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Database: PDB
Entry: 3JV5
LinkDB: 3JV5
Original site: 3JV5 
HEADER    TRANSCRIPTION                           15-SEP-09   3JV5              
TITLE     CRYSTAL STRUCTURE OF THE DIMERIZATION DOMAINS P52 HOMODIMER           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEAR FACTOR NF-KAPPA-B P100 SUBUNIT;                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: DIMERIZATION DOMAIN (UNP RESIDUES 225-328);                
COMPND   5 SYNONYM: DNA-BINDING FACTOR KBF2, NUCLEAR FACTOR NF-KAPPA-B P52      
COMPND   6 SUBUNIT;                                                             
COMPND   7 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: P52;                                                           
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: PET29B                                    
KEYWDS    NF-KB PROTEIN, P52 HOMODIMER, DIMERIZATION DOMAIN, ACTIVATOR, ANK     
KEYWDS   2 REPEAT, DNA-BINDING, ISOPEPTIDE BOND, NUCLEUS, PHOSPHOPROTEIN,       
KEYWDS   3 TRANSCRIPTION, TRANSCRIPTION REGULATION                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.VU,D.B.HUANG,G.GHOSH                                                
REVDAT   1   24-NOV-10 3JV5    0                                                
JRNL        AUTH   D.VU,D.B.HUANG,G.GHOSH                                       
JRNL        TITL   INSTABILITY OF THE RELB DIMERIZATION DOMAIN IS FUNCTIONALLY  
JRNL        TITL 2 IMPORTANT                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 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) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 363383.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 75.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 11799                          
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) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 830                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 38.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 911                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3780                       
REMARK   3   BIN FREE R VALUE                    : 0.4090                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 72                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.048                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3379                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 183                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.60000                                             
REMARK   3    B22 (A**2) : 4.93000                                              
REMARK   3    B33 (A**2) : 1.68000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.27000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.47                            
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) : 0.47                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.55                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.01                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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        : 0.31                                                 
REMARK   3   BSOL        : 54.85                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : &_1_PARAMETER_INFILE_2                         
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   : &_1_TOPOLOGY_INFILE_2                          
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 3JV5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055198.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 106                                
REMARK 200  PH                             : 7.0                                
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   : 13577                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
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     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.99000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, PH 7.0, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 291K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       28.43150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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: 1370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 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 B   225                                                      
REMARK 465     ALA C   225                                                      
REMARK 465     SER C   226                                                      
REMARK 465     ALA D   225                                                      
REMARK 465     LEU D   328                                                      
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    SER A 226      -87.67    -81.69                                   
REMARK 500    ASP A 234     -108.19    -38.44                                   
REMARK 500    THR A 236       21.63   -158.20                                   
REMARK 500    LYS A 255      -59.35    -29.40                                   
REMARK 500    ASP A 256       47.01    -97.41                                   
REMARK 500    ASP A 257       21.96   -160.62                                   
REMARK 500    ASP A 266      168.11    -26.25                                   
REMARK 500    ASN A 268       25.07    -75.51                                   
REMARK 500    TRP A 270      149.71    -38.26                                   
REMARK 500    PHE A 276      136.78    179.21                                   
REMARK 500    VAL A 281       49.10   -100.94                                   
REMARK 500    HIS A 282      113.99    -33.81                                   
REMARK 500    LYS A 283       27.44     42.13                                   
REMARK 500    GLN A 284       -4.23     73.86                                   
REMARK 500    ARG A 313      -78.01   -106.42                                   
REMARK 500    VAL A 317     -166.30   -126.76                                   
REMARK 500    LYS B 252      136.36    -32.16                                   
REMARK 500    ASP B 257       48.08   -144.09                                   
REMARK 500    PHE B 276      154.17    166.61                                   
REMARK 500    LYS B 283       29.05     37.96                                   
REMARK 500    LYS B 312     -106.55    -31.65                                   
REMARK 500    PRO B 327     -145.49    -55.36                                   
REMARK 500    LYS C 252      132.52    -23.37                                   
REMARK 500    ASP C 257       50.14   -142.09                                   
REMARK 500    PHE C 276      153.57    167.17                                   
REMARK 500    LYS C 283       27.71     35.91                                   
REMARK 500    LYS C 298       70.73   -101.34                                   
REMARK 500    LYS C 312     -111.88    -27.27                                   
REMARK 500    PRO C 327     -133.58    -62.76                                   
REMARK 500    ASN D 227      107.97     -0.96                                   
REMARK 500    SER D 231      -94.64    -67.25                                   
REMARK 500    ASP D 234      -96.99    -45.41                                   
REMARK 500    ARG D 241        0.34    -69.66                                   
REMARK 500    LYS D 252      126.89    -10.06                                   
REMARK 500    PHE D 276      156.26    172.27                                   
REMARK 500    PRO D 278       -6.30    -54.56                                   
REMARK 500    MET D 297      -70.87    -61.96                                   
REMARK 500    LYS D 298       57.42    -52.01                                   
REMARK 500    PRO D 302      148.30    -38.84                                   
REMARK 500    LYS D 310      140.36   -173.43                                   
REMARK 500    LYS D 312      -66.88     -5.50                                   
REMARK 500    SER D 318     -153.83   -118.18                                   
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 C 442        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH A 460        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH C 514        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH D 509        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH A 618        DISTANCE =  5.36 ANGSTROMS                       
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: 3JV6   RELATED DB: PDB                                   
DBREF  3JV5 A  225   328  UNP    Q9WTK5   NFKB2_MOUSE    225    328             
DBREF  3JV5 B  225   328  UNP    Q9WTK5   NFKB2_MOUSE    225    328             
DBREF  3JV5 C  225   328  UNP    Q9WTK5   NFKB2_MOUSE    225    328             
DBREF  3JV5 D  225   328  UNP    Q9WTK5   NFKB2_MOUSE    225    328             
SEQRES   1 A  104  ALA SER ASN LEU LYS ILE SER ARG MET ASP LYS THR ALA          
SEQRES   2 A  104  GLY SER VAL ARG GLY GLY ASP GLU VAL TYR LEU LEU CYS          
SEQRES   3 A  104  ASP LYS VAL GLN LYS ASP ASP ILE GLU VAL ARG PHE TYR          
SEQRES   4 A  104  GLU ASP ASP GLU ASN GLY TRP GLN ALA PHE GLY ASP PHE          
SEQRES   5 A  104  SER PRO THR ASP VAL HIS LYS GLN TYR ALA ILE VAL PHE          
SEQRES   6 A  104  ARG THR PRO PRO TYR HIS LYS MET LYS ILE GLU ARG PRO          
SEQRES   7 A  104  VAL THR VAL PHE LEU GLN LEU LYS ARG LYS ARG GLY GLY          
SEQRES   8 A  104  ASP VAL SER ASP SER LYS GLN PHE THR TYR TYR PRO LEU          
SEQRES   1 B  104  ALA SER ASN LEU LYS ILE SER ARG MET ASP LYS THR ALA          
SEQRES   2 B  104  GLY SER VAL ARG GLY GLY ASP GLU VAL TYR LEU LEU CYS          
SEQRES   3 B  104  ASP LYS VAL GLN LYS ASP ASP ILE GLU VAL ARG PHE TYR          
SEQRES   4 B  104  GLU ASP ASP GLU ASN GLY TRP GLN ALA PHE GLY ASP PHE          
SEQRES   5 B  104  SER PRO THR ASP VAL HIS LYS GLN TYR ALA ILE VAL PHE          
SEQRES   6 B  104  ARG THR PRO PRO TYR HIS LYS MET LYS ILE GLU ARG PRO          
SEQRES   7 B  104  VAL THR VAL PHE LEU GLN LEU LYS ARG LYS ARG GLY GLY          
SEQRES   8 B  104  ASP VAL SER ASP SER LYS GLN PHE THR TYR TYR PRO LEU          
SEQRES   1 C  104  ALA SER ASN LEU LYS ILE SER ARG MET ASP LYS THR ALA          
SEQRES   2 C  104  GLY SER VAL ARG GLY GLY ASP GLU VAL TYR LEU LEU CYS          
SEQRES   3 C  104  ASP LYS VAL GLN LYS ASP ASP ILE GLU VAL ARG PHE TYR          
SEQRES   4 C  104  GLU ASP ASP GLU ASN GLY TRP GLN ALA PHE GLY ASP PHE          
SEQRES   5 C  104  SER PRO THR ASP VAL HIS LYS GLN TYR ALA ILE VAL PHE          
SEQRES   6 C  104  ARG THR PRO PRO TYR HIS LYS MET LYS ILE GLU ARG PRO          
SEQRES   7 C  104  VAL THR VAL PHE LEU GLN LEU LYS ARG LYS ARG GLY GLY          
SEQRES   8 C  104  ASP VAL SER ASP SER LYS GLN PHE THR TYR TYR PRO LEU          
SEQRES   1 D  104  ALA SER ASN LEU LYS ILE SER ARG MET ASP LYS THR ALA          
SEQRES   2 D  104  GLY SER VAL ARG GLY GLY ASP GLU VAL TYR LEU LEU CYS          
SEQRES   3 D  104  ASP LYS VAL GLN LYS ASP ASP ILE GLU VAL ARG PHE TYR          
SEQRES   4 D  104  GLU ASP ASP GLU ASN GLY TRP GLN ALA PHE GLY ASP PHE          
SEQRES   5 D  104  SER PRO THR ASP VAL HIS LYS GLN TYR ALA ILE VAL PHE          
SEQRES   6 D  104  ARG THR PRO PRO TYR HIS LYS MET LYS ILE GLU ARG PRO          
SEQRES   7 D  104  VAL THR VAL PHE LEU GLN LEU LYS ARG LYS ARG GLY GLY          
SEQRES   8 D  104  ASP VAL SER ASP SER LYS GLN PHE THR TYR TYR PRO LEU          
FORMUL   5  HOH   *183(H2 O)                                                    
HELIX    1   1 GLN A  254  ASP A  256  5                                   3    
HELIX    2   2 SER A  277  GLN A  284  5                                   8    
HELIX    3   3 SER B  277  THR B  279  5                                   3    
HELIX    4   4 SER C  277  THR C  279  5                                   3    
SHEET    1   A 3 ILE A 230  MET A 233  0                                        
SHEET    2   A 3 GLU A 245  CYS A 250 -1  O  LEU A 249   N  SER A 231           
SHEET    3   A 3 ALA A 286  ARG A 290 -1  O  PHE A 289   N  VAL A 246           
SHEET    1   B 5 ALA A 237  SER A 239  0                                        
SHEET    2   B 5 LYS A 321  TYR A 326  1  O  THR A 324   N  GLY A 238           
SHEET    3   B 5 VAL A 303  ARG A 311 -1  N  VAL A 305   O  PHE A 323           
SHEET    4   B 5 ILE A 258  TYR A 263 -1  N  GLU A 259   O  LYS A 310           
SHEET    5   B 5 GLN A 271  PHE A 273 -1  O  ALA A 272   N  PHE A 262           
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  PHE B 289   N  VAL B 246           
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  LYS B 310 -1  N  VAL B 303   O  TYR B 325           
SHEET    4   D 5 GLU B 259  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 4 ILE C 230  MET C 233  0                                        
SHEET    2   E 4 GLU C 245  CYS C 250 -1  O  LEU C 249   N  ARG C 232           
SHEET    3   E 4 ALA C 286  ARG C 290 -1  O  PHE C 289   N  VAL C 246           
SHEET    4   E 4 VAL C 281  HIS C 282 -1  N  HIS C 282   O  ALA C 286           
SHEET    1   F 5 ALA C 237  SER C 239  0                                        
SHEET    2   F 5 LYS C 321  TYR C 326  1  O  TYR C 326   N  GLY C 238           
SHEET    3   F 5 VAL C 303  LYS C 310 -1  N  VAL C 303   O  TYR C 325           
SHEET    4   F 5 GLU C 259  TYR C 263 -1  N  TYR C 263   O  PHE C 306           
SHEET    5   F 5 GLN C 271  PHE C 273 -1  O  ALA C 272   N  PHE C 262           
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  PHE D 289   N  VAL D 246           
SHEET    4   G 4 VAL D 281  HIS D 282 -1  N  HIS D 282   O  ALA D 286           
SHEET    1   H 5 GLY D 238  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  LYS D 310 -1  N  VAL D 305   O  PHE D 323           
SHEET    4   H 5 GLU D 259  TYR D 263 -1  N  TYR D 263   O  PHE D 306           
SHEET    5   H 5 GLN D 271  PHE D 273 -1  O  ALA D 272   N  PHE D 262           
CRYST1   46.433   56.863  102.192  90.00  97.77  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021536  0.000000  0.002939        0.00000                         
SCALE2      0.000000  0.017586  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009876        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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