  MAN    10(C6 H12 O6)                                                
FORMUL   9   CA    8(CA 2+)                                                     
HELIX    1   1 ARG A  407  THR A  411  5                                   5    
HELIX    2   2 ASP A  990  ASN A  998  1                                   9    
HELIX    3   3 PHE A 1034  GLN A 1039  5                                   6    
HELIX    4   4 GLU A 1067  PHE A 1069  5                                   3    
HELIX    5   5 SER B   10  GLU B   16  1                                   7    
HELIX    6   6 ASP B   36  ILE B   38  5                                   3    
HELIX    7   7 THR B   42  GLY B   50  1                                   9    
HELIX    8   8 MET B  117  ASN B  123  1                                   7    
HELIX    9   9 ASP B  130  GLU B  137  1                                   8    
HELIX   10  10 SER B  192  LYS B  201  1                                  10    
HELIX   11  11 GLY B  213  ALA B  222  1                                  10    
HELIX   12  12 CYS B  224  GLY B  229  1                                   6    
HELIX   13  13 GLY B  249  ALA B  255  5                                   7    
HELIX   14  14 ARG B  273  PHE B  277  5                                   5    
HELIX   15  15 GLY B  283  ASN B  292  1                                  10    
HELIX   16  16 THR B  301  VAL B  305  5                                   5    
HELIX   17  17 LYS B  306  ILE B  315  1                                  10    
HELIX   18  18 VAL B  331  ASN B  336  1                                   6    
HELIX   19  19 ASN B  336  SER B  342  1                                   7    
HELIX   20  20 LEU B  436  GLY B  439  5                                   4    
HELIX   21  21 GLN B  469  GLY B  473  5                                   5    
HELIX   22  22 ILE B  482  GLY B  486  5                                   5    
HELIX   23  23 GLY B  528  ARG B  532  1                                   5    
HELIX   24  24 TYR B  603  GLU B  608  1                                   6    
HELIX   25  25 ARG C  407  THR C  411  5                                   5    
HELIX   26  26 ASP C  990  ASN C  998  1                                   9    
HELIX   27  27 PHE C 1034  GLN C 1039  5                                   6    
HELIX   28  28 GLU C 1067  PHE C 1069  5                                   3    
HELIX   29  29 SER D   10  GLU D   16  1                                   7    
HELIX   30  30 ASP D   36  ILE D   38  5                                   3    
HELIX   31  31 THR D   42  GLY D   50  1                                   9    
HELIX   32  32 MET D  117  ASN D  123  1                                   7    
HELIX   33  33 ASP D  130  GLU D  137  1                                   8    
HELIX   34  34 SER D  192  LYS D  201  1                                  10    
HELIX   35  35 GLY D  213  ALA D  222  1                                  10    
HELIX   36  36 CYS D  224  GLY D  229  1                                   6    
HELIX   37  37 GLY D  249  ALA D  255  5                                   7    
HELIX   38  38 ARG D  273  PHE D  277  5                                   5    
HELIX   39  39 GLY D  283  ASN D  292  1                                  10    
HELIX   40  40 THR D  301  VAL D  305  5                                   5    
HELIX   41  41 LYS D  306  ILE D  315  1                                  10    
HELIX   42  42 VAL D  330  ILE D  334  5                                   5    
HELIX   43  43 ASN D  336  SER D  342  1                                   7    
HELIX   44  44 GLN D  469  GLY D  473  5                                   5    
HELIX   45  45 ILE D  482  GLY D  486  5                                   5    
HELIX   46  46 GLY D  528  ARG D  532  1                                   5    
HELIX   47  47 TYR D  603  GLU D  608  1                                   6    
SHEET    1   A 4 THR A   9  PHE A  11  0                                        
SHEET    2   A 4 VAL A 591  ARG A 595 -1  O  VAL A 591   N  PHE A  11           
SHEET    3   A 4 ASP A 582  ALA A 587 -1  N  VAL A 585   O  LEU A 592           
SHEET    4   A 4 PHE A 565  GLN A 573 -1  N  GLY A 566   O  GLY A 586           
SHEET    1   B 4 SER A  21  GLN A  24  0                                        
SHEET    2   B 4 TRP A  29  GLY A  33 -1  O  VAL A  31   N  VAL A  23           
SHEET    3   B 4 LEU A  47  GLY A  51 -1  O  TYR A  48   N  VAL A  32           
SHEET    4   B 4 ALA A  56  PRO A  59 -1  O  GLU A  58   N  GLN A  49           
SHEET    1   C 4 SER A  76  THR A  80  0                                        
SHEET    2   C 4 GLN A  85  GLY A  90 -1  O  LEU A  87   N  ALA A  78           
SHEET    3   C 4 LEU A 106  LEU A 110 -1  O  LEU A 106   N  GLY A  90           
SHEET    4   C 4 THR A 116  GLN A 117 -1  O  THR A 116   N  LEU A 109           
SHEET    1   D 2 HIS A  94  HIS A  95  0                                        
SHEET    2   D 2 TYR A 102  LEU A 103 -1  O  TYR A 102   N  HIS A  95           
SHEET    1   E 3 VAL A 347  ALA A 350  0                                        
SHEET    2   E 3 GLY A 359  LEU A 362 -1  O  GLY A 359   N  ALA A 350           
SHEET    3   E 3 THR A 370  ILE A 372 -1  O  THR A 370   N  LEU A 362           
SHEET    1   F 4 THR A 390  GLU A 391  0                                        
SHEET    2   F 4 SER A 400  ALA A 405 -1  O  VAL A 402   N  GLU A 391           
SHEET    3   F 4 LYS A 413  THR A 418 -1  O  PHE A 417   N  LEU A 401           
SHEET    4   F 4 MET A 426  VAL A 430 -1  O  ALA A 428   N  ILE A 416           
SHEET    1   G 3 LEU A 443  VAL A 446  0                                        
SHEET    2   G 3 LEU A 456  GLY A 460 -1  O  LEU A 458   N  CYS A 444           
SHEET    3   G 3 VAL A 473  PRO A 477 -1  O  CYS A 476   N  VAL A 457           
SHEET    1   H 3 LEU A 506  GLY A 510  0                                        
SHEET    2   H 3 ASP A 519  GLY A 523 -1  O  ASP A 519   N  GLY A 510           
SHEET    3   H 3 VAL A 534  HIS A 538 -1  O  PHE A 537   N  VAL A 520           
SHEET    1   I 3 VAL A 602  PHE A 608  0                                        
SHEET    2   I 3 THR A 629  ILE A 639 -1  O  TYR A 638   N  GLY A 603           
SHEET    3   I 3 CYS A 693  LEU A 700 -1  O  PHE A 696   N  SER A 633           
SHEET    1   J 4 SER A 680  LEU A 687  0                                        
SHEET    2   J 4 SER A 654  LEU A 662 -1  N  SER A 654   O  LEU A 687           
SHEET    3   J 4 ILE A 711  PHE A 717 -1  O  ARG A 714   N  ALA A 661           
SHEET    4   J 4 TYR A 741  LEU A 746 -1  O  LEU A 746   N  ILE A 711           
SHEET    1   K 4 ILE A 764  SER A 767  0                                        
SHEET    2   K 4 ASN A 783  VAL A 788 -1  O  MET A 787   N  SER A 765           
SHEET    3   K 4 ILE A 857  VAL A 865 -1  O  PHE A 859   N  VAL A 786           
SHEET    4   K 4 LEU A 808  ARG A 811 -1  N  ARG A 811   O  THR A 862           
SHEET    1   L 3 LEU A 775  VAL A 776  0                                        
SHEET    2   L 3 LYS A 902  VAL A 905  1  O  ALA A 904   N  VAL A 776           
SHEET    3   L 3 TYR A1060  GLN A1062  1  O  SER A1061   N  TYR A 903           
SHEET    1   M10 THR A 828  PRO A 833  0                                        
SHEET    2   M10 THR A 839  ARG A 845 -1  O  SER A 843   N  ASP A 830           
SHEET    3   M10 THR A 799  PRO A 805 -1  N  HIS A 804   O  TRP A 840           
SHEET    4   M10 ARG A 874  SER A 882 -1  O  ASN A 880   N  THR A 801           
SHEET    5   M10 GLN A 896  PRO A 900 -1  O  LEU A 899   N  LEU A 875           
SHEET    6   M10 GLN C 896  PRO C 900 -1  O  GLU C 898   N  GLN A 896           
SHEET    7   M10 ARG C 874  SER C 882 -1  N  LEU C 875   O  LEU C 899           
SHEET    8   M10 THR C 799  PRO C 805 -1  N  THR C 801   O  ASN C 880           
SHEET    9   M10 THR C 839  ARG C 845 -1  O  TRP C 840   N  HIS C 804           
SHEET   10   M10 THR C 828  PRO C 833 -1  N  ASP C 830   O  SER C 843           
SHEET    1   N 4 THR A 907  SER A 911  0                                        
SHEET    2   N 4 ALA A 932  ASN A 940 -1  O  GLN A 937   N  SER A 910           
SHEET    3   N 4 ASP A1025  GLY A1030 -1  O  LEU A1028   N  HIS A 934           
SHEET    4   N 4 GLU A 968  SER A 970 -1  N  GLU A 968   O  LYS A1029           
SHEET    1   O 5 CYS A 979  ILE A 984  0                                        
SHEET    2   O 5 CYS A1008  VAL A1015 -1  O  ARG A1010   N  GLU A 982           
SHEET    3   O 5 VAL A 948  TRP A 953 -1  N  ILE A 950   O  CYS A1013           
SHEET    4   O 5 SER A1046  THR A1054 -1  O  GLU A1052   N  ASN A 951           
SHEET    5   O 5 VAL A1000  LEU A1001  1  N  LEU A1001   O  VAL A1048           
SHEET    1   P 5 CYS A 979  ILE A 984  0                                        
SHEET    2   P 5 CYS A1008  VAL A1015 -1  O  ARG A1010   N  GLU A 982           
SHEET    3   P 5 VAL A 948  TRP A 953 -1  N  ILE A 950   O  CYS A1013           
SHEET    4   P 5 SER A1046  THR A1054 -1  O  GLU A1052   N  ASN A 951           
SHEET    5   P 5 ARG A1071  VAL A1077 -1  O  THR A1076   N  VAL A1047           
SHEET    1   Q 3 CYS B  40  ASP B  41  0                                        
SHEET    2   Q 3 THR B  22  CYS B  24 -1  N  THR B  22   O  ASP B  41           
SHEET    3   Q 3 ILE B  56  MET B  57 -1  O  MET B  57   N  TRP B  23           
SHEET    1   R 3 LEU B  83  LEU B  85  0                                        
SHEET    2   R 3 THR B 416  PRO B 421  1  O  LEU B 420   N  LEU B  83           
SHEET    3   R 3 GLN B 402  VAL B 405 -1  N  GLN B 402   O  VAL B 419           
SHEET    1   S 3 ALA B  91  PHE B  97  0                                        
SHEET    2   S 3 ILE B 387  ALA B 395 -1  O  VAL B 393   N  ALA B  91           
SHEET    3   S 3 LEU B 356  THR B 359 -1  N  LYS B 357   O  THR B 394           
SHEET    1   T 4 ARG B 183  THR B 189  0                                        
SHEET    2   T 4 ILE B 144  PHE B 149 -1  N  ILE B 144   O  THR B 189           
SHEET    3   T 4 LEU B 107  ASP B 112  1  N  TYR B 109   O  GLY B 147           
SHEET    4   T 4 LEU B 236  ALA B 240  1  O  ALA B 240   N  ASP B 112           
SHEET    1   U 2 PHE B 298  VAL B 300  0                                        
SHEET    2   U 2 VAL B 320  GLU B 322  1  O  GLY B 321   N  VAL B 300           
SHEET    1   V 2 GLY B 441  LEU B 443  0                                        
SHEET    2   V 2 CYS B 448  CYS B 450 -1  O  ARG B 449   N  PHE B 442           
SHEET    1   W 2 TYR B 454  ILE B 455  0                                        
SHEET    2   W 2 CYS B 461  GLN B 462 -1  O  CYS B 461   N  ILE B 455           
SHEET    1   X 2 GLY B 488  VAL B 491  0                                        
SHEET    2   X 2 GLN B 494  CYS B 497 -1  O  GLN B 494   N  VAL B 491           
SHEET    1   Y 2 ILE B 507  TYR B 508  0                                        
SHEET    2   Y 2 CYS B 514  ASP B 515 -1  O  CYS B 514   N  TYR B 508           
SHEET    1   Z 2 GLY B 533  PHE B 536  0                                        
SHEET    2   Z 2 LYS B 539  CYS B 542 -1  O  LYS B 539   N  PHE B 536           
SHEET    1  AA 3 CYS B 640  ARG B 643  0                                        
SHEET    2  AA 3 TRP B 649  LEU B 654 -1  O  TYR B 652   N  CYS B 640           
SHEET    3  AA 3 ILE B 665  VAL B 667 -1  O  TYR B 666   N  THR B 653           
SHEET    1  AB 4 THR C   9  PHE C  11  0                                        
SHEET    2  AB 4 VAL C 591  ARG C 595 -1  O  VAL C 591   N  PHE C  11           
SHEET    3  AB 4 ASP C 582  ALA C 587 -1  N  VAL C 585   O  LEU C 592           
SHEET    4  AB 4 PHE C 565  GLN C 573 -1  N  GLY C 566   O  GLY C 586           
SHEET    1  AC 4 SER C  21  GLN C  24  0                                        
SHEET    2  AC 4 TRP C  29  GLY C  33 -1  O  VAL C  31   N  VAL C  23           
SHEET    3  AC 4 LEU C  47  GLY C  51 -1  O  TYR C  48   N  VAL C  32           
SHEET    4  AC 4 ALA C  56  PRO C  59 -1  O  GLU C  58   N  GLN C  49           
SHEET    1  AD 4 SER C  76  THR C  80  0                                        
SHEET    2  AD 4 GLN C  85  GLY C  90 -1  O  LEU C  87   N  ALA C  78           
SHEET    3  AD 4 LEU C 106  LEU C 110 -1  O  LEU C 106   N  GLY C  90           
SHEET    4  AD 4 THR C 116  GLN C 117 -1  O  THR C 116   N  LEU C 109           
SHEET    1  AE 2 HIS C  94  HIS C  95  0                                        
SHEET    2  AE 2 TYR C 102  LEU C 103 -1  O  TYR C 102   N  HIS C  95           
SHEET    1  AF 3 VAL C 347  ALA C 350  0                                        
SHEET    2  AF 3 GLY C 359  LEU C 362 -1  O  GLY C 359   N  ALA C 350           
SHEET    3  AF 3 THR C 370  ILE C 372 -1  O  THR C 370   N  LEU C 362           
SHEET    1  AG 4 THR C 390  GLU C 391  0                                        
SHEET    2  AG 4 SER C 400  ALA C 405 -1  O  VAL C 402   N  GLU C 391           
SHEET    3  AG 4 LYS C 413  THR C 418 -1  O  PHE C 417   N  LEU C 401           
SHEET    4  AG 4 MET C 426  VAL C 430 -1  O  ALA C 428   N  ILE C 416           
SHEET    1  AH 3 LEU C 443  VAL C 446  0                                        
SHEET    2  AH 3 LEU C 456  GLY C 460 -1  O  LEU C 458   N  CYS C 444           
SHEET    3  AH 3 VAL C 473  PRO C 477 -1  O  CYS C 476   N  VAL C 457           
SHEET    1  AI 3 LEU C 506  GLY C 510  0                                        
SHEET    2  AI 3 ASP C 519  GLY C 523 -1  O  ASP C 519   N  GLY C 510           
SHEET    3  AI 3 VAL C 534  HIS C 538 -1  O  PHE C 537   N  VAL C 520           
SHEET    1  AJ 3 VAL C 602  PHE C 608  0                                        
SHEET    2  AJ 3 THR C 629  ILE C 639 -1  O  TYR C 638   N  GLY C 603           
SHEET    3  AJ 3 CYS C 693  LEU C 700 -1  O  PHE C 696   N  SER C 633           
SHEET    1  AK 4 SER C 680  LEU C 687  0                                        
SHEET    2  AK 4 SER C 654  LEU C 662 -1  N  SER C 654   O  LEU C 687           
SHEET    3  AK 4 ILE C 711  PHE C 717 -1  O  ARG C 714   N  ALA C 661           
SHEET    4  AK 4 TYR C 741  LEU C 746 -1  O  LEU C 746   N  ILE C 711           
SHEET    1  AL 4 ILE C 764  SER C 767  0                                        
SHEET    2  AL 4 GLU C 781  VAL C 788 -1  O  MET C 787   N  SER C 765           
SHEET    3  AL 4 ILE C 857  VAL C 865 -1  O  PHE C 859   N  VAL C 786           
SHEET    4  AL 4 LEU C 808  ARG C 811 -1  N  ARG C 811   O  THR C 862           
SHEET    1  AM 3 LEU C 775  VAL C 776  0                                        
SHEET    2  AM 3 LYS C 902  VAL C 905  1  O  ALA C 904   N  VAL C 776           
SHEET    3  AM 3 TYR C1060  GLN C1062  1  O  SER C1061   N  TYR C 903           
SHEET    1  AN 4 THR C 907  SER C 911  0                                        
SHEET    2  AN 4 ALA C 932  ASN C 940 -1  O  GLN C 937   N  SER C 910           
SHEET    3  AN 4 ASP C1025  GLY C1030 -1  O  LEU C1028   N  HIS C 934           
SHEET    4  AN 4 GLU C 968  SER C 970 -1  N  GLU C 968   O  LYS C1029           
SHEET    1  AO 5 CYS C 979  ILE C 984  0                                        
SHEET    2  AO 5 CYS C1008  VAL C1015 -1  O  ARG C1010   N  GLU C 982           
SHEET    3  AO 5 VAL C 948  TRP C 953 -1  N  ILE C 950   O  CYS C1013           
SHEET    4  AO 5 SER C1046  THR C1054 -1  O  GLU C1052   N  ASN C 951           
SHEET    5  AO 5 VAL C1000  LEU C1001  1  N  LEU C1001   O  VAL C1048           
SHEET    1  AP 5 CYS C 979  ILE C 984  0                                        
SHEET    2  AP 5 CYS C1008  VAL C1015 -1  O  ARG C1010   N  GLU C 982           
SHEET    3  AP 5 VAL C 948  TRP C 953 -1  N  ILE C 950   O  CYS C1013           
SHEET    4  AP 5 SER C1046  THR C1054 -1  O  GLU C1052   N  ASN C 951           
SHEET    5  AP 5 ARG C1071  VAL C1077 -1  O  THR C1076   N  VAL C1047           
SHEET    1  AQ 3 CYS D  40  ASP D  41  0                                        
SHEET    2  AQ 3 THR D  22  CYS D  24 -1  N  THR D  22   O  ASP D  41           
SHEET    3  AQ 3 ILE D  56  MET D  57 -1  O  MET D  57   N  TRP D  23           
SHEET    1  AR 3 LEU D  83  LEU D  85  0                                        
SHEET    2  AR 3 THR D 416  PRO D 421  1  O  LEU D 420   N  LEU D  83           
SHEET    3  AR 3 GLN D 402  VAL D 405 -1  N  PHE D 404   O  VAL D 417           
SHEET    1  AS 3 ALA D  91  PHE D  97  0                                        
SHEET    2  AS 3 ILE D 387  ALA D 395 -1  O  VAL D 393   N  ALA D  91           
SHEET    3  AS 3 LEU D 356  THR D 359 -1  N  LYS D 357   O  THR D 394           
SHEET    1  AT 4 ARG D 183  THR D 189  0                                        
SHEET    2  AT 4 ILE D 144  PHE D 149 -1  N  ILE D 144   O  THR D 189           
SHEET    3  AT 4 LEU D 107  ASP D 112  1  N  TYR D 109   O  GLY D 147           
SHEET    4  AT 4 LEU D 236  ALA D 240  1  O  ALA D 240   N  ASP D 112           
SHEET    1  AU 2 PHE D 298  VAL D 300  0                                        
SHEET    2  AU 2 VAL D 320  GLU D 322  1  O  GLY D 321   N  VAL D 300           
SHEET    1  AV 2 GLY D 441  LEU D 443  0                                        
SHEET    2  AV 2 CYS D 448  CYS D 450 -1  O  ARG D 449   N  PHE D 442           
SHEET    1  AW 2 TYR D 454  ILE D 455  0                                        
SHEET    2  AW 2 CYS D 461  GLN D 462 -1  O  CYS D 461   N  ILE D 455           
SHEET    1  AX 2 GLY D 488  VAL D 491  0                                        
SHEET    2  AX 2 GLN D 494  CYS D 497 -1  O  GLN D 494   N  VAL D 491           
SHEET    1  AY 2 ILE D 507  TYR D 508  0                                        
SHEET    2  AY 2 CYS D 514  ASP D 515 -1  O  CYS D 514   N  TYR D 508           
SHEET    1  AZ 2 GLY D 533  PHE D 536  0                                        
SHEET    2  AZ 2 LYS D 539  CYS D 542 -1  O  LYS D 539   N  PHE D 536           
SHEET    1  BA 3 CYS D 640  ARG D 643  0                                        
SHEET    2  BA 3 TRP D 649  LEU D 654 -1  O  TYR D 652   N  CYS D 640           
SHEET    3  BA 3 ILE D 665  VAL D 667 -1  O  TYR D 666   N  THR D 653           
SSBOND   1 CYS A   50    CYS A   57                          1555   1555  2.03  
SSBOND   2 CYS A   89    CYS A  107                          1555   1555  2.04  
SSBOND   3 CYS A   97    CYS A  126                          1555   1555  2.03  
SSBOND   4 CYS A  476    CYS A  487                          1555   1555  2.03  
SSBOND   5 CYS A  620    CYS A  703                          1555   1555  2.04  
SSBOND   6 CYS A  636    CYS A  693                          1555   1555  2.04  
SSBOND   7 CYS A  752    CYS A  758                          1555   1555  2.01  
SSBOND   8 CYS A  829    CYS A  844                          1555   1555  2.04  
SSBOND   9 CYS A  979    CYS A 1013                          1555   1555  2.03  
SSBOND  10 CYS A 1003    CYS A 1008                          1555   1555  2.03  
SSBOND  11 CYS B    3    CYS B   21                          1555   1555  2.03  
SSBOND  12 CYS B   11    CYS B  425                          1555   1555  2.02  
SSBOND  13 CYS B   14    CYS B   40                          1555   1555  2.03  
SSBOND  14 CYS B   24    CYS B   51                          1555   1555  2.03  
SSBOND  15 CYS B  169    CYS B  176                          1555   1555  2.03  
SSBOND  16 CYS B  224    CYS B  264                          1555   1555  2.03  
SSBOND  17 CYS B  364    CYS B  378                          1555   1555  2.03  
SSBOND  18 CYS B  398    CYS B  423                          1555   1555  2.06  
SSBOND  19 CYS B  427    CYS B  445                          1555   1555  2.06  
SSBOND  20 CYS B  437    CYS B  448                          1555   1555  2.03  
SSBOND  21 CYS B  450    CYS B  459                          1555   1555  2.03  
SSBOND  22 CYS B  461    CYS B  492                          1555   1555  2.06  
SSBOND  23 CYS B  475    CYS B  490                          1555   1555  2.03  
SSBOND  24 CYS B  484    CYS B  495                          1555   1555  2.03  
SSBOND  25 CYS B  497    CYS B  512                          1555   1555  2.02  
SSBOND  26 CYS B  514    CYS B  537                          1555   1555  2.03  
SSBOND  27 CYS B  519    CYS B  535                          1555   1555  2.03  
SSBOND  28 CYS B  527    CYS B  540                          1555   1555  2.03  
SSBOND  29 CYS B  542    CYS B  551                          1555   1555  2.04  
SSBOND  30 CYS B  553    CYS B  576                          1555   1555  2.03  
SSBOND  31 CYS B  560    CYS B  574                          1555   1555  2.03  
SSBOND  32 CYS B  568    CYS B  579                          1555   1555  2.03  
SSBOND  33 CYS B  581    CYS B  590                          1555   1555  2.03  
SSBOND  34 CYS B  593    CYS B  596                          1555   1555  2.03  
SSBOND  35 CYS B  600    CYS B  640                          1555   1555  2.03  
SSBOND  36 CYS B  606    CYS B  625                          1555   1555  2.03  
SSBOND  37 CYS B  609    CYS B  621                          1555   1555  2.03  
SSBOND  38 CYS B  648    CYS B  673                          1555   1555  2.03  
SSBOND  39 CYS C   50    CYS C   57                          1555   1555  2.03  
SSBOND  40 CYS C   89    CYS C  107                          1555   1555  2.06  
SSBOND  41 CYS C   97    CYS C  126                          1555   1555  2.03  
SSBOND  42 CYS C  476    CYS C  487                          1555   1555  2.03  
SSBOND  43 CYS C  620    CYS C  703                          1555   1555  2.01  
SSBOND  44 CYS C  636    CYS C  693                          1555   1555  2.04  
SSBOND  45 CYS C  752    CYS C  758                          1555   1555  2.01  
SSBOND  46 CYS C  829    CYS C  844                          1555   1555  2.04  
SSBOND  47 CYS C  979    CYS C 1013                          1555   1555  2.04  
SSBOND  48 CYS C 1003    CYS C 1008                          1555   1555  2.02  
SSBOND  49 CYS D    3    CYS D   21                          1555   1555  2.03  
SSBOND  50 CYS D   11    CYS D  425                          1555   1555  1.96  
SSBOND  51 CYS D   14    CYS D   40                          1555   1555  2.03  
SSBOND  52 CYS D   24    CYS D   51                          1555   1555  2.03  
SSBOND  53 CYS D  169    CYS D  176                          1555   1555  2.03  
SSBOND  54 CYS D  224    CYS D  264                          1555   1555  2.03  
SSBOND  55 CYS D  364    CYS D  378                          1555   1555  2.03  
SSBOND  56 CYS D  398    CYS D  423                          1555   1555  2.02  
SSBOND  57 CYS D  427    CYS D  445                          1555   1555  2.13  
SSBOND  58 CYS D  437    CYS D  448                          1555   1555  2.29  
SSBOND  59 CYS D  450    CYS D  459                          1555   1555  2.03  
SSBOND  60 CYS D  461    CYS D  492                          1555   1555  1.99  
SSBOND  61 CYS D  475    CYS D  490                          1555   1555  2.04  
SSBOND  62 CYS D  484    CYS D  495                          1555   1555  2.03  
SSBOND  63 CYS D  497    CYS D  512                          1555   1555  2.03  
SSBOND  64 CYS D  514    CYS D  537                          1555   1555  2.04  
SSBOND  65 CYS D  519    CYS D  535                          1555   1555  2.03  
SSBOND  66 CYS D  527    CYS D  540                          1555   1555  2.03  
SSBOND  67 CYS D  542    CYS D  551                          1555   1555  2.04  
SSBOND  68 CYS D  553    CYS D  576                          1555   1555  2.03  
SSBOND  69 CYS D  560    CYS D  574                          1555   1555  2.03  
SSBOND  70 CYS D  568    CYS D  579                          1555   1555  2.03  
SSBOND  71 CYS D  581    CYS D  590                          1555   1555  2.03  
SSBOND  72 CYS D  593    CYS D  596                          1555   1555  2.06  
SSBOND  73 CYS D  600    CYS D  640                          1555   1555  2.03  
SSBOND  74 CYS D  606    CYS D  625                          1555   1555  2.03  
SSBOND  75 CYS D  609    CYS D  621                          1555   1555  2.03  
SSBOND  76 CYS D  648    CYS D  673                          1555   1555  2.03  
LINK         ND2 ASN A  42                 C1  NAG A3042     1555   1555  1.44  
LINK         ND2 ASN A 373                 C1  NAG A3373     1555   1555  1.45  
LINK         OD1 ASP A 447                CA    CA A2005     1555   1555  2.76  
LINK         OD1 ASP A 449                CA    CA A2005     1555   1555  2.90  
LINK         O   SER A 453                CA    CA A2005     1555   1555  2.58  
LINK         OD2 ASP A 455                CA    CA A2005     1555   1555  2.92  
LINK         O   LEU A 517                CA    CA A2006     1555   1555  2.60  
LINK         OD1 ASP A 574                CA    CA A2007     1555   1555  2.93  
LINK         O   ASP A 578                CA    CA A2007     1555   1555  2.69  
LINK         OD1 ASP A 578                CA    CA A2007     1555   1555  2.50  
LINK         O   LEU A 580                CA    CA A2007     1555   1555  2.49  
LINK         OD1 ASP A 582                CA    CA A2007     1555   1555  2.81  
LINK         OD2 ASP A 582                CA    CA A2007     1555   1555  2.67  
LINK         ND2 ASN A 678                 C1  NAG A3678     1555   1555  1.44  
LINK         ND2 ASN A 716                 C1  NAG A3716     1555   1555  1.46  
LINK         ND2 ASN A 880                 C1  NAG A3880     1555   1555  1.44  
LINK         ND2 ASN B  94                 C1  NAG B3094     1555   1555  1.44  
LINK         O   SER B 116                CA    CA B2002     1555   1555  2.53  
LINK         OD1 ASP B 119                CA    CA B2002     1555   1555  2.32  
LINK         OD1 ASP B 120                CA    CA B2002     1555   1555  2.10  
LINK         O   GLU B 325                CA    CA B2002     1555   1555  2.70  
LINK         OE2 GLU B 325                CA    CA B2002     1555   1555  2.33  
LINK         ND2 ASN B 479                 C1  NAG B3479     1555   1555  1.41  
LINK         ND2 ASN C  42                 C1  NAG C3042     1555   1555  1.45  
LINK         ND2 ASN C 373                 C1  NAG C3373     1555   1555  1.45  
LINK         OD1 ASP C 447                CA    CA C2005     1555   1555  2.76  
LINK         OD1 ASP C 449                CA    CA C2005     1555   1555  2.87  
LINK         O   SER C 453                CA    CA C2005     1555   1555  2.61  
LINK         OD2 ASP C 455                CA    CA C2005     1555   1555  2.93  
LINK         O   LEU C 517                CA    CA C2006     1555   1555  2.62  
LINK         OD1 ASP C 574                CA    CA C2007     1555   1555  2.93  
LINK         O   ASP C 578                CA    CA C2007     1555   1555  2.71  
LINK         OD1 ASP C 578                CA    CA C2007     1555   1555  2.49  
LINK         O   LEU C 580                CA    CA C2007     1555   1555  2.53  
LINK         OD1 ASP C 582                CA    CA C2007     1555   1555  2.82  
LINK         OD2 ASP C 582                CA    CA C2007     1555   1555  2.67  
LINK         ND2 ASN C 678                 C1  NAG C3678     1555   1555  1.44  
LINK         ND2 ASN C 716                 C1  NAG C3716     1555   1555  1.44  
LINK         ND2 ASN C 880                 C1  NAG C3880     1555   1555  1.46  
LINK         ND2 ASN D  94                 C1  NAG D3094     1555   1555  1.43  
LINK         O   SER D 116                CA    CA D2002     1555   1555  2.50  
LINK         OD1 ASP D 119                CA    CA D2002     1555   1555  2.35  
LINK         OD1 ASP D 120                CA    CA D2002     1555   1555  2.10  
LINK         O   GLU D 325                CA    CA D2002     1555   1555  2.70  
LINK         OE2 GLU D 325                CA    CA D2002     1555   1555  2.30  
LINK         ND2 ASN D 479                 C1  NAG D3479     1555   1555  1.51  
LINK         O4  NAG A3042                 C1  NAG A3043     1555   1555  1.45  
LINK         O4  NAG A3373                 C1  NAG A3374     1555   1555  1.45  
LINK         O4  NAG A3374                 C1  MAN A3375     1555   1555  1.45  
LINK         O3  MAN A3375                 C1  MAN A3376     1555   1555  1.44  
LINK         O6  MAN A3375                 C1  MAN A3377     1555   1555  1.44  
LINK         O4  NAG A3716                 C1  NAG A3717     1555   1555  1.45  
LINK         O4  NAG A3717                 C1  MAN A3718     1555   1555  1.44  
LINK         O4  NAG A3880                 C1  NAG A3881     1555   1555  1.47  
LINK         O4  NAG A3881                 C1  MAN A3882     1555   1555  1.48  
LINK         O4  NAG C3042                 C1  NAG C3043     1555   1555  1.46  
LINK         O4  NAG C3373                 C1  NAG C3374     1555   1555  1.45  
LINK         O4  NAG C3374                 C1  MAN C3375     1555   1555  1.46  
LINK         O3  MAN C3375                 C1  MAN C3376     1555   1555  1.44  
LINK         O6  MAN C3375                 C1  MAN C3377     1555   1555  1.44  
LINK         O4  NAG C3716                 C1  NAG C3717     1555   1555  1.43  
LINK         O4  NAG C3717                 C1  MAN C3718     1555   1555  1.44  
CISPEP   1 LEU A  119    PRO A  120          0        -9.18                     
CISPEP   2 GLN A  817    LYS A  818          0         8.14                     
CISPEP   3 GLN A  819    GLY A  820          0        -7.92                     
CISPEP   4 SER B   77    PRO B   78          0         1.54                     
CISPEP   5 LEU B  155    PRO B  156          0        -3.41                     
CISPEP   6 HIS B  161    PRO B  162          0       -10.00                     
CISPEP   7 LEU B  587    PRO B  588          0         1.05                     
CISPEP   8 LEU C  119    PRO C  120          0        -7.32                     
CISPEP   9 SER D   77    PRO D   78          0         1.74                     
CISPEP  10 LEU D  155    PRO D  156          0        -3.36                     
CISPEP  11 HIS D  161    PRO D  162          0        -9.34                     
CISPEP  12 LEU D  587    PRO D  588          0         1.05                     
SITE     1 AC1  4 ALA A  40  ALA A  41  ASN A  42  NAG A3043                    
SITE     1 AC2  1 NAG A3042                                                     
SITE     1 AC3  5 PHE A 354  ASN A 373  SER A 375  GLN A 376                    
SITE     2 AC3  5 NAG A3374                                                     
SITE     1 AC4  3 GLN A 376  NAG A3373  MAN A3375                               
SITE     1 AC5  3 NAG A3374  MAN A3376  MAN A3377                               
SITE     1 AC6  1 MAN A3375                                                     
SITE     1 AC7  1 MAN A3375                                                     
SITE     1 AC8  2 THR A 676  ASN A 678                                          
SITE     1 AC9  5 THR A 657  ASP A 659  ASN A 716  TYR A 741                    
SITE     2 AC9  5 NAG A3717                                                     
SITE     1 BC1  2 NAG A3716  MAN A3718                                          
SITE     1 BC2  1 NAG A3717                                                     
SITE     1 BC3  5 ASP A 447  ASP A 449  ASP A 451  SER A 453                    
SITE     2 BC3  5 ASP A 455                                                     
SITE     1 BC4  6 ASP A 511  VAL A 512  ASN A 513  ASP A 515                    
SITE     2 BC4  6 LEU A 517  ASP A 519                                          
SITE     1 BC5  5 ASP A 574  THR A 576  ASP A 578  LEU A 580                    
SITE     2 BC5  5 ASP A 582                                                     
SITE     1 BC6  3 ASN A 880  SER A 882  NAG A3881                               
SITE     1 BC7  3 VAL A 834  NAG A3880  MAN A3882                               
SITE     1 BC8  1 NAG A3881                                                     
SITE     1 BC9  2 ALA B  92  ASN B  94                                          
SITE     1 CC1  4 SER B 116  ASP B 119  ASP B 120  GLU B 325                    
SITE     1 CC2  1 ASN B 479                                                     
SITE     1 CC3  4 ALA C  40  ALA C  41  ASN C  42  NAG C3043                    
SITE     1 CC4  1 NAG C3042                                                     
SITE     1 CC5  5 PHE C 354  ASN C 373  SER C 375  GLN C 376                    
SITE     2 CC5  5 NAG C3374                                                     
SITE     1 CC6  3 GLN C 376  NAG C3373  MAN C3375                               
SITE     1 CC7  3 NAG C3374  MAN C3376  MAN C3377                               
SITE     1 CC8  1 MAN C3375                                                     
SITE     1 CC9  2 MAN C3375  MAN C3378                                          
SITE     1 DC1  1 MAN C3377                                                     
SITE     1 DC2  2 THR C 676  ASN C 678                                          
SITE     1 DC3  5 THR C 657  ASP C 659  ASN C 716  TYR C 741                    
SITE     2 DC3  5 NAG C3717                                                     
SITE     1 DC4  2 NAG C3716  MAN C3718                                          
SITE     1 DC5  1 NAG C3717                                                     
SITE     1 DC6  3 VAL C 834  ASN C 880  THR C 887                               
SITE     1 DC7  5 ASP C 447  ASP C 449  ASP C 451  SER C 453                    
SITE     2 DC7  5 ASP C 455                                                     
SITE     1 DC8  5 ASP C 511  VAL C 512  ASN C 513  ASP C 515                    
SITE     2 DC8  5 LEU C 517                                                     
SITE     1 DC9  5 ASP C 574  THR C 576  ASP C 578  LEU C 580                    
SITE     2 DC9  5 ASP C 582                                                     
SITE     1 EC1  1 ASN D  94                                                     
SITE     1 EC2  4 SER D 116  ASP D 119  ASP D 120  GLU D 325                    
SITE     1 EC3  1 ASN D 479                                                     
CRYST1  160.962  165.549  536.178  90.00  90.00  90.00 I 21 21 21   16          
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      0.006213  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006041  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.001865        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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