GenomeNet

Database: PDB
Entry: 4P3F
LinkDB: 4P3F
Original site: 4P3F 
HEADER    RNA BINDING PROTEIN                     19-FEB-14   4P3F              
TITLE     STRUCTURE OF THE HUMAN SRP68-RBD                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIGNAL RECOGNITION PARTICLE SUBUNIT SRP68;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 47-254;                                       
COMPND   5 SYNONYM: SRP68, SIGNAL RECOGNITION PARTICLE 68 KDA PROTEIN;          
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SRP68;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SRPSRP68RNA-BINDING DOMAIN (RBD), TETRATRICOPEPTIDE REPEAT (TPR), RNA 
KEYWDS   2 BINDING PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.T.GROTWINKEL,K.WILD,I.SINNING                                       
REVDAT   3   08-JAN-20 4P3F    1       REMARK                                   
REVDAT   2   27-SEP-17 4P3F    1       SOURCE JRNL   REMARK                     
REVDAT   1   16-APR-14 4P3F    0                                                
JRNL        AUTH   J.T.GROTWINKEL,K.WILD,B.SEGNITZ,I.SINNING                    
JRNL        TITL   SRP RNA REMODELING BY SRP68 EXPLAINS ITS ROLE IN PROTEIN     
JRNL        TITL 2 TRANSLOCATION.                                               
JRNL        REF    SCIENCE                       V. 344   101 2014              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   24700861                                                     
JRNL        DOI    10.1126/SCIENCE.1249094                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 42901                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2145                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 35.6842 -  4.1882    0.99     2773   146  0.1684 0.2028        
REMARK   3     2  4.1882 -  3.3251    0.99     2747   144  0.1511 0.1682        
REMARK   3     3  3.3251 -  2.9050    1.00     2734   144  0.1705 0.2112        
REMARK   3     4  2.9050 -  2.6395    1.00     2753   145  0.1744 0.2120        
REMARK   3     5  2.6395 -  2.4503    0.98     2691   142  0.1779 0.2196        
REMARK   3     6  2.4503 -  2.3059    1.00     2717   143  0.1721 0.2371        
REMARK   3     7  2.3059 -  2.1904    1.00     2742   144  0.1800 0.2500        
REMARK   3     8  2.1904 -  2.0951    1.00     2723   144  0.1755 0.2273        
REMARK   3     9  2.0951 -  2.0145    0.99     2710   142  0.1869 0.2716        
REMARK   3    10  2.0145 -  1.9449    0.99     2741   144  0.1992 0.2637        
REMARK   3    11  1.9449 -  1.8841    1.00     2669   141  0.1974 0.2421        
REMARK   3    12  1.8841 -  1.8303    1.00     2772   146  0.2015 0.2645        
REMARK   3    13  1.8303 -  1.7821    1.00     2736   144  0.2153 0.2589        
REMARK   3    14  1.7821 -  1.7386    1.00     2722   143  0.2213 0.2900        
REMARK   3    15  1.7386 -  1.6991    0.93     2526   133  0.2458 0.2788        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.850           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.78                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.06                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           3421                                  
REMARK   3   ANGLE     :  1.226           4577                                  
REMARK   3   CHIRALITY :  0.090            478                                  
REMARK   3   PLANARITY :  0.005            589                                  
REMARK   3   DIHEDRAL  : 15.516           1352                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 65 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4429 -23.5238 -18.0485              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0794 T22:   0.1388                                     
REMARK   3      T33:   0.1402 T12:   0.0354                                     
REMARK   3      T13:   0.0050 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7034 L22:   0.3680                                     
REMARK   3      L33:   6.3348 L12:   0.5029                                     
REMARK   3      L13:   3.2387 L23:   0.9511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1567 S12:  -0.0417 S13:  -0.3711                       
REMARK   3      S21:  -0.0812 S22:   0.0161 S23:  -0.0219                       
REMARK   3      S31:   0.2597 S32:   0.2349 S33:  -0.1441                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 66 THROUGH 106 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6398 -28.9921  -8.7660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1052 T22:   0.0994                                     
REMARK   3      T33:   0.1378 T12:  -0.0059                                     
REMARK   3      T13:  -0.0006 T23:  -0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7659 L22:   4.6944                                     
REMARK   3      L33:   6.1083 L12:  -1.3772                                     
REMARK   3      L13:   1.4076 L23:  -4.1794                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0839 S12:  -0.0185 S13:  -0.0317                       
REMARK   3      S21:   0.2091 S22:  -0.0820 S23:  -0.1132                       
REMARK   3      S31:   0.0864 S32:   0.0508 S33:   0.1400                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 142 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.5647 -17.5057 -12.7885              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0512 T22:   0.1280                                     
REMARK   3      T33:   0.0899 T12:   0.0036                                     
REMARK   3      T13:   0.0065 T23:  -0.0322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1319 L22:   6.4053                                     
REMARK   3      L33:   4.6422 L12:  -0.9837                                     
REMARK   3      L13:   1.4738 L23:  -2.7642                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0424 S12:   0.0115 S13:   0.0942                       
REMARK   3      S21:   0.1095 S22:   0.0087 S23:   0.1581                       
REMARK   3      S31:  -0.1815 S32:  -0.0296 S33:   0.0249                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 143 THROUGH 171 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0048 -11.3324  -8.0070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1322 T22:   0.1163                                     
REMARK   3      T33:   0.0959 T12:  -0.0501                                     
REMARK   3      T13:   0.0088 T23:  -0.0464                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3963 L22:   8.0048                                     
REMARK   3      L33:   4.1708 L12:  -4.9929                                     
REMARK   3      L13:   2.7058 L23:  -3.2762                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2219 S12:  -0.2727 S13:   0.1277                       
REMARK   3      S21:   0.6083 S22:   0.1043 S23:  -0.0246                       
REMARK   3      S31:  -0.3754 S32:  -0.0305 S33:   0.1013                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 172 THROUGH 244 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5029  -8.5316 -17.6704              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0704 T22:   0.1251                                     
REMARK   3      T33:   0.1019 T12:  -0.0353                                     
REMARK   3      T13:  -0.0215 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2969 L22:   2.7698                                     
REMARK   3      L33:   1.3482 L12:  -0.9206                                     
REMARK   3      L13:  -0.3535 L23:  -0.5146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0920 S12:   0.0307 S13:  -0.0116                       
REMARK   3      S21:  -0.0329 S22:  -0.0812 S23:  -0.1619                       
REMARK   3      S31:  -0.0983 S32:   0.1539 S33:  -0.0125                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 47 THROUGH 71 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1057 -42.8848  -8.6757              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2136 T22:   0.0945                                     
REMARK   3      T33:   0.1074 T12:   0.0110                                     
REMARK   3      T13:   0.0097 T23:  -0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4755 L22:   3.9566                                     
REMARK   3      L33:   4.0109 L12:   0.3022                                     
REMARK   3      L13:  -0.7616 L23:  -0.2588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1422 S12:  -0.3653 S13:   0.0567                       
REMARK   3      S21:   0.5454 S22:   0.0294 S23:   0.0908                       
REMARK   3      S31:  -0.2075 S32:  -0.0149 S33:  -0.1181                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 72 THROUGH 105 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   0.9058 -33.9543 -24.8963              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2283 T22:   0.1663                                     
REMARK   3      T33:   0.1536 T12:   0.0592                                     
REMARK   3      T13:   0.0227 T23:  -0.0287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9087 L22:   7.1392                                     
REMARK   3      L33:   4.9131 L12:   3.9165                                     
REMARK   3      L13:  -3.2917 L23:  -4.1802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1458 S12:  -0.0149 S13:   0.0730                       
REMARK   3      S21:  -0.2783 S22:   0.1021 S23:  -0.1809                       
REMARK   3      S31:  -0.2223 S32:   0.0027 S33:   0.0395                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 106 THROUGH 140 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.8447 -47.6694 -18.8171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1092 T22:   0.1064                                     
REMARK   3      T33:   0.0980 T12:   0.0473                                     
REMARK   3      T13:   0.0066 T23:  -0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6049 L22:   6.7725                                     
REMARK   3      L33:   3.8366 L12:   4.3902                                     
REMARK   3      L13:  -2.1894 L23:  -1.8008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0181 S12:  -0.0172 S13:   0.1212                       
REMARK   3      S21:  -0.0268 S22:   0.0174 S23:   0.2318                       
REMARK   3      S31:   0.1141 S32:  -0.2562 S33:   0.0166                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 141 THROUGH 171 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6889 -53.9998 -21.3154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1722 T22:   0.0997                                     
REMARK   3      T33:   0.0879 T12:   0.0405                                     
REMARK   3      T13:   0.0186 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9880 L22:   8.1480                                     
REMARK   3      L33:   2.5480 L12:   7.0649                                     
REMARK   3      L13:   0.0510 L23:  -0.0575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1416 S12:  -0.0735 S13:  -0.1436                       
REMARK   3      S21:  -0.1702 S22:   0.0278 S23:  -0.0999                       
REMARK   3      S31:   0.3585 S32:  -0.0299 S33:   0.1028                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 172 THROUGH 218 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.1667 -57.1130  -9.9699              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2365 T22:   0.1757                                     
REMARK   3      T33:   0.1028 T12:   0.0824                                     
REMARK   3      T13:   0.0281 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2363 L22:   3.9653                                     
REMARK   3      L33:   2.2319 L12:   1.5572                                     
REMARK   3      L13:   0.4919 L23:  -0.6660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0038 S12:  -0.2572 S13:  -0.1074                       
REMARK   3      S21:   0.1675 S22:  -0.1247 S23:  -0.2605                       
REMARK   3      S31:   0.4305 S32:   0.2225 S33:   0.1188                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 219 THROUGH 244 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9283 -57.6962  -1.0596              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2878 T22:   0.2521                                     
REMARK   3      T33:   0.0854 T12:  -0.0398                                     
REMARK   3      T13:   0.0120 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4508 L22:   8.1822                                     
REMARK   3      L33:   1.5113 L12:   1.9942                                     
REMARK   3      L13:  -0.4639 L23:  -2.0339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3168 S12:  -0.4038 S13:   0.1509                       
REMARK   3      S21:   0.5712 S22:  -0.4447 S23:   0.2926                       
REMARK   3      S31:   0.3814 S32:  -0.0084 S33:   0.1232                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4P3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200347.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0723                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42912                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.699                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.02000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: 4P3G                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: K/NA TARTRATE, PEG5000MME, PH 8.5,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       46.65500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: 2940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 27.0 KCAL/MOL                         
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 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    31                                                      
REMARK 465     GLY A    32                                                      
REMARK 465     HIS A    33                                                      
REMARK 465     HIS A    34                                                      
REMARK 465     HIS A    35                                                      
REMARK 465     HIS A    36                                                      
REMARK 465     HIS A    37                                                      
REMARK 465     HIS A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     LYS A    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     ASN A    43                                                      
REMARK 465     LYS A    44                                                      
REMARK 465     GLU A    45                                                      
REMARK 465     PHE A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     ASN A   138                                                      
REMARK 465     THR A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     ASP A   245                                                      
REMARK 465     GLN A   246                                                      
REMARK 465     MET B    31                                                      
REMARK 465     GLY B    32                                                      
REMARK 465     HIS B    33                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     HIS B    35                                                      
REMARK 465     HIS B    36                                                      
REMARK 465     HIS B    37                                                      
REMARK 465     HIS B    38                                                      
REMARK 465     GLY B    39                                                      
REMARK 465     SER B    40                                                      
REMARK 465     LYS B    41                                                      
REMARK 465     ALA B    42                                                      
REMARK 465     ASN B    43                                                      
REMARK 465     LYS B    44                                                      
REMARK 465     GLU B    45                                                      
REMARK 465     PHE B    46                                                      
REMARK 465     ASP B   245                                                      
REMARK 465     GLN B   246                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   406     O    HOH A   436              2.08            
REMARK 500   OG1  THR B   218     OE1  GLN B   221              2.15            
REMARK 500   O    HOH B   432     O    HOH B   435              2.17            
REMARK 500   OD1  ASN A   168     O    HOH A   401              2.18            
REMARK 500   O    HOH A   435     O    HOH A   462              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   410     O    HOH B   339     2554     2.12            
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    ASP A  71       74.93   -101.21                                   
REMARK 500    GLU A 136       83.84    -69.59                                   
REMARK 500    PHE A 217     -146.27   -116.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 307                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4P3G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P3E   RELATED DB: PDB                                   
DBREF  4P3F A   39   246  UNP    Q9UHB9   SRP68_HUMAN     47    254             
DBREF  4P3F B   39   246  UNP    Q9UHB9   SRP68_HUMAN     47    254             
SEQADV 4P3F MET A   31  UNP  Q9UHB9              INITIATING METHIONINE          
SEQADV 4P3F GLY A   32  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS A   33  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS A   34  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS A   35  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS A   36  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS A   37  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS A   38  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F ASP A  108  UNP  Q9UHB9    GLU   116 ENGINEERED MUTATION            
SEQADV 4P3F MET B   31  UNP  Q9UHB9              INITIATING METHIONINE          
SEQADV 4P3F GLY B   32  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS B   33  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS B   34  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS B   35  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS B   36  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS B   37  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F HIS B   38  UNP  Q9UHB9              EXPRESSION TAG                 
SEQADV 4P3F ASP B  108  UNP  Q9UHB9    GLU   116 ENGINEERED MUTATION            
SEQRES   1 A  216  MET GLY HIS HIS HIS HIS HIS HIS GLY SER LYS ALA ASN          
SEQRES   2 A  216  LYS GLU PHE GLY ASP SER LEU SER LEU GLU ILE LEU GLN          
SEQRES   3 A  216  ILE ILE LYS GLU SER GLN GLN GLN HIS GLY LEU ARG HIS          
SEQRES   4 A  216  GLY ASP PHE GLN ARG TYR ARG GLY TYR CYS SER ARG ARG          
SEQRES   5 A  216  GLN ARG ARG LEU ARG LYS THR LEU ASN PHE LYS MET GLY          
SEQRES   6 A  216  ASN ARG HIS LYS PHE THR GLY LYS LYS VAL THR GLU ASP          
SEQRES   7 A  216  LEU LEU THR ASP ASN ARG TYR LEU LEU LEU VAL LEU MET          
SEQRES   8 A  216  ASP ALA GLU ARG ALA TRP SER TYR ALA MET GLN LEU LYS          
SEQRES   9 A  216  GLN GLU ALA ASN THR GLU PRO ARG LYS ARG PHE HIS LEU          
SEQRES  10 A  216  LEU SER ARG LEU ARG LYS ALA VAL LYS HIS ALA GLU GLU          
SEQRES  11 A  216  LEU GLU ARG LEU CYS GLU SER ASN ARG VAL ASP ALA LYS          
SEQRES  12 A  216  THR LYS LEU GLU ALA GLN ALA TYR THR ALA TYR LEU SER          
SEQRES  13 A  216  GLY MET LEU ARG PHE GLU HIS GLN GLU TRP LYS ALA ALA          
SEQRES  14 A  216  ILE GLU ALA PHE ASN LYS CYS LYS THR ILE TYR GLU LYS          
SEQRES  15 A  216  LEU ALA SER ALA PHE THR GLU GLU GLN ALA VAL LEU TYR          
SEQRES  16 A  216  ASN GLN ARG VAL GLU GLU ILE SER PRO ASN ILE ARG TYR          
SEQRES  17 A  216  CYS ALA TYR ASN ILE GLY ASP GLN                              
SEQRES   1 B  216  MET GLY HIS HIS HIS HIS HIS HIS GLY SER LYS ALA ASN          
SEQRES   2 B  216  LYS GLU PHE GLY ASP SER LEU SER LEU GLU ILE LEU GLN          
SEQRES   3 B  216  ILE ILE LYS GLU SER GLN GLN GLN HIS GLY LEU ARG HIS          
SEQRES   4 B  216  GLY ASP PHE GLN ARG TYR ARG GLY TYR CYS SER ARG ARG          
SEQRES   5 B  216  GLN ARG ARG LEU ARG LYS THR LEU ASN PHE LYS MET GLY          
SEQRES   6 B  216  ASN ARG HIS LYS PHE THR GLY LYS LYS VAL THR GLU ASP          
SEQRES   7 B  216  LEU LEU THR ASP ASN ARG TYR LEU LEU LEU VAL LEU MET          
SEQRES   8 B  216  ASP ALA GLU ARG ALA TRP SER TYR ALA MET GLN LEU LYS          
SEQRES   9 B  216  GLN GLU ALA ASN THR GLU PRO ARG LYS ARG PHE HIS LEU          
SEQRES  10 B  216  LEU SER ARG LEU ARG LYS ALA VAL LYS HIS ALA GLU GLU          
SEQRES  11 B  216  LEU GLU ARG LEU CYS GLU SER ASN ARG VAL ASP ALA LYS          
SEQRES  12 B  216  THR LYS LEU GLU ALA GLN ALA TYR THR ALA TYR LEU SER          
SEQRES  13 B  216  GLY MET LEU ARG PHE GLU HIS GLN GLU TRP LYS ALA ALA          
SEQRES  14 B  216  ILE GLU ALA PHE ASN LYS CYS LYS THR ILE TYR GLU LYS          
SEQRES  15 B  216  LEU ALA SER ALA PHE THR GLU GLU GLN ALA VAL LEU TYR          
SEQRES  16 B  216  ASN GLN ARG VAL GLU GLU ILE SER PRO ASN ILE ARG TYR          
SEQRES  17 B  216  CYS ALA TYR ASN ILE GLY ASP GLN                              
HET    PEG  A 301       7                                                       
HET    PEG  A 302       7                                                       
HET    PEG  A 303       7                                                       
HET    EDO  A 304       4                                                       
HET    EDO  A 305       4                                                       
HET    EDO  A 306       4                                                       
HET    EDO  A 307       4                                                       
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  PEG    3(C4 H10 O3)                                                 
FORMUL   6  EDO    4(C2 H6 O2)                                                  
FORMUL  10  HOH   *367(H2 O)                                                    
HELIX    1 AA1 GLU A   53  HIS A   65  1                                  13    
HELIX    2 AA2 GLY A   66  GLY A   70  5                                   5    
HELIX    3 AA3 ASP A   71  ASN A   96  1                                  26    
HELIX    4 AA4 ASN A  113  GLU A  136  1                                  24    
HELIX    5 AA5 LYS A  143  CYS A  165  1                                  23    
HELIX    6 AA6 ASP A  171  HIS A  193  1                                  23    
HELIX    7 AA7 GLU A  195  SER A  215  1                                  21    
HELIX    8 AA8 THR A  218  GLY A  244  1                                  27    
HELIX    9 AA9 GLU B   53  HIS B   65  1                                  13    
HELIX   10 AB1 GLY B   66  GLY B   70  5                                   5    
HELIX   11 AB2 ASP B   71  ASN B   96  1                                  26    
HELIX   12 AB3 ASN B  113  ASN B  138  1                                  26    
HELIX   13 AB4 GLU B  140  ARG B  142  5                                   3    
HELIX   14 AB5 LYS B  143  GLU B  166  1                                  24    
HELIX   15 AB6 ASP B  171  HIS B  193  1                                  23    
HELIX   16 AB7 GLU B  195  ALA B  216  1                                  22    
HELIX   17 AB8 THR B  218  TYR B  241  1                                  24    
SITE     1 AC1  4 PHE A 191  PEG A 302  EDO A 304  HOH A 406                    
SITE     1 AC2  7 LYS A 134  ALA A 137  LEU A 147  GLU A 192                    
SITE     2 AC2  7 PEG A 301  EDO A 306  HOH A 554                               
SITE     1 AC3  3 EDO A 307  HOH A 406  HOH A 436                               
SITE     1 AC4  3 TYR A 238  PEG A 301  HOH A 406                               
SITE     1 AC5  3 EDO A 307  HOH A 404  HOH A 459                               
SITE     1 AC6  2 PEG A 302  HOH A 459                                          
SITE     1 AC7  2 PEG A 303  EDO A 305                                          
CRYST1   37.810   93.310   60.100  90.00 109.34  90.00 P 1 21 1      4          
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      0.026448  0.000000  0.009283        0.00000                         
SCALE2      0.000000  0.010717  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017634        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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