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Database: PDB
Entry: 6CKB
LinkDB: 6CKB
Original site: 6CKB 
HEADER    CELL ADHESION                           27-FEB-18   6CKB              
TITLE     CRYSTAL STRUCTURE OF AN EXTENDED BETA3 INTEGRIN P33                   
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_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    INTEGRIN, CELL ADHESION                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.ZHOU,J.ZHU                                                          
REVDAT   2   12-SEP-18 6CKB    1       JRNL                                     
REVDAT   1   01-AUG-18 6CKB    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.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 29394                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1479                            
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 58.7293 -  6.2249    1.00     2626   120  0.1844 0.2279        
REMARK   3     2  6.2249 -  4.9417    1.00     2549   149  0.2121 0.2570        
REMARK   3     3  4.9417 -  4.3173    1.00     2555   145  0.1789 0.2579        
REMARK   3     4  4.3173 -  3.9226    1.00     2555   135  0.2129 0.2836        
REMARK   3     5  3.9226 -  3.6415    1.00     2515   131  0.2647 0.3371        
REMARK   3     6  3.6415 -  3.4268    1.00     2553   119  0.3183 0.4041        
REMARK   3     7  3.4268 -  3.2552    1.00     2532   108  0.3265 0.3619        
REMARK   3     8  3.2552 -  3.1135    1.00     2503   154  0.3856 0.4366        
REMARK   3     9  3.1135 -  2.9937    1.00     2563   125  0.4626 0.5430        
REMARK   3    10  2.9937 -  2.8904    0.99     2508   138  0.4578 0.4999        
REMARK   3    11  2.8904 -  2.8000    0.98     2456   155  0.4120 0.4391        
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)     : 0.810            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.020           
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      :  0.009           7467                                  
REMARK   3   ANGLE     :  1.052          10088                                  
REMARK   3   CHIRALITY :  0.071           1120                                  
REMARK   3   PLANARITY :  0.005           1324                                  
REMARK   3   DIHEDRAL  : 18.459           4639                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 46 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -90.1262-102.9404 130.3059              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5199 T22:   1.0630                                     
REMARK   3      T33:   1.6837 T12:   0.4646                                     
REMARK   3      T13:   0.4567 T23:  -0.0976                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2998 L22:   6.8324                                     
REMARK   3      L33:   7.4478 L12:   4.5372                                     
REMARK   3      L13:  -2.8260 L23:  -3.4835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2550 S12:   1.8182 S13:   0.2967                       
REMARK   3      S21:  -0.5257 S22:   0.5195 S23:  -2.1111                       
REMARK   3      S31:  -0.2171 S32:  -0.5426 S33:  -0.9106                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 47 THROUGH 125 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -72.1739 -77.0016 148.9856              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2002 T22:   0.8608                                     
REMARK   3      T33:   1.0479 T12:  -0.2508                                     
REMARK   3      T13:   0.1796 T23:   0.2734                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0390 L22:   2.3157                                     
REMARK   3      L33:   0.0338 L12:   3.9220                                     
REMARK   3      L13:   2.3927 L23:   1.8180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0500 S12:  -0.0345 S13:   0.7353                       
REMARK   3      S21:   0.5055 S22:  -0.1487 S23:   0.6877                       
REMARK   3      S31:  -0.1803 S32:   0.0537 S33:   0.1614                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 126 THROUGH 288 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.9721 -69.1093 155.7430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0468 T22:   0.5846                                     
REMARK   3      T33:   0.5430 T12:  -0.1603                                     
REMARK   3      T13:  -0.0495 T23:  -0.0633                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2630 L22:   4.4161                                     
REMARK   3      L33:   5.9132 L12:  -0.1983                                     
REMARK   3      L13:  -2.6672 L23:  -1.1746                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3896 S12:  -0.3919 S13:   0.3136                       
REMARK   3      S21:   0.1226 S22:   0.0345 S23:  -0.2438                       
REMARK   3      S31:  -1.3474 S32:   0.0120 S33:  -0.4134                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 289 THROUGH 409 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -76.0846 -90.9379 143.4911              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9361 T22:   0.8258                                     
REMARK   3      T33:   0.9954 T12:   0.1046                                     
REMARK   3      T13:   0.2177 T23:   0.0826                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8501 L22:   7.7557                                     
REMARK   3      L33:   4.3722 L12:   3.5134                                     
REMARK   3      L13:   2.9959 L23:   2.9228                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5002 S12:   0.6291 S13:  -0.2006                       
REMARK   3      S21:   0.3209 S22:  -0.1841 S23:  -0.2344                       
REMARK   3      S31:   0.5157 S32:   0.3728 S33:  -0.1714                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 410 THROUGH 439 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -91.3674-127.4508 119.7065              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1895 T22:   1.2744                                     
REMARK   3      T33:   1.6149 T12:  -0.2165                                     
REMARK   3      T13:   0.2314 T23:  -0.2675                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4070 L22:   6.0467                                     
REMARK   3      L33:   4.8450 L12:   5.6909                                     
REMARK   3      L13:   5.1456 L23:   5.4028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2862 S12:   1.2595 S13:   0.7825                       
REMARK   3      S21:  -0.7251 S22:   1.4144 S23:  -0.7318                       
REMARK   3      S31:   0.1484 S32:   1.5133 S33:  -0.4021                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 440 THROUGH 464 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -92.5095-139.7817 124.9880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8663 T22:   0.9774                                     
REMARK   3      T33:   1.0246 T12:  -0.1496                                     
REMARK   3      T13:  -0.0179 T23:  -0.2588                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2016 L22:   2.7045                                     
REMARK   3      L33:   4.3167 L12:   0.6875                                     
REMARK   3      L13:  -0.2418 L23:  -3.3571                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.3643 S12:  -0.9382 S13:   1.2131                       
REMARK   3      S21:   1.6397 S22:  -1.4610 S23:   0.9458                       
REMARK   3      S31:  -1.0886 S32:   0.1068 S33:   0.4826                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 125 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -57.0003 -59.1799 208.0241              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8856 T22:   0.9810                                     
REMARK   3      T33:   1.0029 T12:   0.2900                                     
REMARK   3      T13:  -0.0292 T23:  -0.2882                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2377 L22:  -0.0631                                     
REMARK   3      L33:   1.7023 L12:  -0.8663                                     
REMARK   3      L13:   1.3182 L23:  -1.1086                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3640 S12:   0.6654 S13:  -0.3363                       
REMARK   3      S21:  -0.1889 S22:  -0.5871 S23:   0.0023                       
REMARK   3      S31:   0.5886 S32:   0.5554 S33:   0.2770                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 126 THROUGH 281 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -94.3795 -50.9343 188.7254              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1066 T22:   1.6957                                     
REMARK   3      T33:   0.7956 T12:  -0.1063                                     
REMARK   3      T13:  -0.0062 T23:  -0.3069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5636 L22:   6.2875                                     
REMARK   3      L33:   5.4746 L12:   1.4646                                     
REMARK   3      L13:   1.4180 L23:  -1.9567                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2856 S12:   0.0049 S13:  -0.4661                       
REMARK   3      S21:  -0.4355 S22:   0.0197 S23:  -0.5094                       
REMARK   3      S31:  -0.9776 S32:   0.8891 S33:   0.3043                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 282 THROUGH 420 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -59.6925 -64.8375 211.8257              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6096 T22:   0.9791                                     
REMARK   3      T33:   0.8152 T12:   0.0158                                     
REMARK   3      T13:   0.0849 T23:  -0.2242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3948 L22:   7.8511                                     
REMARK   3      L33:   6.4230 L12:  -1.6883                                     
REMARK   3      L13:   1.6486 L23:  -3.7835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0333 S12:  -0.0188 S13:  -0.2545                       
REMARK   3      S21:  -0.6014 S22:  -0.0060 S23:   0.3682                       
REMARK   3      S31:   1.1010 S32:  -0.0511 S33:   0.0810                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 421 THROUGH 465 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -49.2457 -75.3945 245.0763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3266 T22:   1.0659                                     
REMARK   3      T33:   1.0847 T12:   0.0467                                     
REMARK   3      T13:  -0.2518 T23:  -0.1085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7130 L22:   9.4427                                     
REMARK   3      L33:   4.8774 L12:  -1.2992                                     
REMARK   3      L13:   0.8146 L23:  -3.4189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1533 S12:   0.4646 S13:  -0.7502                       
REMARK   3      S21:  -1.7183 S22:  -0.5115 S23:   0.6035                       
REMARK   3      S31:   1.0257 S32:   1.6088 S33:  -0.6621                       
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 6CKB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232911.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-AUG-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          : RAYONIX MX300HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29474                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.700                             
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  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 6000, 0.1 M TRIS-HCL (PH 8.5),   
REMARK 280  VAPOR DIFFUSION, 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       40.45500            
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     PHE A   465                                                      
REMARK 465     GLN A   466                                                      
REMARK 465     GLN B   466                                                      
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   OG   SER B   123     OD2  ASP B   221              1.51            
REMARK 500   OG   SER A   123     OD2  ASP A   221              1.85            
REMARK 500   OG   SER A   121     OG   SER A   123              2.03            
REMARK 500   ND2  ASN A   308     O5   NAG A   503              2.05            
REMARK 500   OG   SER A   121     O    HOH A   601              2.12            
REMARK 500   OD1  ASP B   164     OG   SER B   166              2.16            
REMARK 500   O    ALA A    50     OG   SER A    53              2.16            
REMARK 500   O    LYS A   286     OG   SER A   290              2.16            
REMARK 500   O    ARG A    67     OG   SER A    84              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A   327     OD1  ASN B   386     2458     2.19            
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  44   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    CYS B 443   CA  -  CB  -  SG  ANGL. DEV. =   9.2 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   3     -161.96   -105.86                                   
REMARK 500    CYS A   5      173.89    -51.88                                   
REMARK 500    THR A   6      -59.79     58.27                                   
REMARK 500    SER A  27       37.56   -151.56                                   
REMARK 500    GLU A  29      -26.29     66.24                                   
REMARK 500    ASP A  39     -140.97   -137.11                                   
REMARK 500    ALA A  50      127.14    -38.14                                   
REMARK 500    GLU A  52      -17.57     89.13                                   
REMARK 500    LEU A  64      -73.72    -91.68                                   
REMARK 500    ASP A  76       60.64    -61.52                                   
REMARK 500    GLN A  79      173.28     66.34                                   
REMARK 500    SER A 121      130.78    -33.99                                   
REMARK 500    SER A 156     -112.78   -150.67                                   
REMARK 500    PHE A 163      143.81   -176.37                                   
REMARK 500    LEU A 187     -157.58    -76.40                                   
REMARK 500    THR A 273      -73.50   -117.59                                   
REMARK 500    PHE A 274      -20.79    112.50                                   
REMARK 500    ASN A 308      110.82    176.20                                   
REMARK 500    CYS A 311     -121.65   -130.84                                   
REMARK 500    ASN A 314       28.25     31.84                                   
REMARK 500    SER A 322      111.78   -160.60                                   
REMARK 500    CYS A 370      -50.92   -152.79                                   
REMARK 500    GLU A 379       72.03     51.51                                   
REMARK 500    ASN A 387       86.55     60.43                                   
REMARK 500    SER A 406      -85.48    -51.48                                   
REMARK 500    TYR A 415     -174.42     60.02                                   
REMARK 500    SER A 418     -120.02     60.89                                   
REMARK 500    ASP A 421       -0.63    -57.24                                   
REMARK 500    SER A 433       20.74     45.29                                   
REMARK 500    CYS A 458        7.46     58.97                                   
REMARK 500    ASN B   3     -169.69    -78.70                                   
REMARK 500    LYS B  41        0.29    -68.72                                   
REMARK 500    LYS B  46      -71.97    -67.10                                   
REMARK 500    ASN B  48       98.08    -69.28                                   
REMARK 500    ASP B  66       35.71    -90.45                                   
REMARK 500    ASP B  76       32.33    -76.66                                   
REMARK 500    GLN B  79     -136.84     58.21                                   
REMARK 500    ARG B  87      134.35   -176.36                                   
REMARK 500    ASP B 113       85.44   -153.80                                   
REMARK 500    THR B 146     -162.96    -78.31                                   
REMARK 500    SER B 156     -110.65   -169.28                                   
REMARK 500    GLU B 162      -71.08     51.28                                   
REMARK 500    PHE B 163     -151.60   -143.60                                   
REMARK 500    TYR B 168      -53.85   -122.20                                   
REMARK 500    VAL B 169      -80.19    -77.52                                   
REMARK 500    LYS B 170        7.24    -67.23                                   
REMARK 500    LEU B 186     -146.21   -131.90                                   
REMARK 500    LEU B 187     -155.84    -80.82                                   
REMARK 500    ALA B 212       89.79    -59.62                                   
REMARK 500    ALA B 233       61.71   -105.06                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      65 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 LEU B  206     GLY B  207                 -148.42                    
REMARK 500 ASP B  279     LEU B  280                 -148.19                    
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                              MG A 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 121   OG                                                     
REMARK 620 2 SER A 123   OG   55.9                                              
REMARK 620 3 ASP A 221   O   159.0 139.7                                        
REMARK 620 4 ASP A 221   OD1 126.9  91.6  52.9                                  
REMARK 620 5 ASP A 221   OD2  64.7  57.6 109.0  62.3                            
REMARK 620 6 HOH A 601   O    47.5  96.0 123.9 160.3 107.1                      
REMARK 620 7 HOH A 602   O    76.2  81.5 115.7 145.5 134.3  54.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 121   OG                                                     
REMARK 620 2 SER B 123   OG   77.6                                              
REMARK 620 3 ASP B 221   OD1  62.6  77.8                                        
REMARK 620 4 ASP B 221   OD2  87.8  34.6  53.2                                  
REMARK 620 5 ASP B  66   OD2  69.8 117.4  40.0  91.4                            
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 MG A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 502 bound   
REMARK 800  to ASN A 145                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 503 bound   
REMARK 800  to ASN A 308                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 502 bound   
REMARK 800  to ASN B 99                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6BXB   RELATED DB: PDB                                   
REMARK 900 DIFFERENT RESOLUTION DUE TO CRYSTAL DEHYDRATION                      
DBREF  6CKB A    1   109  UNP    P05106   ITB3_HUMAN      27    135             
DBREF  6CKB A  110   286  UNP    P20701   ITAL_HUMAN     153    329             
DBREF  6CKB A  287   459  UNP    P05106   ITB3_HUMAN     376    548             
DBREF  6CKB B    1   109  UNP    P05106   ITB3_HUMAN      27    135             
DBREF  6CKB B  110   286  UNP    P20701   ITAL_HUMAN     153    329             
DBREF  6CKB B  287   459  UNP    P05106   ITB3_HUMAN     376    548             
SEQADV 6CKB PRO A   33  UNP  P05106    LEU    59 CONFLICT                       
SEQADV 6CKB TRP A  171  UNP  P20701    ARG   214 CONFLICT                       
SEQADV 6CKB THR A  460  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB ARG A  461  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB GLU A  462  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB LEU A  463  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB TYR A  464  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB PHE A  465  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB GLN A  466  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB PRO B   33  UNP  P05106    LEU    59 CONFLICT                       
SEQADV 6CKB TRP B  171  UNP  P20701    ARG   214 CONFLICT                       
SEQADV 6CKB THR B  460  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB ARG B  461  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB GLU B  462  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB LEU B  463  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB TYR B  464  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB PHE B  465  UNP  P05106              EXPRESSION TAG                 
SEQADV 6CKB 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 PRO 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 PRO 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     MG  A 501       1                                                       
HET    NAG  A 502      14                                                       
HET    NAG  A 503      14                                                       
HET    NAG  B 501      14                                                       
HET    NAG  B 502      14                                                       
HET    NAG  B 503      14                                                       
HET     CA  B 504       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  NAG    5(C8 H15 N O6)                                               
FORMUL   9   CA    CA 2+                                                        
FORMUL  10  HOH   *4(H2 O)                                                      
HELIX    1 AA1 SER A   12  SER A   20  1                                   9    
HELIX    2 AA2 LEU A   40  LEU A   45  1                                   6    
HELIX    3 AA3 GLN A  125  LEU A  143  1                                  19    
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  VAL A  201  1                                  13    
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 LYS A  245  GLN A  248  5                                   4    
HELIX   10 AB1 THR A  249  THR A  255  1                                   7    
HELIX   11 AB2 PRO A  263  PHE A  267  1                                   5    
HELIX   12 AB3 GLU A  275  GLN A  285  1                                  11    
HELIX   13 AB4 CYS A  372  ALA A  376  5                                   5    
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 SER B   12  SER B   20  1                                   9    
HELIX   17 AB8 GLU B   42  ASP B   47  1                                   6    
HELIX   18 AB9 GLN B  125  LYS B  142  1                                  18    
HELIX   19 AC1 ASP B  164  TYR B  168  5                                   5    
HELIX   20 AC2 ASP B  173  LEU B  178  1                                   6    
HELIX   21 AC3 ASN B  189  ALA B  198  1                                  10    
HELIX   22 AC4 ARG B  203  GLY B  207  5                                   5    
HELIX   23 AC5 LYS B  245  GLN B  248  5                                   4    
HELIX   24 AC6 THR B  249  LYS B  258  1                                  10    
HELIX   25 AC7 THR B  273  LEU B  277  5                                   5    
HELIX   26 AC8 LYS B  278  THR B  282  5                                   5    
HELIX   27 AC9 GLU B  283  ILE B  288  1                                   6    
HELIX   28 AD1 CYS B  372  ALA B  376  5                                   5    
HELIX   29 AD2 PRO B  430  GLN B  434  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 5 GLU A  60  GLU A  65  0                                        
SHEET    2 AA2 5 ARG A  87  LEU A  92 -1  O  ARG A  87   N  GLU A  65           
SHEET    3 AA2 5 LEU A 362  PHE A 368  1  O  GLN A 365   N  ILE A  88           
SHEET    4 AA2 5 LYS A 349  PRO A 355 -1  N  ILE A 353   O  LEU A 362           
SHEET    5 AA2 5 LEU A 294  ARG A 297 -1  N  GLU A 295   O  LYS A 354           
SHEET    1 AA3 4 VAL A  83  SER A  84  0                                        
SHEET    2 AA3 4 SER A  97  ARG A 105 -1  O  GLN A 103   N  SER A  84           
SHEET    3 AA3 4 THR A 331  VAL A 340 -1  O  ILE A 336   N  PHE A 100           
SHEET    4 AA3 4 LEU A 303  SER A 306 -1  N  SER A 304   O  LYS A 339           
SHEET    1 AA4 5 VAL A  83  SER A  84  0                                        
SHEET    2 AA4 5 SER A  97  ARG A 105 -1  O  GLN A 103   N  SER A  84           
SHEET    3 AA4 5 THR A 331  VAL A 340 -1  O  ILE A 336   N  PHE A 100           
SHEET    4 AA4 5 ALA A 309  THR A 310 -1  N  THR A 310   O  SER A 333           
SHEET    5 AA4 5 VAL A 316  ILE A 317 -1  O  ILE A 317   N  ALA A 309           
SHEET    1 AA5 6 TYR A 159  PHE A 163  0                                        
SHEET    2 AA5 6 TYR A 148  PHE A 155 -1  N  GLN A 154   O  LYS A 160           
SHEET    3 AA5 6 VAL A 112  ASP A 119  1  N  LEU A 114   O  GLN A 149           
SHEET    4 AA5 6 THR A 213  THR A 220  1  O  THR A 213   N  ASP A 113           
SHEET    5 AA5 6 ILE A 237  ILE A 243  1  O  TYR A 239   N  LEU A 216           
SHEET    6 AA5 6 VAL A 268  LEU A 271  1  O  LYS A 269   N  ILE A 240           
SHEET    1 AA6 2 GLY A 390  GLU A 393  0                                        
SHEET    2 AA6 2 VAL A 396  CYS A 399 -1  O  ARG A 398   N  THR A 391           
SHEET    1 AA7 2 GLY A 436  CYS A 438  0                                        
SHEET    2 AA7 2 CYS A 443  CYS A 445 -1  O  VAL A 444   N  GLU A 437           
SHEET    1 AA8 2 GLY A 451  ILE A 453  0                                        
SHEET    2 AA8 2 ARG A 461  LEU A 463 -1  O  GLU A 462   N  LYS A 452           
SHEET    1 AA9 5 GLU B  60  VAL B  63  0                                        
SHEET    2 AA9 5 ARG B  87  LEU B  92 -1  O  ARG B  91   N  GLU B  60           
SHEET    3 AA9 5 LEU B 362  PHE B 368  1  O  GLN B 365   N  ILE B  88           
SHEET    4 AA9 5 GLU B 348  LYS B 354 -1  N  ILE B 353   O  LEU B 362           
SHEET    5 AA9 5 GLU B 295  ARG B 297 -1  N  GLU B 295   O  LYS B 354           
SHEET    1 AB1 5 VAL B  83  SER B  84  0                                        
SHEET    2 AB1 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3 AB1 5 THR B 331  VAL B 340 -1  O  ILE B 336   N  PHE B 100           
SHEET    4 AB1 5 LEU B 303  THR B 310 -1  N  ASN B 308   O  SER B 335           
SHEET    5 AB1 5 VAL B 316  ILE B 317 -1  O  ILE B 317   N  ALA B 309           
SHEET    1 AB2 6 TYR B 159  LYS B 160  0                                        
SHEET    2 AB2 6 PHE B 150  PHE B 155 -1  N  GLN B 154   O  LYS B 160           
SHEET    3 AB2 6 LEU B 114  ASP B 119  1  N  PHE B 116   O  ALA B 151           
SHEET    4 AB2 6 VAL B 215  THR B 220  1  O  ILE B 219   N  LEU B 117           
SHEET    5 AB2 6 ILE B 237  ILE B 243  1  O  ILE B 241   N  ILE B 218           
SHEET    6 AB2 6 VAL B 268  LEU B 271  1  O  LYS B 269   N  GLY B 242           
SHEET    1 AB3 2 GLY B 390  GLU B 393  0                                        
SHEET    2 AB3 2 VAL B 396  CYS B 399 -1  O  ARG B 398   N  THR B 391           
SHEET    1 AB4 2 TRP B 403  LEU B 404  0                                        
SHEET    2 AB4 2 CYS B 410  SER B 411 -1  O  CYS B 410   N  LEU B 404           
SHEET    1 AB5 2 GLY B 436  CYS B 438  0                                        
SHEET    2 AB5 2 CYS B 443  CYS B 445 -1  O  VAL B 444   N  GLU B 437           
SHEET    1 AB6 2 GLY B 451  THR B 454  0                                        
SHEET    2 AB6 2 THR B 460  LEU B 463 -1  O  THR B 460   N  THR B 454           
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  2.01  
SSBOND   4 CYS A   26    CYS A   49                          1555   1555  2.02  
SSBOND   5 CYS A  311    CYS A  323                          1555   1555  2.03  
SSBOND   6 CYS A  343    CYS A  370                          1555   1555  2.02  
SSBOND   7 CYS A  374    CYS A  394                          1555   1555  2.02  
SSBOND   8 CYS A  385    CYS A  397                          1555   1555  2.02  
SSBOND   9 CYS A  399    CYS A  408                          1555   1555  2.02  
SSBOND  10 CYS A  410    CYS A  440                          1555   1555  2.03  
SSBOND  11 CYS A  423    CYS A  438                          1555   1555  2.04  
SSBOND  12 CYS A  432    CYS A  443                          1555   1555  2.00  
SSBOND  13 CYS A  445    CYS A  458                          1555   1555  2.05  
SSBOND  14 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND  15 CYS B   13    CYS B  372                          1555   1555  2.02  
SSBOND  16 CYS B   16    CYS B   38                          1555   1555  2.01  
SSBOND  17 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND  18 CYS B  311    CYS B  323                          1555   1555  2.02  
SSBOND  19 CYS B  343    CYS B  370                          1555   1555  2.02  
SSBOND  20 CYS B  374    CYS B  394                          1555   1555  2.03  
SSBOND  21 CYS B  385    CYS B  397                          1555   1555  2.02  
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  2.02  
SSBOND  26 CYS B  445    CYS B  458                          1555   1555  2.04  
LINK         OG  SER A 121                MG    MG A 501     1555   1555  2.29  
LINK         OG  SER A 123                MG    MG A 501     1555   1555  2.00  
LINK         ND2 ASN A 145                 C1  NAG A 502     1555   1555  1.42  
LINK         O   ASP A 221                MG    MG A 501     1555   1555  2.22  
LINK         OD1 ASP A 221                MG    MG A 501     1555   1555  2.33  
LINK         OD2 ASP A 221                MG    MG A 501     1555   1555  1.84  
LINK         ND2 ASN A 308                 C1  NAG A 503     1555   1555  1.42  
LINK         ND2 ASN B  99                 C1  NAG B 502     1555   1555  1.45  
LINK         OG  SER B 121                CA    CA B 504     1555   1555  2.23  
LINK         OG  SER B 123                CA    CA B 504     1555   1555  2.49  
LINK         OD1 ASP B 221                CA    CA B 504     1555   1555  2.26  
LINK         OD2 ASP B 221                CA    CA B 504     1555   1555  2.57  
LINK         ND2 ASN B 308                 C1  NAG B 501     1555   1555  1.44  
LINK         ND2 ASN B 389                 C1  NAG B 503     1555   1555  1.47  
LINK        MG    MG A 501                 O   HOH A 601     1555   1555  2.83  
LINK         OD2 ASP B  66                CA    CA B 504     1555   1655  2.27  
LINK        MG    MG A 501                 O   HOH A 602     1555   1655  1.90  
CISPEP   1 SER A   84    PRO A   85          0        -3.29                     
CISPEP   2 LYS A  262    PRO A  263          0         3.77                     
CISPEP   3 SER B   84    PRO B   85          0        -2.76                     
CISPEP   4 LYS B  262    PRO B  263          0        -8.32                     
SITE     1 AC1  6 SER A 121  SER A 123  ASP A 221  GLY A 222                    
SITE     2 AC1  6 HOH A 601  HOH A 602                                          
SITE     1 AC2  5 SER B 306  ASN B 308  SER B 335  GLU B 337                    
SITE     2 AC2  5 NAG B 502                                                     
SITE     1 AC3  4 ASN B 386  ASN B 387  GLY B 388  ASN B 389                    
SITE     1 AC4  4 ASP B  66  SER B 121  SER B 123  ASP B 221                    
SITE     1 AC5  1 ASN A 145                                                     
SITE     1 AC6  3 SER A 306  PHE A 307  ASN A 308                               
SITE     1 AC7  2 ASN B  99  NAG B 501                                          
CRYST1   59.080   80.910  126.720  90.00  96.36  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      0.016926  0.000000  0.001887        0.00000                         
SCALE2      0.000000  0.012359  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007940        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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