GenomeNet

Database: PDB
Entry: 2WT7
LinkDB: 2WT7
Original site: 2WT7 
HEADER    TRANSCRIPTION                           11-SEP-09   2WT7              
TITLE     CRYSTAL STRUCTURE OF THE BZIP HETERODIMERIC COMPLEX MAFB:CFOS BOUND TO
TITLE    2 DNA                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE PROTEIN C-FOS;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 138-200;                                          
COMPND   5 SYNONYM: CFOS, CELLULAR ONCOGENE FOS;                                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TRANSCRIPTION FACTOR MAFB;                                 
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: RESIDUES 214-303;                                          
COMPND  11 SYNONYM: MAFB, MAF-B, V-MAF MUSCULOAPONEUROTIC FIBROSARCOMA ONCOGENE 
COMPND  12 HOMOLOG B, TRANSCRIPTION FACTOR MAF-1, SEGMENTATION PROTEIN KR,      
COMPND  13 KREISLER;                                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES;                                                       
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: MODIFIED T-MARE MOTIF;                                     
COMPND  18 CHAIN: C;                                                            
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: MODIFIED T-MARE MOTIF;                                     
COMPND  22 CHAIN: D;                                                            
COMPND  23 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: CODON PLUS RIL;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET-M11;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VARIANT: CODON PLUS RIL;                           
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: PET-M11;                                   
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  22 ORGANISM_TAXID: 32630;                                               
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 SYNTHETIC: YES;                                                      
SOURCE  25 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  26 ORGANISM_TAXID: 32630                                                
KEYWDS    TRANSCRIPTION, TRANSCRIPTION REGULATION, NUCLEUS, ACTIVATOR,          
KEYWDS   2 REPRESSOR, DNA-BINDING, PHOSPHOPROTEIN, DIFFERENTIATION, TUMOR       
KEYWDS   3 SUPPRESSOR, PROLIFERATION, PROTO-ONCOGENE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.POGENBERG,S.HOLTON,M.WILMANNS                                       
REVDAT   5   17-JUL-19 2WT7    1       REMARK                                   
REVDAT   4   19-MAR-14 2WT7    1       JRNL                                     
REVDAT   3   26-FEB-14 2WT7    1       JRNL                                     
REVDAT   2   05-FEB-14 2WT7    1       SOURCE JRNL   REMARK VERSN               
REVDAT   1   29-SEP-10 2WT7    0                                                
JRNL        AUTH   V.POGENBERG,L.CONSANI TEXTOR,L.VANHILLE,S.J.HOLTON,          
JRNL        AUTH 2 M.H.SIEWEKE,M.WILMANNS                                       
JRNL        TITL   DESIGN OF A BZIP TRANSCRIPTION FACTOR WITH                   
JRNL        TITL 2 HOMO/HETERODIMER-INDUCED DNA-BINDING PREFERENCE.             
JRNL        REF    STRUCTURE                     V.  22   466 2014              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   24530283                                                     
JRNL        DOI    10.1016/J.STR.2013.12.017                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 127.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 26707                          
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 + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1415                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1962                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2930                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 102                          
REMARK   3   BIN FREE R VALUE                    : 0.3410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1290                                    
REMARK   3   NUCLEIC ACID ATOMS       : 650                                     
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 172                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 57.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.48000                                              
REMARK   3    B22 (A**2) : 0.48000                                              
REMARK   3    B33 (A**2) : -0.72000                                             
REMARK   3    B12 (A**2) : 0.24000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.186         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.171         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.433         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2094 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2946 ; 1.391 ; 2.362       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   165 ; 4.150 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    81 ;27.771 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   307 ;15.994 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;21.959 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   321 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1366 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   796 ; 0.686 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1285 ; 1.366 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1298 ; 1.814 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1658 ; 2.856 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   138        A   200                          
REMARK   3    RESIDUE RANGE :   B   214        B   303                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.3500 -39.3040  -6.1900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1627 T22:  -0.1296                                     
REMARK   3      T33:   0.0803 T12:  -0.0491                                     
REMARK   3      T13:   0.0039 T23:  -0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4351 L22:   7.6839                                     
REMARK   3      L33:   0.1211 L12:  -1.0811                                     
REMARK   3      L13:  -0.2257 L23:   0.4193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0677 S12:   0.0833 S13:  -0.0734                       
REMARK   3      S21:  -0.3980 S22:   0.0364 S23:  -0.3381                       
REMARK   3      S31:   0.0521 S32:   0.0016 S33:  -0.1042                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C    16                          
REMARK   3    RESIDUE RANGE :   D     1        D    16                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9090 -18.1860  -1.6940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1501 T22:  -0.2515                                     
REMARK   3      T33:  -0.2050 T12:  -0.0516                                     
REMARK   3      T13:  -0.0070 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5458 L22:   3.0048                                     
REMARK   3      L33:  10.0205 L12:  -0.5869                                     
REMARK   3      L13:   1.4164 L23:   0.1197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0288 S12:  -0.0575 S13:  -0.0189                       
REMARK   3      S21:   0.1965 S22:   0.0521 S23:   0.0441                       
REMARK   3      S31:  -0.0852 S32:  -0.1527 S33:  -0.0234                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B           
REMARK   3  FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U           
REMARK   3  FACTORS.                                                            
REMARK   4                                                                      
REMARK   4 2WT7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-SEP-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290041083.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUN-06; NULL                    
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL                          
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG; EMBL/DESY,     
REMARK 200                                   HAMBURG                            
REMARK 200  BEAMLINE                       : X11; BW7A                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8162; 1.50100                    
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; CCD                   
REMARK 200  DETECTOR MANUFACTURER          : MAR555 FLAT PANEL; MARESEARCH      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28122                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.400                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 11.90                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD                                                
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.07800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       17.03900            
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  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       34.07800            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       17.03900            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2034  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 298 TO SER                        
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     DA C   1   O4' -  C1' -  C2' ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DT C   4   O4' -  C1' -  N1  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DT C  14   C3' -  C2' -  C1' ANGL. DEV. =  -6.8 DEGREES          
REMARK 500     DT C  14   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DT C  14   C5  -  C4  -  O4  ANGL. DEV. =  -4.4 DEGREES          
REMARK 500     DA C  15   O4' -  C1' -  N9  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DA D   3   O4' -  C1' -  N9  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500     DG D   5   O4' -  C1' -  N9  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DC D   9   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DT D  15   O4' -  C1' -  N1  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 1017                
DBREF  2WT7 A  138   200  UNP    P01101   FOS_MOUSE      138    200             
DBREF  2WT7 B  214   303  UNP    P54841   MAFB_MOUSE     214    303             
DBREF  2WT7 C    1    16  PDB    2WT7     2WT7             1     16             
DBREF  2WT7 D    1    16  PDB    2WT7     2WT7             1     16             
SEQADV 2WT7 SER B  298  UNP  P54841    CYS   298 ENGINEERED MUTATION            
SEQRES   1 A   63  GLU LYS ARG ARG ILE ARG ARG GLU ARG ASN LYS MET ALA          
SEQRES   2 A   63  ALA ALA LYS CYS ARG ASN ARG ARG ARG GLU LEU THR ASP          
SEQRES   3 A   63  THR LEU GLN ALA GLU THR ASP GLN LEU GLU ASP GLU LYS          
SEQRES   4 A   63  SER ALA LEU GLN THR GLU ILE ALA ASN LEU LEU LYS GLU          
SEQRES   5 A   63  LYS GLU LYS LEU GLU PHE ILE LEU ALA ALA HIS                  
SEQRES   1 B   90  ASP GLN LEU VAL SER MET SER VAL ARG GLU LEU ASN ARG          
SEQRES   2 B   90  HIS LEU ARG GLY PHE THR LYS ASP GLU VAL ILE ARG LEU          
SEQRES   3 B   90  LYS GLN LYS ARG ARG THR LEU LYS ASN ARG GLY TYR ALA          
SEQRES   4 B   90  GLN SER CYS ARG TYR LYS ARG VAL GLN GLN LYS HIS HIS          
SEQRES   5 B   90  LEU GLU ASN GLU LYS THR GLN LEU ILE GLN GLN VAL GLU          
SEQRES   6 B   90  GLN LEU LYS GLN GLU VAL SER ARG LEU ALA ARG GLU ARG          
SEQRES   7 B   90  ASP ALA TYR LYS VAL LYS SER GLU LYS LEU ALA ASN              
SEQRES   1 C   16   DA  DA  DT  DT  DG  DC  DT  DG  DA  DC  DT  DC  DA          
SEQRES   2 C   16   DT  DA  DG                                                  
SEQRES   1 D   16   DC  DT  DA  DT  DG  DA  DG  DT  DC  DA  DG  DC  DA          
SEQRES   2 D   16   DA  DT  DT                                                  
HET    PO4  C1017       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   5  PO4    O4 P 3-                                                      
FORMUL   6  HOH   *172(H2 O)                                                    
HELIX    1   1 GLU A  138  HIS A  200  1                                  63    
HELIX    2   2 ASP B  214  MET B  219  1                                   6    
HELIX    3   3 SER B  220  ARG B  229  1                                  10    
HELIX    4   4 THR B  232  ALA B  302  1                                  71    
SITE     1 AC1  9 ARG A 155  ARG A 158  ARG B 256  ARG B 259                    
SITE     2 AC1  9  DG C   8   DA C   9  HOH C2032  HOH C2033                    
SITE     3 AC1  9 HOH C2034                                                     
CRYST1  146.676  146.676   51.117  90.00  90.00 120.00 P 62          6          
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      0.006818  0.003936  0.000000        0.00000                         
SCALE2      0.000000  0.007872  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019563        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system