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Database: PDB
Entry: 6EJM
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Original site: 6EJM 
HEADER    CELL ADHESION                           22-SEP-17   6EJM              
TITLE     CRYSTAL STRUCTURE OF HUMAN CD81 LARGE EXTRACELLULAR LOOP IN COMPLEX   
TITLE    2 WITH SINGLE CHAIN FV FRAGMENT 5                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD81 ANTIGEN;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 26 KDA CELL SURFACE PROTEIN TAPA-1,TARGET OF THE            
COMPND   5 ANTIPROLIFERATIVE ANTIBODY 1,TETRASPANIN-28,TSPAN-28;                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SINGLE CHAIN FV FRAGMENT;                                  
COMPND   9 CHAIN: H, I;                                                         
COMPND  10 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: CD81, TAPA1, TSPAN28;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_TAXID: 10090;                                               
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HELICAL BUNDLE, ANTIBODY-ANTIGEN COMPLEX, CELL ADHESION               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KUGLSTATTER,S.F.HARRIS,A.VILLASENOR                                 
REVDAT   2   20-JUN-18 6EJM    1       JRNL                                     
REVDAT   1   30-MAY-18 6EJM    0                                                
JRNL        AUTH   B.NELSON,J.ADAMS,A.KUGLSTATTER,Z.LI,S.F.HARRIS,Y.LIU,        
JRNL        AUTH 2 S.BOHINI,H.MA,K.KLUMPP,J.GAO,S.S.SIDHU                       
JRNL        TITL   STRUCTURE-GUIDED COMBINATORIAL ENGINEERING FACILITATES       
JRNL        TITL 2 AFFINITY AND SPECIFICITY OPTIMIZATION OF ANTI-CD81           
JRNL        TITL 3 ANTIBODIES.                                                  
JRNL        REF    J. MOL. BIOL.                 V. 430  2139 2018              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   29778602                                                     
JRNL        DOI    10.1016/J.JMB.2018.05.018                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 38497                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2064                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 895                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 26.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 37                           
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4843                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 229                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.51000                                             
REMARK   3    B22 (A**2) : 0.82000                                              
REMARK   3    B33 (A**2) : 0.70000                                              
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.262         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.233         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.169         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.573         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4941 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6691 ; 1.973 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   627 ; 7.267 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   194 ;37.240 ;24.330       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   836 ;19.554 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;22.124 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   771 ; 0.140 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3632 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3129 ; 1.128 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5033 ; 2.123 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1812 ; 3.190 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1658 ; 5.139 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6EJM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006705.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40627                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.1                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 30.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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   (%): 57.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 1.75 M AMMONIUM          
REMARK 280  SULFATE, 1 M SODIUM CHLORIDE, PH 6.0, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.67550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.33300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.25100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.33300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.67550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.25100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, I                            
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   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     ASP A   138                                                      
REMARK 465     ASP A   139                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     GLY B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     GLY B   112                                                      
REMARK 465     ASP B   138                                                      
REMARK 465     ASP B   139                                                      
REMARK 465     ALA B   140                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     HIS B   208                                                      
REMARK 465     ALA H    38                                                      
REMARK 465     GLU H    39                                                      
REMARK 465     GLY H   157                                                      
REMARK 465     GLY H   158                                                      
REMARK 465     SER H   159                                                      
REMARK 465     GLY H   160                                                      
REMARK 465     GLY H   161                                                      
REMARK 465     GLY H   162                                                      
REMARK 465     GLY H   163                                                      
REMARK 465     SER H   164                                                      
REMARK 465     GLY H   165                                                      
REMARK 465     GLY H   166                                                      
REMARK 465     GLY H   167                                                      
REMARK 465     GLY H   168                                                      
REMARK 465     SER H   169                                                      
REMARK 465     GLY H   170                                                      
REMARK 465     GLY H   171                                                      
REMARK 465     GLY H   172                                                      
REMARK 465     GLY H   173                                                      
REMARK 465     SER H   174                                                      
REMARK 465     ALA I    38                                                      
REMARK 465     GLU I    39                                                      
REMARK 465     GLY I   155                                                      
REMARK 465     GLY I   156                                                      
REMARK 465     GLY I   157                                                      
REMARK 465     GLY I   158                                                      
REMARK 465     SER I   159                                                      
REMARK 465     GLY I   160                                                      
REMARK 465     GLY I   161                                                      
REMARK 465     GLY I   162                                                      
REMARK 465     GLY I   163                                                      
REMARK 465     SER I   164                                                      
REMARK 465     GLY I   165                                                      
REMARK 465     GLY I   166                                                      
REMARK 465     GLY I   167                                                      
REMARK 465     GLY I   168                                                      
REMARK 465     SER I   169                                                      
REMARK 465     GLY I   170                                                      
REMARK 465     GLY I   171                                                      
REMARK 465     GLY I   172                                                      
REMARK 465     GLY I   173                                                      
REMARK 465     SER I   174                                                      
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   OD1  ASP I   207     OH   TYR I   211              2.07            
REMARK 500   OD2  ASP H   207     OH   TYR H   211              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU H 260   CG    GLU H 260   CD      0.093                       
REMARK 500    GLU I  44   CG    GLU I  44   CD     -0.099                       
REMARK 500    CYS I  60   CB    CYS I  60   SG     -0.113                       
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    ARG H  76   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    MET H 178   CG  -  SD  -  CE  ANGL. DEV. = -10.8 DEGREES          
REMARK 500    LEU H 212   CA  -  CB  -  CG  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    LEU H 215   CA  -  CB  -  CG  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    LEU I  56   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    ARG I  76   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    LEU I 215   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    LEU I 226   CB  -  CG  -  CD1 ANGL. DEV. = -11.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 162       67.49   -118.48                                   
REMARK 500    SER A 177      -68.49   -109.86                                   
REMARK 500    VAL B 114      118.17    -25.93                                   
REMARK 500    ASP B 155       65.76     71.09                                   
REMARK 500    LEU B 162       56.48   -140.98                                   
REMARK 500    SER B 177      -99.59    -66.96                                   
REMARK 500    PRO H  52      134.62    -38.06                                   
REMARK 500    LYS H  81       31.26     73.11                                   
REMARK 500    ALA H  87      149.79   -175.46                                   
REMARK 500    SER H 123       47.08     36.40                                   
REMARK 500    ILE H 189      122.00    -29.15                                   
REMARK 500    ASP H 207      -35.46     -8.70                                   
REMARK 500    VAL H 230      -54.04     79.93                                   
REMARK 500    SER I 136       53.35    -92.02                                   
REMARK 500    ASP I 207      -33.12    -22.88                                   
REMARK 500    VAL I 230      -54.03     71.98                                   
REMARK 500    ARG I 256      102.85     50.81                                   
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 THR H  206     ASP H  207                  147.36                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DFW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6EJG   RELATED DB: PDB                                   
DBREF  6EJM A  112   202  UNP    P60033   CD81_HUMAN     112    202             
DBREF  6EJM B  112   202  UNP    P60033   CD81_HUMAN     112    202             
DBREF  6EJM H   38   286  PDB    6EJM     6EJM            38    286             
DBREF  6EJM I   38   286  PDB    6EJM     6EJM            38    286             
SEQADV 6EJM GLY A  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM SER A  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS A  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS A  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS A  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS A  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS A  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS A  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM GLY B  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM SER B  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS B  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS B  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS B  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS B  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS B  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 6EJM HIS B  208  UNP  P60033              EXPRESSION TAG                 
SEQRES   1 A   99  GLY SER GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 A   99  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 A   99  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 A   99  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 A   99  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 A   99  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 A   99  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 A   99  LYS LEU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B   99  GLY SER GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 B   99  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 B   99  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 B   99  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 B   99  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 B   99  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 B   99  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 B   99  LYS LEU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 H  249  ALA GLU VAL MET LEU VAL GLU SER GLY GLY GLY PHE VAL          
SEQRES   2 H  249  LYS PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER          
SEQRES   3 H  249  GLY PHE THR PHE ARG SER TYR ILE MET SER TRP VAL ARG          
SEQRES   4 H  249  GLN THR PRO GLU LYS ARG LEU GLU TRP VAL ALA THR ILE          
SEQRES   5 H  249  SER GLY GLY GLY GLY ASN THR TYR TYR PRO ASP SER VAL          
SEQRES   6 H  249  LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN          
SEQRES   7 H  249  THR LEU TYR LEU GLN LEU SER SER LEU ARG SER GLU ASP          
SEQRES   8 H  249  THR ALA LEU TYR TYR CYS ALA SER LEU THR ALA VAL GLY          
SEQRES   9 H  249  ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER          
SEQRES  10 H  249  GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY          
SEQRES  11 H  249  GLY SER GLY GLY GLY GLY SER ASP VAL VAL MET THR GLN          
SEQRES  12 H  249  THR PRO LEU THR LEU SER VAL THR ILE GLY GLN PRO ALA          
SEQRES  13 H  249  SER ILE SER CYS LYS SER SER GLN SER LEU PHE ASP THR          
SEQRES  14 H  249  ASP GLY LYS THR TYR LEU THR TRP LEU LEU GLN ARG PRO          
SEQRES  15 H  249  GLY GLN SER PRO LYS ARG LEU ILE TYR LEU VAL SER LYS          
SEQRES  16 H  249  LEU ALA SER GLY VAL PRO ASP ARG PHE THR GLY SER GLY          
SEQRES  17 H  249  SER GLY THR ASP PHE THR LEU LYS ILE SER ARG VAL GLU          
SEQRES  18 H  249  ALA GLU ASP LEU GLY VAL TYR TYR CYS LEU GLN GLY THR          
SEQRES  19 H  249  HIS PHE PRO LEU THR PHE GLY ALA GLY THR LYS LEU ASP          
SEQRES  20 H  249  LEU LYS                                                      
SEQRES   1 I  249  ALA GLU VAL MET LEU VAL GLU SER GLY GLY GLY PHE VAL          
SEQRES   2 I  249  LYS PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER          
SEQRES   3 I  249  GLY PHE THR PHE ARG SER TYR ILE MET SER TRP VAL ARG          
SEQRES   4 I  249  GLN THR PRO GLU LYS ARG LEU GLU TRP VAL ALA THR ILE          
SEQRES   5 I  249  SER GLY GLY GLY GLY ASN THR TYR TYR PRO ASP SER VAL          
SEQRES   6 I  249  LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN          
SEQRES   7 I  249  THR LEU TYR LEU GLN LEU SER SER LEU ARG SER GLU ASP          
SEQRES   8 I  249  THR ALA LEU TYR TYR CYS ALA SER LEU THR ALA VAL GLY          
SEQRES   9 I  249  ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER          
SEQRES  10 I  249  GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY          
SEQRES  11 I  249  GLY SER GLY GLY GLY GLY SER ASP VAL VAL MET THR GLN          
SEQRES  12 I  249  THR PRO LEU THR LEU SER VAL THR ILE GLY GLN PRO ALA          
SEQRES  13 I  249  SER ILE SER CYS LYS SER SER GLN SER LEU PHE ASP THR          
SEQRES  14 I  249  ASP GLY LYS THR TYR LEU THR TRP LEU LEU GLN ARG PRO          
SEQRES  15 I  249  GLY GLN SER PRO LYS ARG LEU ILE TYR LEU VAL SER LYS          
SEQRES  16 I  249  LEU ALA SER GLY VAL PRO ASP ARG PHE THR GLY SER GLY          
SEQRES  17 I  249  SER GLY THR ASP PHE THR LEU LYS ILE SER ARG VAL GLU          
SEQRES  18 I  249  ALA GLU ASP LEU GLY VAL TYR TYR CYS LEU GLN GLY THR          
SEQRES  19 I  249  HIS PHE PRO LEU THR PHE GLY ALA GLY THR LYS LEU ASP          
SEQRES  20 I  249  LEU LYS                                                      
FORMUL   5  HOH   *229(H2 O)                                                    
HELIX    1 AA1 ASN A  115  VAL A  135  1                                  21    
HELIX    2 AA2 ASN A  141  LEU A  154  1                                  14    
HELIX    3 AA3 LEU A  162  LYS A  171  1                                  10    
HELIX    4 AA4 ASP A  189  SER A  199  1                                  11    
HELIX    5 AA5 ASN B  115  ASP B  137  1                                  23    
HELIX    6 AA6 ASN B  142  ASP B  155  1                                  14    
HELIX    7 AA7 SER B  159  THR B  161  5                                   3    
HELIX    8 AA8 LEU B  162  SER B  168  1                                   7    
HELIX    9 AA9 VAL B  169  ASN B  173  5                                   5    
HELIX   10 AB1 ASP B  189  SER B  199  1                                  11    
HELIX   11 AB2 THR H   66  TYR H   70  5                                   5    
HELIX   12 AB3 ASN H  112  LYS H  114  5                                   3    
HELIX   13 AB4 ARG H  125  THR H  129  5                                   5    
HELIX   14 AB5 GLU H  258  LEU H  262  5                                   5    
HELIX   15 AB6 THR I   66  TYR I   70  5                                   5    
HELIX   16 AB7 ARG I  125  THR I  129  5                                   5    
SHEET    1 AA1 4 MET H  41  SER H  45  0                                        
SHEET    2 AA1 4 LEU H  56  SER H  63 -1  O  SER H  59   N  SER H  45           
SHEET    3 AA1 4 THR H 116  LEU H 121 -1  O  LEU H 121   N  LEU H  56           
SHEET    4 AA1 4 THR H 107  ASP H 111 -1  N  SER H 109   O  TYR H 118           
SHEET    1 AA2 6 GLY H  48  VAL H  50  0                                        
SHEET    2 AA2 6 THR H 148  VAL H 152  1  O  SER H 149   N  GLY H  48           
SHEET    3 AA2 6 ALA H 130  ALA H 135 -1  N  TYR H 132   O  THR H 148           
SHEET    4 AA2 6 MET H  72  GLN H  77 -1  N  VAL H  75   O  TYR H 133           
SHEET    5 AA2 6 LEU H  83  ILE H  89 -1  O  GLU H  84   N  ARG H  76           
SHEET    6 AA2 6 THR H  96  TYR H  97 -1  O  TYR H  97   N  THR H  88           
SHEET    1 AA3 4 MET H 178  THR H 181  0                                        
SHEET    2 AA3 4 ALA H 193  SER H 199 -1  O  LYS H 198   N  THR H 179           
SHEET    3 AA3 4 ASP H 249  ILE H 254 -1  O  LEU H 252   N  ILE H 195           
SHEET    4 AA3 4 PHE H 241  SER H 246 -1  N  THR H 242   O  LYS H 253           
SHEET    1 AA4 6 THR H 184  VAL H 187  0                                        
SHEET    2 AA4 6 THR H 281  LEU H 285  1  O  ASP H 284   N  VAL H 187           
SHEET    3 AA4 6 GLY H 263  GLN H 269 -1  N  GLY H 263   O  LEU H 283           
SHEET    4 AA4 6 LEU H 212  GLN H 217 -1  N  THR H 213   O  LEU H 268           
SHEET    5 AA4 6 PRO H 223  TYR H 228 -1  O  LEU H 226   N  TRP H 214           
SHEET    6 AA4 6 LYS H 232  LEU H 233 -1  O  LYS H 232   N  TYR H 228           
SHEET    1 AA5 4 THR H 184  VAL H 187  0                                        
SHEET    2 AA5 4 THR H 281  LEU H 285  1  O  ASP H 284   N  VAL H 187           
SHEET    3 AA5 4 GLY H 263  GLN H 269 -1  N  GLY H 263   O  LEU H 283           
SHEET    4 AA5 4 THR H 276  PHE H 277 -1  O  THR H 276   N  GLN H 269           
SHEET    1 AA6 4 MET I  41  SER I  45  0                                        
SHEET    2 AA6 4 LEU I  56  SER I  63 -1  O  SER I  59   N  SER I  45           
SHEET    3 AA6 4 THR I 116  LEU I 121 -1  O  LEU I 117   N  CYS I  60           
SHEET    4 AA6 4 THR I 107  ASP I 111 -1  N  SER I 109   O  TYR I 118           
SHEET    1 AA7 6 GLY I  48  VAL I  50  0                                        
SHEET    2 AA7 6 THR I 148  VAL I 152  1  O  THR I 151   N  VAL I  50           
SHEET    3 AA7 6 ALA I 130  ALA I 135 -1  N  ALA I 130   O  VAL I 150           
SHEET    4 AA7 6 MET I  72  GLN I  77 -1  N  SER I  73   O  ALA I 135           
SHEET    5 AA7 6 LEU I  83  ILE I  89 -1  O  GLU I  84   N  ARG I  76           
SHEET    6 AA7 6 THR I  96  TYR I  97 -1  O  TYR I  97   N  THR I  88           
SHEET    1 AA8 4 MET I 178  THR I 181  0                                        
SHEET    2 AA8 4 ALA I 193  SER I 199 -1  O  LYS I 198   N  THR I 179           
SHEET    3 AA8 4 ASP I 249  ILE I 254 -1  O  LEU I 252   N  ILE I 195           
SHEET    4 AA8 4 PHE I 241  SER I 246 -1  N  SER I 244   O  THR I 251           
SHEET    1 AA9 6 THR I 184  VAL I 187  0                                        
SHEET    2 AA9 6 THR I 281  LEU I 285  1  O  LYS I 282   N  LEU I 185           
SHEET    3 AA9 6 VAL I 264  GLN I 269 -1  N  TYR I 265   O  THR I 281           
SHEET    4 AA9 6 LEU I 212  GLN I 217 -1  N  GLN I 217   O  VAL I 264           
SHEET    5 AA9 6 PRO I 223  TYR I 228 -1  O  LEU I 226   N  TRP I 214           
SHEET    6 AA9 6 LYS I 232  LEU I 233 -1  O  LYS I 232   N  TYR I 228           
SHEET    1 AB1 4 THR I 184  VAL I 187  0                                        
SHEET    2 AB1 4 THR I 281  LEU I 285  1  O  LYS I 282   N  LEU I 185           
SHEET    3 AB1 4 VAL I 264  GLN I 269 -1  N  TYR I 265   O  THR I 281           
SHEET    4 AB1 4 THR I 276  PHE I 277 -1  O  THR I 276   N  GLN I 269           
SSBOND   1 CYS A  156    CYS A  190                          1555   1555  2.08  
SSBOND   2 CYS A  157    CYS A  175                          1555   1555  2.04  
SSBOND   3 CYS B  156    CYS B  190                          1555   1555  2.06  
SSBOND   4 CYS B  157    CYS B  175                          1555   1555  2.04  
SSBOND   5 CYS H   60    CYS H  134                          1555   1555  2.02  
SSBOND   6 CYS H  197    CYS H  267                          1555   1555  2.04  
SSBOND   7 CYS I   60    CYS I  134                          1555   1555  1.98  
SSBOND   8 CYS I  197    CYS I  267                          1555   1555  2.07  
CISPEP   1 THR H  181    PRO H  182          0         1.35                     
CISPEP   2 PHE H  273    PRO H  274          0        -1.67                     
CISPEP   3 THR I  181    PRO I  182          0       -15.34                     
CISPEP   4 PHE I  273    PRO I  274          0        -2.56                     
CRYST1   73.351  100.502  116.666  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      0.013633  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009950  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008571        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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