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Database: PDB
Entry: 3HI9
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Original site: 3HI9 
HEADER    TRANSCRIPTION                           19-MAY-09   3HI9              
TITLE     THE X-RAY CRYSTAL STRUCTURE OF THE FIRST RNA RECOGNITION              
TITLE    2 MOTIF (RRM1) OF THE AU-RICH ELEMENT (ARE) BINDING PROTEIN            
TITLE    3 HUR AT 2.0 ANGSTROM RESOLUTION                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELAV-LIKE PROTEIN 1;                                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RRM1 DOMAIN: UNP RESIDUES 18-99;                           
COMPND   5 SYNONYM: HU-ANTIGEN R, HUR;                                          
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ELAVL1, HUR;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    BETA1-ALPHA1-BETA2-BETA3-ALPHA2-BETA4 TOPOLOGY, METHYLATION,          
KEYWDS   2 PHOSPHOPROTEIN, RNA-BINDING, TRANSCRIPTION                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.M.BENOIT,J.KALLEN                                                   
REVDAT   2   07-APR-10 3HI9    1       JRNL                                     
REVDAT   1   31-MAR-10 3HI9    0                                                
JRNL        AUTH   R.M.BENOIT,N.C.MEISNER,J.KALLEN,P.GRAFF,R.HEMMIG,            
JRNL        AUTH 2 R.CEBE,C.OSTERMEIER,H.WIDMER,M.AUER                          
JRNL        TITL   THE X-RAY CRYSTAL STRUCTURE OF THE FIRST RNA                 
JRNL        TITL 2 RECOGNITION MOTIF AND SITE-DIRECTED MUTAGENESIS              
JRNL        TITL 3 SUGGEST A POSSIBLE HUR REDOX SENSING MECHANISM.              
JRNL        REF    J.MOL.BIOL.                   V. 397  1231 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20219472                                                     
JRNL        DOI    10.1016/J.JMB.2010.02.043                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0063                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 32762                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1639                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2239                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.45                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 118                          
REMARK   3   BIN FREE R VALUE                    : 0.3450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2504                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 197                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
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): 0.147         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.139         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.104         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.764         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2539 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3430 ; 1.361 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   324 ; 5.276 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   119 ;36.591 ;23.529       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   470 ;14.225 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;15.798 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   398 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1887 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1574 ; 0.942 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2536 ; 1.818 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   965 ; 2.769 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   887 ; 4.815 ; 4.500       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS. 2. U VALUES: REFINED INDIVIDUALLY.                
REMARK   4                                                                      
REMARK   4 3HI9 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053166.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUN-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00778                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32767                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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 1FXL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M DI-AMMONIUM CITRATE, 20% W/V       
REMARK 280  PEG 3350, 5% GLYCEROL, PH 5.6, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
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       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.12033            
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       98.24067            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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       98.24067            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       49.12033            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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 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 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     ARG A    97                                                      
REMARK 465     PRO A    98                                                      
REMARK 465     SER A    99                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     PRO B    17                                                      
REMARK 465     ASP B    54                                                      
REMARK 465     LYS B    55                                                      
REMARK 465     VAL B    56                                                      
REMARK 465     ALA B    57                                                      
REMARK 465     GLY B    58                                                      
REMARK 465     HIS B    59                                                      
REMARK 465     SER B    99                                                      
REMARK 465     GLY C    16                                                      
REMARK 465     PRO C    17                                                      
REMARK 465     ARG C    97                                                      
REMARK 465     PRO C    98                                                      
REMARK 465     SER C    99                                                      
REMARK 465     GLY D    16                                                      
REMARK 465     PRO D    17                                                      
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    TYR A  26       41.64     72.32                                   
REMARK 500    GLN A  87     -122.43     45.21                                   
REMARK 500    TYR B  26       44.85     70.32                                   
REMARK 500    GLN B  87     -116.70     56.65                                   
REMARK 500    GLN C  87       61.92     34.86                                   
REMARK 500    SER C  88       -1.12     71.74                                   
REMARK 500    VAL D  56      -73.79    -95.88                                   
REMARK 500    ALA D  57       -1.13    -58.75                                   
REMARK 500    GLN D  87     -113.17     51.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FXL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUD AND AU-RICH ELEMENT OF THE C-FOS            
REMARK 900 RNA                                                                  
DBREF  3HI9 A   18    99  UNP    Q15717   ELAV1_HUMAN     18     99             
DBREF  3HI9 B   18    99  UNP    Q15717   ELAV1_HUMAN     18     99             
DBREF  3HI9 C   18    99  UNP    Q15717   ELAV1_HUMAN     18     99             
DBREF  3HI9 D   18    99  UNP    Q15717   ELAV1_HUMAN     18     99             
SEQADV 3HI9 GLY A   16  UNP  Q15717              EXPRESSION TAG                 
SEQADV 3HI9 PRO A   17  UNP  Q15717              EXPRESSION TAG                 
SEQADV 3HI9 GLY B   16  UNP  Q15717              EXPRESSION TAG                 
SEQADV 3HI9 PRO B   17  UNP  Q15717              EXPRESSION TAG                 
SEQADV 3HI9 GLY C   16  UNP  Q15717              EXPRESSION TAG                 
SEQADV 3HI9 PRO C   17  UNP  Q15717              EXPRESSION TAG                 
SEQADV 3HI9 GLY D   16  UNP  Q15717              EXPRESSION TAG                 
SEQADV 3HI9 PRO D   17  UNP  Q15717              EXPRESSION TAG                 
SEQRES   1 A   84  GLY PRO GLY ARG THR ASN LEU ILE VAL ASN TYR LEU PRO          
SEQRES   2 A   84  GLN ASN MET THR GLN ASP GLU LEU ARG SER LEU PHE SER          
SEQRES   3 A   84  SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE ARG ASP          
SEQRES   4 A   84  LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE VAL ASN          
SEQRES   5 A   84  TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE ASN THR          
SEQRES   6 A   84  LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE LYS VAL          
SEQRES   7 A   84  SER TYR ALA ARG PRO SER                                      
SEQRES   1 B   84  GLY PRO GLY ARG THR ASN LEU ILE VAL ASN TYR LEU PRO          
SEQRES   2 B   84  GLN ASN MET THR GLN ASP GLU LEU ARG SER LEU PHE SER          
SEQRES   3 B   84  SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE ARG ASP          
SEQRES   4 B   84  LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE VAL ASN          
SEQRES   5 B   84  TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE ASN THR          
SEQRES   6 B   84  LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE LYS VAL          
SEQRES   7 B   84  SER TYR ALA ARG PRO SER                                      
SEQRES   1 C   84  GLY PRO GLY ARG THR ASN LEU ILE VAL ASN TYR LEU PRO          
SEQRES   2 C   84  GLN ASN MET THR GLN ASP GLU LEU ARG SER LEU PHE SER          
SEQRES   3 C   84  SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE ARG ASP          
SEQRES   4 C   84  LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE VAL ASN          
SEQRES   5 C   84  TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE ASN THR          
SEQRES   6 C   84  LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE LYS VAL          
SEQRES   7 C   84  SER TYR ALA ARG PRO SER                                      
SEQRES   1 D   84  GLY PRO GLY ARG THR ASN LEU ILE VAL ASN TYR LEU PRO          
SEQRES   2 D   84  GLN ASN MET THR GLN ASP GLU LEU ARG SER LEU PHE SER          
SEQRES   3 D   84  SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE ARG ASP          
SEQRES   4 D   84  LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE VAL ASN          
SEQRES   5 D   84  TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE ASN THR          
SEQRES   6 D   84  LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE LYS VAL          
SEQRES   7 D   84  SER TYR ALA ARG PRO SER                                      
FORMUL   5  HOH   *197(H2 O)                                                    
HELIX    1   1 THR A   32  SER A   42  1                                  11    
HELIX    2   2 THR A   70  ASN A   82  1                                  13    
HELIX    3   3 THR B   32  SER B   42  1                                  11    
HELIX    4   4 THR B   70  ASN B   82  1                                  13    
HELIX    5   5 THR C   32  SER C   42  1                                  11    
HELIX    6   6 THR C   70  ASN C   82  1                                  13    
HELIX    7   7 THR D   32  SER D   42  1                                  11    
HELIX    8   8 THR D   70  ASN D   82  1                                  13    
SHEET    1   A 4 VAL A  46  ARG A  53  0                                        
SHEET    2   A 4 SER A  60  TYR A  68 -1  O  ASN A  67   N  SER A  48           
SHEET    3   A 4 ASN A  21  ASN A  25 -1  N  LEU A  22   O  VAL A  66           
SHEET    4   A 4 LYS A  92  TYR A  95 -1  O  LYS A  92   N  ASN A  25           
SHEET    1   B 2 ARG A  85  LEU A  86  0                                        
SHEET    2   B 2 LYS A  89  THR A  90 -1  O  LYS A  89   N  LEU A  86           
SHEET    1   C 4 VAL B  46  LEU B  51  0                                        
SHEET    2   C 4 TYR B  63  TYR B  68 -1  O  ASN B  67   N  GLU B  47           
SHEET    3   C 4 ASN B  21  ASN B  25 -1  N  VAL B  24   O  GLY B  64           
SHEET    4   C 4 LYS B  92  TYR B  95 -1  O  SER B  94   N  ILE B  23           
SHEET    1   D 2 ARG B  85  LEU B  86  0                                        
SHEET    2   D 2 LYS B  89  THR B  90 -1  O  LYS B  89   N  LEU B  86           
SHEET    1   E 4 VAL C  46  ARG C  53  0                                        
SHEET    2   E 4 SER C  60  TYR C  68 -1  O  LEU C  61   N  ILE C  52           
SHEET    3   E 4 ASN C  21  ASN C  25 -1  N  LEU C  22   O  VAL C  66           
SHEET    4   E 4 LYS C  92  TYR C  95 -1  O  SER C  94   N  ILE C  23           
SHEET    1   F 2 ARG C  85  LEU C  86  0                                        
SHEET    2   F 2 LYS C  89  THR C  90 -1  O  LYS C  89   N  LEU C  86           
SHEET    1   G 4 VAL D  46  ARG D  53  0                                        
SHEET    2   G 4 SER D  60  TYR D  68 -1  O  TYR D  63   N  ILE D  52           
SHEET    3   G 4 ASN D  21  ASN D  25 -1  N  LEU D  22   O  VAL D  66           
SHEET    4   G 4 LYS D  92  TYR D  95 -1  O  SER D  94   N  ILE D  23           
SHEET    1   H 2 ARG D  85  LEU D  86  0                                        
SHEET    2   H 2 LYS D  89  THR D  90 -1  O  LYS D  89   N  LEU D  86           
CRYST1   74.804   74.804  147.361  90.00  90.00 120.00 P 31 2 1     24          
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      0.013368  0.007718  0.000000        0.00000                         
SCALE2      0.000000  0.015436  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006786        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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