GenomeNet

Database: PDB
Entry: 3KG5
LinkDB: 3KG5
Original site: 3KG5 
HEADER    PROTEIN BINDING                         28-OCT-09   3KG5              
TITLE     CRYSTAL STRUCTURE OF HUMAN IG-BETA HOMODIMER                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: B-CELL ANTIGEN RECEPTOR COMPLEX-ASSOCIATED PROTEIN BETA    
COMPND   3 CHAIN;                                                               
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND   6 SYNONYM: IG-BETA, B-CELL-SPECIFIC GLYCOPROTEIN B29, IMMUNOGLOBULIN-  
COMPND   7 ASSOCIATED B29 PROTEIN;                                              
COMPND   8 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: B29, CD79B, IGB;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CD79B, IG-BETA, BCR, IMMUNOGLOBULIN DOMAIN, PROTEIN BINDING           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.RADAEV,P.D.SUN                                                      
REVDAT   1   25-AUG-10 3KG5    0                                                
JRNL        AUTH   S.RADAEV,Z.ZOU,P.TOLAR,K.NGUYEN,A.NGUYEN,P.D.KRUEGER,        
JRNL        AUTH 2 N.STUTZMAN,S.PIERCE,P.D.SUN                                  
JRNL        TITL   STRUCTURAL AND FUNCTIONAL STUDIES OF IGALPHABETA AND ITS     
JRNL        TITL 2 ASSEMBLY WITH THE B CELL ANTIGEN RECEPTOR.                   
JRNL        REF    STRUCTURE                     V.  18   934 2010              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   20696394                                                     
JRNL        DOI    10.1016/J.STR.2010.04.019                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 6407                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 358                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.31                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2070                       
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1676                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 2                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 75.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3KG5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055950.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6616                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 27.600                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 55.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 28.70                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.33900                            
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6M NA FORMATE, 100MM NA ACETATE, PH    
REMARK 280  4.0, VAPOR DIFFUSION, TEMPERATURE 298K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2                         
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       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4                                      
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4                                    
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4                                      
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4                                      
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4                                      
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4                                      
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4                                    
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4                                      
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4                                      
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4                                      
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4                                      
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4                                    
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       64.90000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.90000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       64.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.90000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       64.90000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       64.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       64.90000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       64.90000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       64.90000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       64.90000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       64.90000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       64.90000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       64.90000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       64.90000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       64.90000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       64.90000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       64.90000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       64.90000            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000       97.35000            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       32.45000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       32.45000            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000       97.35000            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000       97.35000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       97.35000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       32.45000            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       32.45000            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       97.35000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       32.45000            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000       97.35000            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       32.45000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000       97.35000            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       32.45000            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       32.45000            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       32.45000            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000       97.35000            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       32.45000            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000       97.35000            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000       97.35000            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000       97.35000            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       32.45000            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       32.45000            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000       97.35000            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000       97.35000            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       32.45000            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       32.45000            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       32.45000            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       32.45000            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000       97.35000            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       32.45000            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000       97.35000            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       32.45000            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000       97.35000            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000       97.35000            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000       97.35000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     ARG A    30                                                      
REMARK 465     SER A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     ASP A    33                                                      
REMARK 465     ARG A    34                                                      
REMARK 465     TYR A    35                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     ASN A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     LYS A    39                                                      
REMARK 465     GLY A    40                                                      
REMARK 465     SER A    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     SER A   146                                                      
REMARK 465     THR A   147                                                      
REMARK 465     LEU A   148                                                      
REMARK 465     ALA A   149                                                      
REMARK 465     GLN A   150                                                      
REMARK 465     LEU A   151                                                      
REMARK 465     LYS A   152                                                      
REMARK 465     GLN A   153                                                      
REMARK 465     ARG A   154                                                      
REMARK 465     ASN A   155                                                      
REMARK 465     THR A   156                                                      
REMARK 465     LEU A   157                                                      
REMARK 465     LYS A   158                                                      
REMARK 465     ASP A   159                                                      
REMARK 465     VAL B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     ALA B    29                                                      
REMARK 465     ARG B    30                                                      
REMARK 465     SER B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     ASP B    33                                                      
REMARK 465     ARG B    34                                                      
REMARK 465     TYR B    35                                                      
REMARK 465     ARG B    36                                                      
REMARK 465     ASN B    37                                                      
REMARK 465     PRO B    38                                                      
REMARK 465     LYS B    39                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     SER B    41                                                      
REMARK 465     ALA B    42                                                      
REMARK 465     SER B   146                                                      
REMARK 465     THR B   147                                                      
REMARK 465     LEU B   148                                                      
REMARK 465     ALA B   149                                                      
REMARK 465     GLN B   150                                                      
REMARK 465     LEU B   151                                                      
REMARK 465     LYS B   152                                                      
REMARK 465     GLN B   153                                                      
REMARK 465     ARG B   154                                                      
REMARK 465     ASN B   155                                                      
REMARK 465     THR B   156                                                      
REMARK 465     LEU B   157                                                      
REMARK 465     LYS B   158                                                      
REMARK 465     ASP B   159                                                      
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    CYS B  43   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES          
REMARK 500    CYS B  65   CA  -  CB  -  SG  ANGL. DEV. =   7.6 DEGREES          
REMARK 500    CYS B 126   CA  -  CB  -  SG  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    GLY B 144   N   -  CA  -  C   ANGL. DEV. =  19.7 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    MET A  67     -146.46   -139.62                                   
REMARK 500    SER A  71       19.13     53.96                                   
REMARK 500    ASN A  73       93.53     37.14                                   
REMARK 500    GLU A  84      179.54    -53.75                                   
REMARK 500    PRO A  86       87.75    -48.28                                   
REMARK 500    LYS A  93      138.98    -27.23                                   
REMARK 500    ARG A  95       -0.26   -173.60                                   
REMARK 500    GLN A 100      167.50    176.40                                   
REMARK 500    ASN A 101     -157.21   -153.55                                   
REMARK 500    ASN A 117      135.07    -35.98                                   
REMARK 500    ASN A 127      -90.49    -52.37                                   
REMARK 500    ASN A 128      -77.45    -44.38                                   
REMARK 500    ARG B  57      124.35    -28.37                                   
REMARK 500    PHE B  59     -142.21    -87.28                                   
REMARK 500    MET B  67     -154.90   -167.62                                   
REMARK 500    ASN B  73       99.52     55.01                                   
REMARK 500    GLU B  84      152.64    -45.10                                   
REMARK 500    PRO B  86      144.07    -36.03                                   
REMARK 500    GLN B  88      128.29    -39.12                                   
REMARK 500    GLU B  92      122.47    -38.12                                   
REMARK 500    ARG B  95      -29.12   -148.45                                   
REMARK 500    GLN B 100      126.17    179.52                                   
REMARK 500    ASN B 101     -152.62   -108.80                                   
REMARK 500    ILE B 112      119.60    -23.69                                   
REMARK 500    GLU B 115       -2.03    -59.11                                   
REMARK 500    ASN B 127      -70.90    -67.70                                   
REMARK 500    ASN B 128      -82.08    -60.97                                   
REMARK 500    THR B 129      -16.26    -49.10                                   
REMARK 500    MET B 143     -179.53   -174.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3KG5 A   26   159  UNP    P40259   CD79B_HUMAN     26    159             
DBREF  3KG5 B   26   159  UNP    P40259   CD79B_HUMAN     26    159             
SEQRES   1 A  134  VAL PRO ALA ALA ARG SER GLU ASP ARG TYR ARG ASN PRO          
SEQRES   2 A  134  LYS GLY SER ALA CYS SER ARG ILE TRP GLN SER PRO ARG          
SEQRES   3 A  134  PHE ILE ALA ARG LYS ARG GLY PHE THR VAL LYS MET HIS          
SEQRES   4 A  134  CYS TYR MET ASN SER ALA SER GLY ASN VAL SER TRP LEU          
SEQRES   5 A  134  TRP LYS GLN GLU MET ASP GLU ASN PRO GLN GLN LEU LYS          
SEQRES   6 A  134  LEU GLU LYS GLY ARG MET GLU GLU SER GLN ASN GLU SER          
SEQRES   7 A  134  LEU ALA THR LEU THR ILE GLN GLY ILE ARG PHE GLU ASP          
SEQRES   8 A  134  ASN GLY ILE TYR PHE CYS GLN GLN LYS CYS ASN ASN THR          
SEQRES   9 A  134  SER GLU VAL TYR GLN GLY CYS GLY THR GLU LEU ARG VAL          
SEQRES  10 A  134  MET GLY PHE SER THR LEU ALA GLN LEU LYS GLN ARG ASN          
SEQRES  11 A  134  THR LEU LYS ASP                                              
SEQRES   1 B  134  VAL PRO ALA ALA ARG SER GLU ASP ARG TYR ARG ASN PRO          
SEQRES   2 B  134  LYS GLY SER ALA CYS SER ARG ILE TRP GLN SER PRO ARG          
SEQRES   3 B  134  PHE ILE ALA ARG LYS ARG GLY PHE THR VAL LYS MET HIS          
SEQRES   4 B  134  CYS TYR MET ASN SER ALA SER GLY ASN VAL SER TRP LEU          
SEQRES   5 B  134  TRP LYS GLN GLU MET ASP GLU ASN PRO GLN GLN LEU LYS          
SEQRES   6 B  134  LEU GLU LYS GLY ARG MET GLU GLU SER GLN ASN GLU SER          
SEQRES   7 B  134  LEU ALA THR LEU THR ILE GLN GLY ILE ARG PHE GLU ASP          
SEQRES   8 B  134  ASN GLY ILE TYR PHE CYS GLN GLN LYS CYS ASN ASN THR          
SEQRES   9 B  134  SER GLU VAL TYR GLN GLY CYS GLY THR GLU LEU ARG VAL          
SEQRES  10 B  134  MET GLY PHE SER THR LEU ALA GLN LEU LYS GLN ARG ASN          
SEQRES  11 B  134  THR LEU LYS ASP                                              
FORMUL   3  HOH   *2(H2 O)                                                      
HELIX    1   1 ARG B  113  ASN B  117  5                                   5    
SHEET    1   A 4 TRP A  47  SER A  49  0                                        
SHEET    2   A 4 VAL A  61  TYR A  66 -1  O  TYR A  66   N  TRP A  47           
SHEET    3   A 4 LEU A 104  ILE A 109 -1  O  ILE A 109   N  VAL A  61           
SHEET    4   A 4 MET A  96  GLN A 100 -1  N  GLU A  97   O  THR A 108           
SHEET    1   B 5 PHE A  52  LYS A  56  0                                        
SHEET    2   B 5 THR A 138  MET A 143  1  O  GLU A 139   N  ILE A  53           
SHEET    3   B 5 GLY A 118  LYS A 125 -1  N  GLY A 118   O  LEU A 140           
SHEET    4   B 5 SER A  75  LYS A  79 -1  N  SER A  75   O  GLN A 123           
SHEET    5   B 5 GLN A  87  GLN A  88 -1  O  GLN A  87   N  TRP A  78           
SHEET    1   C 4 PHE A  52  LYS A  56  0                                        
SHEET    2   C 4 THR A 138  MET A 143  1  O  GLU A 139   N  ILE A  53           
SHEET    3   C 4 GLY A 118  LYS A 125 -1  N  GLY A 118   O  LEU A 140           
SHEET    4   C 4 VAL A 132  GLN A 134 -1  O  TYR A 133   N  GLN A 124           
SHEET    1   D 4 TRP B  47  SER B  49  0                                        
SHEET    2   D 4 THR B  60  TYR B  66 -1  O  HIS B  64   N  SER B  49           
SHEET    3   D 4 LEU B 107  GLN B 110 -1  O  ILE B 109   N  VAL B  61           
SHEET    4   D 4 MET B  96  GLU B  98 -1  N  GLU B  97   O  THR B 108           
SHEET    1   E 5 PHE B  52  LYS B  56  0                                        
SHEET    2   E 5 THR B 138  MET B 143  1  O  ARG B 141   N  ARG B  55           
SHEET    3   E 5 GLY B 118  LYS B 125 -1  N  GLY B 118   O  LEU B 140           
SHEET    4   E 5 VAL B  74  LYS B  79 -1  N  LEU B  77   O  PHE B 121           
SHEET    5   E 5 GLN B  87  GLN B  88 -1  O  GLN B  87   N  TRP B  78           
SHEET    1   F 4 PHE B  52  LYS B  56  0                                        
SHEET    2   F 4 THR B 138  MET B 143  1  O  ARG B 141   N  ARG B  55           
SHEET    3   F 4 GLY B 118  LYS B 125 -1  N  GLY B 118   O  LEU B 140           
SHEET    4   F 4 VAL B 132  GLN B 134 -1  O  TYR B 133   N  GLN B 124           
SSBOND   1 CYS A   43    CYS A  126                          1555   1555  2.04  
SSBOND   2 CYS A   65    CYS A  122                          1555   1555  2.04  
SSBOND   3 CYS A  136    CYS B  136                          1555   1555  2.04  
SSBOND   4 CYS B   43    CYS B  126                          1555   1555  2.03  
SSBOND   5 CYS B   65    CYS B  122                          1555   1555  2.04  
CISPEP   1 SER A   49    PRO A   50          0        -0.36                     
CISPEP   2 SER B   49    PRO B   50          0        -1.70                     
CRYST1  129.800  129.800  129.800  90.00  90.00  90.00 P 41 3 2     48          
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      0.007704  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007704  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007704        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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