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Database: PDB
Entry: 3B4D
LinkDB: 3B4D
Original site: 3B4D 
HEADER    RNA BINDING PROTEIN                     24-OCT-07   3B4D              
TITLE     CRYSTAL STRUCTURE OF HUMAN PABPN1 RRM                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLYADENYLATE-BINDING PROTEIN 2;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 167-254;                                      
COMPND   5 SYNONYM: POLY(A)-BINDING PROTEIN 2, POLY(A)-BINDING PROTEIN II,      
COMPND   6 PABII, POLYADENYLATE-BINDING NUCLEAR PROTEIN 1, NUCLEAR POLY(A)-     
COMPND   7 BINDING PROTEIN 1;                                                   
COMPND   8 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: PABPN1, PAB2, PABP2;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B(+)                                 
KEYWDS    RRM FOLD, ALPHA-BETA SANDWICH STRUCTURE, RNA BINDING DOMAIN, RNA      
KEYWDS   2 RECOGNITION MOTIF, ACETYLATION, ALTERNATIVE SPLICING, COILED COIL,   
KEYWDS   3 CYTOPLASM, DISEASE MUTATION, METHYLATION, MRNA PROCESSING, NUCLEUS,  
KEYWDS   4 POLYMORPHISM, RNA-BINDING, TRIPLET REPEAT EXPANSION, RNA BINDING     
KEYWDS   5 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.GE,S.TONG,M.TENG,L.NIU                                              
REVDAT   4   13-MAR-24 3B4D    1       SEQADV                                   
REVDAT   3   24-FEB-09 3B4D    1       VERSN                                    
REVDAT   2   08-APR-08 3B4D    1       JRNL                                     
REVDAT   1   15-JAN-08 3B4D    0                                                
JRNL        AUTH   H.GE,D.ZHOU,S.TONG,Y.GAO,M.TENG,L.NIU                        
JRNL        TITL   CRYSTAL STRUCTURE AND POSSIBLE DIMERIZATION OF THE SINGLE    
JRNL        TITL 2 RRM OF HUMAN PABPN1                                          
JRNL        REF    PROTEINS                      V.  71  1539 2008              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   18275081                                                     
JRNL        DOI    10.1002/PROT.21973                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 8561                           
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 425                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 631                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 29                           
REMARK   3   BIN FREE R VALUE                    : 0.2460                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 625                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 97                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.126         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.123         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.080         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.789         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   637 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):   856 ; 1.312 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    79 ; 5.212 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    31 ;35.356 ;22.581       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   108 ;13.623 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;18.896 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):    92 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   487 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   248 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   435 ; 0.294 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    62 ; 0.172 ; 0.200       
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):    30 ; 0.192 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.250 ; 0.200       
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):   408 ; 1.051 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   629 ; 1.716 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   255 ; 2.775 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   227 ; 4.300 ; 4.500       
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  : 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 3B4D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-OCT-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045063.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54179                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AUTOMAR                            
REMARK 200  DATA SCALING SOFTWARE          : AUTOMAR                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9002                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.001                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.233                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 12.70                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.70                              
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: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 4.2M SODIUM CHLORIDE,        
REMARK 280  PH7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       46.17300            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       46.17300            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       46.17300            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       46.17300            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       46.17300            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       46.17300            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       46.17300            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       46.17300            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       46.17300            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       46.17300            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       46.17300            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       46.17300            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       46.17300            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       46.17300            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       46.17300            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       46.17300            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       46.17300            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       46.17300            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       46.17300            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       46.17300            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       46.17300            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       46.17300            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       46.17300            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       46.17300            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       46.17300            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       46.17300            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8110 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.7 KCAL/MOL                         
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   BIOMT1   2 -1.000000  0.000000  0.000000       92.34600            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     MET A   167                                                      
REMARK 465     GLU A   168                                                      
REMARK 465     THR A   249                                                      
REMARK 465     ASN A   250                                                      
REMARK 465     ARG A   251                                                      
REMARK 465     PRO A   252                                                      
REMARK 465     GLY A   253                                                      
REMARK 465     ILE A   254                                                      
REMARK 465     LEU A   255                                                      
REMARK 465     GLU A   256                                                      
REMARK 465     HIS A   257                                                      
REMARK 465     HIS A   258                                                      
REMARK 465     HIS A   259                                                      
REMARK 465     HIS A   260                                                      
REMARK 465     HIS A   261                                                      
REMARK 465     HIS A   262                                                      
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 178       50.01     72.65                                   
REMARK 500    GLU A 234       -2.97     72.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3B4M   RELATED DB: PDB                                   
DBREF  3B4D A  167   254  UNP    Q86U42   PABP2_HUMAN    167    254             
SEQADV 3B4D LEU A  255  UNP  Q86U42              EXPRESSION TAG                 
SEQADV 3B4D GLU A  256  UNP  Q86U42              EXPRESSION TAG                 
SEQADV 3B4D HIS A  257  UNP  Q86U42              EXPRESSION TAG                 
SEQADV 3B4D HIS A  258  UNP  Q86U42              EXPRESSION TAG                 
SEQADV 3B4D HIS A  259  UNP  Q86U42              EXPRESSION TAG                 
SEQADV 3B4D HIS A  260  UNP  Q86U42              EXPRESSION TAG                 
SEQADV 3B4D HIS A  261  UNP  Q86U42              EXPRESSION TAG                 
SEQADV 3B4D HIS A  262  UNP  Q86U42              EXPRESSION TAG                 
SEQRES   1 A   96  MET GLU ALA ASP ALA ARG SER ILE TYR VAL GLY ASN VAL          
SEQRES   2 A   96  ASP TYR GLY ALA THR ALA GLU GLU LEU GLU ALA HIS PHE          
SEQRES   3 A   96  HIS GLY CYS GLY SER VAL ASN ARG VAL THR ILE LEU CYS          
SEQRES   4 A   96  ASP LYS PHE SER GLY HIS PRO LYS GLY PHE ALA TYR ILE          
SEQRES   5 A   96  GLU PHE SER ASP LYS GLU SER VAL ARG THR SER LEU ALA          
SEQRES   6 A   96  LEU ASP GLU SER LEU PHE ARG GLY ARG GLN ILE LYS VAL          
SEQRES   7 A   96  ILE PRO LYS ARG THR ASN ARG PRO GLY ILE LEU GLU HIS          
SEQRES   8 A   96  HIS HIS HIS HIS HIS                                          
FORMUL   2  HOH   *97(H2 O)                                                     
HELIX    1   1 ALA A  169  ALA A  171  5                                   3    
HELIX    2   2 THR A  184  HIS A  193  1                                  10    
HELIX    3   3 GLY A  194  GLY A  196  5                                   3    
HELIX    4   4 LYS A  223  LEU A  230  1                                   8    
HELIX    5   5 ALA A  231  ASP A  233  5                                   3    
SHEET    1   A 4 VAL A 198  CYS A 205  0                                        
SHEET    2   A 4 GLY A 214  PHE A 220 -1  O  GLU A 219   N  ASN A 199           
SHEET    3   A 4 SER A 173  GLY A 177 -1  N  VAL A 176   O  ALA A 216           
SHEET    4   A 4 LYS A 243  PRO A 246 -1  O  LYS A 243   N  GLY A 177           
SHEET    1   B 2 LEU A 236  PHE A 237  0                                        
SHEET    2   B 2 ARG A 240  GLN A 241 -1  O  ARG A 240   N  PHE A 237           
CRYST1   92.346   92.346   92.346  90.00  90.00  90.00 I 2 3        24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010829  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010829  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010829        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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