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Database: PDB
Entry: 3QU3
LinkDB: 3QU3
Original site: 3QU3 
HEADER    DNA BINDING PROTEIN                     23-FEB-11   3QU3              
TITLE     CRYSTAL STRUCTURE OF IRF-7 DBD APO FORM                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERFERON REGULATORY FACTOR 7;                            
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: DNA BINDING DOMAIN;                                        
COMPND   5 SYNONYM: IRF-7;                                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: IRF7;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    HELIX-TURN-HELIX, GENE REGULATION, DNA BINDING PROTEIN                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.E.DE IOANNES,C.R.ESCALANTE,A.K.AGGARWAL                             
REVDAT   3   01-FEB-12 3QU3    1       REMARK                                   
REVDAT   2   14-SEP-11 3QU3    1       JRNL   VERSN                             
REVDAT   1   01-JUN-11 3QU3    0                                                
JRNL        AUTH   P.DE IOANNES,C.R.ESCALANTE,A.K.AGGARWAL                      
JRNL        TITL   STRUCTURES OF APO IRF-3 AND IRF-7 DNA BINDING DOMAINS:       
JRNL        TITL 2 EFFECT OF LOOP L1 ON DNA BINDING.                            
JRNL        REF    NUCLEIC ACIDS RES.            V.  39  7300 2011              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   21596780                                                     
JRNL        DOI    10.1093/NAR/GKR325                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 85702                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.370                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2027                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.7072 -  3.1365    0.96     6081   165  0.0922 0.1597        
REMARK   3     2  3.1365 -  2.4899    0.97     6132   149  0.1414 0.1793        
REMARK   3     3  2.4899 -  2.1753    0.96     6104   146  0.1674 0.1895        
REMARK   3     4  2.1753 -  1.9764    0.96     6000   146  0.1864 0.1871        
REMARK   3     5  1.9764 -  1.8348    0.96     6107   146  0.2182 0.2244        
REMARK   3     6  1.8348 -  1.7266    0.95     5986   148  0.2368 0.3068        
REMARK   3     7  1.7266 -  1.6402    0.95     5989   138  0.2599 0.2652        
REMARK   3     8  1.6402 -  1.5688    0.94     5944   134  0.2586 0.2641        
REMARK   3     9  1.5688 -  1.5084    0.94     5901   142  0.2687 0.2389        
REMARK   3    10  1.5084 -  1.4563    0.93     5931   143  0.2876 0.3198        
REMARK   3    11  1.4563 -  1.4108    0.93     5852   144  0.3311 0.3161        
REMARK   3    12  1.4108 -  1.3705    0.93     5807   136  0.3636 0.3832        
REMARK   3    13  1.3705 -  1.3344    0.92     5837   144  0.4096 0.4732        
REMARK   3    14  1.3344 -  1.3000    0.92     5848   144  0.4397 0.4206        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.39                                          
REMARK   3   B_SOL              : 58.10                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.36780                                             
REMARK   3    B22 (A**2) : -0.36780                                             
REMARK   3    B33 (A**2) : 0.73570                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: 0.3810                                                   
REMARK   3   OPERATOR: -K,-H,-L                                                 
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           3037                                  
REMARK   3   ANGLE     :  1.029           4130                                  
REMARK   3   CHIRALITY :  0.066            404                                  
REMARK   3   PLANARITY :  0.005            554                                  
REMARK   3   DIHEDRAL  : 13.469           1110                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3QU3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064104.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-AUG-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.001                              
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE CRYSTAL      
REMARK 200                                   SAGITTAL FOCUSING MONOCHROMATOR    
REMARK 200  OPTICS                         : VERTICAL FOCUSING MIRROR           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85736                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
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: PDB ENTRY 2O61                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 1500, VAPOR DIFFUSION, HANGING   
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       22.87000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       45.74000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     THR A   131                                                      
REMARK 465     VAL A   132                                                      
REMARK 465     GLY A   133                                                      
REMARK 465     PRO A   134                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     VAL B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     ARG B   126                                                      
REMARK 465     GLU B   127                                                      
REMARK 465     LEU B   128                                                      
REMARK 465     GLY B   129                                                      
REMARK 465     SER B   130                                                      
REMARK 465     THR B   131                                                      
REMARK 465     VAL B   132                                                      
REMARK 465     GLY B   133                                                      
REMARK 465     PRO B   134                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ARG C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     VAL C     7                                                      
REMARK 465     ARG C   126                                                      
REMARK 465     GLU C   127                                                      
REMARK 465     LEU C   128                                                      
REMARK 465     GLY C   129                                                      
REMARK 465     SER C   130                                                      
REMARK 465     THR C   131                                                      
REMARK 465     VAL C   132                                                      
REMARK 465     GLY C   133                                                      
REMARK 465     PRO C   134                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  48    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 130    OG                                                  
REMARK 470     ARG B   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  33    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  43    CE   NZ                                             
REMARK 470     ARG B  67    NE   CZ   NH1  NH2                                  
REMARK 470     ASN B  74    CG   OD1  ND2                                       
REMARK 470     LYS C  43    CG   CD   CE   NZ                                   
REMARK 470     ARG C  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  48    CG   CD   NE   CZ   NH1  NH2                        
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    TRP A  42       80.02   -156.27                                   
REMARK 500    ASP A 117       63.98   -164.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 135  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE B 105   O                                                      
REMARK 620 2 LEU B  99   O   143.5                                              
REMARK 620 3 THR B 102   O    80.7  75.0                                        
REMARK 620 4 HOH B 162   O   114.2  92.4 165.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 135  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A  99   O                                                      
REMARK 620 2 THR A 102   O    76.3                                              
REMARK 620 3 PHE A 105   O   137.1  74.4                                        
REMARK 620 4 HOH A 199   O   110.9 172.2  97.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 135  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE C 105   O                                                      
REMARK 620 2 LEU C  99   O   126.1                                              
REMARK 620 3 HOH C 145   O   120.1 110.9                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 135                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 135                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 136                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 137                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 138                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 135                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 136                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QU6   RELATED DB: PDB                                   
DBREF  3QU3 A    1   134  UNP    P70434   IRF7_MOUSE       1    134             
DBREF  3QU3 B    1   134  UNP    P70434   IRF7_MOUSE       1    134             
DBREF  3QU3 C    1   134  UNP    P70434   IRF7_MOUSE       1    134             
SEQADV 3QU3 GLY A   -2  UNP  P70434              EXPRESSION TAG                 
SEQADV 3QU3 SER A   -1  UNP  P70434              EXPRESSION TAG                 
SEQADV 3QU3 HIS A    0  UNP  P70434              EXPRESSION TAG                 
SEQADV 3QU3 GLY B   -2  UNP  P70434              EXPRESSION TAG                 
SEQADV 3QU3 SER B   -1  UNP  P70434              EXPRESSION TAG                 
SEQADV 3QU3 HIS B    0  UNP  P70434              EXPRESSION TAG                 
SEQADV 3QU3 GLY C   -2  UNP  P70434              EXPRESSION TAG                 
SEQADV 3QU3 SER C   -1  UNP  P70434              EXPRESSION TAG                 
SEQADV 3QU3 HIS C    0  UNP  P70434              EXPRESSION TAG                 
SEQRES   1 A  137  GLY SER HIS MET ALA GLU VAL ARG GLY VAL GLN ARG VAL          
SEQRES   2 A  137  LEU PHE GLY ASP TRP LEU LEU GLY GLU VAL SER SER GLY          
SEQRES   3 A  137  GLN TYR GLU GLY LEU GLN TRP LEU ASN GLU ALA ARG THR          
SEQRES   4 A  137  VAL PHE ARG VAL PRO TRP LYS HIS PHE GLY ARG ARG ASP          
SEQRES   5 A  137  LEU ASP GLU GLU ASP ALA GLN ILE PHE LYS ALA TRP ALA          
SEQRES   6 A  137  VAL ALA ARG GLY ARG TRP PRO PRO SER GLY VAL ASN LEU          
SEQRES   7 A  137  PRO PRO PRO GLU ALA GLU ALA ALA GLU ARG ARG GLU ARG          
SEQRES   8 A  137  ARG GLY TRP LYS THR ASN PHE ARG CYS ALA LEU HIS SER          
SEQRES   9 A  137  THR GLY ARG PHE ILE LEU ARG GLN ASP ASN SER GLY ASP          
SEQRES  10 A  137  PRO VAL ASP PRO HIS LYS VAL TYR GLU LEU SER ARG GLU          
SEQRES  11 A  137  LEU GLY SER THR VAL GLY PRO                                  
SEQRES   1 B  137  GLY SER HIS MET ALA GLU VAL ARG GLY VAL GLN ARG VAL          
SEQRES   2 B  137  LEU PHE GLY ASP TRP LEU LEU GLY GLU VAL SER SER GLY          
SEQRES   3 B  137  GLN TYR GLU GLY LEU GLN TRP LEU ASN GLU ALA ARG THR          
SEQRES   4 B  137  VAL PHE ARG VAL PRO TRP LYS HIS PHE GLY ARG ARG ASP          
SEQRES   5 B  137  LEU ASP GLU GLU ASP ALA GLN ILE PHE LYS ALA TRP ALA          
SEQRES   6 B  137  VAL ALA ARG GLY ARG TRP PRO PRO SER GLY VAL ASN LEU          
SEQRES   7 B  137  PRO PRO PRO GLU ALA GLU ALA ALA GLU ARG ARG GLU ARG          
SEQRES   8 B  137  ARG GLY TRP LYS THR ASN PHE ARG CYS ALA LEU HIS SER          
SEQRES   9 B  137  THR GLY ARG PHE ILE LEU ARG GLN ASP ASN SER GLY ASP          
SEQRES  10 B  137  PRO VAL ASP PRO HIS LYS VAL TYR GLU LEU SER ARG GLU          
SEQRES  11 B  137  LEU GLY SER THR VAL GLY PRO                                  
SEQRES   1 C  137  GLY SER HIS MET ALA GLU VAL ARG GLY VAL GLN ARG VAL          
SEQRES   2 C  137  LEU PHE GLY ASP TRP LEU LEU GLY GLU VAL SER SER GLY          
SEQRES   3 C  137  GLN TYR GLU GLY LEU GLN TRP LEU ASN GLU ALA ARG THR          
SEQRES   4 C  137  VAL PHE ARG VAL PRO TRP LYS HIS PHE GLY ARG ARG ASP          
SEQRES   5 C  137  LEU ASP GLU GLU ASP ALA GLN ILE PHE LYS ALA TRP ALA          
SEQRES   6 C  137  VAL ALA ARG GLY ARG TRP PRO PRO SER GLY VAL ASN LEU          
SEQRES   7 C  137  PRO PRO PRO GLU ALA GLU ALA ALA GLU ARG ARG GLU ARG          
SEQRES   8 C  137  ARG GLY TRP LYS THR ASN PHE ARG CYS ALA LEU HIS SER          
SEQRES   9 C  137  THR GLY ARG PHE ILE LEU ARG GLN ASP ASN SER GLY ASP          
SEQRES  10 C  137  PRO VAL ASP PRO HIS LYS VAL TYR GLU LEU SER ARG GLU          
SEQRES  11 C  137  LEU GLY SER THR VAL GLY PRO                                  
HET     NA  A 135       1                                                       
HET     NA  B 135       1                                                       
HET    EDO  B 136       4                                                       
HET    EDO  B 137       4                                                       
HET    EDO  B 138       4                                                       
HET     NA  C 135       1                                                       
HET    EDO  C 136       4                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   4   NA    3(NA 1+)                                                     
FORMUL   6  EDO    4(C2 H6 O2)                                                  
FORMUL  11  HOH   *287(H2 O)                                                    
HELIX    1   1 LEU A   11  GLY A   23  1                                  13    
HELIX    2   2 ASP A   51  ASP A   54  5                                   4    
HELIX    3   3 ALA A   55  ARG A   65  1                                  11    
HELIX    4   4 PRO A   76  ARG A   86  1                                  11    
HELIX    5   5 GLU A   87  SER A  101  1                                  15    
HELIX    6   6 LEU B   11  GLY B   23  1                                  13    
HELIX    7   7 ASP B   51  ASP B   54  5                                   4    
HELIX    8   8 ALA B   55  ARG B   65  1                                  11    
HELIX    9   9 PRO B   76  SER B  101  1                                  26    
HELIX   10  10 LEU C   11  GLY C   23  1                                  13    
HELIX   11  11 GLU C   52  ASP C   54  5                                   3    
HELIX   12  12 ALA C   55  ARG C   65  1                                  11    
HELIX   13  13 PRO C   76  SER C  101  1                                  26    
SHEET    1   A 4 GLN A  29  TRP A  30  0                                        
SHEET    2   A 4 VAL A  37  PRO A  41 -1  O  ARG A  39   N  GLN A  29           
SHEET    3   A 4 HIS A 119  LEU A 124 -1  O  TYR A 122   N  PHE A  38           
SHEET    4   A 4 PHE A 105  ASN A 111 -1  N  ARG A 108   O  VAL A 121           
SHEET    1   B 4 GLN B  29  TRP B  30  0                                        
SHEET    2   B 4 VAL B  37  PRO B  41 -1  O  ARG B  39   N  GLN B  29           
SHEET    3   B 4 HIS B 119  LEU B 124 -1  O  TYR B 122   N  PHE B  38           
SHEET    4   B 4 PHE B 105  ASN B 111 -1  N  ARG B 108   O  VAL B 121           
SHEET    1   C 4 GLN C  29  TRP C  30  0                                        
SHEET    2   C 4 VAL C  37  PRO C  41 -1  O  ARG C  39   N  GLN C  29           
SHEET    3   C 4 HIS C 119  LEU C 124 -1  O  TYR C 122   N  PHE C  38           
SHEET    4   C 4 PHE C 105  ASN C 111 -1  N  ARG C 108   O  VAL C 121           
LINK         O   PHE B 105                NA    NA B 135     1555   1555  2.69  
LINK         O   LEU A  99                NA    NA A 135     1555   1555  2.76  
LINK         O   PHE C 105                NA    NA C 135     1555   1555  2.85  
LINK         O   LEU B  99                NA    NA B 135     1555   1555  2.91  
LINK         O   THR B 102                NA    NA B 135     1555   1555  2.93  
LINK         O   LEU C  99                NA    NA C 135     1555   1555  3.08  
LINK         O   THR A 102                NA    NA A 135     1555   1555  3.17  
LINK         O   PHE A 105                NA    NA A 135     1555   1555  3.18  
LINK        NA    NA C 135                 O   HOH C 145     1555   1555  2.39  
LINK        NA    NA B 135                 O   HOH B 162     1555   1555  2.91  
LINK        NA    NA A 135                 O   HOH A 199     1555   1555  2.95  
SITE     1 AC1  5 LEU A  99  HIS A 100  THR A 102  PHE A 105                    
SITE     2 AC1  5 HOH A 199                                                     
SITE     1 AC2  4 LEU B  99  THR B 102  PHE B 105  HOH B 162                    
SITE     1 AC3  4 LEU B 107  ARG B 108  HOH B 278  VAL C 116                    
SITE     1 AC4  4 GLY B  18  SER B  21  SER B  22  EDO B 138                    
SITE     1 AC5  4 SER B  21  TRP B  30  EDO B 137  HOH B 271                    
SITE     1 AC6  4 LEU C  99  THR C 102  PHE C 105  HOH C 145                    
SITE     1 AC7  9 LEU C  11  ASP C  14  TRP C  68  GLY C  72                    
SITE     2 AC7  9 VAL C  73  ALA C  80  GLU C  84  HOH C 194                    
SITE     3 AC7  9 HOH C 252                                                     
CRYST1   68.588   68.588   68.610  90.00  90.00 120.00 P 31          9          
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      0.014580  0.008418  0.000000        0.00000                         
SCALE2      0.000000  0.016835  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014575        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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