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    HEADER    VIRAL PROTEIN                           17-SEP-15   5DSD              
    TITLE     THE CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF EBOLA (BUNDIBUGYO)  
    TITLE    2 NUCLEOPROTEIN                                                        
    COMPND    MOL_ID: 1;                                                            
    COMPND   2 MOLECULE: NUCLEOPROTEIN;                                             
    COMPND   3 CHAIN: A;                                                            
    COMPND   4 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 641-739);                  
    COMPND   5 ENGINEERED: YES                                                      
    SOURCE    MOL_ID: 1;                                                            
    SOURCE   2 ORGANISM_SCIENTIFIC: BUNDIBUGYO VIRUS;                               
    SOURCE   3 ORGANISM_TAXID: 565995;                                              
    SOURCE   4 GENE: NP, DH33_45404GPNP;                                            
    SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
    SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
    SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) RIL;                            
    SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
    SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PARALLEL1-MBPHIS                          
    KEYWDS    VIRAL PROTEIN, FILOVIRIDAE                                            
    EXPDTA    X-RAY DIFFRACTION                                                     
    AUTHOR    L.BAKER,K.B.HANDING,D.UTEPBERGENOV,U.DEREWENDA,Z.S.DEREWENDA          
    REVDAT   2   02-MAR-16 5DSD    1       JRNL                                     
    REVDAT   1   30-SEP-15 5DSD    0                                                
    SPRSDE     30-SEP-15 5DSD      5CIJ                                             
    JRNL        AUTH   L.E.BAKER,J.F.ELLENA,K.B.HANDING,U.DEREWENDA,D.UTEPBERGENOV, 
    JRNL        AUTH 2 D.A.ENGEL,Z.S.DEREWENDA                                      
    JRNL        TITL   MOLECULAR ARCHITECTURE OF THE NUCLEOPROTEIN C-TERMINAL       
    JRNL        TITL 2 DOMAIN FROM THE EBOLA AND MARBURG VIRUSES.                   
    JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  72    49 2016              
    JRNL        REF  2 BIOL                                                         
    JRNL        REFN                   ISSN 2059-7983                               
    JRNL        PMID   26894534                                                     
    JRNL        DOI    10.1107/S2059798315021439                                    
    REMARK   1                                                                      
    REMARK   1 REFERENCE 1                                                          
    REMARK   1  AUTH   P.J.DZIUBANSKA,U.DEREWENDA,J.F.ELLENA,D.A.ENGEL,             
    REMARK   1  AUTH 2 Z.S.DEREWENDA                                                
    REMARK   1  TITL   THE STRUCTURE OF THE C-TERMINAL DOMAIN OF THE ZAIRE          
    REMARK   1  TITL 2 EBOLAVIRUS NUCLEOPROTEIN.                                    
    REMARK   1  REF    ACTA CRYSTALLOGR. D BIOL.     V.  70  2420 2014              
    REMARK   1  REF  2 CRYSTALLOGR.                                                 
    REMARK   1  REFN                   ESSN 1399-0047                               
    REMARK   1  PMID   25195755                                                     
    REMARK   1  DOI    10.1107/S1399004714014710                                    
    REMARK   2                                                                      
    REMARK   2 RESOLUTION.    2.31 ANGSTROMS.                                       
    REMARK   3                                                                      
    REMARK   3 REFINEMENT.                                                          
    REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
    REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
    REMARK   3                                                                      
    REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
    REMARK   3                                                                      
    REMARK   3  DATA USED IN REFINEMENT.                                            
    REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31                           
    REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 80.00                          
    REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
    REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.0                           
    REMARK   3   NUMBER OF REFLECTIONS             : 11792                          
    REMARK   3                                                                      
    REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
    REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
    REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
    REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
    REMARK   3   R VALUE            (WORKING SET) : 0.168                           
    REMARK   3   FREE R VALUE                     : 0.203                           
    REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
    REMARK   3   FREE R VALUE TEST SET COUNT      : 604                             
    REMARK   3                                                                      
    REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
    REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
    REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.31                         
    REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.37                         
    REMARK   3   REFLECTION IN BIN     (WORKING SET) : 534                          
    REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 59.49                        
    REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780                       
    REMARK   3   BIN FREE R VALUE SET COUNT          : 27                           
    REMARK   3   BIN FREE R VALUE                    : 0.3120                       
    REMARK   3                                                                      
    REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
    REMARK   3   PROTEIN ATOMS            : 861                                     
    REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
    REMARK   3   HETEROGEN ATOMS          : 13                                      
    REMARK   3   SOLVENT ATOMS            : 112                                     
    REMARK   3                                                                      
    REMARK   3  B VALUES.                                                           
    REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
    REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 81.78                          
    REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
    REMARK   3    B11 (A**2) : 0.68000                                              
    REMARK   3    B22 (A**2) : 0.68000                                              
    REMARK   3    B33 (A**2) : -2.20000                                             
    REMARK   3    B12 (A**2) : 0.34000                                              
    REMARK   3    B13 (A**2) : 0.00000                                              
    REMARK   3    B23 (A**2) : 0.00000                                              
    REMARK   3                                                                      
    REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
    REMARK   3   ESU BASED ON R VALUE                            (A): 0.144         
    REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
    REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
    REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.710         
    REMARK   3                                                                      
    REMARK   3 CORRELATION COEFFICIENTS.                                            
    REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
    REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.964                         
    REMARK   3                                                                      
    REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
    REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   908 ; 0.008 ; 0.019       
    REMARK   3   BOND LENGTHS OTHERS               (A):   806 ; 0.001 ; 0.020       
    REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1225 ; 1.253 ; 1.936       
    REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1866 ; 0.899 ; 3.000       
    REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   104 ; 5.678 ; 5.000       
    REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    51 ;40.102 ;24.902       
    REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   153 ;13.360 ;15.000       
    REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ;10.807 ;15.000       
    REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   119 ; 0.071 ; 0.200       
    REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1027 ; 0.005 ; 0.021       
    REMARK   3   GENERAL PLANES OTHERS             (A):   222 ; 0.001 ; 0.020       
    REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
    REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
    REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
    REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
    REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
    REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
    REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
    REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
    REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
    REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
    REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
    REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
    REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
    REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
    REMARK   3                                                                      
    REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
    REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   413 ;13.696 ; 3.935       
    REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   412 ;13.629 ; 3.925       
    REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   515 ;14.363 ; 5.917       
    REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3                                                                      
    REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
    REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
    REMARK   3                                                                      
    REMARK   3  NCS RESTRAINTS STATISTICS                                           
    REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
    REMARK   3                                                                      
    REMARK   3  TLS DETAILS                                                         
    REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
    REMARK   3                                                                      
    REMARK   3   TLS GROUP : 1                                                      
    REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
    REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
    REMARK   3    RESIDUE RANGE :   A   637        A   645                          
    REMARK   3    ORIGIN FOR THE GROUP (A):  -8.6520  66.0300  27.4230              
    REMARK   3    T TENSOR                                                          
    REMARK   3      T11:   0.8102 T22:   0.6334                                     
    REMARK   3      T33:   0.0736 T12:  -0.1367                                     
    REMARK   3      T13:   0.0481 T23:  -0.0990                                     
    REMARK   3    L TENSOR                                                          
    REMARK   3      L11:   6.9694 L22:  10.9071                                     
    REMARK   3      L33:  22.4559 L12:  -4.8245                                     
    REMARK   3      L13:  -5.6534 L23:   6.1529                                     
    REMARK   3    S TENSOR                                                          
    REMARK   3      S11:  -0.2281 S12:  -0.0362 S13:  -0.5299                       
    REMARK   3      S21:   0.8334 S22:  -0.3809 S23:   0.7254                       
    REMARK   3      S31:   1.9299 S32:  -1.4008 S33:   0.6090                       
    REMARK   3                                                                      
    REMARK   3   TLS GROUP : 2                                                      
    REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
    REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
    REMARK   3    RESIDUE RANGE :   A   646        A   661                          
    REMARK   3    ORIGIN FOR THE GROUP (A):  -4.8680  57.1170  13.5580              
    REMARK   3    T TENSOR                                                          
    REMARK   3      T11:   0.4049 T22:   0.4396                                     
    REMARK   3      T33:   0.0621 T12:   0.0005                                     
    REMARK   3      T13:  -0.0096 T23:  -0.0658                                     
    REMARK   3    L TENSOR                                                          
    REMARK   3      L11:   5.2256 L22:  13.2604                                     
    REMARK   3      L33:   6.0221 L12:   0.8350                                     
    REMARK   3      L13:  -0.3475 L23:   5.3052                                     
    REMARK   3    S TENSOR                                                          
    REMARK   3      S11:  -0.0726 S12:   0.2498 S13:  -0.3232                       
    REMARK   3      S21:  -0.0731 S22:  -0.2151 S23:   0.6502                       
    REMARK   3      S31:   0.0341 S32:  -0.6076 S33:   0.2877                       
    REMARK   3                                                                      
    REMARK   3   TLS GROUP : 3                                                      
    REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
    REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
    REMARK   3    RESIDUE RANGE :   A   662        A   671                          
    REMARK   3    ORIGIN FOR THE GROUP (A):   3.4450  55.9580  17.4600              
    REMARK   3    T TENSOR                                                          
    REMARK   3      T11:   0.5052 T22:   0.4583                                     
    REMARK   3      T33:   0.1231 T12:  -0.0008                                     
    REMARK   3      T13:  -0.0070 T23:  -0.0344                                     
    REMARK   3    L TENSOR                                                          
    REMARK   3      L11:   3.4309 L22:   8.3868                                     
    REMARK   3      L33:   6.5105 L12:   0.3435                                     
    REMARK   3      L13:   2.0397 L23:   0.2650                                     
    REMARK   3    S TENSOR                                                          
    REMARK   3      S11:  -0.1390 S12:   0.0581 S13:  -0.5016                       
    REMARK   3      S21:   0.0040 S22:  -0.0394 S23:   0.1470                       
    REMARK   3      S31:  -0.2002 S32:   0.0832 S33:   0.1784                       
    REMARK   3                                                                      
    REMARK   3   TLS GROUP : 4                                                      
    REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
    REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
    REMARK   3    RESIDUE RANGE :   A   672        A   698                          
    REMARK   3    ORIGIN FOR THE GROUP (A):   5.8880  46.0570  24.5100              
    REMARK   3    T TENSOR                                                          
    REMARK   3      T11:   0.4192 T22:   0.4413                                     
    REMARK   3      T33:   0.0845 T12:   0.0425                                     
    REMARK   3      T13:   0.1337 T23:   0.0155                                     
    REMARK   3    L TENSOR                                                          
    REMARK   3      L11:   4.0368 L22:   9.6449                                     
    REMARK   3      L33:   4.7331 L12:  -2.6128                                     
    REMARK   3      L13:  -1.7662 L23:   2.1589                                     
    REMARK   3    S TENSOR                                                          
    REMARK   3      S11:  -0.6915 S12:  -0.2001 S13:  -0.4183                       
    REMARK   3      S21:   0.6160 S22:   0.1832 S23:   0.3146                       
    REMARK   3      S31:   0.2982 S32:  -0.1934 S33:   0.5083                       
    REMARK   3                                                                      
    REMARK   3   TLS GROUP : 5                                                      
    REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
    REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
    REMARK   3    RESIDUE RANGE :   A   699        A   715                          
    REMARK   3    ORIGIN FOR THE GROUP (A):  12.6620  31.1950  22.9920              
    REMARK   3    T TENSOR                                                          
    REMARK   3      T11:   0.4757 T22:   0.2858                                     
    REMARK   3      T33:   0.3764 T12:   0.0380                                     
    REMARK   3      T13:   0.3090 T23:   0.0511                                     
    REMARK   3    L TENSOR                                                          
    REMARK   3      L11:  12.2717 L22:   9.0614                                     
    REMARK   3      L33:  15.8036 L12:  -3.0546                                     
    REMARK   3      L13:  -6.4357 L23:  -0.4431                                     
    REMARK   3    S TENSOR                                                          
    REMARK   3      S11:  -0.7594 S12:  -0.7271 S13:  -1.3264                       
    REMARK   3      S21:   0.7681 S22:   0.3045 S23:   0.2732                       
    REMARK   3      S31:   1.0297 S32:   0.1933 S33:   0.4548                       
    REMARK   3                                                                      
    REMARK   3   TLS GROUP : 6                                                      
    REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
    REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
    REMARK   3    RESIDUE RANGE :   A   716        A   739                          
    REMARK   3    ORIGIN FOR THE GROUP (A):   8.4510  38.7780  14.9760              
    REMARK   3    T TENSOR                                                          
    REMARK   3      T11:   0.5341 T22:   0.4981                                     
    REMARK   3      T33:   0.3339 T12:  -0.1077                                     
    REMARK   3      T13:   0.2018 T23:  -0.1408                                     
    REMARK   3    L TENSOR                                                          
    REMARK   3      L11:   5.5817 L22:   6.6894                                     
    REMARK   3      L33:   5.6811 L12:  -5.3055                                     
    REMARK   3      L13:  -0.7765 L23:   1.0737                                     
    REMARK   3    S TENSOR                                                          
    REMARK   3      S11:  -0.1280 S12:   0.6475 S13:  -1.0672                       
    REMARK   3      S21:  -0.2807 S22:  -0.2164 S23:   0.9318                       
    REMARK   3      S31:   0.2186 S32:  -0.4450 S33:   0.3445                       
    REMARK   3                                                                      
    REMARK   3  BULK SOLVENT MODELLING.                                             
    REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
    REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
    REMARK   3   VDW PROBE RADIUS   : 1.20                                          
    REMARK   3   ION PROBE RADIUS   : 0.80                                          
    REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
    REMARK   3                                                                      
    REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS       
    REMARK   3  HAVE BEEN ADDED IN THE RIDING POSITIONS                             
    REMARK   4                                                                      
    REMARK   4 5DSD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
    REMARK 100                                                                      
    REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-15.                  
    REMARK 100 THE DEPOSITION ID IS D_1000213732.                                   
    REMARK 200                                                                      
    REMARK 200 EXPERIMENTAL DETAILS                                                 
    REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
    REMARK 200  DATE OF DATA COLLECTION        : 14-AUG-14                          
    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               : APS                                
    REMARK 200  BEAMLINE                       : 21-ID-D                            
    REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
    REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
    REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99                               
    REMARK 200  MONOCHROMATOR                  : SI(111)                            
    REMARK 200  OPTICS                         : NULL                               
    REMARK 200                                                                      
    REMARK 200  DETECTOR TYPE                  : CCD                                
    REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HE                    
    REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
    REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
    REMARK 200                                                                      
    REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12398                              
    REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
    REMARK 200  RESOLUTION RANGE LOW       (A) : 80.000                             
    REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
    REMARK 200                                                                      
    REMARK 200 OVERALL.                                                             
    REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
    REMARK 200  DATA REDUNDANCY                : 14.80                              
    REMARK 200  R MERGE                    (I) : 0.08400                            
    REMARK 200  R SYM                      (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3000                            
    REMARK 200                                                                      
    REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
    REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.7                               
    REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
    REMARK 200  R MERGE FOR SHELL          (I) : 0.43200                            
    REMARK 200  R SYM FOR SHELL            (I) : 0.43200                            
    REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
    REMARK 200                                                                      
    REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
    REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
    REMARK 200 SOFTWARE USED: HKL-3000                                              
    REMARK 200 STARTING MODEL: 4QB0                                                 
    REMARK 200                                                                      
    REMARK 200 REMARK: NULL                                                         
    REMARK 280                                                                      
    REMARK 280 CRYSTAL                                                              
    REMARK 280 SOLVENT CONTENT, VS   (%): 79.00                                     
    REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.94                     
    REMARK 280                                                                      
    REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION SOLUTION: 1.33 M         
    REMARK 280  LISO4, 0.1 M TRIS PH 8.5. 1:1 RATIO (250 NL: 250 NL) OF             
    REMARK 280  PRECIPITANT TO PROTEIN (AT A CONCENTRATION OF 13.9 MG/ML). 60       
    REMARK 280  MCL RESERVOIR. PROTEIN PURIFICATION BUFFER 50MM TRIS-HCL, 150 MM    
    REMARK 280  NACL; PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K       
    REMARK 290                                                                      
    REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
    REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2                         
    REMARK 290                                                                      
    REMARK 290      SYMOP   SYMMETRY                                                
    REMARK 290     NNNMMM   OPERATOR                                                
    REMARK 290       1555   X,Y,Z                                                   
    REMARK 290       2555   -Y,X-Y,Z+1/3                                            
    REMARK 290       3555   -X+Y,-X,Z+2/3                                           
    REMARK 290       4555   -X,-Y,Z                                                 
    REMARK 290       5555   Y,-X+Y,Z+1/3                                            
    REMARK 290       6555   X-Y,X,Z+2/3                                             
    REMARK 290       7555   Y,X,-Z+1/3                                              
    REMARK 290       8555   X-Y,-Y,-Z                                               
    REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
    REMARK 290      10555   -Y,-X,-Z+1/3                                            
    REMARK 290      11555   -X+Y,Y,-Z                                               
    REMARK 290      12555   X,X-Y,-Z+2/3                                            
    REMARK 290                                                                      
    REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
    REMARK 290           MMM -> TRANSLATION VECTOR                                  
    REMARK 290                                                                      
    REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
    REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
    REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
    REMARK 290 RELATED MOLECULES.                                                   
    REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
    REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
    REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       27.57867            
    REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
    REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       55.15733            
    REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
    REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
    REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       27.57867            
    REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
    REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       55.15733            
    REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
    REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       27.57867            
    REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
    REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
    REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       55.15733            
    REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
    REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       27.57867            
    REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
    REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
    REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
    REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       55.15733            
    REMARK 290                                                                      
    REMARK 290 REMARK: NULL                                                         
    REMARK 300                                                                      
    REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
    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: MONOMERIC                         
    REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
    REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
    REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
    REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
    REMARK 350                                                                      
    REMARK 350 BIOMOLECULE: 2                                                       
    REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
    REMARK 350 SOFTWARE USED: PISA                                                  
    REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2                          
    REMARK 350 SURFACE AREA OF THE COMPLEX: 12490 ANGSTROM**2                       
    REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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  0.500000  0.866025  0.000000      -54.47850            
    REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       94.35953            
    REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       55.15733            
    REMARK 350                                                                      
    REMARK 350 BIOMOLECULE: 3                                                       
    REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
    REMARK 350 SOFTWARE USED: PISA                                                  
    REMARK 350 TOTAL BURIED SURFACE AREA: 2050 ANGSTROM**2                          
    REMARK 350 SURFACE AREA OF THE COMPLEX: 13350 ANGSTROM**2                       
    REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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  0.500000 -0.866025  0.000000       54.47850            
    REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       94.35953            
    REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       27.57867            
    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    ALA A 638      171.85    -59.24                                   
    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 GOL A 801                 
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: AC2                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 802                 
    REMARK 800                                                                      
    REMARK 800 SITE_IDENTIFIER: AC3                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 803                  
    REMARK 900                                                                      
    REMARK 900 RELATED ENTRIES                                                      
    REMARK 900 RELATED ID: 4QAZ   RELATED DB: PDB                                   
    REMARK 900 THE CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF EBOLA (ZAIRE)      
    REMARK 900 NUCLEOPROTEIN                                                        
    REMARK 900 RELATED ID: 4QB0   RELATED DB: PDB                                   
    REMARK 900 THE CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF EBOLA (ZAIRE)      
    REMARK 900 NUCLEOPROTEIN                                                        
    DBREF  5DSD A  641   739  UNP    B8XCM7   B8XCM7_9MONO   641    739             
    SEQADV 5DSD GLY A  637  UNP  B8XCM7              EXPRESSION TAG                 
    SEQADV 5DSD ALA A  638  UNP  B8XCM7              EXPRESSION TAG                 
    SEQADV 5DSD MET A  639  UNP  B8XCM7              EXPRESSION TAG                 
    SEQADV 5DSD ALA A  640  UNP  B8XCM7              EXPRESSION TAG                 
    SEQRES   1 A  103  GLY ALA MET ALA ASN ALA GLN SER GLU GLN SER ILE ALA          
    SEQRES   2 A  103  GLU MET TYR GLN HIS ILE LEU LYS THR GLN GLY PRO PHE          
    SEQRES   3 A  103  ASP ALA ILE LEU TYR TYR HIS MET MET LYS GLU GLU PRO          
    SEQRES   4 A  103  ILE ILE PHE SER THR SER ASP GLY LYS GLU TYR THR TYR          
    SEQRES   5 A  103  PRO ASP SER LEU GLU ASP GLU TYR PRO PRO TRP LEU SER          
    SEQRES   6 A  103  GLU LYS GLU ALA MET ASN GLU ASP ASN ARG PHE ILE THR          
    SEQRES   7 A  103  MET ASP GLY GLN GLN PHE TYR TRP PRO VAL MET ASN HIS          
    SEQRES   8 A  103  ARG ASN LYS PHE MET ALA ILE LEU GLN HIS HIS ARG              
    HET    GOL  A 801       6                                                       
    HET    GOL  A 802       6                                                       
    HET     CL  A 803       1                                                       
    HETNAM     GOL GLYCEROL                                                         
    HETNAM      CL CHLORIDE ION                                                     
    HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
    FORMUL   2  GOL    2(C3 H8 O3)                                                  
    FORMUL   4   CL    CL 1-                                                        
    FORMUL   5  HOH   *112(H2 O)                                                    
    HELIX    1 AA1 SER A  644  GLN A  659  1                                  16    
    HELIX    2 AA2 GLY A  660  GLU A  673  1                                  14    
    HELIX    3 AA3 PRO A  689  GLU A  693  5                                   5    
    HELIX    4 AA4 LYS A  703  ASN A  710  5                                   8    
    HELIX    5 AA5 PRO A  723  MET A  725  5                                   3    
    HELIX    6 AA6 ASN A  726  HIS A  738  1                                  13    
    SHEET    1 AA1 2 ILE A 676  SER A 679  0                                        
    SHEET    2 AA1 2 GLU A 685  TYR A 688 -1  O  TYR A 688   N  ILE A 676           
    SHEET    1 AA2 2 PHE A 712  THR A 714  0                                        
    SHEET    2 AA2 2 GLN A 719  TYR A 721 -1  O  PHE A 720   N  ILE A 713           
    CISPEP   1 TYR A  688    PRO A  689          0         3.93                     
    SITE     1 AC1  2 LYS A 703  ASN A 707                                          
    SITE     1 AC2  5 ASN A 726  ARG A 728  HOH A 927  HOH A 936                    
    SITE     2 AC2  5 HOH A1009                                                     
    SITE     1 AC3  1 SER A 679                                                     
    CRYST1  108.957  108.957   82.736  90.00  90.00 120.00 P 64 2 2     12          
    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      0.009178  0.005299  0.000000        0.00000                         
    SCALE2      0.000000  0.010598  0.000000        0.00000                         
    SCALE3      0.000000  0.000000  0.012087        0.00000                         

    3D molecular view of vibration

    Displacement vectors
    Display
    Animation
    Display

    Still image of displacement vectors and GIF animation


    Mode 1

    Time-average properties and properties of the 10 lowest-frequency modes

    Fluctuation of atoms:
    Time average and for the 3 lowest-frequency modes.
    Fluctuation of dihedral angles:
    Time average and for the 3 lowest-frequency modes.
    Fluctuation of atomsFluctuation of dihedral angles

    Correlations between fluctuations of atoms

    Mode 1
    Correlations between fluctuations of atoms - Mode 1
    Time Average
    Time Average
    Distance map
    Distance map

    Calculation note

    PDB file name : pdb5dsd.ent

    Chains and HETATMs selected: 
      ATOM        A

    The following atoms are removed from PDB data on concern that they may have 
    abnormally large fluctuations, because they interact with few atoms.
      ATOM    157  CG  LYS A 657      -8.809  53.111   8.304  1.00 83.75           C  
      ATOM    158  CD  LYS A 657     -10.205  53.546   8.739  1.00153.91           C  
      ATOM    159  CE  LYS A 657     -11.181  53.595   7.574  1.00129.93           C  
      ATOM    160  NZ  LYS A 657     -11.109  54.903   6.871  1.00125.04           N  
      ATOM    267  CG  MET A 670       6.562  61.730  17.290  1.00121.24           C  
      ATOM    268  SD  MET A 670       6.953  62.103  15.554  1.00 89.68           S  
      ATOM    269  CE  MET A 670       6.380  60.614  14.719  1.00 84.04           C  

    = Normal mode analysis calculation =

    No. of modes used in the calculation : All modes.

    Parameters of potential energies:
      1-4 and 1-5 non-bonded interactions: E(d) = A*exp(-d(PDB)**2/B**2)(d-d(PDB))**2.
      Loop-closing potential:              E(d) = A*(d-d(PDB))**2.
        for a disulfide bond and one of the bonds in the DNA and RNA sugar ring.
      where d and d(PDB) are distances between atoms in calculation and in PDB data, 
      respectively.

      Interaction type   A       B      Cutoff distance (A)
        1-4             1.00    5.00      100.00
        1-5             1.00    5.00      100.00
        Loop-closing  100.00

    Temperature adjustment by magnitude of fluctuation:
      Set to mean displacements of atoms       0.500 A

    Animation
      No. of frames: 11
      Mean displacements (A):    0.50

    Displacement vector
      Mean length of vectors (A):    3.00