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Database: PDB
Entry: 6BXF
LinkDB: 6BXF
Original site: 6BXF 
HEADER    CELL ADHESION                           18-DEC-17   6BXF              
TITLE     CRYSTAL STRUCTURE OF AN EXTENDED B3 INTEGRIN L33                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHIMERA PROTEIN OF INTEGRIN BETA-3 AND INTEGRIN ALPHA-L;   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA,GPIIIA,CD11 ANTIGEN-LIKE
COMPND   5 FAMILY MEMBER A,LEUKOCYTE ADHESION GLYCOPROTEIN LFA-1 ALPHA CHAIN,   
COMPND   6 LFA-1A,LEUKOCYTE FUNCTION-ASSOCIATED MOLECULE 1 ALPHA CHAIN;         
COMPND   7 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: ITGB3, GP3A, ITGAL, CD11A;                                     
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    INTEGRIN, CELL ADHESION                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.ZHOU,J.ZHU                                                          
REVDAT   2   12-SEP-18 6BXF    1       JRNL                                     
REVDAT   1   01-AUG-18 6BXF    0                                                
JRNL        AUTH   D.ZHOU,A.M.M.THINN,Y.ZHAO,Z.WANG,J.ZHU                       
JRNL        TITL   STRUCTURE OF AN EXTENDED BETA3INTEGRIN.                      
JRNL        REF    BLOOD                         V. 132   962 2018              
JRNL        REFN                   ESSN 1528-0020                               
JRNL        PMID   30018079                                                     
JRNL        DOI    10.1182/BLOOD-2018-01-829572                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20063                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.268                           
REMARK   3   R VALUE            (WORKING SET) : 0.265                           
REMARK   3   FREE R VALUE                     : 0.335                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1019                            
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 63.5060 -  6.1200    1.00     2800   142  0.2085 0.3037        
REMARK   3     2  6.1200 -  4.8582    1.00     2732   161  0.2631 0.3047        
REMARK   3     3  4.8582 -  4.2442    1.00     2709   129  0.2392 0.2937        
REMARK   3     4  4.2442 -  3.8562    1.00     2739   141  0.3001 0.3598        
REMARK   3     5  3.8562 -  3.5798    1.00     2710   138  0.3562 0.4524        
REMARK   3     6  3.5798 -  3.3688    1.00     2679   152  0.3982 0.4335        
REMARK   3     7  3.3688 -  3.2001    0.99     2675   156  0.4119 0.4384        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.710            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 44.060           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           7490                                  
REMARK   3   ANGLE     :  0.625          10096                                  
REMARK   3   CHIRALITY :  0.043           1124                                  
REMARK   3   PLANARITY :  0.004           1317                                  
REMARK   3   DIHEDRAL  : 16.804           4649                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -70.5244 -59.6924 177.1142              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8630 T22:   0.6080                                     
REMARK   3      T33:   0.7624 T12:  -0.0732                                     
REMARK   3      T13:   0.0332 T23:   0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3914 L22:   0.3293                                     
REMARK   3      L33:   0.9131 L12:  -0.1331                                     
REMARK   3      L13:   0.2890 L23:   0.4143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1329 S12:  -0.1593 S13:  -0.0502                       
REMARK   3      S21:   0.1893 S22:  -0.0396 S23:   0.0231                       
REMARK   3      S31:   0.0860 S32:  -0.2182 S33:   0.1938                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6BXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000231754.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 130 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20112                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.490                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 8000, 0.2 M NACL, 0.1 M HEPES    
REMARK 280  (PH 7.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.73500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     TYR A   464                                                      
REMARK 465     PHE A   465                                                      
REMARK 465     GLN A   466                                                      
REMARK 465     PHE B   465                                                      
REMARK 465     GLN B   466                                                      
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   3     -159.78    -99.13                                   
REMARK 500    SER A  27       39.54   -148.36                                   
REMARK 500    GLU A  29      -54.59     67.42                                   
REMARK 500    ALA A  30       64.56   -102.21                                   
REMARK 500    SER A  35      109.33   -165.35                                   
REMARK 500    ASP A  39     -150.32   -165.47                                   
REMARK 500    ALA A  50      165.42     66.75                                   
REMARK 500    LEU A  64      -66.61    -98.54                                   
REMARK 500    ASP A  76       83.36    -60.99                                   
REMARK 500    GLN A  79     -153.91     57.00                                   
REMARK 500    SER A 156      -90.16   -161.89                                   
REMARK 500    LEU A 186     -132.00   -141.76                                   
REMARK 500    LEU A 187     -149.92   -100.40                                   
REMARK 500    PHE A 202       41.96    -72.30                                   
REMARK 500    ASP A 226     -169.67   -108.40                                   
REMARK 500    ALA A 233       62.69   -103.44                                   
REMARK 500    LYS A 276        0.52    -64.85                                   
REMARK 500    ILE A 288      -60.67    -90.42                                   
REMARK 500    CYS A 311      -98.12    -98.40                                   
REMARK 500    LEU A 312      -83.07    -64.29                                   
REMARK 500    GLU A 346      109.35    -42.38                                   
REMARK 500    GLU A 379       87.29     61.66                                   
REMARK 500    ASN A 381       78.59     38.19                                   
REMARK 500    ASN A 386      145.26     65.48                                   
REMARK 500    PHE A 392       75.22   -107.25                                   
REMARK 500    SER A 406      -86.61    -66.35                                   
REMARK 500    CYS A 408      102.71     58.53                                   
REMARK 500    GLU A 409      -43.73   -149.99                                   
REMARK 500    SER A 411      -87.89    -90.33                                   
REMARK 500    GLU A 413     -164.69     36.41                                   
REMARK 500    ARG A 416      146.74    164.98                                   
REMARK 500    SER A 418     -123.72     59.28                                   
REMARK 500    ARG A 435       52.65   -144.62                                   
REMARK 500    PHE A 450      -63.35   -101.59                                   
REMARK 500    ILE A 453       79.12   -103.29                                   
REMARK 500    CYS A 458       85.89     54.77                                   
REMARK 500    SER B  27       97.45   -170.30                                   
REMARK 500    PRO B  32       68.52    -69.65                                   
REMARK 500    LEU B  33      -57.60     11.32                                   
REMARK 500    ASN B  48       78.40    -52.33                                   
REMARK 500    LEU B  64      -82.02    -98.32                                   
REMARK 500    ASP B  71      -89.91    -83.16                                   
REMARK 500    LYS B  72       33.24   -140.06                                   
REMARK 500    SER B  74      -76.20     44.88                                   
REMARK 500    GLN B  79      140.33     64.16                                   
REMARK 500    SER B 123       18.10    -66.50                                   
REMARK 500    ASN B 145      -32.21     69.96                                   
REMARK 500    ALA B 151      111.23   -162.84                                   
REMARK 500    SER B 156     -116.98   -140.96                                   
REMARK 500    LEU B 186     -132.63   -140.90                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      75 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 505  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 121   OG                                                     
REMARK 620 2 SER A 123   OG   72.0                                              
REMARK 620 3 ASP A 221   OD1  77.2  97.5                                        
REMARK 620 4 HOH A 601   O   134.2  69.6  83.8                                  
REMARK 620 5 HOH A 602   O    96.7  89.9 168.3 107.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 119   OD2                                                    
REMARK 620 2 SER B 121   OG   95.3                                              
REMARK 620 3 SER B 123   OG  126.7  64.9                                        
REMARK 620 4 THR B 188   OG1  85.6  89.1 138.2                                  
REMARK 620 5 ASP B 221   OD1  63.0 109.0  77.1 144.5                            
REMARK 620 6 HOH B 601   O   147.2  86.6  83.6  61.7 146.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 503 bound   
REMARK 800  to ASN A 145                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 502 bound   
REMARK 800  to ASN A 308                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 504 bound   
REMARK 800  to ASN A 389                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 505 bound   
REMARK 800  to ASN B 99                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 506 bound   
REMARK 800  to ASN B 145                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6BXB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6BXJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CKB   RELATED DB: PDB                                   
DBREF  6BXF A    1   109  UNP    P05106   ITB3_HUMAN      27    135             
DBREF  6BXF A  110   286  UNP    P20701   ITAL_HUMAN     153    329             
DBREF  6BXF A  287   459  UNP    P05106   ITB3_HUMAN     376    548             
DBREF  6BXF B    1   109  UNP    P05106   ITB3_HUMAN      27    135             
DBREF  6BXF B  110   286  UNP    P20701   ITAL_HUMAN     153    329             
DBREF  6BXF B  287   459  UNP    P05106   ITB3_HUMAN     376    548             
SEQADV 6BXF TRP A  171  UNP  P20701    ARG   214 CONFLICT                       
SEQADV 6BXF THR A  460  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF ARG A  461  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF GLU A  462  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF LEU A  463  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF TYR A  464  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF PHE A  465  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF GLN A  466  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF TRP B  171  UNP  P20701    ARG   214 CONFLICT                       
SEQADV 6BXF THR B  460  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF ARG B  461  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF GLU B  462  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF LEU B  463  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF TYR B  464  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF PHE B  465  UNP  P05106              EXPRESSION TAG                 
SEQADV 6BXF GLN B  466  UNP  P05106              EXPRESSION TAG                 
SEQRES   1 A  466  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 A  466  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 A  466  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 A  466  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 A  466  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 A  466  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 A  466  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 A  466  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 A  466  ARG GLN VAL GLU ASP GLY ASN VAL ASP LEU VAL PHE LEU          
SEQRES  10 A  466  PHE ASP GLY SER MET SER LEU GLN PRO ASP GLU PHE GLN          
SEQRES  11 A  466  LYS ILE LEU ASP PHE MET LYS ASP VAL MET LYS LYS LEU          
SEQRES  12 A  466  SER ASN THR SER TYR GLN PHE ALA ALA VAL GLN PHE SER          
SEQRES  13 A  466  THR SER TYR LYS THR GLU PHE ASP PHE SER ASP TYR VAL          
SEQRES  14 A  466  LYS TRP LYS ASP PRO ASP ALA LEU LEU LYS HIS VAL LYS          
SEQRES  15 A  466  HIS MET LEU LEU LEU THR ASN THR PHE GLY ALA ILE ASN          
SEQRES  16 A  466  TYR VAL ALA THR GLU VAL PHE ARG GLU GLU LEU GLY ALA          
SEQRES  17 A  466  ARG PRO ASP ALA THR LYS VAL LEU ILE ILE ILE THR ASP          
SEQRES  18 A  466  GLY GLU ALA THR ASP SER GLY ASN ILE ASP ALA ALA LYS          
SEQRES  19 A  466  ASP ILE ILE ARG TYR ILE ILE GLY ILE GLY LYS HIS PHE          
SEQRES  20 A  466  GLN THR LYS GLU SER GLN GLU THR LEU HIS LYS PHE ALA          
SEQRES  21 A  466  SER LYS PRO ALA SER GLU PHE VAL LYS ILE LEU ASP THR          
SEQRES  22 A  466  PHE GLU LYS LEU LYS ASP LEU PHE THR GLU LEU GLN LYS          
SEQRES  23 A  466  LYS ILE ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU          
SEQRES  24 A  466  PRO GLU GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU          
SEQRES  25 A  466  ASN ASN GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY          
SEQRES  26 A  466  LEU LYS ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA          
SEQRES  27 A  466  LYS VAL ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE          
SEQRES  28 A  466  THR ILE LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL          
SEQRES  29 A  466  GLN VAL THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN          
SEQRES  30 A  466  ALA GLU PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY          
SEQRES  31 A  466  THR PHE GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP          
SEQRES  32 A  466  LEU GLY SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG          
SEQRES  33 A  466  PRO SER GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN          
SEQRES  34 A  466  PRO VAL CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN          
SEQRES  35 A  466  CYS VAL CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY          
SEQRES  36 A  466  LYS TYR CYS GLU THR ARG GLU LEU TYR PHE GLN                  
SEQRES   1 B  466  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  466  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  466  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  466  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  466  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  466  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  466  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  466  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  466  ARG GLN VAL GLU ASP GLY ASN VAL ASP LEU VAL PHE LEU          
SEQRES  10 B  466  PHE ASP GLY SER MET SER LEU GLN PRO ASP GLU PHE GLN          
SEQRES  11 B  466  LYS ILE LEU ASP PHE MET LYS ASP VAL MET LYS LYS LEU          
SEQRES  12 B  466  SER ASN THR SER TYR GLN PHE ALA ALA VAL GLN PHE SER          
SEQRES  13 B  466  THR SER TYR LYS THR GLU PHE ASP PHE SER ASP TYR VAL          
SEQRES  14 B  466  LYS TRP LYS ASP PRO ASP ALA LEU LEU LYS HIS VAL LYS          
SEQRES  15 B  466  HIS MET LEU LEU LEU THR ASN THR PHE GLY ALA ILE ASN          
SEQRES  16 B  466  TYR VAL ALA THR GLU VAL PHE ARG GLU GLU LEU GLY ALA          
SEQRES  17 B  466  ARG PRO ASP ALA THR LYS VAL LEU ILE ILE ILE THR ASP          
SEQRES  18 B  466  GLY GLU ALA THR ASP SER GLY ASN ILE ASP ALA ALA LYS          
SEQRES  19 B  466  ASP ILE ILE ARG TYR ILE ILE GLY ILE GLY LYS HIS PHE          
SEQRES  20 B  466  GLN THR LYS GLU SER GLN GLU THR LEU HIS LYS PHE ALA          
SEQRES  21 B  466  SER LYS PRO ALA SER GLU PHE VAL LYS ILE LEU ASP THR          
SEQRES  22 B  466  PHE GLU LYS LEU LYS ASP LEU PHE THR GLU LEU GLN LYS          
SEQRES  23 B  466  LYS ILE ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU          
SEQRES  24 B  466  PRO GLU GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU          
SEQRES  25 B  466  ASN ASN GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY          
SEQRES  26 B  466  LEU LYS ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA          
SEQRES  27 B  466  LYS VAL ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE          
SEQRES  28 B  466  THR ILE LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL          
SEQRES  29 B  466  GLN VAL THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN          
SEQRES  30 B  466  ALA GLU PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY          
SEQRES  31 B  466  THR PHE GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP          
SEQRES  32 B  466  LEU GLY SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG          
SEQRES  33 B  466  PRO SER GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN          
SEQRES  34 B  466  PRO VAL CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN          
SEQRES  35 B  466  CYS VAL CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY          
SEQRES  36 B  466  LYS TYR CYS GLU THR ARG GLU LEU TYR PHE GLN                  
HET    GOL  A 501       6                                                       
HET    NAG  A 502      14                                                       
HET    NAG  A 503      14                                                       
HET    NAG  A 504      14                                                       
HET     CA  A 505       1                                                       
HET     MG  B 501       1                                                       
HET    GOL  B 502       6                                                       
HET    NAG  B 503      14                                                       
HET    NAG  B 504      14                                                       
HET    NAG  B 505      14                                                       
HET    NAG  B 506      14                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   4  NAG    7(C8 H15 N O6)                                               
FORMUL   7   CA    CA 2+                                                        
FORMUL   8   MG    MG 2+                                                        
FORMUL  14  HOH   *8(H2 O)                                                      
HELIX    1 AA1 ASN A    3  ARG A    8  1                                   6    
HELIX    2 AA2 SER A   12  ALA A   18  1                                   7    
HELIX    3 AA3 GLN A  125  LYS A  142  1                                  18    
HELIX    4 AA4 ASP A  164  LYS A  172  1                                   9    
HELIX    5 AA5 ASP A  173  LEU A  178  1                                   6    
HELIX    6 AA6 ASN A  189  GLU A  200  1                                  12    
HELIX    7 AA7 ARG A  203  GLY A  207  5                                   5    
HELIX    8 AA8 ILE A  230  LYS A  234  5                                   5    
HELIX    9 AA9 GLY A  244  GLN A  248  5                                   5    
HELIX   10 AB1 GLU A  251  PHE A  259  5                                   9    
HELIX   11 AB2 PRO A  263  VAL A  268  1                                   6    
HELIX   12 AB3 THR A  273  GLU A  275  5                                   3    
HELIX   13 AB4 LYS A  276  GLN A  285  1                                  10    
HELIX   14 AB5 GLN A  419  SER A  424  5                                   6    
HELIX   15 AB6 PRO A  430  GLN A  434  5                                   5    
HELIX   16 AB7 ASN B    3  ARG B    8  1                                   6    
HELIX   17 AB8 SER B   12  LEU B   17  1                                   6    
HELIX   18 AB9 LEU B   40  ASP B   47  1                                   8    
HELIX   19 AC1 GLN B  125  LEU B  143  1                                  19    
HELIX   20 AC2 ASP B  164  LYS B  172  1                                   9    
HELIX   21 AC3 ASP B  173  LEU B  178  1                                   6    
HELIX   22 AC4 ASN B  189  VAL B  201  1                                  13    
HELIX   23 AC5 GLY B  244  GLN B  248  5                                   5    
HELIX   24 AC6 THR B  249  THR B  255  1                                   7    
HELIX   25 AC7 THR B  273  LYS B  278  5                                   6    
HELIX   26 AC8 LEU B  284  ARG B  289  1                                   6    
HELIX   27 AC9 CYS B  372  ALA B  376  5                                   5    
HELIX   28 AD1 SER B  411  TYR B  415  5                                   5    
SHEET    1 AA1 2 ALA A  24  TRP A  25  0                                        
SHEET    2 AA1 2 CYS A  38  ASP A  39 -1  O  ASP A  39   N  ALA A  24           
SHEET    1 AA2 6 GLU A  60  GLU A  65  0                                        
SHEET    2 AA2 6 ARG A  87  LEU A  92 -1  O  ARG A  87   N  LEU A  64           
SHEET    3 AA2 6 LEU A 362  PHE A 368  1  O  GLN A 365   N  LEU A  90           
SHEET    4 AA2 6 GLU A 348  PRO A 355 -1  N  ILE A 353   O  LEU A 362           
SHEET    5 AA2 6 VAL A 292  ARG A 297 -1  N  ARG A 297   O  THR A 352           
SHEET    6 AA2 6 SER A 322  CYS A 323 -1  O  CYS A 323   N  VAL A 292           
SHEET    1 AA3 5 VAL A  83  SER A  84  0                                        
SHEET    2 AA3 5 SER A  97  ARG A 105 -1  O  GLN A 103   N  SER A  84           
SHEET    3 AA3 5 THR A 331  LYS A 339 -1  O  ILE A 336   N  PHE A 100           
SHEET    4 AA3 5 PHE A 307  THR A 310 -1  N  THR A 310   O  SER A 333           
SHEET    5 AA3 5 VAL A 316  PRO A 318 -1  O  ILE A 317   N  ALA A 309           
SHEET    1 AA4 5 TYR A 159  PHE A 163  0                                        
SHEET    2 AA4 5 TYR A 148  PHE A 155 -1  N  ALA A 152   O  GLU A 162           
SHEET    3 AA4 5 VAL A 112  ASP A 119  1  N  PHE A 116   O  VAL A 153           
SHEET    4 AA4 5 THR A 213  THR A 220  1  O  ILE A 219   N  ASP A 119           
SHEET    5 AA4 5 ILE A 237  GLY A 242  1  O  TYR A 239   N  ILE A 218           
SHEET    1 AA5 2 GLY A 390  GLU A 393  0                                        
SHEET    2 AA5 2 VAL A 396  CYS A 399 -1  O  ARG A 398   N  THR A 391           
SHEET    1 AA6 2 GLY A 436  LEU A 439  0                                        
SHEET    2 AA6 2 GLN A 442  CYS A 445 -1  N  VAL A 444   O  GLU A 437           
SHEET    1 AA7 2 ALA B  24  TRP B  25  0                                        
SHEET    2 AA7 2 CYS B  38  ASP B  39 -1  O  ASP B  39   N  ALA B  24           
SHEET    1 AA8 6 GLU B  60  VAL B  63  0                                        
SHEET    2 AA8 6 ARG B  87  LEU B  92 -1  O  ALA B  89   N  ARG B  62           
SHEET    3 AA8 6 LEU B 362  PHE B 368  1  O  GLN B 365   N  LEU B  90           
SHEET    4 AA8 6 GLU B 348  PRO B 355 -1  N  PHE B 351   O  VAL B 364           
SHEET    5 AA8 6 LYS B 291  ARG B 297 -1  N  ARG B 297   O  THR B 352           
SHEET    6 AA8 6 SER B 322  MET B 324 -1  O  CYS B 323   N  VAL B 292           
SHEET    1 AA9 5 VAL B  83  SER B  84  0                                        
SHEET    2 AA9 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3 AA9 5 THR B 331  VAL B 340 -1  O  ILE B 336   N  PHE B 100           
SHEET    4 AA9 5 LEU B 303  THR B 310 -1  N  THR B 310   O  SER B 333           
SHEET    5 AA9 5 VAL B 316  PRO B 318 -1  O  ILE B 317   N  ALA B 309           
SHEET    1 AB1 5 TYR B 159  THR B 161  0                                        
SHEET    2 AB1 5 TYR B 148  PHE B 155 -1  N  GLN B 154   O  LYS B 160           
SHEET    3 AB1 5 VAL B 112  ASP B 119  1  N  PHE B 116   O  VAL B 153           
SHEET    4 AB1 5 THR B 213  THR B 220  1  O  ILE B 219   N  LEU B 117           
SHEET    5 AB1 5 ILE B 237  GLY B 242  1  O  TYR B 239   N  ILE B 218           
SHEET    1 AB2 2 GLY B 390  GLU B 393  0                                        
SHEET    2 AB2 2 VAL B 396  CYS B 399 -1  O  ARG B 398   N  THR B 391           
SSBOND   1 CYS A    5    CYS A   23                          1555   1555  2.03  
SSBOND   2 CYS A   13    CYS A  372                          1555   1555  2.03  
SSBOND   3 CYS A   16    CYS A   38                          1555   1555  2.03  
SSBOND   4 CYS A   26    CYS A   49                          1555   1555  2.03  
SSBOND   5 CYS A  311    CYS A  323                          1555   1555  2.03  
SSBOND   6 CYS A  343    CYS A  370                          1555   1555  2.03  
SSBOND   7 CYS A  374    CYS A  394                          1555   1555  2.03  
SSBOND   8 CYS A  385    CYS A  397                          1555   1555  2.03  
SSBOND   9 CYS A  399    CYS A  408                          1555   1555  2.03  
SSBOND  10 CYS A  410    CYS A  440                          1555   1555  2.03  
SSBOND  11 CYS A  423    CYS A  438                          1555   1555  2.03  
SSBOND  12 CYS A  432    CYS A  443                          1555   1555  2.03  
SSBOND  13 CYS A  445    CYS A  458                          1555   1555  2.03  
SSBOND  14 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND  15 CYS B   13    CYS B  372                          1555   1555  2.03  
SSBOND  16 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND  17 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND  18 CYS B  311    CYS B  323                          1555   1555  2.03  
SSBOND  19 CYS B  343    CYS B  370                          1555   1555  2.03  
SSBOND  20 CYS B  374    CYS B  394                          1555   1555  2.02  
SSBOND  21 CYS B  385    CYS B  397                          1555   1555  2.03  
SSBOND  22 CYS B  399    CYS B  408                          1555   1555  2.03  
SSBOND  23 CYS B  410    CYS B  440                          1555   1555  2.02  
SSBOND  24 CYS B  423    CYS B  438                          1555   1555  2.03  
SSBOND  25 CYS B  432    CYS B  443                          1555   1555  2.03  
SSBOND  26 CYS B  445    CYS B  458                          1555   1555  2.03  
LINK         OG  SER A 121                CA    CA A 505     1555   1555  2.33  
LINK         OG  SER A 123                CA    CA A 505     1555   1555  2.37  
LINK         ND2 ASN A 145                 C1  NAG A 503     1555   1555  1.44  
LINK         OD1 ASP A 221                CA    CA A 505     1555   1555  2.39  
LINK         ND2 ASN A 308                 C1  NAG A 502     1555   1555  1.46  
LINK         ND2 ASN A 389                 C1  NAG A 504     1555   1555  1.46  
LINK         ND2 ASN B  99                 C1  NAG B 505     1555   1555  1.43  
LINK         OD2 ASP B 119                MG    MG B 501     1555   1555  2.21  
LINK         OG  SER B 121                MG    MG B 501     1555   1555  1.98  
LINK         OG  SER B 123                MG    MG B 501     1555   1555  2.45  
LINK         ND2 ASN B 145                 C1  NAG B 506     1555   1555  1.45  
LINK         OG1 THR B 188                MG    MG B 501     1555   1555  2.48  
LINK         OD1 ASP B 221                MG    MG B 501     1555   1555  2.18  
LINK         ND2 ASN B 308                 C1  NAG B 503     1555   1555  1.42  
LINK         ND2 ASN B 389                 C1  NAG B 504     1555   1555  1.46  
LINK        CA    CA A 505                 O   HOH A 601     1555   1555  2.34  
LINK        CA    CA A 505                 O   HOH A 602     1555   1555  2.41  
LINK        MG    MG B 501                 O   HOH B 601     1555   1555  2.14  
CISPEP   1 SER A   84    PRO A   85          0        -0.40                     
CISPEP   2 LYS A  262    PRO A  263          0         3.21                     
CISPEP   3 SER B   84    PRO B   85          0        -0.69                     
CISPEP   4 LYS B  262    PRO B  263          0         1.64                     
SITE     1 AC1  2 VAL A 268  LYS A 269                                          
SITE     1 AC2  8 ASP A  66  ASP A 119  SER A 121  SER A 123                    
SITE     2 AC2  8 THR A 188  ASP A 221  HOH A 601  HOH A 602                    
SITE     1 AC3  6 ASP B 119  SER B 121  SER B 123  THR B 188                    
SITE     2 AC3  6 ASP B 221  HOH B 601                                          
SITE     1 AC4  1 LYS B  46                                                     
SITE     1 AC5  3 SER B 306  ASN B 308  SER B 335                               
SITE     1 AC6  3 ASN B 386  GLY B 388  ASN B 389                               
SITE     1 AC7  1 ASN A 145                                                     
SITE     1 AC8  4 ASN A 308  SER A 335  ILE A 336  GLU A 337                    
SITE     1 AC9  5 ASN A 386  ASN A 387  GLY A 388  ASN A 389                    
SITE     2 AC9  5 TRP A 403                                                     
SITE     1 AD1  2 ASN B  99  PHE B 100                                          
SITE     1 AD2  1 ASN B 145                                                     
CRYST1   59.070   81.470  127.960  90.00  97.07  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016929  0.000000  0.002100        0.00000                         
SCALE2      0.000000  0.012274  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007875        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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