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Database: PDB
Entry: 3JV6
LinkDB: 3JV6
Original site: 3JV6 
HEADER    TRANSCRIPTION                           15-SEP-09   3JV6              
TITLE     CRYSTAL STRUCTURE OF THE DIMERIZATION DOMAINS P52 AND RELB            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSCRIPTION FACTOR RELB;                                 
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 FRAGMENT: DIMERIZATION DOMAIN (UNP RESIDUES 278-378);                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NUCLEAR FACTOR NF-KAPPA-B P100 SUBUNIT;                    
COMPND   8 CHAIN: B, D, F;                                                      
COMPND   9 FRAGMENT: DIMERIZATION DOMAIN (UNP RESIDUES 225-331);                
COMPND  10 SYNONYM: DNA-BINDING FACTOR KBF2, NUCLEAR FACTOR NF-KAPPA-B P52      
COMPND  11 SUBUNIT;                                                             
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: RELB;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PROMOTER;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: P52;                                                           
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PROMOTER;                          
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET29B                                    
KEYWDS    NF-KB PROTEIN, HETERODIMER, RELB AND P52, ACTIVATOR, NUCLEUS,         
KEYWDS   2 PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION REGULATION, ANK REPEAT, 
KEYWDS   3 DNA-BINDING, ISOPEPTIDE BOND                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.VU,D.B.HUANG,G.GHOSH                                                
REVDAT   3   04-SEP-13 3JV6    1       JRNL                                     
REVDAT   2   27-MAR-13 3JV6    1       JRNL   VERSN                             
REVDAT   1   24-NOV-10 3JV6    0                                                
JRNL        AUTH   D.VU,D.B.HUANG,A.VEMU,G.GHOSH                                
JRNL        TITL   A STRUCTURAL BASIS FOR SELECTIVE DIMERIZATION BY NF-KAPPA B  
JRNL        TITL 2 RELB.                                                        
JRNL        REF    J.MOL.BIOL.                   V. 425  1934 2013              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   23485337                                                     
JRNL        DOI    10.1016/J.JMB.2013.02.020                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.78 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) : 2.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 136706.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 70.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 26839                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1338                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.78                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 35.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1561                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4450                       
REMARK   3   BIN FREE R VALUE                    : 0.4960                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 85                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.054                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5000                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -33.02000                                            
REMARK   3    B22 (A**2) : 67.79000                                             
REMARK   3    B33 (A**2) : -34.77000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.44                            
REMARK   3   ESD FROM SIGMAA              (A) : 1.19                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.50                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.10                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 44.26                                                
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   GROUP  2  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  2  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : AS.PARAM                                       
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : AS.TOP                                         
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3JV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055199.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRROR                       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30666                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.55400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM SULFATE, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       63.16750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       70.57200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       84.49300            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       63.16750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       70.57200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       84.49300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       63.16750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       70.57200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       84.49300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       63.16750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       70.57200            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       84.49300            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     ASP D   331                                                      
REMARK 465     GLU F   330                                                      
REMARK 465     ASP F   331                                                      
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    ARG A 285      157.99    172.81                                   
REMARK 500    LYS A 305      126.05    -33.91                                   
REMARK 500    ASP A 310       58.40   -162.27                                   
REMARK 500    GLU A 321      105.02    178.24                                   
REMARK 500    PRO A 377      170.31    -57.27                                   
REMARK 500    ASP B 234      -63.74    -19.48                                   
REMARK 500    LYS B 252      108.53    -24.69                                   
REMARK 500    LYS B 255      -40.94    -28.14                                   
REMARK 500    ASP B 265       12.68    -63.96                                   
REMARK 500    ASP B 266     -166.30    -73.39                                   
REMARK 500    PHE B 276      146.73   -173.35                                   
REMARK 500    LYS B 283       38.78     34.31                                   
REMARK 500    LYS B 298       44.56    -95.25                                   
REMARK 500    PRO B 302      103.04    -47.84                                   
REMARK 500    VAL B 328      102.46    -56.87                                   
REMARK 500    GLU B 330     -174.84    -58.50                                   
REMARK 500    ARG C 285      158.25    177.23                                   
REMARK 500    LYS C 305      130.42    -38.95                                   
REMARK 500    ASP C 310       55.90   -162.45                                   
REMARK 500    GLU C 321      102.88    174.03                                   
REMARK 500    PRO C 377     -178.93    -59.48                                   
REMARK 500    ASP D 234      -77.16    -40.56                                   
REMARK 500    LYS D 252      130.73    -30.75                                   
REMARK 500    LYS D 255      -47.38    -27.41                                   
REMARK 500    TYR D 263      149.07    178.89                                   
REMARK 500    ASP D 266     -146.91   -158.14                                   
REMARK 500    ASP D 280        5.78    -57.42                                   
REMARK 500    LYS D 283       53.20     31.66                                   
REMARK 500    GLN D 284      -18.48     68.25                                   
REMARK 500    ARG D 313      -81.85    -71.91                                   
REMARK 500    LYS E 305      126.56    -33.95                                   
REMARK 500    ASP E 310       56.96   -162.93                                   
REMARK 500    GLU E 321       99.54    176.31                                   
REMARK 500    PRO E 377     -178.58    -66.02                                   
REMARK 500    ASP F 234      -67.50    -17.86                                   
REMARK 500    LYS F 252      110.47    -26.48                                   
REMARK 500    LYS F 255      -39.62    -30.28                                   
REMARK 500    ASP F 266     -154.69   -152.79                                   
REMARK 500    PHE F 276      148.82   -173.31                                   
REMARK 500    GLN F 284       -2.06     70.88                                   
REMARK 500    LYS F 298       39.49    -90.28                                   
REMARK 500    PRO F 302      103.01    -49.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 515        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH E 488        DISTANCE =  5.65 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 609                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3JTC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3JUZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3JV0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3JV4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3JV5   RELATED DB: PDB                                   
DBREF  3JV6 A  278   378  UNP    Q04863   RELB_MOUSE     278    378             
DBREF  3JV6 B  225   331  UNP    Q9WTK5   NFKB2_MOUSE    225    331             
DBREF  3JV6 C  278   378  UNP    Q04863   RELB_MOUSE     278    378             
DBREF  3JV6 D  225   331  UNP    Q9WTK5   NFKB2_MOUSE    225    331             
DBREF  3JV6 E  278   378  UNP    Q04863   RELB_MOUSE     278    378             
DBREF  3JV6 F  225   331  UNP    Q9WTK5   NFKB2_MOUSE    225    331             
SEQADV 3JV6 VAL B  328  UNP  Q9WTK5    LEU   328 CONFLICT                       
SEQADV 3JV6 VAL D  328  UNP  Q9WTK5    LEU   328 CONFLICT                       
SEQADV 3JV6 VAL F  328  UNP  Q9WTK5    LEU   328 CONFLICT                       
SEQRES   1 A  101  THR SER GLU LEU ARG ILE CYS ARG ILE ASN LYS GLU SER          
SEQRES   2 A  101  GLY PRO CYS THR GLY GLY GLU GLU LEU TYR LEU LEU CYS          
SEQRES   3 A  101  ASP LYS VAL GLN LYS GLU ASP ILE SER VAL VAL PHE SER          
SEQRES   4 A  101  THR ALA SER TRP GLU GLY ARG ALA ASP PHE SER GLN ALA          
SEQRES   5 A  101  ASP VAL HIS ARG GLN ILE ALA ILE VAL PHE LYS THR PRO          
SEQRES   6 A  101  PRO TYR GLU ASP LEU GLU ILE SER GLU PRO VAL THR VAL          
SEQRES   7 A  101  ASN VAL PHE LEU GLN ARG LEU THR ASP GLY VAL CYS SER          
SEQRES   8 A  101  GLU PRO LEU PRO PHE THR TYR LEU PRO ARG                      
SEQRES   1 B  107  ALA SER ASN LEU LYS ILE SER ARG MET ASP LYS THR ALA          
SEQRES   2 B  107  GLY SER VAL ARG GLY GLY ASP GLU VAL TYR LEU LEU CYS          
SEQRES   3 B  107  ASP LYS VAL GLN LYS ASP ASP ILE GLU VAL ARG PHE TYR          
SEQRES   4 B  107  GLU ASP ASP GLU ASN GLY TRP GLN ALA PHE GLY ASP PHE          
SEQRES   5 B  107  SER PRO THR ASP VAL HIS LYS GLN TYR ALA ILE VAL PHE          
SEQRES   6 B  107  ARG THR PRO PRO TYR HIS LYS MET LYS ILE GLU ARG PRO          
SEQRES   7 B  107  VAL THR VAL PHE LEU GLN LEU LYS ARG LYS ARG GLY GLY          
SEQRES   8 B  107  ASP VAL SER ASP SER LYS GLN PHE THR TYR TYR PRO VAL          
SEQRES   9 B  107  VAL GLU ASP                                                  
SEQRES   1 C  101  THR SER GLU LEU ARG ILE CYS ARG ILE ASN LYS GLU SER          
SEQRES   2 C  101  GLY PRO CYS THR GLY GLY GLU GLU LEU TYR LEU LEU CYS          
SEQRES   3 C  101  ASP LYS VAL GLN LYS GLU ASP ILE SER VAL VAL PHE SER          
SEQRES   4 C  101  THR ALA SER TRP GLU GLY ARG ALA ASP PHE SER GLN ALA          
SEQRES   5 C  101  ASP VAL HIS ARG GLN ILE ALA ILE VAL PHE LYS THR PRO          
SEQRES   6 C  101  PRO TYR GLU ASP LEU GLU ILE SER GLU PRO VAL THR VAL          
SEQRES   7 C  101  ASN VAL PHE LEU GLN ARG LEU THR ASP GLY VAL CYS SER          
SEQRES   8 C  101  GLU PRO LEU PRO PHE THR TYR LEU PRO ARG                      
SEQRES   1 D  107  ALA SER ASN LEU LYS ILE SER ARG MET ASP LYS THR ALA          
SEQRES   2 D  107  GLY SER VAL ARG GLY GLY ASP GLU VAL TYR LEU LEU CYS          
SEQRES   3 D  107  ASP LYS VAL GLN LYS ASP ASP ILE GLU VAL ARG PHE TYR          
SEQRES   4 D  107  GLU ASP ASP GLU ASN GLY TRP GLN ALA PHE GLY ASP PHE          
SEQRES   5 D  107  SER PRO THR ASP VAL HIS LYS GLN TYR ALA ILE VAL PHE          
SEQRES   6 D  107  ARG THR PRO PRO TYR HIS LYS MET LYS ILE GLU ARG PRO          
SEQRES   7 D  107  VAL THR VAL PHE LEU GLN LEU LYS ARG LYS ARG GLY GLY          
SEQRES   8 D  107  ASP VAL SER ASP SER LYS GLN PHE THR TYR TYR PRO VAL          
SEQRES   9 D  107  VAL GLU ASP                                                  
SEQRES   1 E  101  THR SER GLU LEU ARG ILE CYS ARG ILE ASN LYS GLU SER          
SEQRES   2 E  101  GLY PRO CYS THR GLY GLY GLU GLU LEU TYR LEU LEU CYS          
SEQRES   3 E  101  ASP LYS VAL GLN LYS GLU ASP ILE SER VAL VAL PHE SER          
SEQRES   4 E  101  THR ALA SER TRP GLU GLY ARG ALA ASP PHE SER GLN ALA          
SEQRES   5 E  101  ASP VAL HIS ARG GLN ILE ALA ILE VAL PHE LYS THR PRO          
SEQRES   6 E  101  PRO TYR GLU ASP LEU GLU ILE SER GLU PRO VAL THR VAL          
SEQRES   7 E  101  ASN VAL PHE LEU GLN ARG LEU THR ASP GLY VAL CYS SER          
SEQRES   8 E  101  GLU PRO LEU PRO PHE THR TYR LEU PRO ARG                      
SEQRES   1 F  107  ALA SER ASN LEU LYS ILE SER ARG MET ASP LYS THR ALA          
SEQRES   2 F  107  GLY SER VAL ARG GLY GLY ASP GLU VAL TYR LEU LEU CYS          
SEQRES   3 F  107  ASP LYS VAL GLN LYS ASP ASP ILE GLU VAL ARG PHE TYR          
SEQRES   4 F  107  GLU ASP ASP GLU ASN GLY TRP GLN ALA PHE GLY ASP PHE          
SEQRES   5 F  107  SER PRO THR ASP VAL HIS LYS GLN TYR ALA ILE VAL PHE          
SEQRES   6 F  107  ARG THR PRO PRO TYR HIS LYS MET LYS ILE GLU ARG PRO          
SEQRES   7 F  107  VAL THR VAL PHE LEU GLN LEU LYS ARG LYS ARG GLY GLY          
SEQRES   8 F  107  ASP VAL SER ASP SER LYS GLN PHE THR TYR TYR PRO VAL          
SEQRES   9 F  107  VAL GLU ASP                                                  
HET    SO4  A 606       5                                                       
HET    SO4  B 601       5                                                       
HET    SO4  B 607       5                                                       
HET    SO4  C 605       5                                                       
HET    SO4  D 603       5                                                       
HET    SO4  D 608       5                                                       
HET    SO4  E 604       5                                                       
HET    SO4  F 602       5                                                       
HET    SO4  F 609       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   7  SO4    9(O4 S 2-)                                                   
FORMUL  16  HOH   *146(H2 O)                                                    
HELIX    1   1 SER A  327  GLN A  334  5                                   8    
HELIX    2   2 SER B  277  THR B  279  5                                   3    
HELIX    3   3 SER C  327  GLN C  334  5                                   8    
HELIX    4   4 SER E  327  GLN E  334  5                                   8    
HELIX    5   5 SER F  277  THR F  279  5                                   3    
SHEET    1   A 3 ILE A 283  ILE A 286  0                                        
SHEET    2   A 3 GLU A 298  CYS A 303 -1  O  LEU A 302   N  CYS A 284           
SHEET    3   A 3 ALA A 336  LYS A 340 -1  O  PHE A 339   N  LEU A 299           
SHEET    1   B 5 SER A 290  PRO A 292  0                                        
SHEET    2   B 5 LEU A 371  LEU A 376  1  O  LEU A 376   N  GLY A 291           
SHEET    3   B 5 VAL A 353  GLN A 360 -1  N  VAL A 355   O  PHE A 373           
SHEET    4   B 5 SER A 312  SER A 316 -1  N  SER A 316   O  ASN A 356           
SHEET    5   B 5 GLU A 321  ARG A 323 -1  O  GLY A 322   N  PHE A 315           
SHEET    1   C 4 ILE B 230  MET B 233  0                                        
SHEET    2   C 4 GLU B 245  CYS B 250 -1  O  LEU B 249   N  ARG B 232           
SHEET    3   C 4 ALA B 286  ARG B 290 -1  O  ILE B 287   N  LEU B 248           
SHEET    4   C 4 VAL B 281  HIS B 282 -1  N  HIS B 282   O  ALA B 286           
SHEET    1   D 5 ALA B 237  SER B 239  0                                        
SHEET    2   D 5 LYS B 321  TYR B 326  1  O  TYR B 326   N  GLY B 238           
SHEET    3   D 5 VAL B 303  ARG B 311 -1  N  VAL B 303   O  TYR B 325           
SHEET    4   D 5 ILE B 258  TYR B 263 -1  N  TYR B 263   O  PHE B 306           
SHEET    5   D 5 GLN B 271  PHE B 273 -1  O  ALA B 272   N  PHE B 262           
SHEET    1   E 3 ILE C 283  ILE C 286  0                                        
SHEET    2   E 3 GLU C 298  CYS C 303 -1  O  LEU C 302   N  CYS C 284           
SHEET    3   E 3 ALA C 336  LYS C 340 -1  O  PHE C 339   N  LEU C 299           
SHEET    1   F 5 SER C 290  PRO C 292  0                                        
SHEET    2   F 5 LEU C 371  LEU C 376  1  O  LEU C 376   N  GLY C 291           
SHEET    3   F 5 VAL C 353  GLN C 360 -1  N  VAL C 355   O  PHE C 373           
SHEET    4   F 5 SER C 312  SER C 316 -1  N  SER C 316   O  ASN C 356           
SHEET    5   F 5 GLU C 321  ARG C 323 -1  O  GLY C 322   N  PHE C 315           
SHEET    1   G 4 ILE D 230  MET D 233  0                                        
SHEET    2   G 4 GLU D 245  CYS D 250 -1  O  LEU D 249   N  ARG D 232           
SHEET    3   G 4 ALA D 286  ARG D 290 -1  O  ILE D 287   N  LEU D 248           
SHEET    4   G 4 VAL D 281  HIS D 282 -1  N  HIS D 282   O  ALA D 286           
SHEET    1   H 5 ALA D 237  SER D 239  0                                        
SHEET    2   H 5 LYS D 321  TYR D 326  1  O  THR D 324   N  GLY D 238           
SHEET    3   H 5 VAL D 303  ARG D 311 -1  N  VAL D 305   O  PHE D 323           
SHEET    4   H 5 ILE D 258  TYR D 263 -1  N  ARG D 261   O  GLN D 308           
SHEET    5   H 5 GLN D 271  PHE D 273 -1  O  ALA D 272   N  PHE D 262           
SHEET    1   I 3 ILE E 283  ILE E 286  0                                        
SHEET    2   I 3 GLU E 298  CYS E 303 -1  O  LEU E 302   N  CYS E 284           
SHEET    3   I 3 ALA E 336  LYS E 340 -1  O  PHE E 339   N  LEU E 299           
SHEET    1   J 5 SER E 290  PRO E 292  0                                        
SHEET    2   J 5 LEU E 371  LEU E 376  1  O  LEU E 376   N  GLY E 291           
SHEET    3   J 5 VAL E 353  GLN E 360 -1  N  VAL E 353   O  TYR E 375           
SHEET    4   J 5 SER E 312  SER E 316 -1  N  SER E 316   O  ASN E 356           
SHEET    5   J 5 GLU E 321  ARG E 323 -1  O  GLY E 322   N  PHE E 315           
SHEET    1   K 4 ILE F 230  MET F 233  0                                        
SHEET    2   K 4 GLU F 245  CYS F 250 -1  O  LEU F 249   N  ARG F 232           
SHEET    3   K 4 ALA F 286  ARG F 290 -1  O  ILE F 287   N  LEU F 248           
SHEET    4   K 4 VAL F 281  HIS F 282 -1  N  HIS F 282   O  ALA F 286           
SHEET    1   L 5 ALA F 237  SER F 239  0                                        
SHEET    2   L 5 LYS F 321  TYR F 326  1  O  TYR F 326   N  GLY F 238           
SHEET    3   L 5 VAL F 303  ARG F 311 -1  N  VAL F 303   O  TYR F 325           
SHEET    4   L 5 ILE F 258  TYR F 263 -1  N  ARG F 261   O  GLN F 308           
SHEET    5   L 5 GLN F 271  PHE F 273 -1  O  ALA F 272   N  PHE F 262           
SITE     1 AC1  3 LYS A 308  VAL A 331  ARG A 333                               
SITE     1 AC2  5 LYS B 235  ASP B 244  GLU B 245  ARG B 290                    
SITE     2 AC2  5 GLN D 271                                                     
SITE     1 AC3  4 LYS B 255  LYS B 283  GLN B 284  HOH B 476                    
SITE     1 AC4  4 LYS C 308  VAL C 331  ARG C 333  HOH C 505                    
SITE     1 AC5  5 LYS D 235  GLU D 245  ARG D 290  HOH D 473                    
SITE     2 AC5  5 GLN F 271                                                     
SITE     1 AC6  2 LYS D 283  GLN D 284                                          
SITE     1 AC7  3 LYS E 308  ARG E 333  HOH E 509                               
SITE     1 AC8  3 GLN B 271  GLU F 245  ARG F 290                               
SITE     1 AC9  2 LYS F 255  LYS F 283                                          
CRYST1  126.335  141.144  168.986  90.00  90.00  90.00 I 2 2 2      24          
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      0.007915  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007085  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005918        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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