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Database: PDB
Entry: 4BEH
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Original site: 4BEH 
HEADER    TRANSLATION                             10-MAR-13   4BEH              
TITLE     SOLUTION STRUCTURE OF HUMAN RIBOSOMAL PROTEIN P1.P2 HETERODIMER       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 60S ACIDIC RIBOSOMAL PROTEIN P1;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: 60S ACIDIC RIBOSOMAL PROTEIN P2;                           
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: RENAL CARCINOMA ANTIGEN NY-REN-44;                          
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: C41;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET3A;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VARIANT: C41;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: PET3A                                      
KEYWDS    STALK, RIBOSOME, TRANSLATION                                          
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    K.M.LEE,K.YUSA,L.O.CHU,C.WING-HENG YU,P.C.SHAW,M.OONO,T.MIYOSHI,      
AUTHOR   2 K.ITO,K.B.WONG,T.UCHIUMI                                             
REVDAT   2   30-OCT-13 4BEH    1       JRNL                                     
REVDAT   1   14-AUG-13 4BEH    0                                                
JRNL        AUTH   K.M.LEE,K.YUSA,L.O.CHU,C.WING-HENG YU,M.OONO,T.MIYOSHI,      
JRNL        AUTH 2 K.ITO,P.C.SHAW,K.B.WONG,T.UCHIUMI                            
JRNL        TITL   SOLUTION STRUCTURE OF HUMAN P1*P2 HETERODIMER PROVIDES       
JRNL        TITL 2 INSIGHTS INTO THE ROLE OF EUKARYOTIC STALK IN RECRUITING     
JRNL        TITL 3 THE RIBOSOME-INACTIVATING PROTEIN TRICHOSANTHIN TO THE       
JRNL        TITL 4 RIBOSOME.                                                    
JRNL        REF    NUCLEIC ACIDS RES.            V.  41  8776 2013              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   23892290                                                     
JRNL        DOI    10.1093/NAR/GKT636                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ,         
REMARK   3               : RICE,SIMONSON,WARREN                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4BEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAR-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-56090.                                       
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 210  PH                             : 6.5                                
REMARK 210  IONIC STRENGTH                 : 150 MM                             
REMARK 210  PRESSURE                       : 1.0 ATM                            
REMARK 210  SAMPLE CONTENTS                : 10% WATER/90% D2O                  
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NOESY, TOCSY, COSY                 
REMARK 210  SPECTROMETER FIELD STRENGTH    : 700 MHZ                            
REMARK 210  SPECTROMETER MODEL             : AVANCE                             
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NMRVIEW                            
REMARK 210   METHOD USED                   : ARIA                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : LEAST RESTRAINT VIOLATION          
REMARK 210                                   AND LOWEST ENERGY                  
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8                   
REMARK 210                                                                      
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE          
REMARK 210  NMR SPECTROSCOPY ASYMMETRICALLY LABELED P1.P2 HETERODIMER.          
REMARK 210  C13,N15P1.P2 AND P1.C13,N15P2.                                      
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    95     HZ1  LYS A    98              1.54            
REMARK 500   OD2  ASP B   222     HZ2  LYS B   225              1.59            
REMARK 500   HG   SER B   286     OE1  GLU B   301              1.60            
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  1 HIS A  17      -78.26    -17.27                                   
REMARK 500  1 ASP A  18       73.61   -158.97                                   
REMARK 500  1 ASP A  19     -158.56   -132.46                                   
REMARK 500  1 LEU A  51     -131.02    -88.38                                   
REMARK 500  1 ALA A  52      -12.61     68.97                                   
REMARK 500  1 ASN A  55      -95.55     -7.46                                   
REMARK 500  1 ILE A  56      -66.24   -153.69                                   
REMARK 500  1 ALA A  65      -70.58   -165.89                                   
REMARK 500  1 THR A  84      168.85     54.25                                   
REMARK 500  1 ALA A  86      143.96     67.90                                   
REMARK 500  1 ALA A  96      -62.81   -120.18                                   
REMARK 500  1 GLU A 102       36.80    -86.17                                   
REMARK 500  1 GLU A 103      122.92   -170.30                                   
REMARK 500  1 ASP A 105     -127.30   -139.37                                   
REMARK 500  1 ARG B 202     -128.39   -128.34                                   
REMARK 500  1 PRO B 218       92.69    -59.82                                   
REMARK 500  1 ASN B 247      109.43    -58.84                                   
REMARK 500  1 LEU B 262      -98.05   -114.16                                   
REMARK 500  1 SER B 264     -150.96    168.98                                   
REMARK 500  1 VAL B 271      112.45     43.83                                   
REMARK 500  1 VAL B 273       75.36     51.98                                   
REMARK 500  1 PRO B 277       85.92    -66.11                                   
REMARK 500  1 ALA B 287       85.87     66.32                                   
REMARK 500  1 GLU B 292       65.21   -117.72                                   
REMARK 500  1 LYS B 294        5.50   -162.40                                   
REMARK 500  1 ASP B 296       96.06     66.61                                   
REMARK 500  1 GLU B 300      -89.59   -124.53                                   
REMARK 500  1 GLU B 301       78.83     58.84                                   
REMARK 500  1 GLU B 303      -73.86   -150.77                                   
REMARK 500  1 ASP B 307      117.26     67.55                                   
REMARK 500  1 MET B 309      -34.79     70.32                                   
REMARK 500  1 LEU B 313       76.49   -104.42                                   
REMARK 500  2 ASP A  18      -84.68   -154.31                                   
REMARK 500  2 VAL A  23       95.21    -67.17                                   
REMARK 500  2 PRO A  41      -17.11    -47.13                                   
REMARK 500  2 LEU A  51     -128.29    -83.16                                   
REMARK 500  2 ALA A  52       -1.47     65.41                                   
REMARK 500  2 ASN A  53      -46.74   -144.56                                   
REMARK 500  2 ASN A  62       34.18    -88.75                                   
REMARK 500  2 ALA A  69       75.46     50.92                                   
REMARK 500  2 ALA A  71      114.87     64.30                                   
REMARK 500  2 THR A  84      122.83     71.27                                   
REMARK 500  2 PRO A  88       73.09    -63.60                                   
REMARK 500  2 ALA A  89      -85.74     67.07                                   
REMARK 500  2 GLU A  90       74.05     47.34                                   
REMARK 500  2 ALA A  96       88.10   -163.32                                   
REMARK 500  2 LYS A  98      -48.00   -132.79                                   
REMARK 500  2 GLU A  99       72.23     57.85                                   
REMARK 500  2 GLU A 103      101.94     63.62                                   
REMARK 500  2 ILE B 232      -89.13    -99.25                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     635 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4BEH A    1   114  UNP    P05386   RLA1_HUMAN       1    114             
DBREF  4BEH B  201   315  UNP    P05387   RLA2_HUMAN       1    115             
SEQADV 4BEH ALA B  200  UNP  P05387              EXPRESSION TAG                 
SEQRES   1 A  114  MET ALA SER VAL SER GLU LEU ALA CYS ILE TYR SER ALA          
SEQRES   2 A  114  LEU ILE LEU HIS ASP ASP GLU VAL THR VAL THR GLU ASP          
SEQRES   3 A  114  LYS ILE ASN ALA LEU ILE LYS ALA ALA GLY VAL ASN VAL          
SEQRES   4 A  114  GLU PRO PHE TRP PRO GLY LEU PHE ALA LYS ALA LEU ALA          
SEQRES   5 A  114  ASN VAL ASN ILE GLY SER LEU ILE CYS ASN VAL GLY ALA          
SEQRES   6 A  114  GLY GLY PRO ALA PRO ALA ALA GLY ALA ALA PRO ALA GLY          
SEQRES   7 A  114  GLY PRO ALA PRO SER THR ALA ALA ALA PRO ALA GLU GLU          
SEQRES   8 A  114  LYS LYS VAL GLU ALA LYS LYS GLU GLU SER GLU GLU SER          
SEQRES   9 A  114  ASP ASP ASP MET GLY PHE GLY LEU PHE ASP                      
SEQRES   1 B  116  ALA MET ARG TYR VAL ALA SER TYR LEU LEU ALA ALA LEU          
SEQRES   2 B  116  GLY GLY ASN SER SER PRO SER ALA LYS ASP ILE LYS LYS          
SEQRES   3 B  116  ILE LEU ASP SER VAL GLY ILE GLU ALA ASP ASP ASP ARG          
SEQRES   4 B  116  LEU ASN LYS VAL ILE SER GLU LEU ASN GLY LYS ASN ILE          
SEQRES   5 B  116  GLU ASP VAL ILE ALA GLN GLY ILE GLY LYS LEU ALA SER          
SEQRES   6 B  116  VAL PRO ALA GLY GLY ALA VAL ALA VAL SER ALA ALA PRO          
SEQRES   7 B  116  GLY SER ALA ALA PRO ALA ALA GLY SER ALA PRO ALA ALA          
SEQRES   8 B  116  ALA GLU GLU LYS LYS ASP GLU LYS LYS GLU GLU SER GLU          
SEQRES   9 B  116  GLU SER ASP ASP ASP MET GLY PHE GLY LEU PHE ASP              
HELIX    1   1 SER A    3  HIS A   17  1                                  15    
HELIX    2   2 THR A   24  GLY A   36  1                                  13    
HELIX    3   3 PRO A   41  LEU A   51  1                                  11    
HELIX    4   4 ILE A   56  CYS A   61  5                                   6    
HELIX    5   5 TYR B  203  GLY B  213  1                                  11    
HELIX    6   6 SER B  219  GLY B  231  1                                  13    
HELIX    7   7 ASP B  235  ASN B  247  1                                  13    
HELIX    8   8 ASN B  250  GLN B  257  1                                   8    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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