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Database: PDB
Entry: 5VPD
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Original site: 5VPD 
HEADER    TRANSCRIPTION                           04-MAY-17   5VPD              
TITLE     TRANSCRIPTION FACTOR FOSB/JUND BZIP DOMAIN IN ITS OXIDIZED FORM, TYPE-
TITLE    2 III CRYSTAL                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN FOSB;                                              
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 153-219;                                      
COMPND   5 SYNONYM: G0/G1 SWITCH REGULATORY PROTEIN 3;                          
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TRANSCRIPTION FACTOR JUN-D;                                
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 266-332;                                      
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FOSB, G0S3;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 (DE3);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21-NESG;                               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: JUND;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 (DE3);                           
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    ACTIVATOR PROTEIN-1, BASIC LEUCINE ZIPPER, BZIP, FOS, JUN,            
KEYWDS   2 TRANSCRIPTION FACTOR, DNA-BINDING PROTEIN, REDOX SWITCH, COILED-     
KEYWDS   3 COIL, TRANSCRIPTION                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.YIN,M.MACHIUS,G.RUDENKO                                             
REVDAT   4   11-DEC-19 5VPD    1       REMARK                                   
REVDAT   3   15-NOV-17 5VPD    1       JRNL                                     
REVDAT   2   18-OCT-17 5VPD    1       JRNL                                     
REVDAT   1   06-SEP-17 5VPD    0                                                
JRNL        AUTH   Z.YIN,M.MACHIUS,E.J.NESTLER,G.RUDENKO                        
JRNL        TITL   ACTIVATOR PROTEIN-1: REDOX SWITCH CONTROLLING STRUCTURE AND  
JRNL        TITL 2 DNA-BINDING.                                                 
JRNL        REF    NUCLEIC ACIDS RES.            V.  45 11425 2017              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   28981703                                                     
JRNL        DOI    10.1093/NAR/GKX795                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 10789                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.255                           
REMARK   3   R VALUE            (WORKING SET) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.300                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1068                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.7258 -  5.5765    0.99     1411   158  0.2393 0.2560        
REMARK   3     2  5.5765 -  4.4275    0.99     1353   149  0.2246 0.2830        
REMARK   3     3  4.4275 -  3.8682    1.00     1317   154  0.2023 0.2614        
REMARK   3     4  3.8682 -  3.5147    1.00     1318   148  0.2332 0.2873        
REMARK   3     5  3.5147 -  3.2629    1.00     1315   141  0.2885 0.3715        
REMARK   3     6  3.2629 -  3.0705    0.97     1277   136  0.3098 0.3870        
REMARK   3     7  3.0705 -  2.9168    0.78     1028   112  0.3127 0.3611        
REMARK   3     8  2.9168 -  2.7898    0.54      702    70  0.3263 0.3559        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.31                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           1994                                  
REMARK   3   ANGLE     :  0.585           2655                                  
REMARK   3   CHIRALITY :  0.029            310                                  
REMARK   3   PLANARITY :  0.004            344                                  
REMARK   3   DIHEDRAL  : 12.825           1333                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 176 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.5510   0.0926 -16.8500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3965 T22:   0.8789                                     
REMARK   3      T33:   0.6283 T12:   0.1313                                     
REMARK   3      T13:  -0.2056 T23:  -0.0765                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4829 L22:   0.7508                                     
REMARK   3      L33:   7.1382 L12:   0.3646                                     
REMARK   3      L13:  -0.3510 L23:  -2.0751                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1384 S12:  -0.6256 S13:   0.3110                       
REMARK   3      S21:  -0.3573 S22:   0.3963 S23:   0.2470                       
REMARK   3      S31:   0.7913 S32:  -0.0033 S33:  -0.2896                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 177 THROUGH 218 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.7119  32.2956  -9.8081              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5266 T22:   0.3744                                     
REMARK   3      T33:   0.1926 T12:   0.2514                                     
REMARK   3      T13:   0.0031 T23:  -0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3058 L22:   4.0740                                     
REMARK   3      L33:   1.3071 L12:  -2.1313                                     
REMARK   3      L13:  -1.4688 L23:   1.5899                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3865 S12:  -0.3138 S13:   0.1224                       
REMARK   3      S21:   0.4064 S22:   0.4738 S23:  -0.2062                       
REMARK   3      S31:   0.0113 S32:   0.3688 S33:  -0.1278                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 266 THROUGH 332 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.2733  16.7447 -19.7572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2587 T22:   0.2239                                     
REMARK   3      T33:   0.2133 T12:   0.1296                                     
REMARK   3      T13:   0.0019 T23:   0.0096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5528 L22:   5.1143                                     
REMARK   3      L33:   0.2775 L12:  -2.5757                                     
REMARK   3      L13:  -0.6259 L23:   1.2096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1295 S12:  -0.2123 S13:  -0.1984                       
REMARK   3      S21:  -0.0131 S22:   0.0291 S23:   0.3520                       
REMARK   3      S31:   0.0810 S32:   0.1304 S33:   0.0707                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 161 THROUGH 177 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2806  22.1889 -10.1293              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3634 T22:   0.7049                                     
REMARK   3      T33:   0.4080 T12:   0.0492                                     
REMARK   3      T13:  -0.0908 T23:   0.0443                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5562 L22:   1.5669                                     
REMARK   3      L33:   3.9137 L12:   1.4964                                     
REMARK   3      L13:   0.1822 L23:   0.6089                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0218 S12:   0.4053 S13:   0.3754                       
REMARK   3      S21:   0.1266 S22:   0.5101 S23:   0.4051                       
REMARK   3      S31:  -0.5375 S32:  -0.5253 S33:  -0.4462                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 178 THROUGH 217 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5901 -13.1765 -15.3474              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5344 T22:   0.2322                                     
REMARK   3      T33:   0.2695 T12:  -0.1349                                     
REMARK   3      T13:  -0.1606 T23:  -0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7703 L22:   2.7249                                     
REMARK   3      L33:   1.3777 L12:   2.8956                                     
REMARK   3      L13:   1.6286 L23:   1.5407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2776 S12:   0.4643 S13:  -0.2020                       
REMARK   3      S21:  -0.3369 S22:   0.5010 S23:  -0.2756                       
REMARK   3      S31:   0.0511 S32:   0.2824 S33:  -0.1155                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 270 THROUGH 332 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.9366  -1.3353  -5.9360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2351 T22:   0.2681                                     
REMARK   3      T33:   0.1787 T12:  -0.0324                                     
REMARK   3      T13:   0.0123 T23:  -0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1444 L22:   9.4798                                     
REMARK   3      L33:   1.6102 L12:   5.4043                                     
REMARK   3      L13:   2.0691 L23:   3.7902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1710 S12:   0.2006 S13:   0.1886                       
REMARK   3      S21:   0.0784 S22:   0.2944 S23:   0.3712                       
REMARK   3      S31:  -0.0524 S32:   0.2034 S33:   0.2101                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESID 164 THROUGH 175 OR      
REMARK   3                          (RESID 177 THROUGH 178 AND (NAME N OR       
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 179 THROUGH 191 OR RESID 193       
REMARK   3                          THROUGH 217))                               
REMARK   3     SELECTION          : (CHAIN C AND ((RESID 164 AND (NAME N OR     
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 165 THROUGH 175 OR RESID 177       
REMARK   3                          THROUGH 191 OR RESID 193 THROUGH 217))      
REMARK   3     ATOM PAIRS NUMBER  : 573                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN B AND ((RESID 270 THROUGH 272 AND    
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 273 THROUGH 287 OR      
REMARK   3                          (RESID 288 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB )) OR RESID 289      
REMARK   3                          THROUGH 291 OR RESID 293 THROUGH 307 OR     
REMARK   3                          RESID 309 THROUGH 332))                     
REMARK   3     SELECTION          : (CHAIN D AND (RESID 270 THROUGH 291 OR      
REMARK   3                          RESID 293 THROUGH 307 OR RESID 309          
REMARK   3                          THROUGH 332))                               
REMARK   3     ATOM PAIRS NUMBER  : 696                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VPD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227767.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-OCT-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787                             
REMARK 200  MONOCHROMATOR                  : DIAMOND [111]                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11778                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.10800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.90600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
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: PHASER                                                
REMARK 200 STARTING MODEL: 5VPA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (V/V) 2-METHYL-2,4-PENTANEDIOL       
REMARK 280  (MPD), 0.1 M NACL, 50 MM SODIUM CACODYLATE PH 6 AND 10 MM           
REMARK 280  SPERMINE, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+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       46.00400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.02550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.00400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.02550            
REMARK 290   SMTRY3   4  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: 3050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9960 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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: 3040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9700 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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     SER A   152                                                      
REMARK 465     GLU A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     GLU A   155                                                      
REMARK 465     GLU A   156                                                      
REMARK 465     LYS A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     ARG A   159                                                      
REMARK 465     VAL A   160                                                      
REMARK 465     ARG A   161                                                      
REMARK 465     ARG A   162                                                      
REMARK 465     GLU A   163                                                      
REMARK 465     LYS A   219                                                      
REMARK 465     SER B   265                                                      
REMARK 465     SER C   152                                                      
REMARK 465     GLU C   153                                                      
REMARK 465     GLU C   154                                                      
REMARK 465     GLU C   155                                                      
REMARK 465     GLU C   156                                                      
REMARK 465     LYS C   157                                                      
REMARK 465     ARG C   158                                                      
REMARK 465     ARG C   159                                                      
REMARK 465     VAL C   160                                                      
REMARK 465     HIS C   218                                                      
REMARK 465     LYS C   219                                                      
REMARK 465     SER D   265                                                      
REMARK 465     GLN D   266                                                      
REMARK 465     GLU D   267                                                      
REMARK 465     ARG D   268                                                      
REMARK 465     ILE D   269                                                      
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     ARG A 164    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 162    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 177    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 178    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 270    CG   CD   CE   NZ                                   
REMARK 470     GLU D 272    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 288    CG   CD   NE   CZ   NH1  NH2                        
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   HE   ARG A   173     OD1  ASP C   188              1.57            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 304                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VPA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VPB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VPC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VPE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VPF   RELATED DB: PDB                                   
DBREF  5VPD A  153   219  UNP    P53539   FOSB_HUMAN     153    219             
DBREF  5VPD B  266   332  UNP    P17535   JUND_HUMAN     266    332             
DBREF  5VPD C  153   219  UNP    P53539   FOSB_HUMAN     153    219             
DBREF  5VPD D  266   332  UNP    P17535   JUND_HUMAN     266    332             
SEQADV 5VPD SER A  152  UNP  P53539              EXPRESSION TAG                 
SEQADV 5VPD SER B  265  UNP  P17535              EXPRESSION TAG                 
SEQADV 5VPD SER C  152  UNP  P53539              EXPRESSION TAG                 
SEQADV 5VPD SER D  265  UNP  P17535              EXPRESSION TAG                 
SEQRES   1 A   68  SER GLU GLU GLU GLU LYS ARG ARG VAL ARG ARG GLU ARG          
SEQRES   2 A   68  ASN LYS LEU ALA ALA ALA LYS CYS ARG ASN ARG ARG ARG          
SEQRES   3 A   68  GLU LEU THR ASP ARG LEU GLN ALA GLU THR ASP GLN LEU          
SEQRES   4 A   68  GLU GLU GLU LYS ALA GLU LEU GLU SER GLU ILE ALA GLU          
SEQRES   5 A   68  LEU GLN LYS GLU LYS GLU ARG LEU GLU PHE VAL LEU VAL          
SEQRES   6 A   68  ALA HIS LYS                                                  
SEQRES   1 B   68  SER GLN GLU ARG ILE LYS ALA GLU ARG LYS ARG LEU ARG          
SEQRES   2 B   68  ASN ARG ILE ALA ALA SER LYS CYS ARG LYS ARG LYS LEU          
SEQRES   3 B   68  GLU ARG ILE SER ARG LEU GLU GLU LYS VAL LYS THR LEU          
SEQRES   4 B   68  LYS SER GLN ASN THR GLU LEU ALA SER THR ALA SER LEU          
SEQRES   5 B   68  LEU ARG GLU GLN VAL ALA GLN LEU LYS GLN LYS VAL LEU          
SEQRES   6 B   68  SER HIS VAL                                                  
SEQRES   1 C   68  SER GLU GLU GLU GLU LYS ARG ARG VAL ARG ARG GLU ARG          
SEQRES   2 C   68  ASN LYS LEU ALA ALA ALA LYS CYS ARG ASN ARG ARG ARG          
SEQRES   3 C   68  GLU LEU THR ASP ARG LEU GLN ALA GLU THR ASP GLN LEU          
SEQRES   4 C   68  GLU GLU GLU LYS ALA GLU LEU GLU SER GLU ILE ALA GLU          
SEQRES   5 C   68  LEU GLN LYS GLU LYS GLU ARG LEU GLU PHE VAL LEU VAL          
SEQRES   6 C   68  ALA HIS LYS                                                  
SEQRES   1 D   68  SER GLN GLU ARG ILE LYS ALA GLU ARG LYS ARG LEU ARG          
SEQRES   2 D   68  ASN ARG ILE ALA ALA SER LYS CYS ARG LYS ARG LYS LEU          
SEQRES   3 D   68  GLU ARG ILE SER ARG LEU GLU GLU LYS VAL LYS THR LEU          
SEQRES   4 D   68  LYS SER GLN ASN THR GLU LEU ALA SER THR ALA SER LEU          
SEQRES   5 D   68  LEU ARG GLU GLN VAL ALA GLN LEU LYS GLN LYS VAL LEU          
SEQRES   6 D   68  SER HIS VAL                                                  
HET     NA  A 301       1                                                       
HET     CL  C 301       1                                                       
HET     CL  C 302       1                                                       
HET     CL  C 303       1                                                       
HET     NA  C 304       1                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5   NA    2(NA 1+)                                                     
FORMUL   6   CL    3(CL 1-)                                                     
FORMUL  10  HOH   *4(H2 O)                                                      
HELIX    1 AA1 ASN A  165  ARG A  173  1                                   9    
HELIX    2 AA2 ARG A  177  ALA A  217  1                                  41    
HELIX    3 AA3 ARG B  268  HIS B  331  1                                  64    
HELIX    4 AA4 ASN C  165  ARG C  173  1                                   9    
HELIX    5 AA5 ARG C  177  LEU C  215  1                                  39    
HELIX    6 AA6 VAL C  216  ALA C  217  5                                   2    
HELIX    7 AA7 LYS D  270  LYS D  270  5                                   1    
HELIX    8 AA8 ALA D  271  HIS D  331  1                                  61    
SSBOND   1 CYS A  172    CYS B  285                          1555   1555  2.02  
SSBOND   2 CYS C  172    CYS D  285                          1555   1555  2.03  
SITE     1 AC1  1 LYS A 206                                                     
SITE     1 AC2  1 ARG A 210                                                     
SITE     1 AC3  2 GLU C 200  ARG D 318                                          
CRYST1   92.008   98.051   50.251  90.00  90.00  90.00 P 21 21 2     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      0.010869  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010199  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019900        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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