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Database: PDB
Entry: 3G9W
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HEADER    CELL ADHESION                           15-FEB-09   3G9W              
TITLE     CRYSTAL STRUCTURE OF TALIN2 F2-F3 IN COMPLEX WITH THE INTEGRIN BETA1D 
TITLE    2 CYTOPLASMIC TAIL                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TALIN-2;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: F2-F3 DOMAIN;                                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: INTEGRIN BETA-1D;                                          
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: CYTOPLASMIC TAIL;                                          
COMPND  10 SYNONYM: FIBRONECTIN RECEPTOR SUBUNIT BETA, INTEGRIN VLA-4 SUBUNIT   
COMPND  11 BETA;                                                                
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: TLN2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET151;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: ITGB1;                                                         
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET16B                                    
KEYWDS    PROTEIN-PROTEIN COMPLEX, PH DOMAIN SUPERFOLD, PTB DOMAIN, HELICAL     
KEYWDS   2 BUNDLE, INTRINSICALLY UNSTRUCTURED, CELL ADHESION                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.J.ANTHIS,K.L.WEGENER,F.YE,C.KIM,E.D.LOWE,I.VAKONAKIS,N.BATE,        
AUTHOR   2 D.R.CRITCHLEY,M.H.GINSBERG,I.D.CAMPBELL                              
REVDAT   3   05-FEB-14 3G9W    1       JRNL                                     
REVDAT   2   13-JUL-11 3G9W    1       VERSN                                    
REVDAT   1   20-OCT-09 3G9W    0                                                
JRNL        AUTH   N.J.ANTHIS,K.L.WEGENER,F.YE,C.KIM,B.T.GOULT,E.D.LOWE,        
JRNL        AUTH 2 I.VAKONAKIS,N.BATE,D.R.CRITCHLEY,M.H.GINSBERG,I.D.CAMPBELL   
JRNL        TITL   THE STRUCTURE OF AN INTEGRIN/TALIN COMPLEX REVEALS THE BASIS 
JRNL        TITL 2 OF INSIDE-OUT SIGNAL TRANSDUCTION                            
JRNL        REF    EMBO J.                       V.  28  3623 2009              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   19798053                                                     
JRNL        DOI    10.1038/EMBOJ.2009.287                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 41362                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2068                            
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 41.9490 -  6.5660    0.95     2568   127  0.1670 0.1490        
REMARK   3     2  6.5660 -  5.2150    0.96     2558   148  0.1630 0.2060        
REMARK   3     3  5.2150 -  4.5570    0.97     2601   123  0.1520 0.1680        
REMARK   3     4  4.5570 -  4.1400    0.97     2551   169  0.1590 0.2130        
REMARK   3     5  4.1400 -  3.8440    0.97     2598   136  0.1690 0.1620        
REMARK   3     6  3.8440 -  3.6170    0.97     2596   160  0.1740 0.2150        
REMARK   3     7  3.6170 -  3.4360    0.98     2621   137  0.1930 0.2210        
REMARK   3     8  3.4360 -  3.2870    0.98     2587   123  0.1960 0.2970        
REMARK   3     9  3.2870 -  3.1600    0.98     2618   145  0.2010 0.2240        
REMARK   3    10  3.1600 -  3.0510    0.98     2643   145  0.2090 0.2430        
REMARK   3    11  3.0510 -  2.9560    0.99     2565   159  0.2220 0.2470        
REMARK   3    12  2.9560 -  2.8710    0.99     2701   131  0.2250 0.2490        
REMARK   3    13  2.8710 -  2.7960    0.99     2598   145  0.2270 0.2450        
REMARK   3    14  2.7960 -  2.7280    0.99     2691   136  0.2330 0.3250        
REMARK   3    15  2.7280 -  2.6660    0.99     2648   134  0.2320 0.2840        
REMARK   3    16  2.6660 -  2.6090    1.00     2678   142  0.2380 0.2830        
REMARK   3    17  2.6090 -  2.5570    1.00     2686   124  0.2400 0.3540        
REMARK   3    18  2.5570 -  2.5090    1.00     2650   144  0.2390 0.2830        
REMARK   3    19  2.5090 -  2.4640    1.00     2665   148  0.2410 0.2800        
REMARK   3    20  2.4640 -  2.4220    1.00     2604   132  0.2400 0.2920        
REMARK   3    21  2.4220 -  2.3830    1.00     2712   148  0.2410 0.3410        
REMARK   3    22  2.3830 -  2.3460    1.00     2690   174  0.2500 0.2710        
REMARK   3    23  2.3460 -  2.3120    1.00     2618   121  0.2400 0.3170        
REMARK   3    24  2.3120 -  2.2790    1.00     2709   125  0.2430 0.2550        
REMARK   3    25  2.2790 -  2.2480    1.00     2698   140  0.2500 0.2980        
REMARK   3    26  2.2480 -  2.2190    1.00     2640   105  0.2430 0.3160        
REMARK   3    27  2.2190 -  2.1910    1.00     2722   153  0.2480 0.2760        
REMARK   3    28  2.1910 -  2.1650    0.97     2547   168  0.2630 0.2790        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 36.25                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.31                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.19720                                             
REMARK   3    B22 (A**2) : 2.58870                                              
REMARK   3    B33 (A**2) : -5.18020                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
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      :  0.005           4277                                  
REMARK   3   ANGLE     :  0.874           5729                                  
REMARK   3   CHIRALITY :  0.063            597                                  
REMARK   3   PLANARITY :  0.004            730                                  
REMARK   3   DIHEDRAL  : 16.317           1657                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2091  -3.8933 -22.0990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1074 T22:   0.1080                                     
REMARK   3      T33:   0.1143 T12:  -0.0043                                     
REMARK   3      T13:   0.0031 T23:  -0.0238                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1339 L22:  -0.0152                                     
REMARK   3      L33:   1.1358 L12:  -0.1017                                     
REMARK   3      L13:   0.2667 L23:   0.3335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0491 S12:  -0.0112 S13:   0.0303                       
REMARK   3      S21:   0.0587 S22:   0.0788 S23:   0.0246                       
REMARK   3      S31:  -0.0486 S32:   0.0097 S33:  -0.0152                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9590   7.5175   7.1256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1009 T22:   0.1155                                     
REMARK   3      T33:   0.1440 T12:   0.0302                                     
REMARK   3      T13:  -0.0122 T23:   0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0123 L22:   0.4876                                     
REMARK   3      L33:   1.0843 L12:  -0.0835                                     
REMARK   3      L13:  -0.1563 L23:   0.1370                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1796 S12:   0.0887 S13:   0.0422                       
REMARK   3      S21:  -0.1610 S22:  -0.0637 S23:   0.1473                       
REMARK   3      S31:  -0.0020 S32:  -0.0902 S33:  -0.1011                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  41.4702  -1.7207  25.5769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1894 T22:   0.0900                                     
REMARK   3      T33:   0.1035 T12:  -0.0119                                     
REMARK   3      T13:   0.0087 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3819 L22:  -0.3197                                     
REMARK   3      L33:   0.6451 L12:  -0.2377                                     
REMARK   3      L13:   0.4421 L23:  -0.2080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0627 S12:  -0.0448 S13:  -0.0238                       
REMARK   3      S21:  -0.1101 S22:  -0.0922 S23:  -0.0010                       
REMARK   3      S31:   0.1964 S32:  -0.0957 S33:  -0.0011                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7068 -14.0325 -40.9435              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1251 T22:   0.1490                                     
REMARK   3      T33:   0.1547 T12:  -0.1136                                     
REMARK   3      T13:  -0.0318 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.2491 L22:   0.2870                                     
REMARK   3      L33:   0.0190 L12:  -0.0979                                     
REMARK   3      L13:  -0.1063 L23:  -0.1878                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1198 S12:  -0.0053 S13:   0.0500                       
REMARK   3      S21:   0.1366 S22:  -0.1729 S23:   0.1144                       
REMARK   3      S31:  -0.0939 S32:   0.0327 S33:   0.0405                       
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 3G9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051606.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
REMARK 200  MONOCHROMATOR                  : HORIZONTALLY DIFFRACTING           
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : MONOCHROMATOR (HORIZONTALLY SIDE   
REMARK 200                                   DIFFRACTING SILICON 111 CRYSTAL)   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41362                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.165                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : 0.11400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
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: PDB ENTRIES 1MIX, 1MK7, 1MK9                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM ACETATE, 0.02M MAGNESIUM   
REMARK 280  CHLORIDE, 0.05M HEPES, 5% PEG 8K, PH 7.0, VAPOR DIFFUSION,          
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.63000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.92500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.36000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.92500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.63000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.36000            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   186                                                      
REMARK 465     ILE A   187                                                      
REMARK 465     ASP A   188                                                      
REMARK 465     PRO A   189                                                      
REMARK 465     PHE A   190                                                      
REMARK 465     THR A   191                                                      
REMARK 465     GLY B   186                                                      
REMARK 465     ILE B   187                                                      
REMARK 465     ASP B   188                                                      
REMARK 465     PRO B   189                                                      
REMARK 465     PHE B   190                                                      
REMARK 465     THR B   191                                                      
REMARK 465     GLY B   192                                                      
REMARK 465     ILE B   193                                                      
REMARK 465     ASP B   194                                                      
REMARK 465     PRO B   195                                                      
REMARK 465     PHE B   196                                                      
REMARK 465     THR B   197                                                      
REMARK 465     LYS B   198                                                      
REMARK 465     PHE B   199                                                      
REMARK 465     PHE B   200                                                      
REMARK 465     TYR B   201                                                      
REMARK 465     SER B   202                                                      
REMARK 465     ASP B   203                                                      
REMARK 465     GLN B   204                                                      
REMARK 465     ASN C   789                                                      
REMARK 465     PHE C   790                                                      
REMARK 465     LYS C   791                                                      
REMARK 465     ASN C   792                                                      
REMARK 465     PRO C   793                                                      
REMARK 465     ASN C   794                                                      
REMARK 465     TYR C   795                                                      
REMARK 465     GLY C   796                                                      
REMARK 465     ARG C   797                                                      
REMARK 465     LYS C   798                                                      
REMARK 465     ALA C   799                                                      
REMARK 465     GLY C   800                                                      
REMARK 465     LEU C   801                                                      
REMARK 465     PHE D   790                                                      
REMARK 465     LYS D   791                                                      
REMARK 465     ASN D   792                                                      
REMARK 465     PRO D   793                                                      
REMARK 465     ASN D   794                                                      
REMARK 465     TYR D   795                                                      
REMARK 465     GLY D   796                                                      
REMARK 465     ARG D   797                                                      
REMARK 465     LYS D   798                                                      
REMARK 465     ALA D   799                                                      
REMARK 465     GLY D   800                                                      
REMARK 465     LEU D   801                                                      
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    ILE A 193      160.51    152.05                                   
REMARK 500    THR A 385      146.61   -171.82                                   
REMARK 500    PRO B 259      132.30    -37.92                                   
REMARK 500    THR B 385      146.19   -171.17                                   
REMARK 500    THR C 777      -35.41    -37.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 618        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH A 622        DISTANCE =  5.59 ANGSTROMS                       
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 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 16158   RELATED DB: BMRB                                 
REMARK 900 NMR ASSIGNMENTS OF THE BETA1D INTEGRIN TAIL                          
REMARK 900 RELATED ID: 16159   RELATED DB: BMRB                                 
REMARK 900 NMR ASSIGNMENTS OF THE BETA1A INTEGRIN TAIL                          
REMARK 900 RELATED ID: 16162   RELATED DB: BMRB                                 
REMARK 900 NMR ASSIGNMENTS OF THE BETA1D INTEGRIN TAIL WITH A C-                
REMARK 900 TERMINAL POLYHISTIDINE TAG                                           
REMARK 900 RELATED ID: 15552   RELATED DB: BMRB                                 
REMARK 900 NMR ASSIGNMENTS OF THE BETA3 INTEGRIN TAIL                           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF CHAIN C, D IS ISOFORM BETA-1D                        
REMARK 999 AS LISTED IN UNP ENTRY, P05556-5                                     
DBREF  3G9W A  198   408  UNP    Q71LX4   TLN2_MOUSE     198    408             
DBREF  3G9W B  198   408  UNP    Q71LX4   TLN2_MOUSE     198    408             
DBREF  3G9W C  752   801  UNP    P05556   ITB1_HUMAN     752    801             
DBREF  3G9W D  752   801  UNP    P05556   ITB1_HUMAN     752    801             
SEQADV 3G9W GLY A  186  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W ILE A  187  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W ASP A  188  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W PRO A  189  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W PHE A  190  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W THR A  191  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W GLY A  192  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W ILE A  193  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W ASP A  194  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W PRO A  195  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W PHE A  196  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W THR A  197  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W GLY B  186  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W ILE B  187  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W ASP B  188  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W PRO B  189  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W PHE B  190  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W THR B  191  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W GLY B  192  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W ILE B  193  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W ASP B  194  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W PRO B  195  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W PHE B  196  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W THR B  197  UNP  Q71LX4              EXPRESSION TAG                 
SEQADV 3G9W GLY C  750  UNP  P05556              EXPRESSION TAG                 
SEQADV 3G9W PRO C  751  UNP  P05556              EXPRESSION TAG                 
SEQADV 3G9W GLY D  750  UNP  P05556              EXPRESSION TAG                 
SEQADV 3G9W PRO D  751  UNP  P05556              EXPRESSION TAG                 
SEQRES   1 A  223  GLY ILE ASP PRO PHE THR GLY ILE ASP PRO PHE THR LYS          
SEQRES   2 A  223  PHE PHE TYR SER ASP GLN ASN VAL ASP SER ARG ASP PRO          
SEQRES   3 A  223  VAL GLN LEU ASN LEU LEU TYR VAL GLN ALA ARG ASP ASP          
SEQRES   4 A  223  ILE LEU ASN GLY SER HIS PRO VAL SER PHE GLU LYS ALA          
SEQRES   5 A  223  CYS GLU PHE GLY GLY PHE GLN ALA GLN ILE GLN PHE GLY          
SEQRES   6 A  223  PRO HIS VAL GLU HIS LYS HIS LYS PRO GLY PHE LEU ASP          
SEQRES   7 A  223  LEU LYS GLU PHE LEU PRO LYS GLU TYR ILE LYS GLN ARG          
SEQRES   8 A  223  GLY ALA GLU LYS ARG ILE PHE GLN GLU HIS LYS ASN CYS          
SEQRES   9 A  223  GLY GLU MET SER GLU ILE GLU ALA LYS VAL LYS TYR VAL          
SEQRES  10 A  223  LYS LEU ALA ARG SER LEU ARG THR TYR GLY VAL SER PHE          
SEQRES  11 A  223  PHE LEU VAL LYS GLU LYS MET LYS GLY LYS ASN LYS LEU          
SEQRES  12 A  223  VAL PRO ARG LEU LEU GLY ILE THR LYS ASP SER VAL MET          
SEQRES  13 A  223  ARG VAL ASP GLU LYS THR LYS GLU VAL LEU GLN GLU TRP          
SEQRES  14 A  223  PRO LEU THR THR VAL LYS ARG TRP ALA ALA SER PRO LYS          
SEQRES  15 A  223  SER PHE THR LEU ASP PHE GLY GLU TYR GLN GLU SER TYR          
SEQRES  16 A  223  TYR SER VAL GLN THR THR GLU GLY GLU GLN ILE SER GLN          
SEQRES  17 A  223  LEU ILE ALA GLY TYR ILE ASP ILE ILE LEU LYS LYS LYS          
SEQRES  18 A  223  GLN SER                                                      
SEQRES   1 B  223  GLY ILE ASP PRO PHE THR GLY ILE ASP PRO PHE THR LYS          
SEQRES   2 B  223  PHE PHE TYR SER ASP GLN ASN VAL ASP SER ARG ASP PRO          
SEQRES   3 B  223  VAL GLN LEU ASN LEU LEU TYR VAL GLN ALA ARG ASP ASP          
SEQRES   4 B  223  ILE LEU ASN GLY SER HIS PRO VAL SER PHE GLU LYS ALA          
SEQRES   5 B  223  CYS GLU PHE GLY GLY PHE GLN ALA GLN ILE GLN PHE GLY          
SEQRES   6 B  223  PRO HIS VAL GLU HIS LYS HIS LYS PRO GLY PHE LEU ASP          
SEQRES   7 B  223  LEU LYS GLU PHE LEU PRO LYS GLU TYR ILE LYS GLN ARG          
SEQRES   8 B  223  GLY ALA GLU LYS ARG ILE PHE GLN GLU HIS LYS ASN CYS          
SEQRES   9 B  223  GLY GLU MET SER GLU ILE GLU ALA LYS VAL LYS TYR VAL          
SEQRES  10 B  223  LYS LEU ALA ARG SER LEU ARG THR TYR GLY VAL SER PHE          
SEQRES  11 B  223  PHE LEU VAL LYS GLU LYS MET LYS GLY LYS ASN LYS LEU          
SEQRES  12 B  223  VAL PRO ARG LEU LEU GLY ILE THR LYS ASP SER VAL MET          
SEQRES  13 B  223  ARG VAL ASP GLU LYS THR LYS GLU VAL LEU GLN GLU TRP          
SEQRES  14 B  223  PRO LEU THR THR VAL LYS ARG TRP ALA ALA SER PRO LYS          
SEQRES  15 B  223  SER PHE THR LEU ASP PHE GLY GLU TYR GLN GLU SER TYR          
SEQRES  16 B  223  TYR SER VAL GLN THR THR GLU GLY GLU GLN ILE SER GLN          
SEQRES  17 B  223  LEU ILE ALA GLY TYR ILE ASP ILE ILE LEU LYS LYS LYS          
SEQRES  18 B  223  GLN SER                                                      
SEQRES   1 C   52  GLY PRO LYS LEU LEU MET ILE ILE HIS ASP ARG ARG GLU          
SEQRES   2 C   52  PHE ALA LYS PHE GLU LYS GLU LYS MET ASN ALA LYS TRP          
SEQRES   3 C   52  ASP THR GLN GLU ASN PRO ILE TYR LYS SER PRO ILE ASN          
SEQRES   4 C   52  ASN PHE LYS ASN PRO ASN TYR GLY ARG LYS ALA GLY LEU          
SEQRES   1 D   52  GLY PRO LYS LEU LEU MET ILE ILE HIS ASP ARG ARG GLU          
SEQRES   2 D   52  PHE ALA LYS PHE GLU LYS GLU LYS MET ASN ALA LYS TRP          
SEQRES   3 D   52  ASP THR GLN GLU ASN PRO ILE TYR LYS SER PRO ILE ASN          
SEQRES   4 D   52  ASN PHE LYS ASN PRO ASN TYR GLY ARG LYS ALA GLY LEU          
HET    GOL  A   1       6                                                       
HET    GOL  A 409       6                                                       
HET    PEG  A 410       7                                                       
HET    GOL  B   1       6                                                       
HET    GOL  B 409       6                                                       
HET    PEG  B 410       7                                                       
HET    GOL  B 411       6                                                       
HET    GOL  C   1       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    6(C3 H8 O3)                                                  
FORMUL   7  PEG    2(C4 H10 O3)                                                 
FORMUL  13  HOH   *381(H2 O)                                                    
HELIX    1   1 ASP A  194  LYS A  198  5                                   5    
HELIX    2   2 ASP A  210  ASN A  227  1                                  18    
HELIX    3   3 SER A  233  GLY A  250  1                                  18    
HELIX    4   4 ASP A  263  PHE A  267  5                                   5    
HELIX    5   5 PRO A  269  ILE A  273  5                                   5    
HELIX    6   6 GLY A  277  CYS A  289  1                                  13    
HELIX    7   7 SER A  293  LEU A  308  1                                  16    
HELIX    8   8 THR A  357  VAL A  359  5                                   3    
HELIX    9   9 PHE A  373  GLN A  377  5                                   5    
HELIX   10  10 GLU A  387  SER A  408  1                                  22    
HELIX   11  11 ASP B  210  ASN B  227  1                                  18    
HELIX   12  12 SER B  233  GLY B  250  1                                  18    
HELIX   13  13 ASP B  263  PHE B  267  5                                   5    
HELIX   14  14 PRO B  269  ILE B  273  5                                   5    
HELIX   15  15 GLY B  277  CYS B  289  1                                  13    
HELIX   16  16 SER B  293  LEU B  308  1                                  16    
HELIX   17  17 THR B  357  VAL B  359  5                                   3    
HELIX   18  18 PHE B  373  GLN B  377  5                                   5    
HELIX   19  19 GLU B  387  GLN B  407  1                                  21    
HELIX   20  20 GLY C  750  LYS C  770  1                                  21    
HELIX   21  21 MET C  771  ALA C  773  5                                   3    
HELIX   22  22 GLY D  750  LYS D  770  1                                  21    
HELIX   23  23 MET D  771  ALA D  773  5                                   3    
HELIX   24  24 SER D  785  ASN D  789  5                                   5    
SHEET    1   A 4 SER A 314  LYS A 321  0                                        
SHEET    2   A 4 LEU A 328  ILE A 335 -1  O  LEU A 333   N  PHE A 316           
SHEET    3   A 4 SER A 339  VAL A 343 -1  O  VAL A 343   N  LEU A 332           
SHEET    4   A 4 VAL A 350  PRO A 355 -1  O  TRP A 354   N  VAL A 340           
SHEET    1   B 4 TYR A 381  GLN A 384  0                                        
SHEET    2   B 4 SER A 368  ASP A 372 -1  N  LEU A 371   O  TYR A 381           
SHEET    3   B 4 ARG A 361  SER A 365 -1  N  ARG A 361   O  ASP A 372           
SHEET    4   B 4 LYS D 774  TRP D 775 -1  O  LYS D 774   N  ALA A 364           
SHEET    1   C 4 SER B 314  LYS B 321  0                                        
SHEET    2   C 4 LEU B 328  ILE B 335 -1  O  ARG B 331   N  VAL B 318           
SHEET    3   C 4 SER B 339  VAL B 343 -1  O  VAL B 343   N  LEU B 332           
SHEET    4   C 4 VAL B 350  PRO B 355 -1  O  TRP B 354   N  VAL B 340           
SHEET    1   D 4 TYR B 381  GLN B 384  0                                        
SHEET    2   D 4 SER B 368  ASP B 372 -1  N  LEU B 371   O  TYR B 381           
SHEET    3   D 4 ARG B 361  ALA B 364 -1  N  ARG B 361   O  ASP B 372           
SHEET    4   D 4 LYS C 774  TRP C 775 -1  O  LYS C 774   N  ALA B 364           
SITE     1 AC1  5 GLY A 228  HOH A 559  HOH A 603  HOH A 605                    
SITE     2 AC1  5 HOH B 509                                                     
SITE     1 AC2 10 ASP A 224  SER A 229  HIS A 230  GLY A 312                    
SITE     2 AC2 10 VAL A 313  SER A 314  HOH A 657  HOH A 663                    
SITE     3 AC2 10 HOH A 665  ILE C 757                                          
SITE     1 AC3  6 ARG A 342  GLN A 352  GLN A 377  TYR A 380                    
SITE     2 AC3  6 HOH A 565  HOH A 695                                          
SITE     1 AC4  8 GLY B 228  SER B 229  PHE B 315  HOH B 491                    
SITE     2 AC4  8 HOH B 496  HOH B 528  HOH B 578  HOH B 581                    
SITE     1 AC5  5 GLU A 387  LYS B 321  GLY B 324  LYS B 325                    
SITE     2 AC5  5 ASN B 326                                                     
SITE     1 AC6  8 GLU B 320  LYS B 321  ARG B 342  GLN B 352                    
SITE     2 AC6  8 GLN B 377  HOH B 681  HOH B 692  HOH B 699                    
SITE     1 AC7  8 ASP B 224  SER B 229  HIS B 230  GLY B 312                    
SITE     2 AC7  8 VAL B 313  HOH B 430  HOH B 659  ILE D 757                    
SITE     1 AC8  4 LYS C 770  MET C 771  ALA C 773  TRP C 775                    
CRYST1   53.260  108.720  131.850  90.00  90.00  90.00 P 21 21 21    8          
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      0.018776  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009198  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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