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Database: PDB
Entry: 5ZMC
LinkDB: 5ZMC
Original site: 5ZMC 
HEADER    TRANSCRIPTION/DNA                       02-APR-18   5ZMC              
TITLE     STRUCTURAL BASIS FOR REACTIVATION OF -146C>T MUTANT TERT PROMOTER BY  
TITLE    2 COOPERATIVE BINDING OF P52 AND ETS1/2                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (5'-                                                   
COMPND   3 D(P*CP*GP*GP*GP*GP*AP*CP*CP*CP*GP*GP*AP*AP*GP*GP*G)-3');             
COMPND   4 CHAIN: C;                                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA (5'-                                                   
COMPND   8 D(P*GP*CP*CP*CP*TP*TP*CP*CP*GP*GP*GP*TP*CP*CP*CP*C)-3');             
COMPND   9 CHAIN: D;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PROTEIN C-ETS-1;                                           
COMPND  13 CHAIN: B;                                                            
COMPND  14 SYNONYM: P54;                                                        
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: NUCLEAR FACTOR NF-KAPPA-B P100 SUBUNIT;                    
COMPND  18 CHAIN: A;                                                            
COMPND  19 SYNONYM: DNA-BINDING FACTOR KBF2,H2TF1,LYMPHOCYTE TRANSLOCATION      
COMPND  20 CHROMOSOME 10 PROTEIN,NUCLEAR FACTOR OF KAPPA LIGHT POLYPEPTIDE GENE 
COMPND  21 ENHANCER IN B-CELLS 2,ONCOGENE LYT-10,LYT10;                         
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 SYNTHETIC: YES;                                                      
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: ETS1, EWSR2;                                                   
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 GENE: NFKB2, LYT10;                                                  
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ETS1, P52, TRANSCRIPTION FACTOR, TRANSCRIPTION, -146C>T MUTANT TERT   
KEYWDS   2 PROMOTER ACTIVATION, TRANSCRIPTION-DNA COMPLEX                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.XU,S.R.BHARATH,H.SONG                                               
REVDAT   2   17-OCT-18 5ZMC    1       JRNL   REMARK                            
REVDAT   1   19-SEP-18 5ZMC    0                                                
JRNL        AUTH   X.XU,Y.LI,S.R.BHARATH,M.B.OZTURK,M.W.BOWLER,B.Z.L.LOO,       
JRNL        AUTH 2 V.TERGAONKAR,H.SONG                                          
JRNL        TITL   STRUCTURAL BASIS FOR REACTIVATING THE MUTANT TERT PROMOTER   
JRNL        TITL 2 BY COOPERATIVE BINDING OF P52 AND ETS1.                      
JRNL        REF    NAT COMMUN                    V.   9  3183 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30093619                                                     
JRNL        DOI    10.1038/S41467-018-05644-0                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0216                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.41                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12379                          
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) : 0.260                           
REMARK   3   R VALUE            (WORKING SET) : 0.259                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 664                             
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) : 2.99                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 861                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 51                           
REMARK   3   BIN FREE R VALUE                    : 0.3330                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1737                                    
REMARK   3   NUCLEIC ACID ATOMS       : 656                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 101.2                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.52000                                              
REMARK   3    B22 (A**2) : 2.52000                                              
REMARK   3    B33 (A**2) : -5.05000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.755         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.400         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.316         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 38.236        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.902                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.875                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2516 ; 0.008 ; 0.017       
REMARK   3   BOND LENGTHS OTHERS               (A):  2004 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3528 ; 1.251 ; 1.706       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4671 ; 0.918 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   207 ; 7.112 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    89 ;37.505 ;23.258       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   325 ;16.521 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;13.334 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   340 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2343 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   573 ; 0.001 ; 0.020       
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):   834 ; 0.696 ; 4.977       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   833 ; 0.696 ; 4.976       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1039 ; 1.221 ; 7.458       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1040 ; 1.221 ; 7.458       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1680 ; 0.793 ; 4.946       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1681 ; 0.793 ; 4.947       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2489 ; 1.355 ; 7.411       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10161 ; 3.618 ;90.144       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10162 ; 3.618 ;90.143       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    -5        C    10                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.8080 -51.8250 -34.5520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3405 T22:   0.6896                                     
REMARK   3      T33:   0.7589 T12:  -0.3784                                     
REMARK   3      T13:   0.0743 T23:   0.0348                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6976 L22:   7.2473                                     
REMARK   3      L33:   2.9942 L12:   1.5898                                     
REMARK   3      L13:  -0.3145 L23:  -0.0953                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0685 S12:  -0.0034 S13:   0.0655                       
REMARK   3      S21:  -0.2413 S22:  -0.4341 S23:  -0.6045                       
REMARK   3      S31:   0.1731 S32:   0.5472 S33:   0.5026                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   107        D   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.7760 -51.5490 -34.1470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2763 T22:   0.4715                                     
REMARK   3      T33:   0.5069 T12:  -0.2756                                     
REMARK   3      T13:   0.0206 T23:   0.0372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3541 L22:   8.7985                                     
REMARK   3      L33:   2.7262 L12:   3.6774                                     
REMARK   3      L13:  -1.2147 L23:  -0.1918                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3178 S12:   0.4720 S13:   0.2665                       
REMARK   3      S21:  -0.7008 S22:   0.1532 S23:  -0.6121                       
REMARK   3      S31:   0.0726 S32:   0.4190 S33:   0.1647                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   332        B   437                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.1990 -46.2010 -23.1610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3951 T22:   0.3509                                     
REMARK   3      T33:   0.4128 T12:  -0.2619                                     
REMARK   3      T13:  -0.0891 T23:  -0.0805                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7055 L22:   3.8750                                     
REMARK   3      L33:   3.0642 L12:  -2.2279                                     
REMARK   3      L13:   0.0284 L23:  -1.3367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4334 S12:  -0.2030 S13:   0.2297                       
REMARK   3      S21:   0.5821 S22:   0.2753 S23:  -0.3808                       
REMARK   3      S31:  -0.3975 S32:   0.0453 S33:   0.1581                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   226        A   328                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.2570 -62.4490  -9.3530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5541 T22:   0.6293                                     
REMARK   3      T33:   0.5681 T12:  -0.1552                                     
REMARK   3      T13:   0.0430 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2097 L22:   4.3705                                     
REMARK   3      L33:   5.1726 L12:  -0.7901                                     
REMARK   3      L13:  -0.2129 L23:  -2.1852                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3710 S12:   0.2026 S13:  -0.5918                       
REMARK   3      S21:  -0.2213 S22:   0.5358 S23:   0.6383                       
REMARK   3      S31:   0.2930 S32:  -0.9047 S33:  -0.1648                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.10                                          
REMARK   3   ION PROBE RADIUS   : 0.90                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5ZMC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007271.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JAN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15992                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.990                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.410                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.22                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 1A3Q, 1K78                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0 AND 2.0 M AMMONIUM    
REMARK 280  SULPHATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+3/4                                              
REMARK 290       8555   -Y,-X,-Z+1/4                                            
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      131.26000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       65.63000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      196.89000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      131.26000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      196.89000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       65.63000            
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 APPLY THE FOLLOWING TO CHAINS: C, D, B, A                            
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     GLY B   331                                                      
REMARK 465     ASP B   438                                                      
REMARK 465     ALA B   439                                                      
REMARK 465     ASP B   440                                                      
REMARK 465     GLU B   441                                                      
REMARK 465     ALA A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     GLY A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     TYR A    39                                                      
REMARK 465     LEU A    40                                                      
REMARK 465     VAL A    41                                                      
REMARK 465     ILE A    42                                                      
REMARK 465     VAL A    43                                                      
REMARK 465     GLU A    44                                                      
REMARK 465     GLN A    45                                                      
REMARK 465     PRO A    46                                                      
REMARK 465     LYS A    47                                                      
REMARK 465     GLN A    48                                                      
REMARK 465     ARG A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     PHE A    51                                                      
REMARK 465     ARG A    52                                                      
REMARK 465     PHE A    53                                                      
REMARK 465     ARG A    54                                                      
REMARK 465     TYR A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     CYS A    57                                                      
REMARK 465     GLU A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     PRO A    60                                                      
REMARK 465     SER A    61                                                      
REMARK 465     HIS A    62                                                      
REMARK 465     GLY A    63                                                      
REMARK 465     GLY A    64                                                      
REMARK 465     LEU A    65                                                      
REMARK 465     PRO A    66                                                      
REMARK 465     GLY A    67                                                      
REMARK 465     ALA A    68                                                      
REMARK 465     SER A    69                                                      
REMARK 465     SER A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     LYS A    72                                                      
REMARK 465     GLY A    73                                                      
REMARK 465     ARG A    74                                                      
REMARK 465     LYS A    75                                                      
REMARK 465     THR A    76                                                      
REMARK 465     TYR A    77                                                      
REMARK 465     PRO A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     VAL A    80                                                      
REMARK 465     LYS A    81                                                      
REMARK 465     ILE A    82                                                      
REMARK 465     CYS A    83                                                      
REMARK 465     ASN A    84                                                      
REMARK 465     TYR A    85                                                      
REMARK 465     GLU A    86                                                      
REMARK 465     GLY A    87                                                      
REMARK 465     PRO A    88                                                      
REMARK 465     ALA A    89                                                      
REMARK 465     LYS A    90                                                      
REMARK 465     ILE A    91                                                      
REMARK 465     GLU A    92                                                      
REMARK 465     VAL A    93                                                      
REMARK 465     ASP A    94                                                      
REMARK 465     LEU A    95                                                      
REMARK 465     VAL A    96                                                      
REMARK 465     THR A    97                                                      
REMARK 465     HIS A    98                                                      
REMARK 465     SER A    99                                                      
REMARK 465     ASP A   100                                                      
REMARK 465     PRO A   101                                                      
REMARK 465     PRO A   102                                                      
REMARK 465     ARG A   103                                                      
REMARK 465     ALA A   104                                                      
REMARK 465     HIS A   105                                                      
REMARK 465     ALA A   106                                                      
REMARK 465     HIS A   107                                                      
REMARK 465     SER A   108                                                      
REMARK 465     LEU A   109                                                      
REMARK 465     VAL A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     LYS A   112                                                      
REMARK 465     GLN A   113                                                      
REMARK 465     CYS A   114                                                      
REMARK 465     SER A   115                                                      
REMARK 465     GLU A   116                                                      
REMARK 465     LEU A   117                                                      
REMARK 465     GLY A   118                                                      
REMARK 465     ILE A   119                                                      
REMARK 465     CYS A   120                                                      
REMARK 465     ALA A   121                                                      
REMARK 465     VAL A   122                                                      
REMARK 465     SER A   123                                                      
REMARK 465     VAL A   124                                                      
REMARK 465     GLY A   125                                                      
REMARK 465     PRO A   126                                                      
REMARK 465     LYS A   127                                                      
REMARK 465     ASP A   128                                                      
REMARK 465     MET A   129                                                      
REMARK 465     THR A   130                                                      
REMARK 465     ALA A   131                                                      
REMARK 465     GLN A   132                                                      
REMARK 465     PHE A   133                                                      
REMARK 465     ASN A   134                                                      
REMARK 465     ASN A   135                                                      
REMARK 465     LEU A   136                                                      
REMARK 465     GLY A   137                                                      
REMARK 465     VAL A   138                                                      
REMARK 465     LEU A   139                                                      
REMARK 465     HIS A   140                                                      
REMARK 465     VAL A   141                                                      
REMARK 465     THR A   142                                                      
REMARK 465     LYS A   143                                                      
REMARK 465     LYS A   144                                                      
REMARK 465     ASN A   145                                                      
REMARK 465     MET A   146                                                      
REMARK 465     MET A   147                                                      
REMARK 465     GLY A   148                                                      
REMARK 465     THR A   149                                                      
REMARK 465     MET A   150                                                      
REMARK 465     ILE A   151                                                      
REMARK 465     GLN A   152                                                      
REMARK 465     LYS A   153                                                      
REMARK 465     LEU A   154                                                      
REMARK 465     GLN A   155                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     LEU A   159                                                      
REMARK 465     ARG A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     ARG A   162                                                      
REMARK 465     PRO A   163                                                      
REMARK 465     GLN A   164                                                      
REMARK 465     GLY A   165                                                      
REMARK 465     LEU A   166                                                      
REMARK 465     THR A   167                                                      
REMARK 465     GLU A   168                                                      
REMARK 465     ALA A   169                                                      
REMARK 465     GLU A   170                                                      
REMARK 465     GLN A   171                                                      
REMARK 465     ARG A   172                                                      
REMARK 465     GLU A   173                                                      
REMARK 465     LEU A   174                                                      
REMARK 465     GLU A   175                                                      
REMARK 465     GLN A   176                                                      
REMARK 465     GLU A   177                                                      
REMARK 465     ALA A   178                                                      
REMARK 465     LYS A   179                                                      
REMARK 465     GLU A   180                                                      
REMARK 465     LEU A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     LYS A   183                                                      
REMARK 465     VAL A   184                                                      
REMARK 465     MET A   185                                                      
REMARK 465     ASP A   186                                                      
REMARK 465     LEU A   187                                                      
REMARK 465     SER A   188                                                      
REMARK 465     ILE A   189                                                      
REMARK 465     VAL A   190                                                      
REMARK 465     ARG A   191                                                      
REMARK 465     LEU A   192                                                      
REMARK 465     ARG A   193                                                      
REMARK 465     PHE A   194                                                      
REMARK 465     SER A   195                                                      
REMARK 465     ALA A   196                                                      
REMARK 465     PHE A   197                                                      
REMARK 465     LEU A   198                                                      
REMARK 465     ARG A   199                                                      
REMARK 465     ALA A   200                                                      
REMARK 465     SER A   201                                                      
REMARK 465     ASP A   202                                                      
REMARK 465     GLY A   203                                                      
REMARK 465     SER A   204                                                      
REMARK 465     PHE A   205                                                      
REMARK 465     SER A   206                                                      
REMARK 465     LEU A   207                                                      
REMARK 465     PRO A   208                                                      
REMARK 465     LEU A   209                                                      
REMARK 465     LYS A   210                                                      
REMARK 465     PRO A   211                                                      
REMARK 465     VAL A   212                                                      
REMARK 465     ILE A   213                                                      
REMARK 465     SER A   214                                                      
REMARK 465     GLN A   215                                                      
REMARK 465     PRO A   216                                                      
REMARK 465     ILE A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     ASP A   219                                                      
REMARK 465     SER A   220                                                      
REMARK 465     LYS A   221                                                      
REMARK 465     SER A   222                                                      
REMARK 465     PRO A   223                                                      
REMARK 465     GLY A   224                                                      
REMARK 465     ALA A   225                                                      
REMARK 465     VAL A   329                                                      
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    ASN B 400       28.86     47.87                                   
REMARK 500    ILE B 401      -66.33    -99.91                                   
REMARK 500    GLN A 284       -7.04     69.84                                   
REMARK 500    PRO A 327     -161.27    -73.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5ZMC C   -5    10  PDB    5ZMC     5ZMC            -5     10             
DBREF  5ZMC D  107   122  PDB    5ZMC     5ZMC           107    122             
DBREF  5ZMC B  331   441  UNP    P14921   ETS1_HUMAN     331    441             
DBREF  5ZMC A   35   329  UNP    Q00653   NFKB2_HUMAN     35    329             
SEQRES   1 C   16   DC  DG  DG  DG  DG  DA  DC  DC  DC  DG  DG  DA  DA          
SEQRES   2 C   16   DG  DG  DG                                                  
SEQRES   1 D   16   DG  DC  DC  DC  DT  DT  DC  DC  DG  DG  DG  DT  DC          
SEQRES   2 D   16   DC  DC  DC                                                  
SEQRES   1 B  111  GLY SER GLY PRO ILE GLN LEU TRP GLN PHE LEU LEU GLU          
SEQRES   2 B  111  LEU LEU THR ASP LYS SER CYS GLN SER PHE ILE SER TRP          
SEQRES   3 B  111  THR GLY ASP GLY TRP GLU PHE LYS LEU SER ASP PRO ASP          
SEQRES   4 B  111  GLU VAL ALA ARG ARG TRP GLY LYS ARG LYS ASN LYS PRO          
SEQRES   5 B  111  LYS MET ASN TYR GLU LYS LEU SER ARG GLY LEU ARG TYR          
SEQRES   6 B  111  TYR TYR ASP LYS ASN ILE ILE HIS LYS THR ALA GLY LYS          
SEQRES   7 B  111  ARG TYR VAL TYR ARG PHE VAL CYS ASP LEU GLN SER LEU          
SEQRES   8 B  111  LEU GLY TYR THR PRO GLU GLU LEU HIS ALA MET LEU ASP          
SEQRES   9 B  111  VAL LYS PRO ASP ALA ASP GLU                                  
SEQRES   1 A  295  ALA ASP GLY PRO TYR LEU VAL ILE VAL GLU GLN PRO LYS          
SEQRES   2 A  295  GLN ARG GLY PHE ARG PHE ARG TYR GLY CYS GLU GLY PRO          
SEQRES   3 A  295  SER HIS GLY GLY LEU PRO GLY ALA SER SER GLU LYS GLY          
SEQRES   4 A  295  ARG LYS THR TYR PRO THR VAL LYS ILE CYS ASN TYR GLU          
SEQRES   5 A  295  GLY PRO ALA LYS ILE GLU VAL ASP LEU VAL THR HIS SER          
SEQRES   6 A  295  ASP PRO PRO ARG ALA HIS ALA HIS SER LEU VAL GLY LYS          
SEQRES   7 A  295  GLN CYS SER GLU LEU GLY ILE CYS ALA VAL SER VAL GLY          
SEQRES   8 A  295  PRO LYS ASP MET THR ALA GLN PHE ASN ASN LEU GLY VAL          
SEQRES   9 A  295  LEU HIS VAL THR LYS LYS ASN MET MET GLY THR MET ILE          
SEQRES  10 A  295  GLN LYS LEU GLN ARG GLN ARG LEU ARG SER ARG PRO GLN          
SEQRES  11 A  295  GLY LEU THR GLU ALA GLU GLN ARG GLU LEU GLU GLN GLU          
SEQRES  12 A  295  ALA LYS GLU LEU LYS LYS VAL MET ASP LEU SER ILE VAL          
SEQRES  13 A  295  ARG LEU ARG PHE SER ALA PHE LEU ARG ALA SER ASP GLY          
SEQRES  14 A  295  SER PHE SER LEU PRO LEU LYS PRO VAL ILE SER GLN PRO          
SEQRES  15 A  295  ILE HIS ASP SER LYS SER PRO GLY ALA SER ASN LEU LYS          
SEQRES  16 A  295  ILE SER ARG MET ASP LYS THR ALA GLY SER VAL ARG GLY          
SEQRES  17 A  295  GLY ASP GLU VAL TYR LEU LEU CYS ASP LYS VAL GLN LYS          
SEQRES  18 A  295  ASP ASP ILE GLU VAL ARG PHE TYR GLU ASP ASP GLU ASN          
SEQRES  19 A  295  GLY TRP GLN ALA PHE GLY ASP PHE SER PRO THR ASP VAL          
SEQRES  20 A  295  HIS LYS GLN TYR ALA ILE VAL PHE ARG THR PRO PRO TYR          
SEQRES  21 A  295  HIS LYS MET LYS ILE GLU ARG PRO VAL THR VAL PHE LEU          
SEQRES  22 A  295  GLN LEU LYS ARG LYS ARG GLY GLY ASP VAL SER ASP SER          
SEQRES  23 A  295  LYS GLN PHE THR TYR TYR PRO LEU VAL                          
HELIX    1 AA1 GLN B  336  THR B  346  1                                  11    
HELIX    2 AA2 ASP B  347  GLN B  351  5                                   5    
HELIX    3 AA3 ASP B  367  LYS B  379  1                                  13    
HELIX    4 AA4 ASN B  385  TYR B  396  1                                  12    
HELIX    5 AA5 ASP B  417  LEU B  422  1                                   6    
HELIX    6 AA6 THR B  425  LEU B  433  1                                   9    
HELIX    7 AA7 SER A  277  THR A  279  5                                   3    
SHEET    1 AA1 4 SER B 355  TRP B 356  0                                        
SHEET    2 AA1 4 GLU B 362  LYS B 364 -1  O  LYS B 364   N  SER B 355           
SHEET    3 AA1 4 VAL B 411  PHE B 414 -1  O  TYR B 412   N  PHE B 363           
SHEET    4 AA1 4 ILE B 402  LYS B 404 -1  N  HIS B 403   O  ARG B 413           
SHEET    1 AA2 4 ILE A 230  MET A 233  0                                        
SHEET    2 AA2 4 GLU A 245  CYS A 250 -1  O  LEU A 249   N  ARG A 232           
SHEET    3 AA2 4 ALA A 286  ARG A 290 -1  O  ILE A 287   N  LEU A 248           
SHEET    4 AA2 4 VAL A 281  HIS A 282 -1  N  HIS A 282   O  ALA A 286           
SHEET    1 AA3 5 ALA A 237  SER A 239  0                                        
SHEET    2 AA3 5 LYS A 321  TYR A 326  1  O  THR A 324   N  GLY A 238           
SHEET    3 AA3 5 VAL A 303  LYS A 310 -1  N  VAL A 305   O  PHE A 323           
SHEET    4 AA3 5 GLU A 259  TYR A 263 -1  N  TYR A 263   O  PHE A 306           
SHEET    5 AA3 5 GLN A 271  PHE A 273 -1  O  ALA A 272   N  PHE A 262           
CRYST1   71.414   71.414  262.520  90.00  90.00  90.00 P 41 2 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      0.014003  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014003  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003809        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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