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Database: PDB
Entry: 1T2K
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Original site: 1T2K 
HEADER    TRANSCRIPTION/DNA                       21-APR-04   1T2K              
TITLE     STRUCTURE OF THE DNA BINDING DOMAINS OF IRF3, ATF-2 AND JUN           
TITLE    2 BOUND TO DNA                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 31-MER;                                                    
COMPND   3 CHAIN: E;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 OTHER_DETAILS: INTERFERON-B ENHANCER;                                
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: 31-MER;                                                    
COMPND   8 CHAIN: F;                                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 OTHER_DETAILS: INTERFERON-B ENHANCER;                                
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: INTERFERON REGULATORY FACTOR 3;                            
COMPND  13 CHAIN: A, B;                                                         
COMPND  14 FRAGMENT: N-TERMINAL DNA BINDING DOMAIN;                             
COMPND  15 SYNONYM: IRF-3;                                                      
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: TRANSCRIPTION FACTOR AP-1;                                 
COMPND  19 CHAIN: C;                                                            
COMPND  20 FRAGMENT: BZIP DOMAIN;                                               
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 MUTATION: YES;                                                       
COMPND  23 MOL_ID: 5;                                                           
COMPND  24 MOLECULE: CYCLIC-AMP-DEPENDENT TRANSCRIPTION FACTOR ATF-2;           
COMPND  25 CHAIN: D;                                                            
COMPND  26 FRAGMENT: BZIP DOMAIN;                                               
COMPND  27 SYNONYM: ACTIVATING TRANSCRIPTION FACTOR 2, CAMP RESPONSE            
COMPND  28 ELEMENT BINDING PROTEIN CRE- BP1, HB16;                              
COMPND  29 ENGINEERED: YES;                                                     
COMPND  30 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 GENE: IRF3;                                                          
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  12 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PTXB3;                                    
SOURCE  15 MOL_ID: 4;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: JUN;                                                           
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  22 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PET21A;                                   
SOURCE  25 MOL_ID: 5;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  27 ORGANISM_COMMON: HUMAN;                                              
SOURCE  28 ORGANISM_TAXID: 9606;                                                
SOURCE  29 GENE: ATF2, CREB2, CREBP1;                                           
SOURCE  30 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  31 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  32 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  33 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  34 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    PROTEIN DNA COMPLEX, TRANSCRIPTION, TRANSCRIPTION/DNA                 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.PANNE,T.MANIATIS,S.C.HARRISON                                       
REVDAT   2   24-FEB-09 1T2K    1       VERSN                                    
REVDAT   1   16-NOV-04 1T2K    0                                                
JRNL        AUTH   D.PANNE,T.MANIATIS,S.C.HARRISON                              
JRNL        TITL   CRYSTAL STRUCTURE OF ATF-2/C-JUN AND IRF-3 BOUND             
JRNL        TITL 2 TO THE INTERFERON-BETA ENHANCER.                             
JRNL        REF    EMBO J.                       V.  23  4384 2004              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   15510218                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7600453                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2048126.710                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 20140                          
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) : 0.257                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1178                            
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2934                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4130                       
REMARK   3   BIN FREE R VALUE                    : 0.3720                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 206                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2762                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1265                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 8                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 88.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -36.81000                                            
REMARK   3    B22 (A**2) : -17.53000                                            
REMARK   3    B33 (A**2) : 54.34000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 6.64000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.49                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.57                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 30.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.56                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.50                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.73                            
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        : 0.28                                                 
REMARK   3   BSOL        : 27.17                                                
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  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1T2K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022231.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUL-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : BENT TRIANGULAR ASYMMETRIC         
REMARK 200                                   CUT SI(111) MONOCHROMATER; RH-     
REMARK 200                                   COATED SI MIRROR FOR VERTICAL      
REMARK 200                                   FOCUSSING                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20151                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.700                              
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: PDB ENTRY 2IRF AND 2DGC                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NACACODYLATE, PH 6.5, 12.5%       
REMARK 280  (W/V) PEG 6000, 400 MM NH4OAC, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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       93.19000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.60500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       93.19000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.60500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, A, B, 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     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     SER B   112                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 112    OG                                                  
REMARK 470     ARG B   7    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 110    CG1  CG2                                            
REMARK 470     ASN B 111    CG   OD1  ND2                                       
REMARK 470     ARG C 272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 279    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 283    CG   CD   CE   NZ                                   
REMARK 470     LYS C 285    CG   CD   CE   NZ                                   
REMARK 470     MET C 313    CG   SD   CE                                        
REMARK 470     LYS D 364    CG   CD   CE   NZ                                   
REMARK 470     LEU D 372    CG   CD1  CD2                                       
REMARK 470     THR D 381    OG1  CG2                                            
REMARK 470     GLN D 389    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 391    CG   CD   CE   NZ                                   
REMARK 470     GLN D 392    CG   CD   OE1  NE2                                  
REMARK 470     LEU D 393    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN B    47     N    GLU B    49              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  69   CA  -  C   -  N   ANGL. DEV. = -13.3 DEGREES          
REMARK 500    PRO A 100   CA  -  N   -  CD  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    PRO B 103   CA  -  N   -  CD  ANGL. DEV. = -18.7 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    LYS A  29       83.90    -64.85                                   
REMARK 500    SER A  30       21.84    170.88                                   
REMARK 500    ARG A  31       77.17     26.07                                   
REMARK 500    THR A  32      -24.05   -140.36                                   
REMARK 500    TRP A  38       36.93   -140.72                                   
REMARK 500    PRO A  66      137.75    -39.78                                   
REMARK 500    ASP A  72       82.98   -159.40                                   
REMARK 500    ARG A  86       47.27    -98.40                                   
REMARK 500    GLU A  88      103.00      9.32                                   
REMARK 500    ALA A  93      -12.94   -151.09                                   
REMARK 500    ASP A 102       82.54   -179.67                                   
REMARK 500    ASN A 111       92.59    178.49                                   
REMARK 500    LYS B   5       81.96     77.48                                   
REMARK 500    LYS B  29      -61.48    -16.70                                   
REMARK 500    SER B  30       31.07    -70.72                                   
REMARK 500    ARG B  31       56.19     28.38                                   
REMARK 500    GLN B  48       17.05    -27.73                                   
REMARK 500    PRO B  66      -27.12    -29.24                                   
REMARK 500    ARG B  68       11.43     50.45                                   
REMARK 500    LYS B  70      118.02    -25.12                                   
REMARK 500    PRO B  71      153.05    -40.43                                   
REMARK 500    ARG B  86       53.50   -101.47                                   
REMARK 500    GLU B  88      101.36    -18.79                                   
REMARK 500    ALA B  93      -11.50   -144.48                                   
REMARK 500    ASP B 102       82.03   -158.25                                   
REMARK 500    LYS C 254      -54.56   -124.25                                   
REMARK 500    LEU D 395      -82.70   -106.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DG E   6         0.06    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1T2K A    1   112  UNP    Q14653   IRF3_HUMAN       1    112             
DBREF  1T2K B    1   112  UNP    Q14653   IRF3_HUMAN       1    112             
DBREF  1T2K C  253   314  UNP    P05412   JUN_HUMAN      254    314             
DBREF  1T2K D  336   396  UNP    P15336   ATF2_HUMAN     336    396             
DBREF  1T2K E    1    31  PDB    1T2K     1T2K             1     31             
DBREF  1T2K F    1    31  PDB    1T2K     1T2K             1     31             
SEQADV 1T2K MET C  253  UNP  P05412    ILE   253 CLONING ARTIFACT               
SEQADV 1T2K SER C  269  UNP  P05412    CYS   269 ENGINEERED                     
SEQADV 1T2K SER D  351  UNP  P15336    CYS   351 ENGINEERED                     
SEQRES   1 E   31   DT  DA  DA  DA  DT  DG  DA  DC  DA  DT  DA  DG  DG          
SEQRES   2 E   31   DA  DA  DA  DA  DC  DT  DG  DA  DA  DA  DG  DG  DG          
SEQRES   3 E   31   DA  DG  DA  DA  DG                                          
SEQRES   1 F   31   DA  DC  DT  DT  DC  DT  DC  DC  DC  DT  DT  DT  DC          
SEQRES   2 F   31   DA  DG  DT  DT  DT  DT  DC  DC  DT  DA  DT  DG  DT          
SEQRES   3 F   31   DC  DA  DT  DT  DT                                          
SEQRES   1 A  112  MET GLY THR PRO LYS PRO ARG ILE LEU PRO TRP LEU VAL          
SEQRES   2 A  112  SER GLN LEU ASP LEU GLY GLN LEU GLU GLY VAL ALA TRP          
SEQRES   3 A  112  VAL ASN LYS SER ARG THR ARG PHE ARG ILE PRO TRP LYS          
SEQRES   4 A  112  HIS GLY LEU ARG GLN ASP ALA GLN GLN GLU ASP PHE GLY          
SEQRES   5 A  112  ILE PHE GLN ALA TRP ALA GLU ALA THR GLY ALA TYR VAL          
SEQRES   6 A  112  PRO GLY ARG ASP LYS PRO ASP LEU PRO THR TRP LYS ARG          
SEQRES   7 A  112  ASN PHE ARG SER ALA LEU ASN ARG LYS GLU GLY LEU ARG          
SEQRES   8 A  112  LEU ALA GLU ASP ARG SER LYS ASP PRO HIS ASP PRO HIS          
SEQRES   9 A  112  LYS ILE TYR GLU PHE VAL ASN SER                              
SEQRES   1 B  112  MET GLY THR PRO LYS PRO ARG ILE LEU PRO TRP LEU VAL          
SEQRES   2 B  112  SER GLN LEU ASP LEU GLY GLN LEU GLU GLY VAL ALA TRP          
SEQRES   3 B  112  VAL ASN LYS SER ARG THR ARG PHE ARG ILE PRO TRP LYS          
SEQRES   4 B  112  HIS GLY LEU ARG GLN ASP ALA GLN GLN GLU ASP PHE GLY          
SEQRES   5 B  112  ILE PHE GLN ALA TRP ALA GLU ALA THR GLY ALA TYR VAL          
SEQRES   6 B  112  PRO GLY ARG ASP LYS PRO ASP LEU PRO THR TRP LYS ARG          
SEQRES   7 B  112  ASN PHE ARG SER ALA LEU ASN ARG LYS GLU GLY LEU ARG          
SEQRES   8 B  112  LEU ALA GLU ASP ARG SER LYS ASP PRO HIS ASP PRO HIS          
SEQRES   9 B  112  LYS ILE TYR GLU PHE VAL ASN SER                              
SEQRES   1 C   62  MET LYS ALA GLU ARG LYS ARG MET ARG ASN ARG ILE ALA          
SEQRES   2 C   62  ALA SER LYS SER ARG LYS ARG LYS LEU GLU ARG ILE ALA          
SEQRES   3 C   62  ARG LEU GLU GLU LYS VAL LYS THR LEU LYS ALA GLN ASN          
SEQRES   4 C   62  SER GLU LEU ALA SER THR ALA ASN MET LEU ARG GLU GLN          
SEQRES   5 C   62  VAL ALA GLN LEU LYS GLN LYS VAL MET ASN                      
SEQRES   1 D   61  LYS ARG ARG LYS PHE LEU GLU ARG ASN ARG ALA ALA ALA          
SEQRES   2 D   61  SER ARG SER ARG GLN LYS ARG LYS VAL TRP VAL GLN SER          
SEQRES   3 D   61  LEU GLU LYS LYS ALA GLU ASP LEU SER SER LEU ASN GLY          
SEQRES   4 D   61  GLN LEU GLN SER GLU VAL THR LEU LEU ARG ASN GLU VAL          
SEQRES   5 D   61  ALA GLN LEU LYS GLN LEU LEU LEU ALA                          
FORMUL   7  HOH   *8(H2 O)                                                      
HELIX    1   1 ARG A    7  GLY A   19  1                                  13    
HELIX    2   2 GLN A   47  ASP A   50  5                                   4    
HELIX    3   3 PHE A   51  THR A   61  1                                  11    
HELIX    4   4 ASP A   72  ARG A   86  1                                  15    
HELIX    5   5 ILE B    8  GLY B   19  1                                  12    
HELIX    6   6 PHE B   51  THR B   61  1                                  11    
HELIX    7   7 ASP B   72  ARG B   86  1                                  15    
HELIX    8   8 LYS C  254  LYS C  271  1                                  18    
HELIX    9   9 LYS C  273  ALA C  278  1                                   6    
HELIX   10  10 LEU C  280  GLU C  282  5                                   3    
HELIX   11  11 THR C  286  VAL C  312  1                                  27    
HELIX   12  12 LYS D  336  GLU D  363  1                                  28    
HELIX   13  13 LYS D  365  SER D  371  1                                   7    
HELIX   14  14 ASN D  373  VAL D  380  1                                   8    
HELIX   15  15 LEU D  382  ALA D  388  1                                   7    
SHEET    1   A 4 ALA A  25  TRP A  26  0                                        
SHEET    2   A 4 ARG A  33  PRO A  37 -1  O  ARG A  35   N  ALA A  25           
SHEET    3   A 4 HIS A 104  PHE A 109 -1  O  LYS A 105   N  ILE A  36           
SHEET    4   A 4 LEU A  90  ASP A  95 -1  N  ARG A  91   O  GLU A 108           
SHEET    1   B 4 ALA B  25  TRP B  26  0                                        
SHEET    2   B 4 ARG B  33  PRO B  37 -1  O  ARG B  35   N  ALA B  25           
SHEET    3   B 4 HIS B 104  GLU B 108 -1  O  LYS B 105   N  ILE B  36           
SHEET    4   B 4 ARG B  91  ASP B  95 -1  N  ARG B  91   O  GLU B 108           
CRYST1  186.380   65.210   83.850  90.00  93.44  90.00 C 1 2 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      0.005365  0.000000  0.000323        0.00000                         
SCALE2      0.000000  0.015335  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011948        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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