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Database: PDB
Entry: 4PD0
LinkDB: 4PD0
Original site: 4PD0 
HEADER    BIOSYNTHETIC PROTEIN,STRUCTURAL PROTEIN 17-APR-14   4PD0              
TITLE     1.7 A RESOLUTION STRUCTURE OF GEPHYRIN'S E-DOMAIN                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GEPHYRIN;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: E-DOMAIN (UNP RESIDUES 350-768);                           
COMPND   5 SYNONYM: PUTATIVE GLYCINE RECEPTOR-TUBULIN LINKER PROTEIN;           
COMPND   6 EC: 2.7.7.75,2.10.1.1;                                               
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: GPHN, GPH;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    SCAFFOLDING PROTEIN, NEUROTRANSMITTER RECEPTOR ANCHORING PROTEIN,     
KEYWDS   2 MOLYBDENUM COFACTOR BIOSYNTHESIS, BIOSYNTHETIC PROTEIN, STRUCTURAL   
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.B.KASARAGOD,H.M.MARIC,H.SCHINDELIN                                  
REVDAT   7   27-SEP-23 4PD0    1       REMARK                                   
REVDAT   6   08-JAN-20 4PD0    1       REMARK                                   
REVDAT   5   27-SEP-17 4PD0    1       SOURCE REMARK                            
REVDAT   4   03-DEC-14 4PD0    1       JRNL                                     
REVDAT   3   17-SEP-14 4PD0    1       JRNL                                     
REVDAT   2   03-SEP-14 4PD0    1       JRNL                                     
REVDAT   1   27-AUG-14 4PD0    0                                                
JRNL        AUTH   H.M.MARIC,V.B.KASARAGOD,H.SCHINDELIN                         
JRNL        TITL   MODULATION OF GEPHYRIN-GLYCINE RECEPTOR AFFINITY BY          
JRNL        TITL 2 MULTIVALENCY.                                                
JRNL        REF    ACS CHEM.BIOL.                V.   9  2554 2014              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   25137389                                                     
JRNL        DOI    10.1021/CB500303A                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
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) : 43.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 55170                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2800                            
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 43.8420 -  4.6129    1.00     2770   154  0.1702 0.1923        
REMARK   3     2  4.6129 -  3.6620    1.00     2675   150  0.1337 0.1408        
REMARK   3     3  3.6620 -  3.1993    1.00     2666   141  0.1485 0.1724        
REMARK   3     4  3.1993 -  2.9068    1.00     2622   141  0.1571 0.1627        
REMARK   3     5  2.9068 -  2.6985    1.00     2644   140  0.1593 0.2087        
REMARK   3     6  2.6985 -  2.5394    1.00     2607   151  0.1625 0.1673        
REMARK   3     7  2.5394 -  2.4123    1.00     2590   141  0.1489 0.1781        
REMARK   3     8  2.4123 -  2.3073    1.00     2615   148  0.1431 0.1859        
REMARK   3     9  2.3073 -  2.2184    1.00     2614   143  0.1538 0.1931        
REMARK   3    10  2.2184 -  2.1419    1.00     2574   151  0.1596 0.2001        
REMARK   3    11  2.1419 -  2.0749    1.00     2613   138  0.1563 0.1807        
REMARK   3    12  2.0749 -  2.0156    1.00     2595   147  0.1648 0.1903        
REMARK   3    13  2.0156 -  1.9625    1.00     2588   146  0.1783 0.2026        
REMARK   3    14  1.9625 -  1.9147    1.00     2607   126  0.1789 0.1991        
REMARK   3    15  1.9147 -  1.8711    1.00     2589   123  0.2003 0.2540        
REMARK   3    16  1.8711 -  1.8313    1.00     2599   135  0.2067 0.2722        
REMARK   3    17  1.8313 -  1.7947    1.00     2624   111  0.2177 0.2713        
REMARK   3    18  1.7947 -  1.7608    1.00     2590   139  0.2258 0.2452        
REMARK   3    19  1.7608 -  1.7294    1.00     2577   143  0.2308 0.2723        
REMARK   3    20  1.7294 -  1.7000    1.00     2611   132  0.2341 0.2599        
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.890           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.011           3264                                  
REMARK   3   ANGLE     :  1.322           4448                                  
REMARK   3   CHIRALITY :  0.080            520                                  
REMARK   3   PLANARITY :  0.007            588                                  
REMARK   3   DIHEDRAL  : 12.626           1249                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 319 THROUGH 349 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1271  30.7893 107.6308              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1879 T22:   0.1860                                     
REMARK   3      T33:   0.1968 T12:   0.0602                                     
REMARK   3      T13:  -0.0197 T23:   0.0319                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8268 L22:   3.3355                                     
REMARK   3      L33:   5.3516 L12:  -0.7019                                     
REMARK   3      L13:  -1.2758 L23:   3.1679                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0692 S12:   0.0510 S13:  -0.1482                       
REMARK   3      S21:  -0.2599 S22:   0.1980 S23:  -0.3127                       
REMARK   3      S31:   0.0378 S32:   0.4257 S33:  -0.2394                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 350 THROUGH 472 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.6491  30.4972 153.9796              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2463 T22:   0.2915                                     
REMARK   3      T33:   0.2553 T12:  -0.0407                                     
REMARK   3      T13:   0.0093 T23:   0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2089 L22:   0.5367                                     
REMARK   3      L33:   4.1249 L12:   1.2742                                     
REMARK   3      L13:  -3.6185 L23:  -1.2443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2052 S12:  -0.2970 S13:  -0.0697                       
REMARK   3      S21:   0.1401 S22:  -0.1952 S23:   0.0465                       
REMARK   3      S31:  -0.1773 S32:   0.1638 S33:   0.0043                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 473 THROUGH 550 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.6889  39.6064 105.5499              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1680 T22:   0.1880                                     
REMARK   3      T33:   0.2294 T12:   0.0201                                     
REMARK   3      T13:   0.0105 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6068 L22:   0.4915                                     
REMARK   3      L33:   7.3204 L12:  -0.0009                                     
REMARK   3      L13:   1.1719 L23:  -0.8026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0098 S12:   0.1056 S13:  -0.0133                       
REMARK   3      S21:  -0.0625 S22:  -0.0165 S23:  -0.0121                       
REMARK   3      S31:  -0.0963 S32:   0.0234 S33:   0.0532                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 551 THROUGH 627 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0838  36.9477  94.2530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2241 T22:   0.3458                                     
REMARK   3      T33:   0.2275 T12:   0.0234                                     
REMARK   3      T13:   0.0291 T23:   0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4453 L22:   4.7959                                     
REMARK   3      L33:   1.5075 L12:  -0.0547                                     
REMARK   3      L13:  -0.3244 L23:  -0.6618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0341 S12:   0.5790 S13:   0.1686                       
REMARK   3      S21:  -0.6100 S22:   0.0188 S23:  -0.2811                       
REMARK   3      S31:  -0.0108 S32:   0.3163 S33:  -0.0040                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 628 THROUGH 686 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5057  19.6739 104.0162              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2610 T22:   0.1679                                     
REMARK   3      T33:   0.2388 T12:   0.0400                                     
REMARK   3      T13:  -0.0135 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0607 L22:   2.9210                                     
REMARK   3      L33:   1.3131 L12:   1.8006                                     
REMARK   3      L13:   0.0949 L23:  -0.2384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1030 S12:   0.1122 S13:  -0.1454                       
REMARK   3      S21:  -0.2443 S22:   0.1016 S23:   0.0808                       
REMARK   3      S31:   0.3266 S32:  -0.0468 S33:  -0.0083                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 687 THROUGH 712 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2029  18.8355 100.4723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3829 T22:   0.3942                                     
REMARK   3      T33:   0.4881 T12:  -0.0281                                     
REMARK   3      T13:  -0.1137 T23:   0.0683                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9233 L22:   5.0263                                     
REMARK   3      L33:   2.7493 L12:  -3.0106                                     
REMARK   3      L13:  -2.0061 L23:   0.9318                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1901 S12:   1.2673 S13:   0.3651                       
REMARK   3      S21:  -0.8957 S22:  -0.0557 S23:   1.1699                       
REMARK   3      S31:   0.0296 S32:  -0.6296 S33:  -0.0674                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 713 THROUGH 736 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6946   9.6499  99.5824              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3822 T22:   0.1924                                     
REMARK   3      T33:   0.3735 T12:   0.0357                                     
REMARK   3      T13:   0.0579 T23:  -0.0298                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9794 L22:   2.9751                                     
REMARK   3      L33:   4.3878 L12:   1.7941                                     
REMARK   3      L13:   2.0667 L23:  -1.4127                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0714 S12:   0.3437 S13:  -0.6642                       
REMARK   3      S21:  -0.4022 S22:  -0.0261 S23:  -0.2494                       
REMARK   3      S31:   0.6482 S32:   0.1625 S33:  -0.0010                       
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 4PD0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201165.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9198                             
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          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55179                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.00                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 2FU3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM-CITRATE, PH 4.5, 28-34% 2   
REMARK 280  -METHYL-2,4-PENTANEDIOL, VAPOR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
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   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+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  1.000000  0.000000  0.000000       43.82750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.00400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       56.84750            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.82750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.00400            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       56.84750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.82750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.00400            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       56.84750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.82750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.00400            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       56.84750            
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR                   
REMARK 300 CYCLIC POINT SYMMETRY (SCHOENFLIES SYMBOL = C2).                     
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: 6120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      227.39000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 824  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 934  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 936  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1084  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   318                                                      
REMARK 465     MET A   696                                                      
REMARK 465     SER A   697                                                      
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  HE22  GLN A   398     O    HOH A  1126              1.38            
REMARK 500   HZ3  LYS A   362     O    HOH A  1071              1.53            
REMARK 500   O    HOH A  1093     O    HOH A  1125              2.11            
REMARK 500   O    HOH A  1024     O    HOH A  1098              2.19            
REMARK 500   O    HOH A   866     O    HOH A  1067              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   814     O    HOH A   823     3557     2.04            
REMARK 500   O    HOH A   903     O    HOH A   946     8557     2.11            
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    GLU A 578      -20.48    -30.28                                   
REMARK 500    LYS A 579     -147.22    -96.22                                   
REMARK 500    HIS A 682     -109.42     36.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1084        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH A1108        DISTANCE =  6.15 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FU3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PD1   RELATED DB: PDB                                   
DBREF  4PD0 A  318   736  UNP    Q03555   GEPH_RAT       350    768             
SEQRES   1 A  419  MET SER PRO PHE PRO LEU THR SER MET ASP LYS ALA PHE          
SEQRES   2 A  419  ILE THR VAL LEU GLU MET THR PRO VAL LEU GLY THR GLU          
SEQRES   3 A  419  ILE ILE ASN TYR ARG ASP GLY MET GLY ARG VAL LEU ALA          
SEQRES   4 A  419  GLN ASP VAL TYR ALA LYS ASP ASN LEU PRO PRO PHE PRO          
SEQRES   5 A  419  ALA SER VAL LYS ASP GLY TYR ALA VAL ARG ALA ALA ASP          
SEQRES   6 A  419  GLY PRO GLY ASP ARG PHE ILE ILE GLY GLU SER GLN ALA          
SEQRES   7 A  419  GLY GLU GLN PRO THR GLN THR VAL MET PRO GLY GLN VAL          
SEQRES   8 A  419  MET ARG VAL THR THR GLY ALA PRO ILE PRO CYS GLY ALA          
SEQRES   9 A  419  ASP ALA VAL VAL GLN VAL GLU ASP THR GLU LEU ILE ARG          
SEQRES  10 A  419  GLU SER ASP ASP GLY THR GLU GLU LEU GLU VAL ARG ILE          
SEQRES  11 A  419  LEU VAL GLN ALA ARG PRO GLY GLN ASP ILE ARG PRO ILE          
SEQRES  12 A  419  GLY HIS ASP ILE LYS ARG GLY GLU CYS VAL LEU ALA LYS          
SEQRES  13 A  419  GLY THR HIS MET GLY PRO SER GLU ILE GLY LEU LEU ALA          
SEQRES  14 A  419  THR VAL GLY VAL THR GLU VAL GLU VAL ASN LYS PHE PRO          
SEQRES  15 A  419  VAL VAL ALA VAL MET SER THR GLY ASN GLU LEU LEU ASN          
SEQRES  16 A  419  PRO GLU ASP ASP LEU LEU PRO GLY LYS ILE ARG ASP SER          
SEQRES  17 A  419  ASN ARG SER THR LEU LEU ALA THR ILE GLN GLU HIS GLY          
SEQRES  18 A  419  TYR PRO THR ILE ASN LEU GLY ILE VAL GLY ASP ASN PRO          
SEQRES  19 A  419  ASP ASP LEU LEU ASN ALA LEU ASN GLU GLY ILE SER ARG          
SEQRES  20 A  419  ALA ASP VAL ILE ILE THR SER GLY GLY VAL SER MET GLY          
SEQRES  21 A  419  GLU LYS ASP TYR LEU LYS GLN VAL LEU ASP ILE ASP LEU          
SEQRES  22 A  419  HIS ALA GLN ILE HIS PHE GLY ARG VAL PHE MET LYS PRO          
SEQRES  23 A  419  GLY LEU PRO THR THR PHE ALA THR LEU ASP ILE ASP GLY          
SEQRES  24 A  419  VAL ARG LYS ILE ILE PHE ALA LEU PRO GLY ASN PRO VAL          
SEQRES  25 A  419  SER ALA VAL VAL THR CYS ASN LEU PHE VAL VAL PRO ALA          
SEQRES  26 A  419  LEU ARG LYS MET GLN GLY ILE LEU ASP PRO ARG PRO THR          
SEQRES  27 A  419  ILE ILE LYS ALA ARG LEU SER CYS ASP VAL LYS LEU ASP          
SEQRES  28 A  419  PRO ARG PRO GLU TYR HIS ARG CYS ILE LEU THR TRP HIS          
SEQRES  29 A  419  HIS GLN GLU PRO LEU PRO TRP ALA GLN SER THR GLY ASN          
SEQRES  30 A  419  GLN MET SER SER ARG LEU MET SER MET ARG SER ALA ASN          
SEQRES  31 A  419  GLY LEU LEU MET LEU PRO PRO LYS THR GLU GLN TYR VAL          
SEQRES  32 A  419  GLU LEU HIS LYS GLY GLU VAL VAL ASP VAL MET VAL ILE          
SEQRES  33 A  419  GLY ARG LEU                                                  
FORMUL   2  HOH   *329(H2 O)                                                    
HELIX    1 AA1 SER A  325  THR A  337  1                                  13    
HELIX    2 AA2 ARG A  348  GLY A  350  5                                   3    
HELIX    3 AA3 ARG A  379  GLY A  383  5                                   5    
HELIX    4 AA4 GLY A  478  GLY A  489  1                                  12    
HELIX    5 AA5 SER A  525  HIS A  537  1                                  13    
HELIX    6 AA6 ASN A  550  ALA A  565  1                                  16    
HELIX    7 AA7 ASP A  580  ASP A  589  1                                  10    
HELIX    8 AA8 ASN A  627  PHE A  638  1                                  12    
HELIX    9 AA9 PHE A  638  GLN A  647  1                                  10    
HELIX   10 AB1 ARG A  699  ARG A  704  1                                   6    
SHEET    1 AA1 2 LEU A 323  THR A 324  0                                        
SHEET    2 AA1 2 ARG A 598  VAL A 599  1  O  ARG A 598   N  THR A 324           
SHEET    1 AA2 2 THR A 342  ASN A 346  0                                        
SHEET    2 AA2 2 GLU A 492  ASN A 496 -1  O  VAL A 495   N  GLU A 343           
SHEET    1 AA3 2 VAL A 359  TYR A 360  0                                        
SHEET    2 AA3 2 CYS A 469  LEU A 471 -1  O  LEU A 471   N  VAL A 359           
SHEET    1 AA4 2 ALA A 370  SER A 371  0                                        
SHEET    2 AA4 2 ILE A 457  ARG A 458 -1  O  ARG A 458   N  ALA A 370           
SHEET    1 AA5 6 ALA A 423  GLN A 426  0                                        
SHEET    2 AA5 6 GLY A 375  VAL A 378 -1  N  TYR A 376   O  VAL A 425           
SHEET    3 AA5 6 GLN A 407  VAL A 411 -1  O  MET A 409   N  ALA A 377           
SHEET    4 AA5 6 GLY A 385  SER A 393  1  N  SER A 393   O  ARG A 410           
SHEET    5 AA5 6 GLU A 442  ILE A 447 -1  O  ILE A 447   N  GLY A 385           
SHEET    6 AA5 6 THR A 430  GLU A 435 -1  N  GLU A 431   O  ARG A 446           
SHEET    1 AA6 6 THR A 541  VAL A 547  0                                        
SHEET    2 AA6 6 VAL A 501  THR A 506  1  N  SER A 505   O  VAL A 547           
SHEET    3 AA6 6 VAL A 567  SER A 571  1  O  ILE A 569   N  ALA A 502           
SHEET    4 AA6 6 VAL A 617  LEU A 624  1  O  LEU A 624   N  THR A 570           
SHEET    5 AA6 6 THR A 608  ILE A 614 -1  N  LEU A 612   O  LYS A 619           
SHEET    6 AA6 6 GLN A 593  PHE A 596 -1  N  GLN A 593   O  THR A 611           
SHEET    1 AA7 2 LEU A 510  LEU A 511  0                                        
SHEET    2 AA7 2 ILE A 522  ARG A 523  1  O  ILE A 522   N  LEU A 511           
SHEET    1 AA8 6 ILE A 656  LEU A 661  0                                        
SHEET    2 AA8 6 TRP A 688  SER A 691  1  O  ALA A 689   N  ARG A 660           
SHEET    3 AA8 6 GLU A 672  THR A 679 -1  N  THR A 679   O  TRP A 688           
SHEET    4 AA8 6 GLY A 708  LEU A 712 -1  O  LEU A 712   N  GLU A 672           
SHEET    5 AA8 6 VAL A 727  VAL A 732 -1  O  MET A 731   N  LEU A 709           
SHEET    6 AA8 6 ILE A 656  LEU A 661 -1  N  ALA A 659   O  VAL A 728           
SHEET    1 AA9 2 VAL A 665  LYS A 666  0                                        
SHEET    2 AA9 2 GLU A 721  LEU A 722 -1  O  LEU A 722   N  VAL A 665           
CISPEP   1 SER A  319    PRO A  320          0         0.36                     
CISPEP   2 LEU A  365    PRO A  366          0        -7.28                     
CISPEP   3 LYS A  602    PRO A  603          0        -7.87                     
CRYST1   87.655  100.008  113.695  90.00  90.00  90.00 I 2 2 2       8          
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      0.011408  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009999  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008795        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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