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Database: PDB
Entry: 6G2K
LinkDB: 6G2K
Original site: 6G2K 
HEADER    RNA BINDING PROTEIN                     23-MAR-18   6G2K              
TITLE     STRUCTURE OF HUR RRM3 IN COMPLEX WITH RNA (UUUUUU)                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3');                         
COMPND   3 CHAIN: R;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: ELAV-LIKE PROTEIN 1;                                       
COMPND   7 CHAIN: A, B, C;                                                      
COMPND   8 SYNONYM: HU-ANTIGEN R,HUR;                                           
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE   4 ORGANISM_TAXID: 32630;                                               
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 GENE: ELAVL1, HUR;                                                   
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    RNA BINDING PROTEIN                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.PABIS,M.SATTLER                                                     
REVDAT   2   15-MAY-19 6G2K    1       JRNL                                     
REVDAT   1   31-OCT-18 6G2K    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.    2.01 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 : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.98                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 17217                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 862                             
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) : 2.01                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1201                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.61                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1882                                    
REMARK   3   NUCLEIC ACID ATOMS       : 120                                     
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 177                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
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): 0.177         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.172         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.130         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.773         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2081 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1815 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2829 ; 1.767 ; 1.886       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4195 ; 1.118 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   247 ; 6.360 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    89 ;35.735 ;24.607       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   312 ;14.531 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;13.227 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   306 ; 0.139 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2255 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   459 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   973 ; 2.471 ; 2.656       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   972 ; 2.470 ; 2.654       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1213 ; 3.595 ; 3.959       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1214 ; 3.594 ; 3.962       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1108 ; 3.769 ; 3.138       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1108 ; 3.769 ; 3.138       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1613 ; 5.373 ; 4.564       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2342 ; 7.055 ;32.213       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2343 ; 7.054 ;32.241       
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   : 1.20                                          
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 6G2K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009326.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-APR-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               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18274                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.990                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.820                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5 AND 2.25 M AMMONIUM    
REMARK 280  SULPHATE, 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       39.87000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9510 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, A, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 150 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 4810 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
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     LYS A   323                                                      
REMARK 465     SER A   324                                                      
REMARK 465     HIS A   325                                                      
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     MET C   242                                                      
REMARK 465     LYS C   323                                                      
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     MET A 242    CG   SD   CE                                        
REMARK 470     GLN A 253    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 274    NZ                                                  
REMARK 470     ASN A 280    CG   OD1  ND2                                       
REMARK 470     THR A 281    OG1  CG2                                            
REMARK 470     LYS A 283    CG   CD   CE   NZ                                   
REMARK 470     MET B 242    CG   SD   CE                                        
REMARK 470     CME B 245    CZ   OH                                             
REMARK 470     ASN B 282    CG   OD1  ND2                                       
REMARK 470     LYS C 274    CE   NZ                                             
REMARK 470     ASN C 282    CG   OD1  ND2                                       
REMARK 470     GLN C 316    CD   OE1  NE2                                       
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   CE   CME B   245     O    HOH B   514              1.49            
REMARK 500   O    HOH C   432     O    HOH C   443              2.02            
REMARK 500   O    HOH B   501     O    HOH B   523              2.02            
REMARK 500   OE1  GLU B   257     O    HOH B   501              2.09            
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 250       40.62     92.72                                   
REMARK 500    ASN B 250       37.49     89.69                                   
REMARK 500    ASN B 282       18.62     54.77                                   
REMARK 500    ASN C 282        9.57     58.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401                 
DBREF  6G2K R    1     6  PDB    6G2K     6G2K             1      6             
DBREF  6G2K A  243   326  UNP    Q15717   ELAV1_HUMAN    270    353             
DBREF  6G2K B  243   326  UNP    Q15717   ELAV1_HUMAN    270    353             
DBREF  6G2K C  243   326  UNP    Q15717   ELAV1_HUMAN    270    353             
SEQADV 6G2K MET A  242  UNP  Q15717              INITIATING METHIONINE          
SEQADV 6G2K MET B  242  UNP  Q15717              INITIATING METHIONINE          
SEQADV 6G2K MET C  242  UNP  Q15717              INITIATING METHIONINE          
SEQRES   1 R    6    U   U   U   U   U   U                                      
SEQRES   1 A   85  MET GLY TRP CME ILE PHE ILE TYR ASN LEU GLY GLN ASP          
SEQRES   2 A   85  ALA ASP GLU GLY ILE LEU TRP GLN MET PHE GLY PRO PHE          
SEQRES   3 A   85  GLY ALA VAL THR ASN VAL LYS VAL ILE ARG ASP PHE ASN          
SEQRES   4 A   85  THR ASN LYS CYS LYS GLY PHE GLY PHE VAL THR MET THR          
SEQRES   5 A   85  ASN TYR GLU GLU ALA ALA MET ALA ILE ALA SER LEU ASN          
SEQRES   6 A   85  GLY TYR ARG LEU GLY ASP LYS ILE LEU GLN VAL SER PHE          
SEQRES   7 A   85  LYS THR ASN LYS SER HIS LYS                                  
SEQRES   1 B   85  MET GLY TRP CME ILE PHE ILE TYR ASN LEU GLY GLN ASP          
SEQRES   2 B   85  ALA ASP GLU GLY ILE LEU TRP GLN MET PHE GLY PRO PHE          
SEQRES   3 B   85  GLY ALA VAL THR ASN VAL LYS VAL ILE ARG ASP PHE ASN          
SEQRES   4 B   85  THR ASN LYS CYS LYS GLY PHE GLY PHE VAL THR MET THR          
SEQRES   5 B   85  ASN TYR GLU GLU ALA ALA MET ALA ILE ALA SER LEU ASN          
SEQRES   6 B   85  GLY TYR ARG LEU GLY ASP LYS ILE LEU GLN VAL SER PHE          
SEQRES   7 B   85  LYS THR ASN LYS SER HIS LYS                                  
SEQRES   1 C   85  MET GLY TRP CME ILE PHE ILE TYR ASN LEU GLY GLN ASP          
SEQRES   2 C   85  ALA ASP GLU GLY ILE LEU TRP GLN MET PHE GLY PRO PHE          
SEQRES   3 C   85  GLY ALA VAL THR ASN VAL LYS VAL ILE ARG ASP PHE ASN          
SEQRES   4 C   85  THR ASN LYS CYS LYS GLY PHE GLY PHE VAL THR MET THR          
SEQRES   5 C   85  ASN TYR GLU GLU ALA ALA MET ALA ILE ALA SER LEU ASN          
SEQRES   6 C   85  GLY TYR ARG LEU GLY ASP LYS ILE LEU GLN VAL SER PHE          
SEQRES   7 C   85  LYS THR ASN LYS SER HIS LYS                                  
MODRES 6G2K CME A  245  CYS  MODIFIED RESIDUE                                   
MODRES 6G2K CME B  245  CYS  MODIFIED RESIDUE                                   
MODRES 6G2K CME C  245  CYS  MODIFIED RESIDUE                                   
HET    CME  A 245      10                                                       
HET    CME  B 245       8                                                       
HET    CME  C 245      10                                                       
HET    SO4  B 401       5                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  CME    3(C5 H11 N O3 S2)                                            
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *177(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  PHE A 319 -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  PHE B 289   N  LYS B 274           
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  GLN B 316   N  TYR B 249           
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  LYS C 285   N  ILE C 276           
SHEET    3 AA5 4 TRP C 244  TYR C 249 -1  N  TRP C 244   O  MET C 292           
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         C   TRP A 244                 N   CME A 245     1555   1555  1.32  
LINK         C   CME A 245                 N   ILE A 246     1555   1555  1.32  
LINK         C   TRP B 244                 N   CME B 245     1555   1555  1.34  
LINK         C   CME B 245                 N   ILE B 246     1555   1555  1.34  
LINK         C   TRP C 244                 N   CME C 245     1555   1555  1.33  
LINK         C   CME C 245                 N   ILE C 246     1555   1555  1.33  
SITE     1 AC1  5 TRP B 244  THR B 293  ASN B 294  TYR B 295                    
SITE     2 AC1  5 HOH B 516                                                     
CRYST1   34.310   79.740   51.070  90.00  93.14  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      0.029146  0.000000  0.001599        0.00000                         
SCALE2      0.000000  0.012541  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019610        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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