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Database: PDB
Entry: 3OF6
LinkDB: 3OF6
Original site: 3OF6 
HEADER    IMMUNE SYSTEM                           13-AUG-10   3OF6              
TITLE     HUMAN PRE-T CELL RECEPTOR CRYSTAL STRUCTURE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: T CELL RECEPTOR BETA CHAIN;                                
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: ECTODOMAIN;                                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PRE T-CELL ANTIGEN RECEPTOR ALPHA;                         
COMPND   9 CHAIN: D, E, F;                                                      
COMPND  10 FRAGMENT: ECTODOMAIN, UNP RESIDUES 17-135;                           
COMPND  11 SYNONYM: PRE-T ALPHA CHAIN, PT-ALPHA, PTA, PT-ALPHA-TCR;             
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HIFIVE INSECT CELLS;                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PFASTBAC;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: HIFIVE INSECT CELLS;                    
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: PFASTBAC                                   
KEYWDS    IG FOLD, IMMUNE SYSTEM                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.PANG                                                              
REVDAT   3   29-JUL-20 3OF6    1       COMPND REMARK DBREF  SEQADV              
REVDAT   3 2                   1       HETNAM LINK   SITE                       
REVDAT   2   27-OCT-10 3OF6    1       JRNL                                     
REVDAT   1   20-OCT-10 3OF6    0                                                
JRNL        AUTH   S.S.PANG,R.BERRY,Z.CHEN,L.KJER-NIELSEN,M.A.PERUGINI,         
JRNL        AUTH 2 G.F.KING,C.WANG,S.H.CHEW,N.L.LA GRUTA,N.K.WILLIAMS,T.BEDDOE, 
JRNL        AUTH 3 T.TIGANIS,N.P.COWIESON,D.I.GODFREY,A.W.PURCELL,M.C.J.WILCE,  
JRNL        AUTH 4 J.MCCLUSKEY,J.ROSSJOHN                                       
JRNL        TITL   THE STRUCTURAL BASIS FOR AUTONOMOUS DIMERIZATION OF THE      
JRNL        TITL 2 PRE-T-CELL ANTIGEN RECEPTOR                                  
JRNL        REF    NATURE                        V. 467   844 2010              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   20944746                                                     
JRNL        DOI    10.1038/NATURE09448                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.4_4)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.37                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 35090                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.160                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1809                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.6701 -  6.5807    0.95     2722   152  0.1723 0.2282        
REMARK   3     2  6.5807 -  5.2253    0.95     2601   140  0.1747 0.2739        
REMARK   3     3  5.2253 -  4.5653    0.95     2593   140  0.1233 0.1994        
REMARK   3     4  4.5653 -  4.1482    0.95     2561   141  0.1374 0.2028        
REMARK   3     5  4.1482 -  3.8510    0.95     2551   141  0.1578 0.2545        
REMARK   3     6  3.8510 -  3.6240    0.95     2536   138  0.1776 0.2145        
REMARK   3     7  3.6240 -  3.4426    0.95     2537   140  0.1905 0.2002        
REMARK   3     8  3.4426 -  3.2927    0.95     2536   137  0.2054 0.3377        
REMARK   3     9  3.2927 -  3.1660    0.95     2529   138  0.2219 0.2906        
REMARK   3    10  3.1660 -  3.0568    0.95     2544   134  0.2255 0.2644        
REMARK   3    11  3.0568 -  2.9612    0.95     2489   132  0.2407 0.2521        
REMARK   3    12  2.9612 -  2.8766    0.95     2515   136  0.2528 0.3001        
REMARK   3    13  2.8766 -  2.8009    0.95     2531   140  0.2604 0.2847        
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              : 0.34                                          
REMARK   3   B_SOL              : 80.97                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.020           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 86.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.92590                                              
REMARK   3    B22 (A**2) : 4.92590                                              
REMARK   3    B33 (A**2) : -18.49470                                            
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: 0.5150                                                   
REMARK   3   OPERATOR: -K,H+K,L                                                 
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           8196                                  
REMARK   3   ANGLE     :  0.378          11205                                  
REMARK   3   CHIRALITY :  0.021           1226                                  
REMARK   3   PLANARITY :  0.003           1472                                  
REMARK   3   DIHEDRAL  : 10.375           2870                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3OF6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-AUG-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000061038.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-APR-09                          
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               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979461                           
REMARK 200  MONOCHROMATOR                  : SI VORTEX-ES                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35135                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1KGC; E CHAIN                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CACODYLATE, PH 7.0, 0.1M     
REMARK 280  CALCIUM ACETATE, 13-16% PEG 1500, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      122.06733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       61.03367            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       61.03367            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      122.06733            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -199.01610            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       61.03367            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, E, F                            
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     ALA A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     ALA A   246                                                      
REMARK 465     ASP A   247                                                      
REMARK 465     CYS A   248                                                      
REMARK 465     THR A   249                                                      
REMARK 465     SER A   250                                                      
REMARK 465     GLY A   251                                                      
REMARK 465     ASP A   252                                                      
REMARK 465     ASP A   253                                                      
REMARK 465     ASP A   254                                                      
REMARK 465     ASP A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     CYS B   248                                                      
REMARK 465     THR B   249                                                      
REMARK 465     SER B   250                                                      
REMARK 465     GLY B   251                                                      
REMARK 465     ASP B   252                                                      
REMARK 465     ASP B   253                                                      
REMARK 465     ASP B   254                                                      
REMARK 465     ASP B   255                                                      
REMARK 465     LYS B   256                                                      
REMARK 465     ALA C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     CYS C   248                                                      
REMARK 465     THR C   249                                                      
REMARK 465     SER C   250                                                      
REMARK 465     GLY C   251                                                      
REMARK 465     ASP C   252                                                      
REMARK 465     ASP C   253                                                      
REMARK 465     ASP C   254                                                      
REMARK 465     ASP C   255                                                      
REMARK 465     LYS C   256                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     ALA D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     MET D     0                                                      
REMARK 465     LEU D     1                                                      
REMARK 465     PRO D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     GLY D     4                                                      
REMARK 465     VAL D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     GLY D    96                                                      
REMARK 465     ALA D    97                                                      
REMARK 465     GLU D    98                                                      
REMARK 465     GLY D    99                                                      
REMARK 465     GLY D   111                                                      
REMARK 465     GLU D   112                                                      
REMARK 465     ALA D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     THR D   115                                                      
REMARK 465     ALA D   116                                                      
REMARK 465     ARG D   117                                                      
REMARK 465     THR D   118                                                      
REMARK 465     CYS D   119                                                      
REMARK 465     SER D   120                                                      
REMARK 465     GLY D   121                                                      
REMARK 465     ASP D   122                                                      
REMARK 465     ASP D   123                                                      
REMARK 465     ASP D   124                                                      
REMARK 465     ASP D   125                                                      
REMARK 465     LYS D   126                                                      
REMARK 465     GLY E    -3                                                      
REMARK 465     ALA E    -2                                                      
REMARK 465     HIS E    -1                                                      
REMARK 465     MET E     0                                                      
REMARK 465     LEU E     1                                                      
REMARK 465     PRO E     2                                                      
REMARK 465     THR E     3                                                      
REMARK 465     GLY E     4                                                      
REMARK 465     VAL E     5                                                      
REMARK 465     GLY E     6                                                      
REMARK 465     GLY E   111                                                      
REMARK 465     GLU E   112                                                      
REMARK 465     ALA E   113                                                      
REMARK 465     SER E   114                                                      
REMARK 465     THR E   115                                                      
REMARK 465     ALA E   116                                                      
REMARK 465     ARG E   117                                                      
REMARK 465     THR E   118                                                      
REMARK 465     CYS E   119                                                      
REMARK 465     SER E   120                                                      
REMARK 465     GLY E   121                                                      
REMARK 465     ASP E   122                                                      
REMARK 465     ASP E   123                                                      
REMARK 465     ASP E   124                                                      
REMARK 465     ASP E   125                                                      
REMARK 465     LYS E   126                                                      
REMARK 465     GLY F    -3                                                      
REMARK 465     ALA F    -2                                                      
REMARK 465     HIS F    -1                                                      
REMARK 465     MET F     0                                                      
REMARK 465     LEU F     1                                                      
REMARK 465     PRO F     2                                                      
REMARK 465     THR F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 465     VAL F     5                                                      
REMARK 465     GLY F     6                                                      
REMARK 465     GLY F     7                                                      
REMARK 465     GLY F   111                                                      
REMARK 465     GLU F   112                                                      
REMARK 465     ALA F   113                                                      
REMARK 465     SER F   114                                                      
REMARK 465     THR F   115                                                      
REMARK 465     ALA F   116                                                      
REMARK 465     ARG F   117                                                      
REMARK 465     THR F   118                                                      
REMARK 465     CYS F   119                                                      
REMARK 465     SER F   120                                                      
REMARK 465     GLY F   121                                                      
REMARK 465     ASP F   122                                                      
REMARK 465     ASP F   123                                                      
REMARK 465     ASP F   124                                                      
REMARK 465     ASP F   125                                                      
REMARK 465     LYS F   126                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET A   2    CG   SD   CE                                        
REMARK 470     ARG A  22    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  63    CG   OD1  OD2                                       
REMARK 470     GLU A  71    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  78    CG   CD   CE   NZ                                   
REMARK 470     GLN A  83    CG   CD   OE1  NE2                                  
REMARK 470     GLN A  98    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 121    CG   CD   CE   NZ                                   
REMARK 470     LYS A 167    CG   CD   CE   NZ                                   
REMARK 470     GLN A 178    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 187    CG   OD1  ND2                                       
REMARK 470     CYS A 192    SG                                                  
REMARK 470     GLU A 225    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  15    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  83    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 121    CG   CD   CE   NZ                                   
REMARK 470     GLU B 135    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 167    CG   CD   CE   NZ                                   
REMARK 470     CYS B 192    SG                                                  
REMARK 470     GLN B 228    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 229    CG   OD1  OD2                                       
REMARK 470     ASP B 247    CG   OD1  OD2                                       
REMARK 470     HIS C   1    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG C  15    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  52    CG   CD   OE1  OE2                                  
REMARK 470     LEU C  55    CG   CD1  CD2                                       
REMARK 470     ARG C  81    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 121    CG   CD   CE   NZ                                   
REMARK 470     GLU C 127    CG   CD   OE1  OE2                                  
REMARK 470     CYS C 192    SG                                                  
REMARK 470     ASP C 229    CG   OD1  OD2                                       
REMARK 470     LEU D  41    CG   CD1  CD2                                       
REMARK 470     ARG D 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS D 108    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER D 110    OG                                                  
REMARK 470     ARG E 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER E 110    OG                                                  
REMARK 470     GLU F  98    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN D    51     C2   NAG D  1000              1.91            
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    PRO A  25      170.51    -58.47                                   
REMARK 500    PRO A  43      109.96    -54.73                                   
REMARK 500    LEU A  46      -73.13   -126.76                                   
REMARK 500    ASN A  51       70.00     49.48                                   
REMARK 500    GLU A  52       18.13     56.57                                   
REMARK 500    PHE A  66      116.35   -164.96                                   
REMARK 500    GLU A  85        1.53    -69.64                                   
REMARK 500    SER A  87       91.10    -67.30                                   
REMARK 500    PRO A 155     -161.28    -79.47                                   
REMARK 500    ASP A 156       47.13    -82.96                                   
REMARK 500    ALA A 231     -166.59     48.49                                   
REMARK 500    LYS A 232      114.87   -160.84                                   
REMARK 500    PRO A 233       76.76    -66.67                                   
REMARK 500    THR A 235      105.00    -59.05                                   
REMARK 500    PRO B  25     -173.27    -60.19                                   
REMARK 500    LEU B  46      -75.18   -128.34                                   
REMARK 500    ASN B  51       88.69     54.80                                   
REMARK 500    PRO B  61      -71.19    -73.70                                   
REMARK 500    PRO B  70      -91.22    -50.80                                   
REMARK 500    ALA B  88     -173.85   -172.27                                   
REMARK 500    PRO B 155     -156.10    -82.71                                   
REMARK 500    HIS B 157       77.45   -112.97                                   
REMARK 500    GLN B 228       16.13   -143.48                                   
REMARK 500    THR B 235       90.16    -68.05                                   
REMARK 500    ALA B 242      106.69   -168.07                                   
REMARK 500    ALA B 246     -161.09    -75.97                                   
REMARK 500    PRO C  25     -177.96    -65.21                                   
REMARK 500    PRO C  43      106.22    -59.95                                   
REMARK 500    PRO C  61     -103.39    -59.57                                   
REMARK 500    ARG C  69       66.05   -169.52                                   
REMARK 500    PRO C  70      -70.75    -49.44                                   
REMARK 500    SER C  73      -81.49   -122.33                                   
REMARK 500    ARG C  81       76.67     50.52                                   
REMARK 500    HIS C 140      -72.28   -114.23                                   
REMARK 500    ASP C 156       46.54    -82.01                                   
REMARK 500    ALA C 231     -172.09    -64.72                                   
REMARK 500    PRO C 233       85.00    -62.73                                   
REMARK 500    THR C 235       99.75    -59.20                                   
REMARK 500    VAL D  21      -74.29   -116.46                                   
REMARK 500    ALA D  37      170.14    -59.22                                   
REMARK 500    LEU D  41     -131.35    -87.33                                   
REMARK 500    ASP D  42     -177.24   -175.99                                   
REMARK 500    ALA D  49     -158.83   -100.65                                   
REMARK 500    SER D  85      -31.62   -133.06                                   
REMARK 500    VAL E  21      -82.42   -123.49                                   
REMARK 500    ASP E  22       62.03   -119.17                                   
REMARK 500    PRO E  39     -179.53    -46.87                                   
REMARK 500    PRO E  44      152.58    -46.69                                   
REMARK 500    THR E  69     -164.56    -78.29                                   
REMARK 500    VAL F  21      -93.21    -96.32                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KGC   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE NUMBERING OF THE PROTEIN IS BASED THAT OF A T CELL RECEPTOR AND  
REMARK 999 THERE IS A GAP IN THE NUMBERING IN THE CDR3 LOOP REGION (101-104).   
REMARK 999 FOR CHAINS A,B,C, THE UNICODE IS DEFINE AS P01850. THE N-TERMINAL    
REMARK 999 HALF OF THE PROTEIN (RESIDUE 3-117) IS A VARIABLE REGION OF A T      
REMARK 999 CELL RECEPTOR. THE FIRST FOUR RESIDUES AGSH AND LAST 9 RESIDUES      
REMARK 999 CTSGDDDDK ARE EXPRESSION TAG REGIONS.                                
DBREF  3OF6 A   -2   256  PDB    3OF6     3OF6            -2    256             
DBREF  3OF6 B   -2   256  PDB    3OF6     3OF6            -2    256             
DBREF  3OF6 C   -2   256  PDB    3OF6     3OF6            -2    256             
DBREF  3OF6 D    1   119  UNP    Q6ISU1   PTCRA_HUMAN     17    135             
DBREF  3OF6 E    1   119  UNP    Q6ISU1   PTCRA_HUMAN     17    135             
DBREF  3OF6 F    1   119  UNP    Q6ISU1   PTCRA_HUMAN     17    135             
SEQADV 3OF6 GLY D   -3  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ALA D   -2  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 HIS D   -1  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 MET D    0  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 SER D  120  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 GLY D  121  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP D  122  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP D  123  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP D  124  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP D  125  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 LYS D  126  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 GLY E   -3  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ALA E   -2  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 HIS E   -1  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 MET E    0  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 SER E  120  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 GLY E  121  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP E  122  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP E  123  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP E  124  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP E  125  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 LYS E  126  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 GLY F   -3  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ALA F   -2  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 HIS F   -1  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 MET F    0  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 SER F  120  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 GLY F  121  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP F  122  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP F  123  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP F  124  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 ASP F  125  UNP  Q6ISU1              EXPRESSION TAG                 
SEQADV 3OF6 LYS F  126  UNP  Q6ISU1              EXPRESSION TAG                 
SEQRES   1 A  255  ALA GLY SER HIS MET GLY VAL SER GLN SER PRO ARG TYR          
SEQRES   2 A  255  LYS VAL ALA LYS ARG GLY GLN ASP VAL ALA LEU ARG CYS          
SEQRES   3 A  255  ASP PRO ILE SER GLY HIS VAL SER LEU PHE TRP TYR GLN          
SEQRES   4 A  255  GLN ALA LEU GLY GLN GLY PRO GLU PHE LEU THR TYR PHE          
SEQRES   5 A  255  GLN ASN GLU ALA GLN LEU ASP LYS SER GLY LEU PRO SER          
SEQRES   6 A  255  ASP ARG PHE PHE ALA GLU ARG PRO GLU GLY SER VAL SER          
SEQRES   7 A  255  THR LEU LYS ILE GLN ARG THR GLN GLN GLU ASP SER ALA          
SEQRES   8 A  255  VAL TYR LEU CYS ALA SER SER LEU GLY GLN ALA TYR GLU          
SEQRES   9 A  255  GLN TYR PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU          
SEQRES  10 A  255  ASP LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE          
SEQRES  11 A  255  GLU PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA          
SEQRES  12 A  255  THR LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS          
SEQRES  13 A  255  VAL GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS          
SEQRES  14 A  255  SER GLY VAL SER THR ASP PRO GLN PRO LEU LYS GLU GLN          
SEQRES  15 A  255  PRO ALA LEU ASN ASP SER ARG TYR CYS LEU SER SER ARG          
SEQRES  16 A  255  LEU ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN          
SEQRES  17 A  255  HIS PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU          
SEQRES  18 A  255  ASN ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR          
SEQRES  19 A  255  GLN ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP CYS          
SEQRES  20 A  255  THR SER GLY ASP ASP ASP ASP LYS                              
SEQRES   1 B  255  ALA GLY SER HIS MET GLY VAL SER GLN SER PRO ARG TYR          
SEQRES   2 B  255  LYS VAL ALA LYS ARG GLY GLN ASP VAL ALA LEU ARG CYS          
SEQRES   3 B  255  ASP PRO ILE SER GLY HIS VAL SER LEU PHE TRP TYR GLN          
SEQRES   4 B  255  GLN ALA LEU GLY GLN GLY PRO GLU PHE LEU THR TYR PHE          
SEQRES   5 B  255  GLN ASN GLU ALA GLN LEU ASP LYS SER GLY LEU PRO SER          
SEQRES   6 B  255  ASP ARG PHE PHE ALA GLU ARG PRO GLU GLY SER VAL SER          
SEQRES   7 B  255  THR LEU LYS ILE GLN ARG THR GLN GLN GLU ASP SER ALA          
SEQRES   8 B  255  VAL TYR LEU CYS ALA SER SER LEU GLY GLN ALA TYR GLU          
SEQRES   9 B  255  GLN TYR PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU          
SEQRES  10 B  255  ASP LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE          
SEQRES  11 B  255  GLU PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA          
SEQRES  12 B  255  THR LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS          
SEQRES  13 B  255  VAL GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS          
SEQRES  14 B  255  SER GLY VAL SER THR ASP PRO GLN PRO LEU LYS GLU GLN          
SEQRES  15 B  255  PRO ALA LEU ASN ASP SER ARG TYR CYS LEU SER SER ARG          
SEQRES  16 B  255  LEU ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN          
SEQRES  17 B  255  HIS PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU          
SEQRES  18 B  255  ASN ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR          
SEQRES  19 B  255  GLN ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP CYS          
SEQRES  20 B  255  THR SER GLY ASP ASP ASP ASP LYS                              
SEQRES   1 C  255  ALA GLY SER HIS MET GLY VAL SER GLN SER PRO ARG TYR          
SEQRES   2 C  255  LYS VAL ALA LYS ARG GLY GLN ASP VAL ALA LEU ARG CYS          
SEQRES   3 C  255  ASP PRO ILE SER GLY HIS VAL SER LEU PHE TRP TYR GLN          
SEQRES   4 C  255  GLN ALA LEU GLY GLN GLY PRO GLU PHE LEU THR TYR PHE          
SEQRES   5 C  255  GLN ASN GLU ALA GLN LEU ASP LYS SER GLY LEU PRO SER          
SEQRES   6 C  255  ASP ARG PHE PHE ALA GLU ARG PRO GLU GLY SER VAL SER          
SEQRES   7 C  255  THR LEU LYS ILE GLN ARG THR GLN GLN GLU ASP SER ALA          
SEQRES   8 C  255  VAL TYR LEU CYS ALA SER SER LEU GLY GLN ALA TYR GLU          
SEQRES   9 C  255  GLN TYR PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU          
SEQRES  10 C  255  ASP LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE          
SEQRES  11 C  255  GLU PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA          
SEQRES  12 C  255  THR LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS          
SEQRES  13 C  255  VAL GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS          
SEQRES  14 C  255  SER GLY VAL SER THR ASP PRO GLN PRO LEU LYS GLU GLN          
SEQRES  15 C  255  PRO ALA LEU ASN ASP SER ARG TYR CYS LEU SER SER ARG          
SEQRES  16 C  255  LEU ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN          
SEQRES  17 C  255  HIS PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU          
SEQRES  18 C  255  ASN ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR          
SEQRES  19 C  255  GLN ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP CYS          
SEQRES  20 C  255  THR SER GLY ASP ASP ASP ASP LYS                              
SEQRES   1 D  130  GLY ALA HIS MET LEU PRO THR GLY VAL GLY GLY THR PRO          
SEQRES   2 D  130  PHE PRO SER LEU ALA PRO PRO ILE MET LEU LEU VAL ASP          
SEQRES   3 D  130  GLY LYS GLN GLN MET VAL VAL VAL CYS LEU VAL LEU ASP          
SEQRES   4 D  130  VAL ALA PRO PRO GLY LEU ASP SER PRO ILE TRP PHE SER          
SEQRES   5 D  130  ALA GLY ASN GLY SER ALA LEU ASP ALA PHE THR TYR GLY          
SEQRES   6 D  130  PRO SER PRO ALA THR ASP GLY THR TRP THR ASN LEU ALA          
SEQRES   7 D  130  HIS LEU SER LEU PRO SER GLU GLU LEU ALA SER TRP GLU          
SEQRES   8 D  130  PRO LEU VAL CYS HIS THR GLY PRO GLY ALA GLU GLY HIS          
SEQRES   9 D  130  SER ARG SER THR GLN PRO MET HIS LEU SER GLY GLU ALA          
SEQRES  10 D  130  SER THR ALA ARG THR CYS SER GLY ASP ASP ASP ASP LYS          
SEQRES   1 E  130  GLY ALA HIS MET LEU PRO THR GLY VAL GLY GLY THR PRO          
SEQRES   2 E  130  PHE PRO SER LEU ALA PRO PRO ILE MET LEU LEU VAL ASP          
SEQRES   3 E  130  GLY LYS GLN GLN MET VAL VAL VAL CYS LEU VAL LEU ASP          
SEQRES   4 E  130  VAL ALA PRO PRO GLY LEU ASP SER PRO ILE TRP PHE SER          
SEQRES   5 E  130  ALA GLY ASN GLY SER ALA LEU ASP ALA PHE THR TYR GLY          
SEQRES   6 E  130  PRO SER PRO ALA THR ASP GLY THR TRP THR ASN LEU ALA          
SEQRES   7 E  130  HIS LEU SER LEU PRO SER GLU GLU LEU ALA SER TRP GLU          
SEQRES   8 E  130  PRO LEU VAL CYS HIS THR GLY PRO GLY ALA GLU GLY HIS          
SEQRES   9 E  130  SER ARG SER THR GLN PRO MET HIS LEU SER GLY GLU ALA          
SEQRES  10 E  130  SER THR ALA ARG THR CYS SER GLY ASP ASP ASP ASP LYS          
SEQRES   1 F  130  GLY ALA HIS MET LEU PRO THR GLY VAL GLY GLY THR PRO          
SEQRES   2 F  130  PHE PRO SER LEU ALA PRO PRO ILE MET LEU LEU VAL ASP          
SEQRES   3 F  130  GLY LYS GLN GLN MET VAL VAL VAL CYS LEU VAL LEU ASP          
SEQRES   4 F  130  VAL ALA PRO PRO GLY LEU ASP SER PRO ILE TRP PHE SER          
SEQRES   5 F  130  ALA GLY ASN GLY SER ALA LEU ASP ALA PHE THR TYR GLY          
SEQRES   6 F  130  PRO SER PRO ALA THR ASP GLY THR TRP THR ASN LEU ALA          
SEQRES   7 F  130  HIS LEU SER LEU PRO SER GLU GLU LEU ALA SER TRP GLU          
SEQRES   8 F  130  PRO LEU VAL CYS HIS THR GLY PRO GLY ALA GLU GLY HIS          
SEQRES   9 F  130  SER ARG SER THR GLN PRO MET HIS LEU SER GLY GLU ALA          
SEQRES  10 F  130  SER THR ALA ARG THR CYS SER GLY ASP ASP ASP ASP LYS          
MODRES 3OF6 ASN F   51  ASN  GLYCOSYLATION SITE                                 
MODRES 3OF6 ASN E   51  ASN  GLYCOSYLATION SITE                                 
MODRES 3OF6 ASN C  187  ASN  GLYCOSYLATION SITE                                 
MODRES 3OF6 ASN D   51  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C1000      14                                                       
HET    NAG  D1000      14                                                       
HET    NAG  E1000      14                                                       
HET    NAG  F1000      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   7  NAG    4(C8 H15 N O6)                                               
FORMUL  11  HOH   *109(H2 O)                                                    
HELIX    1   1 GLN A   83  SER A   87  5                                   5    
HELIX    2   2 ASP A  119  VAL A  123  5                                   5    
HELIX    3   3 SER A  134  GLN A  142  1                                   9    
HELIX    4   4 ALA A  201  GLN A  205  1                                   5    
HELIX    5   5 GLN B   83  SER B   87  5                                   5    
HELIX    6   6 ASP B  119  VAL B  123  5                                   5    
HELIX    7   7 SER B  134  GLN B  142  1                                   9    
HELIX    8   8 ALA B  201  GLN B  205  1                                   5    
HELIX    9   9 GLN C   83  SER C   87  5                                   5    
HELIX   10  10 ASP C  119  VAL C  123  5                                   5    
HELIX   11  11 SER C  134  SER C  139  1                                   6    
HELIX   12  12 ALA C  201  GLN C  205  1                                   5    
HELIX   13  13 GLU D   81  SER D   85  5                                   5    
HELIX   14  14 LEU E   83  GLU E   87  5                                   5    
HELIX   15  15 GLU F   82  TRP F   86  5                                   5    
SHEET    1   A 4 SER A   5  SER A   7  0                                        
SHEET    2   A 4 VAL A  19  ASP A  24 -1  O  ASP A  24   N  SER A   5           
SHEET    3   A 4 SER A  75  ILE A  79 -1  O  LEU A  77   N  LEU A  21           
SHEET    4   A 4 PHE A  65  GLU A  68 -1  N  PHE A  66   O  LYS A  78           
SHEET    1   B 6 TYR A  10  LYS A  14  0                                        
SHEET    2   B 6 THR A 112  THR A 117  1  O  ARG A 113   N  LYS A  11           
SHEET    3   B 6 VAL A  89  SER A  95 -1  N  TYR A  90   O  THR A 112           
SHEET    4   B 6 SER A  31  GLN A  37 -1  N  PHE A  33   O  ALA A  93           
SHEET    5   B 6 GLU A  44  GLN A  50 -1  O  PHE A  49   N  LEU A  32           
SHEET    6   B 6 GLN A  54  ASP A  56 -1  O  ASP A  56   N  TYR A  48           
SHEET    1   C 4 TYR A  10  LYS A  14  0                                        
SHEET    2   C 4 THR A 112  THR A 117  1  O  ARG A 113   N  LYS A  11           
SHEET    3   C 4 VAL A  89  SER A  95 -1  N  TYR A  90   O  THR A 112           
SHEET    4   C 4 TYR A 107  PHE A 108 -1  O  TYR A 107   N  SER A  94           
SHEET    1   D 4 GLU A 127  PHE A 131  0                                        
SHEET    2   D 4 LYS A 143  PHE A 153 -1  O  VAL A 147   N  PHE A 131           
SHEET    3   D 4 TYR A 191  SER A 200 -1  O  VAL A 199   N  ALA A 144           
SHEET    4   D 4 VAL A 173  THR A 175 -1  N  SER A 174   O  ARG A 196           
SHEET    1   E 4 GLU A 127  PHE A 131  0                                        
SHEET    2   E 4 LYS A 143  PHE A 153 -1  O  VAL A 147   N  PHE A 131           
SHEET    3   E 4 TYR A 191  SER A 200 -1  O  VAL A 199   N  ALA A 144           
SHEET    4   E 4 LEU A 180  LYS A 181 -1  N  LEU A 180   O  CYS A 192           
SHEET    1   F 4 LYS A 167  VAL A 169  0                                        
SHEET    2   F 4 VAL A 158  VAL A 164 -1  N  TRP A 162   O  VAL A 169           
SHEET    3   F 4 HIS A 210  PHE A 217 -1  O  GLN A 214   N  SER A 161           
SHEET    4   F 4 GLN A 236  TRP A 243 -1  O  ALA A 240   N  CYS A 213           
SHEET    1   G 4 SER B   5  SER B   7  0                                        
SHEET    2   G 4 VAL B  19  ASP B  24 -1  O  ASP B  24   N  SER B   5           
SHEET    3   G 4 SER B  75  ILE B  79 -1  O  LEU B  77   N  LEU B  21           
SHEET    4   G 4 PHE B  65  GLU B  68 -1  N  PHE B  66   O  LYS B  78           
SHEET    1   H 6 TYR B  10  LYS B  11  0                                        
SHEET    2   H 6 THR B 112  LEU B 114  1  O  ARG B 113   N  LYS B  11           
SHEET    3   H 6 ALA B  88  LEU B  91 -1  N  ALA B  88   O  LEU B 114           
SHEET    4   H 6 SER B  31  GLN B  37 -1  N  TYR B  35   O  LEU B  91           
SHEET    5   H 6 GLU B  44  GLN B  50 -1  O  PHE B  49   N  LEU B  32           
SHEET    6   H 6 GLN B  54  ASP B  56 -1  O  LEU B  55   N  TYR B  48           
SHEET    1   I 4 GLU B 127  PHE B 131  0                                        
SHEET    2   I 4 LYS B 143  PHE B 153 -1  O  THR B 151   N  GLU B 127           
SHEET    3   I 4 TYR B 191  SER B 200 -1  O  VAL B 199   N  ALA B 144           
SHEET    4   I 4 VAL B 173  THR B 175 -1  N  SER B 174   O  ARG B 196           
SHEET    1   J 4 GLU B 127  PHE B 131  0                                        
SHEET    2   J 4 LYS B 143  PHE B 153 -1  O  THR B 151   N  GLU B 127           
SHEET    3   J 4 TYR B 191  SER B 200 -1  O  VAL B 199   N  ALA B 144           
SHEET    4   J 4 LEU B 180  LYS B 181 -1  N  LEU B 180   O  CYS B 192           
SHEET    1   K 4 LYS B 167  VAL B 169  0                                        
SHEET    2   K 4 VAL B 158  VAL B 164 -1  N  VAL B 164   O  LYS B 167           
SHEET    3   K 4 PHE B 211  PHE B 217 -1  O  GLN B 214   N  SER B 161           
SHEET    4   K 4 ILE B 237  GLU B 241 -1  O  ALA B 240   N  CYS B 213           
SHEET    1   L 4 SER C   5  SER C   7  0                                        
SHEET    2   L 4 VAL C  19  ASP C  24 -1  O  ASP C  24   N  SER C   5           
SHEET    3   L 4 SER C  75  ILE C  79 -1  O  LEU C  77   N  LEU C  21           
SHEET    4   L 4 PHE C  65  GLU C  68 -1  N  GLU C  68   O  THR C  76           
SHEET    1   M 5 TYR C  10  LYS C  14  0                                        
SHEET    2   M 5 THR C 112  THR C 117  1  O  ARG C 113   N  LYS C  11           
SHEET    3   M 5 VAL C  89  SER C  95 -1  N  TYR C  90   O  THR C 112           
SHEET    4   M 5 SER C  31  GLN C  37 -1  N  GLN C  37   O  VAL C  89           
SHEET    5   M 5 GLU C  44  GLN C  50 -1  O  GLU C  44   N  GLN C  36           
SHEET    1   N 4 TYR C  10  LYS C  14  0                                        
SHEET    2   N 4 THR C 112  THR C 117  1  O  ARG C 113   N  LYS C  11           
SHEET    3   N 4 VAL C  89  SER C  95 -1  N  TYR C  90   O  THR C 112           
SHEET    4   N 4 TYR C 107  PHE C 108 -1  O  TYR C 107   N  SER C  94           
SHEET    1   O 4 GLU C 127  PHE C 131  0                                        
SHEET    2   O 4 LYS C 143  PHE C 153 -1  O  VAL C 147   N  PHE C 131           
SHEET    3   O 4 TYR C 191  SER C 200 -1  O  VAL C 199   N  ALA C 144           
SHEET    4   O 4 VAL C 173  THR C 175 -1  N  SER C 174   O  ARG C 196           
SHEET    1   P 4 GLU C 127  PHE C 131  0                                        
SHEET    2   P 4 LYS C 143  PHE C 153 -1  O  VAL C 147   N  PHE C 131           
SHEET    3   P 4 TYR C 191  SER C 200 -1  O  VAL C 199   N  ALA C 144           
SHEET    4   P 4 LEU C 180  LYS C 181 -1  N  LEU C 180   O  CYS C 192           
SHEET    1   Q 4 LYS C 167  GLU C 168  0                                        
SHEET    2   Q 4 VAL C 158  VAL C 164 -1  N  VAL C 164   O  LYS C 167           
SHEET    3   Q 4 HIS C 210  PHE C 217 -1  O  GLN C 214   N  SER C 161           
SHEET    4   Q 4 ILE C 237  TRP C 243 -1  O  ALA C 240   N  CYS C 213           
SHEET    1   R 4 ILE D  17  LEU D  20  0                                        
SHEET    2   R 4 GLN D  25  VAL D  36 -1  O  GLN D  26   N  LEU D  19           
SHEET    3   R 4 THR D  69  PRO D  79 -1  O  LEU D  76   N  VAL D  29           
SHEET    4   R 4 PHE D  58  THR D  59 -1  N  PHE D  58   O  HIS D  75           
SHEET    1   S 4 ILE D  17  LEU D  20  0                                        
SHEET    2   S 4 GLN D  25  VAL D  36 -1  O  GLN D  26   N  LEU D  19           
SHEET    3   S 4 THR D  69  PRO D  79 -1  O  LEU D  76   N  VAL D  29           
SHEET    4   S 4 SER D  63  ALA D  65 -1  N  ALA D  65   O  THR D  69           
SHEET    1   T 4 ALA D  54  LEU D  55  0                                        
SHEET    2   T 4 TRP D  46  SER D  48 -1  N  PHE D  47   O  LEU D  55           
SHEET    3   T 4 VAL D  90  THR D  93 -1  O  VAL D  90   N  SER D  48           
SHEET    4   T 4 ARG D 102  SER D 103 -1  O  ARG D 102   N  THR D  93           
SHEET    1   U 4 ILE E  17  LEU E  20  0                                        
SHEET    2   U 4 GLN E  25  VAL E  36 -1  O  GLN E  26   N  LEU E  19           
SHEET    3   U 4 TRP E  70  PRO E  79 -1  O  LEU E  78   N  MET E  27           
SHEET    4   U 4 PHE E  58  THR E  59 -1  N  PHE E  58   O  HIS E  75           
SHEET    1   V 4 ILE E  17  LEU E  20  0                                        
SHEET    2   V 4 GLN E  25  VAL E  36 -1  O  GLN E  26   N  LEU E  19           
SHEET    3   V 4 TRP E  70  PRO E  79 -1  O  LEU E  78   N  MET E  27           
SHEET    4   V 4 SER E  63  PRO E  64 -1  N  SER E  63   O  THR E  71           
SHEET    1   W 4 ALA E  54  LEU E  55  0                                        
SHEET    2   W 4 TRP E  46  ALA E  49 -1  N  PHE E  47   O  LEU E  55           
SHEET    3   W 4 LEU E  89  THR E  93 -1  O  VAL E  90   N  SER E  48           
SHEET    4   W 4 ARG E 102  SER E 103 -1  O  ARG E 102   N  THR E  93           
SHEET    1   X 4 LEU F  13  LEU F  20  0                                        
SHEET    2   X 4 GLN F  25  VAL F  36 -1  O  GLN F  26   N  LEU F  19           
SHEET    3   X 4 TRP F  70  PRO F  79 -1  O  LEU F  78   N  MET F  27           
SHEET    4   X 4 PHE F  58  THR F  59 -1  N  PHE F  58   O  HIS F  75           
SHEET    1   Y 4 LEU F  13  LEU F  20  0                                        
SHEET    2   Y 4 GLN F  25  VAL F  36 -1  O  GLN F  26   N  LEU F  19           
SHEET    3   Y 4 TRP F  70  PRO F  79 -1  O  LEU F  78   N  MET F  27           
SHEET    4   Y 4 SER F  63  PRO F  64 -1  N  SER F  63   O  THR F  71           
SHEET    1   Z 4 ALA F  54  LEU F  55  0                                        
SHEET    2   Z 4 TRP F  46  SER F  48 -1  N  PHE F  47   O  LEU F  55           
SHEET    3   Z 4 VAL F  90  THR F  93 -1  O  VAL F  90   N  SER F  48           
SHEET    4   Z 4 ARG F 102  SER F 103 -1  O  ARG F 102   N  THR F  93           
SSBOND   1 CYS A   23    CYS A   92                          1555   1555  2.03  
SSBOND   2 CYS A  148    CYS A  213                          1555   1555  2.03  
SSBOND   3 CYS B   23    CYS B   92                          1555   1555  2.03  
SSBOND   4 CYS B  148    CYS B  213                          1555   1555  2.03  
SSBOND   5 CYS C   23    CYS C   92                          1555   1555  2.03  
SSBOND   6 CYS C  148    CYS C  213                          1555   1555  2.03  
SSBOND   7 CYS D   31    CYS D   91                          1555   1555  2.03  
SSBOND   8 CYS E   31    CYS E   91                          1555   1555  2.03  
SSBOND   9 CYS F   31    CYS F   91                          1555   1555  2.03  
LINK         ND2 ASN C 187                 C1  NAG C1000     1555   1555  1.44  
LINK         ND2 ASN D  51                 C1  NAG D1000     1555   1555  1.44  
LINK         ND2 ASN E  51                 C1  NAG E1000     1555   1555  1.44  
LINK         ND2 ASN F  51                 C1  NAG F1000     1555   1555  1.44  
CISPEP   1 MET A    2    GLY A    3          0         0.05                     
CISPEP   2 SER A    7    PRO A    8          0        -2.10                     
CISPEP   3 TYR A  154    PRO A  155          0        -1.67                     
CISPEP   4 GLY B    3    VAL B    4          0         0.44                     
CISPEP   5 SER B    7    PRO B    8          0        -2.59                     
CISPEP   6 TYR B  154    PRO B  155          0        -2.35                     
CISPEP   7 SER C    7    PRO C    8          0        -2.65                     
CISPEP   8 TYR C  154    PRO C  155          0        -2.73                     
CISPEP   9 GLU D   87    PRO D   88          0        -3.78                     
CISPEP  10 GLY D   94    PRO D   95          0        -0.05                     
CISPEP  11 PRO E   39    GLY E   40          0         5.66                     
CISPEP  12 GLU E   87    PRO E   88          0        -2.98                     
CISPEP  13 GLY E   94    PRO E   95          0        -0.45                     
CISPEP  14 LEU E  109    SER E  110          0         0.03                     
CISPEP  15 PRO F   39    GLY F   40          0        -2.21                     
CISPEP  16 GLU F   87    PRO F   88          0        -3.39                     
CISPEP  17 GLY F   94    PRO F   95          0        -1.84                     
CRYST1  114.902  114.902  183.101  90.00  90.00 120.00 P 32 2 1     18          
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      0.008703  0.005025  0.000000        0.00000                         
SCALE2      0.000000  0.010049  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005461        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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