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Database: PDB
Entry: 6GD3
LinkDB: 6GD3
Original site: 6GD3 
HEADER    RNA BINDING PROTEIN                     21-APR-18   6GD3              
TITLE     STRUCTURE OF HUR RRM3 IN COMPLEX WITH RNA (UAUUUA)                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELAV-LIKE PROTEIN 1;                                       
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: HU-ANTIGEN R,HUR;                                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: RNA (5'-R(P*UP*AP*UP*UP*UP*A)-3');                         
COMPND   8 CHAIN: P;                                                            
COMPND   9 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 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    RNA BINDING PROTEIN                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.PABIS,M.SATTLER                                                     
REVDAT   2   15-MAY-19 6GD3    1       JRNL                                     
REVDAT   1   31-OCT-18 6GD3    0                                                
JRNL        AUTH   M.PABIS,G.M.POPOWICZ,R.STEHLE,D.FERNANDEZ-RAMOS,S.ASAMI,     
JRNL        AUTH 2 L.WARNER,S.M.GARCIA-MAURINO,A.SCHLUNDT,M.L.MARTINEZ-CHANTAR, 
JRNL        AUTH 3 I.DIAZ-MORENO,M.SATTLER                                      
JRNL        TITL   HUR BIOLOGICAL FUNCTION INVOLVES RRM3-MEDIATED DIMERIZATION  
JRNL        TITL 2 AND RNA BINDING BY ALL THREE RRMS.                           
JRNL        REF    NUCLEIC ACIDS RES.            V.  47  1011 2019              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   30418581                                                     
JRNL        DOI    10.1093/NAR/GKY1138                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.04                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 59206                          
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3025                            
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) : 1.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.38                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4086                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 228                          
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1946                                    
REMARK   3   NUCLEIC ACID ATOMS       : 124                                     
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 297                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.050         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.053         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.038         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.932         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.970                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2198 ; 0.027 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1917 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3008 ; 2.330 ; 1.877       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4465 ; 1.160 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   271 ; 6.250 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    99 ;39.563 ;24.848       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   346 ;13.565 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ; 8.315 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   320 ; 0.139 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2424 ; 0.014 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   492 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1021 ; 2.306 ; 1.963       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1020 ; 2.296 ; 1.961       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1277 ; 3.293 ; 2.937       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1278 ; 3.292 ; 2.940       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1177 ; 3.600 ; 2.497       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1178 ; 3.599 ; 2.498       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1719 ; 5.169 ; 3.595       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2555 ; 6.702 ;24.917       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2491 ; 6.572 ;24.263       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6GD3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009547.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.007                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62913                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 6.040                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.360                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.180                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, MOLREP                                        
REMARK 200 STARTING MODEL: 6GD1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.01 M CALCIUM   
REMARK 280  CHLORIDE, 0.05 M SODIUM CACODYLATE PH 6.5 AND 10 % (W/V) PEG        
REMARK 280  4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K               
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       39.96500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, P                               
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   240                                                      
REMARK 465     ALA A   241                                                      
REMARK 465     MET A   242                                                      
REMARK 465     LYS A   326                                                      
REMARK 465     LYS B   323                                                      
REMARK 465     SER B   324                                                      
REMARK 465     HIS B   325                                                      
REMARK 465     LYS B   326                                                      
REMARK 465     SER C   324                                                      
REMARK 465     HIS C   325                                                      
REMARK 465     LYS C   326                                                      
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     LYS A 323    CG   CD   CE   NZ                                   
REMARK 470     LYS C 283    CE   NZ                                             
REMARK 470     ASP C 312    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   560     O    HOH A   592              1.47            
REMARK 500   O    HOH C   413     O    HOH C   454              1.51            
REMARK 500   OD1  ASN B   272     O    HOH B   401              1.63            
REMARK 500   OE2  GLU B   257     O    HOH B   402              1.71            
REMARK 500   O    HOH A   620     O    HOH A   628              1.78            
REMARK 500   O    HOH C   428     O    HOH C   449              1.84            
REMARK 500   ND2  ASN B   272     O    HOH B   403              1.91            
REMARK 500   O    HOH A   519     O    HOH A   582              1.98            
REMARK 500   O    HOH A   547     O    HOH A   592              2.00            
REMARK 500   OH   TYR A   308     O    HOH A   501              2.01            
REMARK 500   O    SER A   324     O    HOH A   502              2.11            
REMARK 500   O    HOH A   624     O    HOH A   633              2.16            
REMARK 500   O    HOH B   469     O    HOH B   476              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   577     O    HOH B   458     2756     1.27            
REMARK 500   O    HOH A   567     O    HOH C   401     2655     1.47            
REMARK 500   O    HOH A   617     O    HOH C   474     1655     2.16            
REMARK 500   O    HOH A   632     O    HOH A   633     1455     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A 295   CG    TYR A 295   CD1    -0.080                       
REMARK 500    GLU A 296   CG    GLU A 296   CD      0.099                       
REMARK 500    GLU A 296   CD    GLU A 296   OE1     0.077                       
REMARK 500    TRP B 244   CE3   TRP B 244   CZ3     0.103                       
REMARK 500    GLU B 297   CD    GLU B 297   OE1    -0.078                       
REMARK 500    GLY B 307   N     GLY B 307   CA      0.091                       
REMARK 500    TYR C 249   CE1   TYR C 249   CZ     -0.102                       
REMARK 500    TYR C 295   CZ    TYR C 295   CE2    -0.083                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    MET A 263   CG  -  SD  -  CE  ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ARG A 277   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 277   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    MET C 263   CG  -  SD  -  CE  ANGL. DEV. = -10.7 DEGREES          
REMARK 500    CYS C 284   CA  -  CB  -  SG  ANGL. DEV. =   6.6 DEGREES          
REMARK 500      U P   4   O5' -  P   -  OP2 ANGL. DEV. = -11.1 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    ASN A 282       16.15     58.58                                   
REMARK 500    ASN B 250       28.72     84.28                                   
REMARK 500    ASN C 250       31.21     87.34                                   
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 A 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 279   O                                                      
REMARK 620 2 HOH C 442   O    92.0                                              
REMARK 620 N                    1                                               
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 401                  
DBREF  6GD3 A  243   326  UNP    Q15717   ELAV1_HUMAN    243    326             
DBREF  6GD3 B  243   326  UNP    Q15717   ELAV1_HUMAN    243    326             
DBREF  6GD3 C  243   326  UNP    Q15717   ELAV1_HUMAN    243    326             
DBREF  6GD3 P    1     6  PDB    6GD3     6GD3             1      6             
SEQADV 6GD3 GLY A  240  UNP  Q15717              EXPRESSION TAG                 
SEQADV 6GD3 ALA A  241  UNP  Q15717              EXPRESSION TAG                 
SEQADV 6GD3 MET A  242  UNP  Q15717              EXPRESSION TAG                 
SEQADV 6GD3 GLY B  240  UNP  Q15717              EXPRESSION TAG                 
SEQADV 6GD3 ALA B  241  UNP  Q15717              EXPRESSION TAG                 
SEQADV 6GD3 MET B  242  UNP  Q15717              EXPRESSION TAG                 
SEQADV 6GD3 GLY C  240  UNP  Q15717              EXPRESSION TAG                 
SEQADV 6GD3 ALA C  241  UNP  Q15717              EXPRESSION TAG                 
SEQADV 6GD3 MET C  242  UNP  Q15717              EXPRESSION TAG                 
SEQRES   1 A   87  GLY ALA MET GLY TRP CYS ILE PHE ILE TYR ASN LEU GLY          
SEQRES   2 A   87  GLN ASP ALA ASP GLU GLY ILE LEU TRP GLN MET PHE GLY          
SEQRES   3 A   87  PRO PHE GLY ALA VAL THR ASN VAL LYS VAL ILE ARG ASP          
SEQRES   4 A   87  PHE ASN THR ASN LYS CYS LYS GLY PHE GLY PHE VAL THR          
SEQRES   5 A   87  MET THR ASN TYR GLU GLU ALA ALA MET ALA ILE ALA SER          
SEQRES   6 A   87  LEU ASN GLY TYR ARG LEU GLY ASP LYS ILE LEU GLN VAL          
SEQRES   7 A   87  SER PHE LYS THR ASN LYS SER HIS LYS                          
SEQRES   1 B   87  GLY ALA MET GLY TRP CYS ILE PHE ILE TYR ASN LEU GLY          
SEQRES   2 B   87  GLN ASP ALA ASP GLU GLY ILE LEU TRP GLN MET PHE GLY          
SEQRES   3 B   87  PRO PHE GLY ALA VAL THR ASN VAL LYS VAL ILE ARG ASP          
SEQRES   4 B   87  PHE ASN THR ASN LYS CYS LYS GLY PHE GLY PHE VAL THR          
SEQRES   5 B   87  MET THR ASN TYR GLU GLU ALA ALA MET ALA ILE ALA SER          
SEQRES   6 B   87  LEU ASN GLY TYR ARG LEU GLY ASP LYS ILE LEU GLN VAL          
SEQRES   7 B   87  SER PHE LYS THR ASN LYS SER HIS LYS                          
SEQRES   1 C   87  GLY ALA MET GLY TRP CYS ILE PHE ILE TYR ASN LEU GLY          
SEQRES   2 C   87  GLN ASP ALA ASP GLU GLY ILE LEU TRP GLN MET PHE GLY          
SEQRES   3 C   87  PRO PHE GLY ALA VAL THR ASN VAL LYS VAL ILE ARG ASP          
SEQRES   4 C   87  PHE ASN THR ASN LYS CYS LYS GLY PHE GLY PHE VAL THR          
SEQRES   5 C   87  MET THR ASN TYR GLU GLU ALA ALA MET ALA ILE ALA SER          
SEQRES   6 C   87  LEU ASN GLY TYR ARG LEU GLY ASP LYS ILE LEU GLN VAL          
SEQRES   7 C   87  SER PHE LYS THR ASN LYS SER HIS LYS                          
SEQRES   1 P    6    U   A   U   U   U   A                                      
HET     NA  A 401       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   5   NA    NA 1+                                                        
FORMUL   6  HOH   *297(H2 O)                                                    
HELIX    1 AA1 ASP A  256  GLY A  265  1                                  10    
HELIX    2 AA2 PRO A  266  GLY A  268  5                                   3    
HELIX    3 AA3 ASN A  294  ASN A  306  1                                  13    
HELIX    4 AA4 ASP B  256  GLY B  265  1                                  10    
HELIX    5 AA5 PRO B  266  GLY B  268  5                                   3    
HELIX    6 AA6 ASN B  294  ASN B  306  1                                  13    
HELIX    7 AA7 ASP C  256  GLY C  265  1                                  10    
HELIX    8 AA8 PRO C  266  GLY C  268  5                                   3    
HELIX    9 AA9 ASN C  294  ASN C  306  1                                  13    
SHEET    1 AA1 4 VAL A 270  ARG A 277  0                                        
SHEET    2 AA1 4 CYS A 284  MET A 292 -1  O  LYS A 285   N  ILE A 276           
SHEET    3 AA1 4 TRP A 244  TYR A 249 -1  N  ILE A 246   O  VAL A 290           
SHEET    4 AA1 4 GLN A 316  SER A 318 -1  O  SER A 318   N  PHE A 247           
SHEET    1 AA2 2 ARG A 309  LEU A 310  0                                        
SHEET    2 AA2 2 LYS A 313  ILE A 314 -1  O  LYS A 313   N  LEU A 310           
SHEET    1 AA3 4 VAL B 270  ARG B 277  0                                        
SHEET    2 AA3 4 CYS B 284  MET B 292 -1  O  LYS B 285   N  ILE B 276           
SHEET    3 AA3 4 TRP B 244  TYR B 249 -1  N  ILE B 246   O  VAL B 290           
SHEET    4 AA3 4 GLN B 316  PHE B 319 -1  O  SER B 318   N  PHE B 247           
SHEET    1 AA4 2 ARG B 309  LEU B 310  0                                        
SHEET    2 AA4 2 LYS B 313  ILE B 314 -1  O  LYS B 313   N  LEU B 310           
SHEET    1 AA5 4 VAL C 270  ARG C 277  0                                        
SHEET    2 AA5 4 CYS C 284  MET C 292 -1  O  THR C 291   N  ASN C 272           
SHEET    3 AA5 4 TRP C 244  TYR C 249 -1  N  ILE C 246   O  VAL C 290           
SHEET    4 AA5 4 GLN C 316  PHE C 319 -1  O  SER C 318   N  PHE C 247           
SHEET    1 AA6 2 ARG C 309  LEU C 310  0                                        
SHEET    2 AA6 2 LYS C 313  ILE C 314 -1  O  LYS C 313   N  LEU C 310           
LINK         O   PHE A 279                NA    NA A 401     1555   1555  2.98  
LINK        NA    NA A 401                 O   HOH C 442     1555   2555  2.76  
CISPEP   1 ASN C  322    LYS C  323          0         2.11                     
SITE     1 AC1  2 PHE A 279  ASN A 280                                          
CRYST1   33.740   79.930   54.870  90.00  90.63  90.00 P 1 21 1      6          
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      0.029638  0.000000  0.000327        0.00000                         
SCALE2      0.000000  0.012511  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018226        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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