GenomeNet

Database: PDB
Entry: 4FXV
LinkDB: 4FXV
Original site: 4FXV 
HEADER    RNA BINDING PROTEIN, TRANSCRIPTION      03-JUL-12   4FXV              
TITLE     CRYSTAL STRUCTURE OF AN ELAV-LIKE PROTEIN 1 (ELAVL1) FROM HOMO SAPIENS
TITLE    2 AT 1.90 A RESOLUTION                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELAV-LIKE PROTEIN 1;                                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RRM 1 DOMAIN RESIDUES 20-99;                               
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: BC003376, ELAVL1, HUR;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: PB1;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    RNA RECOGNITION MOTIF, PUTATIVE RNA-BINDING DOMAIN, TRANSCRIPTION,    
KEYWDS   2 STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,     
KEYWDS   3 PROTEIN STRUCTURE INITIATIVE, PSI-BIOLOGY, RNA BINDING PROTEIN,      
KEYWDS   4 PARTNERSHIP FOR T-CELL BIOLOGY, TCELL                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG),PARTNERSHIP FOR T-CELL    
AUTHOR   2 BIOLOGY,PARTNERSHIP FOR T-CELL BIOLOGY (TCELL)                       
REVDAT   2   15-NOV-17 4FXV    1       REMARK                                   
REVDAT   1   03-OCT-12 4FXV    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG),                 
JRNL        AUTH 2 PARTNERSHIP FOR T-CELL BIOLOGY                               
JRNL        TITL   CRYSTAL STRUCTURE OF AN ELAV-LIKE PROTEIN 1 (ELAVL1) FROM    
JRNL        TITL 2 HOMO SAPIENS AT 1.90 A RESOLUTION                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 33271                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1684                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1645                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.6640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 89                           
REMARK   3   BIN FREE R VALUE                    : 0.6630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2492                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 317                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.88                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.03000                                              
REMARK   3    B22 (A**2) : 1.03000                                              
REMARK   3    B33 (A**2) : -1.54000                                             
REMARK   3    B12 (A**2) : 0.51000                                              
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): 0.152         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.094         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2638 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1783 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3588 ; 1.781 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4347 ; 1.051 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   351 ; 3.794 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   126 ;32.347 ;23.810       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   461 ;12.312 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;12.459 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   414 ; 0.103 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3002 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   553 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -3        A    99                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.8406  49.1624   6.5886              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1117 T22:   0.0113                                     
REMARK   3      T33:   0.0335 T12:  -0.0027                                     
REMARK   3      T13:  -0.0308 T23:   0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5458 L22:   4.9835                                     
REMARK   3      L33:   5.9605 L12:   0.6017                                     
REMARK   3      L13:   0.8206 L23:   1.0567                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0346 S12:  -0.1950 S13:  -0.0513                       
REMARK   3      S21:   0.2046 S22:  -0.0325 S23:  -0.0105                       
REMARK   3      S31:   0.1094 S32:  -0.0009 S33:  -0.0021                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -2        B    97                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3326  51.9712  31.9972              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1941 T22:   0.0282                                     
REMARK   3      T33:   0.0969 T12:   0.0182                                     
REMARK   3      T13:  -0.0435 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9562 L22:   4.9705                                     
REMARK   3      L33:   5.5439 L12:   0.3744                                     
REMARK   3      L13:   0.4532 L23:   1.6144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0148 S12:   0.0071 S13:  -0.0206                       
REMARK   3      S21:  -0.0023 S22:   0.0733 S23:   0.1948                       
REMARK   3      S31:   0.4383 S32:  -0.0364 S33:  -0.0584                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    -3        C    99                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.1332  72.7015  13.6955              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0705 T22:   0.0082                                     
REMARK   3      T33:   0.0268 T12:  -0.0099                                     
REMARK   3      T13:   0.0087 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3953 L22:   4.4061                                     
REMARK   3      L33:   4.4323 L12:  -1.2764                                     
REMARK   3      L13:  -0.7850 L23:   0.6114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0598 S12:  -0.0819 S13:  -0.0858                       
REMARK   3      S21:   0.0126 S22:   0.0130 S23:  -0.0494                       
REMARK   3      S31:   0.2280 S32:  -0.0744 S33:  -0.0728                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     0        D    96                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.0221  59.8244  40.6779              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1475 T22:   0.1578                                     
REMARK   3      T33:   0.1747 T12:   0.0622                                     
REMARK   3      T13:  -0.0553 T23:  -0.0654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6452 L22:   5.0658                                     
REMARK   3      L33:   4.0144 L12:  -0.1718                                     
REMARK   3      L13:  -0.3315 L23:   0.7855                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0692 S12:  -0.1746 S13:  -0.0306                       
REMARK   3      S21:   0.2441 S22:   0.1332 S23:  -0.5220                       
REMARK   3      S31:   0.3291 S32:   0.5945 S33:  -0.2023                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR         
REMARK   3  SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE       
REMARK   3  OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO        
REMARK   3  0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET          
REMARK   3  INCORPORATION. 3. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B    
REMARK   3  FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U           
REMARK   3  FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT.     
REMARK   3  5. 309 UNUSUALLY STRONG REFLECTIONS WITH I/<I> > 15, MOSTLY NEAR    
REMARK   3  ICE RINGS AT RESOLUTION 2.25A, 2.24A, 3.46A AND 2.64A, WERE         
REMARK   3  EXCLUDED FROM THE FINAL REFINEMENT. 6. EXPERIMENTAL PHASES (SAD)    
REMARK   3  WERE USED AS RESTRAINTS DURING STRUCTURE REFINEMENT.                
REMARK   4                                                                      
REMARK   4 4FXV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073488.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97923                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : VERTICAL FOCUSING MIRROR; DOUBLE   
REMARK 200                                   CRYSTAL SI(111) MONOCHROMATOR      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.20                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34829                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.823                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 10.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX, SHARP, SHELXD                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE DATA COLLECTION STATISTICS IN REMARK 200 ABOVE ARE       
REMARK 200  BEFORE THE REJECTION OF 309 UNUSUALLY STRONG REFLECTIONS WITH I/<   
REMARK 200  I> > 15, MOSTLY NEAR ICE RINGS AT RESOLUTION 2.25A, 2.24A 3.46A     
REMARK 200  AND 2.64A, WHICH WERE EXCLUDED FROM THE FINAL REFINEMENT.           
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.200M NH4CL, 20.00% PEG-3350, NO        
REMARK 280  BUFFER PH 6.3, NANODROP, VAPOR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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       90.98567            
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      181.97133            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      136.47850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      227.46417            
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       45.49283            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.98567            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      181.97133            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      227.46417            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      136.47850            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       45.49283            
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 300 REMARK: CRYSTAL PACKING ANALYSIS SUGGEST THE ASSIGNMENT OF A         
REMARK 300 MONOMER AS THE SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.        
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 102  LIES ON A SPECIAL POSITION.                          
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     MSE A   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     ASP A   -15                                                      
REMARK 465     LYS A   -14                                                      
REMARK 465     ILE A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     MSE B   -18                                                      
REMARK 465     GLY B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     ASP B   -15                                                      
REMARK 465     LYS B   -14                                                      
REMARK 465     ILE B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     ASN B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     TYR B    -3                                                      
REMARK 465     PRO B    98                                                      
REMARK 465     SER B    99                                                      
REMARK 465     MSE C   -18                                                      
REMARK 465     GLY C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     ASP C   -15                                                      
REMARK 465     LYS C   -14                                                      
REMARK 465     ILE C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     GLU C    -6                                                      
REMARK 465     ASN C    -5                                                      
REMARK 465     LEU C    -4                                                      
REMARK 465     VAL C    56                                                      
REMARK 465     ALA C    57                                                      
REMARK 465     MSE D   -18                                                      
REMARK 465     GLY D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     ASP D   -15                                                      
REMARK 465     LYS D   -14                                                      
REMARK 465     ILE D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     GLU D    -6                                                      
REMARK 465     ASN D    -5                                                      
REMARK 465     LEU D    -4                                                      
REMARK 465     TYR D    -3                                                      
REMARK 465     PHE D    -2                                                      
REMARK 465     GLN D    -1                                                      
REMARK 465     ARG D    97                                                      
REMARK 465     PRO D    98                                                      
REMARK 465     SER D    99                                                      
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     TYR A  -3    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A  50    CD   CE   NZ                                        
REMARK 470     LYS A  55    CG   CD   CE   NZ                                   
REMARK 470     VAL A  56    CG1  CG2                                            
REMARK 470     LYS B  55    CD   CE   NZ                                        
REMARK 470     LYS B  72    CE   NZ                                             
REMARK 470     ARG B  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  55    CG   CD   CE   NZ                                   
REMARK 470     ARG C  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER C  99    OG                                                  
REMARK 470     LYS D  50    CG   CD   CE   NZ                                   
REMARK 470     LYS D  55    CG   CD   CE   NZ                                   
REMARK 470     VAL D  56    CG1  CG2                                            
REMARK 470     HIS D  59    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D  72    CG   CD   CE   NZ                                   
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    LYS C  89   CD  -  CE  -  NZ  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    SER C  99   C   -  N   -  CA  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    SER C  99   N   -  CA  -  C   ANGL. DEV. =  20.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  56      -70.77    -60.55                                   
REMARK 500    GLN A  87     -121.26     53.54                                   
REMARK 500    GLN B  87     -120.39     49.95                                   
REMARK 500    GLN C  87     -115.11     50.39                                   
REMARK 500    VAL D  56      -66.50    -92.02                                   
REMARK 500    GLN D  87     -119.30     55.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: JCSG-422502   RELATED DB: TARGETTRACK                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS CONSTRUCT (RESIDUES 20-99) WAS EXPRESSED WITH A PURIFICATION    
REMARK 999 TAG MGSDKIHHHHHHENLYFQG.                                             
DBREF  4FXV A   20    99  UNP    Q15717   ELAV1_HUMAN     20     99             
DBREF  4FXV B   20    99  UNP    Q15717   ELAV1_HUMAN     20     99             
DBREF  4FXV C   20    99  UNP    Q15717   ELAV1_HUMAN     20     99             
DBREF  4FXV D   20    99  UNP    Q15717   ELAV1_HUMAN     20     99             
SEQADV 4FXV MSE A  -18  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLY A  -17  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV SER A  -16  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ASP A  -15  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV LYS A  -14  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ILE A  -13  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS A  -12  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS A  -11  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS A  -10  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS A   -9  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS A   -8  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS A   -7  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLU A   -6  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ASN A   -5  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV LEU A   -4  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV TYR A   -3  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV PHE A   -2  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLN A   -1  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLY A    0  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV MSE B  -18  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLY B  -17  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV SER B  -16  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ASP B  -15  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV LYS B  -14  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ILE B  -13  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS B  -12  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS B  -11  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS B  -10  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS B   -9  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS B   -8  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS B   -7  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLU B   -6  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ASN B   -5  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV LEU B   -4  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV TYR B   -3  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV PHE B   -2  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLN B   -1  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLY B    0  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV MSE C  -18  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLY C  -17  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV SER C  -16  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ASP C  -15  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV LYS C  -14  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ILE C  -13  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS C  -12  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS C  -11  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS C  -10  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS C   -9  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS C   -8  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS C   -7  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLU C   -6  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ASN C   -5  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV LEU C   -4  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV TYR C   -3  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV PHE C   -2  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLN C   -1  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLY C    0  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV MSE D  -18  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLY D  -17  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV SER D  -16  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ASP D  -15  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV LYS D  -14  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ILE D  -13  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS D  -12  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS D  -11  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS D  -10  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS D   -9  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS D   -8  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV HIS D   -7  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLU D   -6  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV ASN D   -5  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV LEU D   -4  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV TYR D   -3  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV PHE D   -2  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLN D   -1  UNP  Q15717              EXPRESSION TAG                 
SEQADV 4FXV GLY D    0  UNP  Q15717              EXPRESSION TAG                 
SEQRES   1 A   99  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS GLU          
SEQRES   2 A   99  ASN LEU TYR PHE GLN GLY THR ASN LEU ILE VAL ASN TYR          
SEQRES   3 A   99  LEU PRO GLN ASN MSE THR GLN ASP GLU LEU ARG SER LEU          
SEQRES   4 A   99  PHE SER SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE          
SEQRES   5 A   99  ARG ASP LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE          
SEQRES   6 A   99  VAL ASN TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE          
SEQRES   7 A   99  ASN THR LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE          
SEQRES   8 A   99  LYS VAL SER TYR ALA ARG PRO SER                              
SEQRES   1 B   99  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS GLU          
SEQRES   2 B   99  ASN LEU TYR PHE GLN GLY THR ASN LEU ILE VAL ASN TYR          
SEQRES   3 B   99  LEU PRO GLN ASN MSE THR GLN ASP GLU LEU ARG SER LEU          
SEQRES   4 B   99  PHE SER SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE          
SEQRES   5 B   99  ARG ASP LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE          
SEQRES   6 B   99  VAL ASN TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE          
SEQRES   7 B   99  ASN THR LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE          
SEQRES   8 B   99  LYS VAL SER TYR ALA ARG PRO SER                              
SEQRES   1 C   99  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS GLU          
SEQRES   2 C   99  ASN LEU TYR PHE GLN GLY THR ASN LEU ILE VAL ASN TYR          
SEQRES   3 C   99  LEU PRO GLN ASN MSE THR GLN ASP GLU LEU ARG SER LEU          
SEQRES   4 C   99  PHE SER SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE          
SEQRES   5 C   99  ARG ASP LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE          
SEQRES   6 C   99  VAL ASN TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE          
SEQRES   7 C   99  ASN THR LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE          
SEQRES   8 C   99  LYS VAL SER TYR ALA ARG PRO SER                              
SEQRES   1 D   99  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS GLU          
SEQRES   2 D   99  ASN LEU TYR PHE GLN GLY THR ASN LEU ILE VAL ASN TYR          
SEQRES   3 D   99  LEU PRO GLN ASN MSE THR GLN ASP GLU LEU ARG SER LEU          
SEQRES   4 D   99  PHE SER SER ILE GLY GLU VAL GLU SER ALA LYS LEU ILE          
SEQRES   5 D   99  ARG ASP LYS VAL ALA GLY HIS SER LEU GLY TYR GLY PHE          
SEQRES   6 D   99  VAL ASN TYR VAL THR ALA LYS ASP ALA GLU ARG ALA ILE          
SEQRES   7 D   99  ASN THR LEU ASN GLY LEU ARG LEU GLN SER LYS THR ILE          
SEQRES   8 D   99  LYS VAL SER TYR ALA ARG PRO SER                              
MODRES 4FXV MSE A   31  MET  SELENOMETHIONINE                                   
MODRES 4FXV MSE B   31  MET  SELENOMETHIONINE                                   
MODRES 4FXV MSE C   31  MET  SELENOMETHIONINE                                   
MODRES 4FXV MSE D   31  MET  SELENOMETHIONINE                                   
HET    MSE  A  31       8                                                       
HET    MSE  B  31       8                                                       
HET    MSE  C  31       8                                                       
HET    MSE  D  31       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   5  HOH   *317(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  LEU A  61   N  ILE A  52           
SHEET    3   A 4 ASN A  21  ASN A  25 -1  N  VAL A  24   O  GLY A  64           
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  ARG B  53  0                                        
SHEET    2   C 4 SER B  60  TYR B  68 -1  O  LEU B  61   N  ILE B  52           
SHEET    3   C 4 ASN B  21  ASN B  25 -1  N  LEU B  22   O  VAL B  66           
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  LEU D  61   N  ILE D  52           
SHEET    3   G 4 ASN D  21  ASN D  25 -1  N  VAL D  24   O  GLY D  64           
SHEET    4   G 4 LYS D  92  TYR D  95 -1  O  LYS D  92   N  ASN D  25           
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           
LINK         C   ASN A  30                 N   MSE A  31     1555   1555  1.35  
LINK         C   MSE A  31                 N   THR A  32     1555   1555  1.33  
LINK         C   ASN B  30                 N   MSE B  31     1555   1555  1.33  
LINK         C   MSE B  31                 N   THR B  32     1555   1555  1.32  
LINK         C   ASN C  30                 N   MSE C  31     1555   1555  1.33  
LINK         C   MSE C  31                 N   THR C  32     1555   1555  1.32  
LINK         C   ASN D  30                 N   MSE D  31     1555   1555  1.34  
LINK         C   MSE D  31                 N   THR D  32     1555   1555  1.33  
CISPEP   1 PRO C   98    SER C   99          0        11.21                     
CRYST1   73.436   73.436  272.957  90.00  90.00 120.00 P 61 2 2     48          
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      0.013617  0.007862  0.000000        0.00000                         
SCALE2      0.000000  0.015724  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003664        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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