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Database: PDB
Entry: 1A02
LinkDB: 1A02
Original site: 1A02 
HEADER    TRANSCRIPTION/DNA                       08-DEC-97   1A02              
TITLE     STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN             
TITLE    2 BOUND TO DNA                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (5'-                                                   
COMPND   3 D(*DTP*DTP*DGP*DGP*DAP*DAP*DAP*DAP*DTP*DTP*DTP*DGP*DTP*DTP*          
COMPND   4 DTP*DCP*DAP*DTP*DAP*DG)-3');                                         
COMPND   5 CHAIN: A;                                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-                                                   
COMPND   9 D(*DAP*DAP*DCP*DTP*DAP*DTP*DGP*DAP*DAP*DAP*DCP*DAP*DAP*DAP*          
COMPND  10 DTP*DTP*DTP*DTP*DCP*DC)-3');                                         
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: NUCLEAR FACTOR OF ACTIVATED T CELLS;                       
COMPND  15 CHAIN: N;                                                            
COMPND  16 SYNONYM: NFAT;                                                       
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: AP-1 FRAGMENT FOS;                                         
COMPND  20 CHAIN: F;                                                            
COMPND  21 FRAGMENT: FOS;                                                       
COMPND  22 SYNONYM: FOS;                                                        
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 MUTATION: YES;                                                       
COMPND  25 MOL_ID: 5;                                                           
COMPND  26 MOLECULE: AP-1 FRAGMENT JUN;                                         
COMPND  27 CHAIN: J;                                                            
COMPND  28 FRAGMENT: JUN;                                                       
COMPND  29 SYNONYM: JUN;                                                        
COMPND  30 ENGINEERED: YES;                                                     
COMPND  31 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 CELL: T-LYMPHOCYTE;                                                  
SOURCE  10 GENE: NFAT1;                                                         
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PLM1;                                     
SOURCE  15 MOL_ID: 4;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSCRIPTION FACTOR, NFAT, NF-AT, AP-1, FOS-JUN,                     
KEYWDS   2 QUATERNARY PROTEIN-DNA COMPLEX, TRANSCRIPTION SYNERGY,               
KEYWDS   3 COMBINATORIAL GENE REGULATION, TRANSCRIPTION/DNA COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.CHEN,J.N.M.GLOVER,P.G.HOGAN,A.RAO,S.C.HARRISON                      
REVDAT   2   24-FEB-09 1A02    1       VERSN                                    
REVDAT   1   27-MAY-98 1A02    0                                                
JRNL        AUTH   L.CHEN,J.N.GLOVER,P.G.HOGAN,A.RAO,S.C.HARRISON               
JRNL        TITL   STRUCTURE OF THE DNA-BINDING DOMAINS FROM NFAT,              
JRNL        TITL 2 FOS AND JUN BOUND SPECIFICALLY TO DNA.                       
JRNL        REF    NATURE                        V. 392    42 1998              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   9510247                                                      
JRNL        DOI    10.1038/32100                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 21643                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.303                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1671                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1784                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3690                       
REMARK   3   BIN FREE R VALUE                    : 0.3690                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 188                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3073                                    
REMARK   3   NUCLEIC ACID ATOMS       : 814                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 61.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.00                          
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 10.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.500 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.000 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; 2.500                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM_NDBX.DNA                                 
REMARK   3  PARAMETER FILE  3  : PARAM_NDBX.INT                                 
REMARK   3  PARAMETER FILE  4  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOP_NDBX.DNA                                   
REMARK   3  TOPOLOGY FILE  3   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES N 478 - N 485 AND N 628 - N      
REMARK   3  634 ARE DISORDERED                                                  
REMARK   4                                                                      
REMARK   4 1A02 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-SEP-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.00                             
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22079                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR/MAD                      
REMARK 200 SOFTWARE USED: CCP4, X-PLOR                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE COMPLEX WAS CRYSTALLIZED IN          
REMARK 280  300-400 MM AMMONIUM ACETATE SALT, PH 7.5 (10 MM)., VAPOR            
REMARK 280  DIFFUSION, HANGING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       42.73000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, A, B, F, J                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET N   378                                                      
REMARK 465     ARG N   379                                                      
REMARK 465     GLY N   380                                                      
REMARK 465     SER N   381                                                      
REMARK 465     HIS N   382                                                      
REMARK 465     HIS N   383                                                      
REMARK 465     HIS N   384                                                      
REMARK 465     HIS N   385                                                      
REMARK 465     HIS N   386                                                      
REMARK 465     HIS N   387                                                      
REMARK 465     THR N   388                                                      
REMARK 465     ASP N   389                                                      
REMARK 465     PRO N   390                                                      
REMARK 465     HIS N   391                                                      
REMARK 465     ALA N   392                                                      
REMARK 465     SER N   393                                                      
REMARK 465     SER N   394                                                      
REMARK 465     VAL N   395                                                      
REMARK 465     PRO N   396                                                      
REMARK 465     LEU N   397                                                      
REMARK 465     GLU N   398                                                      
REMARK 465     MET F   138                                                      
REMARK 465     LYS F   139                                                      
REMARK 465     LEU F   193                                                      
REMARK 465     MET J   263                                                      
REMARK 465     LYS J   264                                                      
REMARK 465     ALA J   265                                                      
REMARK 465     GLU J   266                                                      
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 N 478    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE N 479    CG1  CG2  CD1                                       
REMARK 470     THR N 480    OG1  CG2                                            
REMARK 470     THR N 483    OG1  CG2                                            
REMARK 470     VAL N 484    CG1  CG2                                            
REMARK 470     THR N 485    OG1  CG2                                            
REMARK 470     ASP N 629    CG   OD1  OD2                                       
REMARK 470     LYS N 630    CG   CD   CE   NZ                                   
REMARK 470     ASP N 631    CG   OD1  OD2                                       
REMARK 470     LYS N 632    CG   CD   CE   NZ                                   
REMARK 470     SER N 633    OG                                                  
REMARK 470     GLN N 634    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DA A4005   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DG A4020   N9  -  C1' -  C2' ANGL. DEV. =   8.6 DEGREES          
REMARK 500     DA B5008   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DC B5011   C3' -  C2' -  C1' ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DC B5011   N1  -  C1' -  C2' ANGL. DEV. =   9.7 DEGREES          
REMARK 500     DC B5011   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG N 411   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG N 466   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG J 282   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER N 405      100.91    -51.63                                   
REMARK 500    GLU N 409       90.38     70.97                                   
REMARK 500    HIS N 420       86.75   -161.88                                   
REMARK 500    ASN N 451       53.96   -146.42                                   
REMARK 500    THR N 462     -172.45    -63.42                                   
REMARK 500    ALA N 463     -146.20   -158.78                                   
REMARK 500    ASP N 464     -162.81     60.49                                   
REMARK 500    THR N 480       -0.98    -52.59                                   
REMARK 500    LYS N 482     -162.09   -110.34                                   
REMARK 500    ASN N 495       -8.57     86.88                                   
REMARK 500    ARG N 537      104.93    -41.22                                   
REMARK 500    CYS N 588      169.94    174.80                                   
REMARK 500    VAL N 590      -30.50    -32.58                                   
REMARK 500    THR N 604     -141.10    -89.57                                   
REMARK 500    ASP N 631      -53.08   -172.49                                   
REMARK 500    SER N 633     -104.65   -168.34                                   
REMARK 500    PRO N 635       13.91    -61.60                                   
REMARK 500    ASN N 636       31.15   -155.42                                   
REMARK 500    LYS N 664      -42.18   -147.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1A02 N  396   678  UNP    Q13469   NFAC2_HUMAN    396    678             
DBREF  1A02 F  138   193  UNP    P01100   FOS_HUMAN      138    193             
DBREF  1A02 J  263   318  UNP    P05412   AP1_HUMAN      253    308             
DBREF  1A02 A 4001  4020  PDB    1A02     1A02          4001   4020             
DBREF  1A02 B 5001  5020  PDB    1A02     1A02          5001   5020             
SEQADV 1A02 MET F  138  UNP  P01100    GLU   138 ENGINEERED                     
SEQADV 1A02 SER F  154  UNP  P01100    CYS   154 ENGINEERED                     
SEQADV 1A02 MET J  263  UNP  P05412    ILE   253 ENGINEERED                     
SEQADV 1A02 SER J  279  UNP  P05412    CYS   269 ENGINEERED                     
SEQRES   1 A   20   DT  DT  DG  DG  DA  DA  DA  DA  DT  DT  DT  DG  DT          
SEQRES   2 A   20   DT  DT  DC  DA  DT  DA  DG                                  
SEQRES   1 B   20   DA  DA  DC  DT  DA  DT  DG  DA  DA  DA  DC  DA  DA          
SEQRES   2 B   20   DA  DT  DT  DT  DT  DC  DC                                  
SEQRES   1 N  301  MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO          
SEQRES   2 N  301  HIS ALA SER SER VAL PRO LEU GLU TRP PRO LEU SER SER          
SEQRES   3 N  301  GLN SER GLY SER TYR GLU LEU ARG ILE GLU VAL GLN PRO          
SEQRES   4 N  301  LYS PRO HIS HIS ARG ALA HIS TYR GLU THR GLU GLY SER          
SEQRES   5 N  301  ARG GLY ALA VAL LYS ALA PRO THR GLY GLY HIS PRO VAL          
SEQRES   6 N  301  VAL GLN LEU HIS GLY TYR MET GLU ASN LYS PRO LEU GLY          
SEQRES   7 N  301  LEU GLN ILE PHE ILE GLY THR ALA ASP GLU ARG ILE LEU          
SEQRES   8 N  301  LYS PRO HIS ALA PHE TYR GLN VAL HIS ARG ILE THR GLY          
SEQRES   9 N  301  LYS THR VAL THR THR THR SER TYR GLU LYS ILE VAL GLY          
SEQRES  10 N  301  ASN THR LYS VAL LEU GLU ILE PRO LEU GLU PRO LYS ASN          
SEQRES  11 N  301  ASN MET ARG ALA THR ILE ASP CYS ALA GLY ILE LEU LYS          
SEQRES  12 N  301  LEU ARG ASN ALA ASP ILE GLU LEU ARG LYS GLY GLU THR          
SEQRES  13 N  301  ASP ILE GLY ARG LYS ASN THR ARG VAL ARG LEU VAL PHE          
SEQRES  14 N  301  ARG VAL HIS ILE PRO GLU SER SER GLY ARG ILE VAL SER          
SEQRES  15 N  301  LEU GLN THR ALA SER ASN PRO ILE GLU CYS SER GLN ARG          
SEQRES  16 N  301  SER ALA HIS GLU LEU PRO MET VAL GLU ARG GLN ASP THR          
SEQRES  17 N  301  ASP SER CYS LEU VAL TYR GLY GLY GLN GLN MET ILE LEU          
SEQRES  18 N  301  THR GLY GLN ASN PHE THR SER GLU SER LYS VAL VAL PHE          
SEQRES  19 N  301  THR GLU LYS THR THR ASP GLY GLN GLN ILE TRP GLU MET          
SEQRES  20 N  301  GLU ALA THR VAL ASP LYS ASP LYS SER GLN PRO ASN MET          
SEQRES  21 N  301  LEU PHE VAL GLU ILE PRO GLU TYR ARG ASN LYS HIS ILE          
SEQRES  22 N  301  ARG THR PRO VAL LYS VAL ASN PHE TYR VAL ILE ASN GLY          
SEQRES  23 N  301  LYS ARG LYS ARG SER GLN PRO GLN HIS PHE THR TYR HIS          
SEQRES  24 N  301  PRO VAL                                                      
SEQRES   1 F   56  MET LYS ARG ARG ILE ARG ARG GLU ARG ASN LYS MET ALA          
SEQRES   2 F   56  ALA ALA LYS SER ARG ASN ARG ARG ARG GLU LEU THR ASP          
SEQRES   3 F   56  THR LEU GLN ALA GLU THR ASP GLN LEU GLU ASP GLU LYS          
SEQRES   4 F   56  SER ALA LEU GLN THR GLU ILE ALA ASN LEU LEU LYS GLU          
SEQRES   5 F   56  LYS GLU LYS LEU                                              
SEQRES   1 J   56  MET LYS ALA GLU ARG LYS ARG MET ARG ASN ARG ILE ALA          
SEQRES   2 J   56  ALA SER LYS SER ARG LYS ARG LYS LEU GLU ARG ILE ALA          
SEQRES   3 J   56  ARG LEU GLU GLU LYS VAL LYS THR LEU LYS ALA GLN ASN          
SEQRES   4 J   56  SER GLU LEU ALA SER THR ALA ASN MET LEU ARG GLU GLN          
SEQRES   5 J   56  VAL ALA GLN LEU                                              
FORMUL   6  HOH   *88(H2 O)                                                     
HELIX    1   1 ARG N  522  GLU N  527  1                                   6    
HELIX    2   2 SER N  570  LEU N  577  1                                   8    
HELIX    3   3 ARG F  140  LYS F  192  1                                  53    
HELIX    4   4 ARG J  267  GLN J  317  1                                  51    
SHEET    1   A 3 LEU N 410  VAL N 414  0                                        
SHEET    2   A 3 VAL N 442  LEU N 445 -1  O  VAL N 442   N  GLU N 413           
SHEET    3   A 3 ARG N 510  THR N 512 -1  O  ALA N 511   N  VAL N 443           
SHEET    1   B 5 GLU N 490  ILE N 492  0                                        
SHEET    2   B 5 VAL N 498  LEU N 503 -1  N  VAL N 498   O  ILE N 492           
SHEET    3   B 5 LEU N 454  GLY N 461 -1  O  LEU N 454   N  LEU N 503           
SHEET    4   B 5 ARG N 541  PRO N 551 -1  O  ARG N 543   N  GLY N 461           
SHEET    5   B 5 ILE N 557  ALA N 563 -1  O  VAL N 558   N  ILE N 550           
SHEET    1   C 5 GLU N 490  ILE N 492  0                                        
SHEET    2   C 5 VAL N 498  LEU N 503 -1  N  VAL N 498   O  ILE N 492           
SHEET    3   C 5 LEU N 454  GLY N 461 -1  O  LEU N 454   N  LEU N 503           
SHEET    4   C 5 ARG N 541  PRO N 551 -1  O  ARG N 543   N  GLY N 461           
SHEET    5   C 5 ILE N 567  GLU N 568 -1  N  ILE N 567   O  VAL N 542           
SHEET    1   D 2 TYR N 474  ARG N 478  0                                        
SHEET    2   D 2 ALA N 516  LYS N 520 -1  N  GLY N 517   O  HIS N 477           
SHEET    1   E 4 MET N 579  GLN N 583  0                                        
SHEET    2   E 4 GLN N 595  GLN N 601 -1  O  THR N 599   N  GLU N 581           
SHEET    3   E 4 MET N 637  GLU N 641 -1  O  LEU N 638   N  LEU N 598           
SHEET    4   E 4 VAL N 628  GLN N 634 -1  N  ASP N 629   O  PHE N 639           
SHEET    1   F 4 GLN N 620  ALA N 626  0                                        
SHEET    2   F 4 LYS N 608  LYS N 614 -1  O  VAL N 609   N  ALA N 626           
SHEET    3   F 4 VAL N 654  ASN N 662 -1  O  ASN N 657   N  THR N 612           
SHEET    4   F 4 LYS N 666  ARG N 667 -1  O  LYS N 666   N  ASN N 662           
SHEET    1   G 5 GLN N 620  ALA N 626  0                                        
SHEET    2   G 5 LYS N 608  LYS N 614 -1  O  VAL N 609   N  ALA N 626           
SHEET    3   G 5 VAL N 654  ASN N 662 -1  O  ASN N 657   N  THR N 612           
SHEET    4   G 5 GLN N 671  HIS N 676 -1  N  GLN N 671   O  PHE N 658           
SHEET    5   G 5 CYS N 588  LEU N 589  1  O  CYS N 588   N  HIS N 676           
CRYST1   64.660   85.460   83.370  90.00 112.03  90.00 P 1 21 1      2          
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      0.015466  0.000000  0.006258        0.00000                         
SCALE2      0.000000  0.011701  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012939        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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