?

Promode Elastic




    Copyright ©  WASEDA Univ,Japan. All rights reserved.

    Header

    HEADER    CHAPERONE                               28-NOV-18   6N86              
    TITLE     RESISTANCE TO INHIBITORS OF CHOLINESTERASE 8A (RIC8A) PROTEIN         
    COMPND    MOL_ID: 1;                                                            
    COMPND   2 MOLECULE: SYNEMBRYN-A;                                               
    COMPND   3 CHAIN: B;                                                            
    COMPND   4 SYNONYM: PROTEIN RIC-8A;                                             
    COMPND   5 ENGINEERED: YES                                                      
    SOURCE    MOL_ID: 1;                                                            
    SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
    SOURCE   3 ORGANISM_COMMON: BOVINE;                                             
    SOURCE   4 ORGANISM_TAXID: 9913;                                                
    SOURCE   5 GENE: RIC8A;                                                         
    SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
    SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
    SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
    SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
    KEYWDS    RIC8A, ARMADILLO REPEAT, G ALPHA, CHAPERONE                           
    EXPDTA    X-RAY DIFFRACTION                                                     
    AUTHOR    D.SRIVASTAVA,L.GAKHAR,N.O.ARTEMYEV                                    
    REVDAT   1   10-JUL-19 6N86    0                                                
    JRNL        AUTH   D.SRIVASTAVA,L.GAKHAR,N.O.ARTEMYEV                           
    JRNL        TITL   STRUCTURAL UNDERPINNINGS OF RIC8A FUNCTION AS A G-PROTEIN    
    JRNL        TITL 2 ALPHA-SUBUNIT CHAPERONE AND GUANINE-NUCLEOTIDE EXCHANGE      
    JRNL        TITL 3 FACTOR                                                       
    JRNL        REF    NAT COMMUN                                 2019              
    JRNL        REFN                   ESSN 2041-1723                               
    REMARK   2                                                                      
    REMARK   2 RESOLUTION.    3.90 ANGSTROMS.                                       
    REMARK   3                                                                      
    REMARK   3 REFINEMENT.                                                          
    REMARK   3   PROGRAM     : PHENIX (1.14_3260: ???)                              
    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) : 3.90                           
    REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 57.45                          
    REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
    REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
    REMARK   3   NUMBER OF REFLECTIONS             : 6641                           
    REMARK   3                                                                      
    REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
    REMARK   3   R VALUE     (WORKING + TEST SET) : 0.258                           
    REMARK   3   R VALUE            (WORKING SET) : 0.257                           
    REMARK   3   FREE R VALUE                     : 0.296                           
    REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.470                           
    REMARK   3   FREE R VALUE TEST SET COUNT      : 297                             
    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 57.4560 -  4.9133    1.00     3231   159  0.2499 0.2759        
    REMARK   3     2  4.9133 -  3.9001    0.99     3113   138  0.2726 0.3584        
    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)     : 0.560            
    REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.500           
    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      :  0.001           3201                                  
    REMARK   3   ANGLE     :  0.392           4325                                  
    REMARK   3   CHIRALITY :  0.030            516                                  
    REMARK   3   PLANARITY :  0.003            557                                  
    REMARK   3   DIHEDRAL  : 13.949           1992                                  
    REMARK   3                                                                      
    REMARK   3  TLS DETAILS                                                         
    REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
    REMARK   3   TLS GROUP : 1                                                      
    REMARK   3    SELECTION: ALL                                                    
    REMARK   3    ORIGIN FOR THE GROUP (A): -33.8906  18.7197 -16.2130              
    REMARK   3    T TENSOR                                                          
    REMARK   3      T11:   1.0013 T22:   0.9718                                     
    REMARK   3      T33:   1.0174 T12:  -0.1139                                     
    REMARK   3      T13:   0.1317 T23:   0.1275                                     
    REMARK   3    L TENSOR                                                          
    REMARK   3      L11:   1.2082 L22:   1.6268                                     
    REMARK   3      L33:   1.2475 L12:  -0.1989                                     
    REMARK   3      L13:   0.3203 L23:   0.2166                                     
    REMARK   3    S TENSOR                                                          
    REMARK   3      S11:  -0.0529 S12:   0.2305 S13:  -0.0365                       
    REMARK   3      S21:   0.3117 S22:   0.4225 S23:  -0.1164                       
    REMARK   3      S31:   0.4815 S32:   0.4819 S33:   0.5924                       
    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 6N86 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
    REMARK 100                                                                      
    REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-18.                  
    REMARK 100 THE DEPOSITION ID IS D_1000238311.                                   
    REMARK 200                                                                      
    REMARK 200 EXPERIMENTAL DETAILS                                                 
    REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
    REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-18                          
    REMARK 200  TEMPERATURE           (KELVIN) : 100                                
    REMARK 200  PH                             : 6.0 - 7.0                          
    REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
    REMARK 200                                                                      
    REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
    REMARK 200  RADIATION SOURCE               : ALS                                
    REMARK 200  BEAMLINE                       : 4.2.2                              
    REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
    REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
    REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
    REMARK 200  MONOCHROMATOR                  : NULL                               
    REMARK 200  OPTICS                         : NULL                               
    REMARK 200                                                                      
    REMARK 200  DETECTOR TYPE                  : CMOS                               
    REMARK 200  DETECTOR MANUFACTURER          : RDI CMOS_8M                        
    REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
    REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.22                       
    REMARK 200                                                                      
    REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6668                               
    REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.900                              
    REMARK 200  RESOLUTION RANGE LOW       (A) : 57.450                             
    REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
    REMARK 200                                                                      
    REMARK 200 OVERALL.                                                             
    REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
    REMARK 200  DATA REDUNDANCY                : 14.30                              
    REMARK 200  R MERGE                    (I) : 0.09700                            
    REMARK 200  R SYM                      (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.4000                            
    REMARK 200                                                                      
    REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.90                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.11                     
    REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
    REMARK 200  DATA REDUNDANCY IN SHELL       : 13.30                              
    REMARK 200  R MERGE FOR SHELL          (I) : 0.79900                            
    REMARK 200  R SYM FOR SHELL            (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
    REMARK 200                                                                      
    REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
    REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
    REMARK 200 SOFTWARE USED: PHASER                                                
    REMARK 200 STARTING MODEL: NULL                                                 
    REMARK 200                                                                      
    REMARK 200 REMARK: NULL                                                         
    REMARK 280                                                                      
    REMARK 280 CRYSTAL                                                              
    REMARK 280 SOLVENT CONTENT, VS   (%): 60.10                                     
    REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
    REMARK 280                                                                      
    REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE, 0.2 M NAI, 12    
    REMARK 280  -20 % PEG3350, SEEDING, PH 6.5, VAPOR DIFFUSION, SITTING DROP,      
    REMARK 280  TEMPERATURE 277K                                                    
    REMARK 290                                                                      
    REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
    REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 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,Y+1/2,Z+1/2                                           
    REMARK 290       6555   -X,-Y+1/2,Z+1/2                                         
    REMARK 290       7555   -X,Y+1/2,-Z+1/2                                         
    REMARK 290       8555   X,-Y+1/2,-Z+1/2                                         
    REMARK 290       9555   X+1/2,Y,Z+1/2                                           
    REMARK 290      10555   -X+1/2,-Y,Z+1/2                                         
    REMARK 290      11555   -X+1/2,Y,-Z+1/2                                         
    REMARK 290      12555   X+1/2,-Y,-Z+1/2                                         
    REMARK 290      13555   X+1/2,Y+1/2,Z                                           
    REMARK 290      14555   -X+1/2,-Y+1/2,Z                                         
    REMARK 290      15555   -X+1/2,Y+1/2,-Z                                         
    REMARK 290      16555   X+1/2,-Y+1/2,-Z                                         
    REMARK 290                                                                      
    REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
    REMARK 290           MMM -> TRANSLATION VECTOR                                  
    REMARK 290                                                                      
    REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
    REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
    REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
    REMARK 290 RELATED MOLECULES.                                                   
    REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
    REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        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        0.00000            
    REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       67.17000            
    REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      110.87500            
    REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       67.17000            
    REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      110.87500            
    REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       67.17000            
    REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      110.87500            
    REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       67.17000            
    REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      110.87500            
    REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       47.57500            
    REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      110.87500            
    REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       47.57500            
    REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000      110.87500            
    REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000       47.57500            
    REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      110.87500            
    REMARK 290   SMTRY1  12  1.000000  0.000000  0.000000       47.57500            
    REMARK 290   SMTRY2  12  0.000000 -1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      110.87500            
    REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       47.57500            
    REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       67.17000            
    REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000        0.00000            
    REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       47.57500            
    REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       67.17000            
    REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000            
    REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       47.57500            
    REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       67.17000            
    REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
    REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       47.57500            
    REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       67.17000            
    REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000        0.00000            
    REMARK 290                                                                      
    REMARK 290 REMARK: NULL                                                         
    REMARK 300                                                                      
    REMARK 300 BIOMOLECULE: 1                                                       
    REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
    REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
    REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
    REMARK 300 BURIED SURFACE AREA.                                                 
    REMARK 350                                                                      
    REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
    REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
    REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
    REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
    REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
    REMARK 350                                                                      
    REMARK 350 BIOMOLECULE: 1                                                       
    REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
    REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
    REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
    REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
    REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
    REMARK 465                                                                      
    REMARK 465 MISSING RESIDUES                                                     
    REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
    REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
    REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
    REMARK 465                                                                      
    REMARK 465   M RES C SSSEQI                                                     
    REMARK 465     MET B   -19                                                      
    REMARK 465     GLY B   -18                                                      
    REMARK 465     SER B   -17                                                      
    REMARK 465     SER B   -16                                                      
    REMARK 465     HIS B   -15                                                      
    REMARK 465     HIS B   -14                                                      
    REMARK 465     HIS B   -13                                                      
    REMARK 465     HIS B   -12                                                      
    REMARK 465     HIS B   -11                                                      
    REMARK 465     HIS B   -10                                                      
    REMARK 465     SER B    -9                                                      
    REMARK 465     SER B    -8                                                      
    REMARK 465     GLY B    -7                                                      
    REMARK 465     LEU B    -6                                                      
    REMARK 465     VAL B    -5                                                      
    REMARK 465     PRO B    -4                                                      
    REMARK 465     ARG B    -3                                                      
    REMARK 465     GLY B    -2                                                      
    REMARK 465     SER B    -1                                                      
    REMARK 465     HIS B     0                                                      
    REMARK 465     GLN B   102                                                      
    REMARK 465     GLY B   103                                                      
    REMARK 465     SER B   104                                                      
    REMARK 465     VAL B   105                                                      
    REMARK 465     PRO B   106                                                      
    REMARK 465     MET B   202                                                      
    REMARK 465     THR B   203                                                      
    REMARK 465     GLU B   204                                                      
    REMARK 465     GLY B   205                                                      
    REMARK 465     GLU B   206                                                      
    REMARK 465     ARG B   207                                                      
    REMARK 465     LEU B   292                                                      
    REMARK 465     GLU B   293                                                      
    REMARK 465     PRO B   294                                                      
    REMARK 465     HIS B   295                                                      
    REMARK 465     GLU B   296                                                      
    REMARK 465     GLY B   297                                                      
    REMARK 465     SER B   298                                                      
    REMARK 465     LEU B   299                                                      
    REMARK 465     GLU B   300                                                      
    REMARK 465     PHE B   301                                                      
    REMARK 465     LEU B   302                                                      
    REMARK 465     GLY B   303                                                      
    REMARK 465     GLY B   423                                                      
    REMARK 465     LEU B   424                                                      
    REMARK 465     MET B   425                                                      
    REMARK 465     ALA B   426                                                      
    REMARK 465     GLY B   427                                                      
    REMARK 465     GLY B   428                                                      
    REMARK 465     ARG B   429                                                      
    REMARK 465     PRO B   430                                                      
    REMARK 465     GLU B   431                                                      
    REMARK 465     GLY B   432                                                      
    REMARK 465     GLN B   433                                                      
    REMARK 465     TYR B   434                                                      
    REMARK 465     SER B   435                                                      
    REMARK 465     GLU B   436                                                      
    REMARK 465     ASP B   437                                                      
    REMARK 465     GLU B   438                                                      
    REMARK 465     ASP B   439                                                      
    REMARK 465     THR B   440                                                      
    REMARK 465     ASP B   441                                                      
    REMARK 465     THR B   442                                                      
    REMARK 465     ASP B   443                                                      
    REMARK 465     GLU B   444                                                      
    REMARK 465     TYR B   445                                                      
    REMARK 465     LYS B   446                                                      
    REMARK 465     GLU B   447                                                      
    REMARK 465     ALA B   448                                                      
    REMARK 465     LYS B   449                                                      
    REMARK 465     ALA B   450                                                      
    REMARK 465     SER B   451                                                      
    REMARK 465     ILE B   452                                                      
    REMARK 465     ASN B   453                                                      
    REMARK 465     PRO B   454                                                      
    REMARK 465     VAL B   455                                                      
    REMARK 465     THR B   456                                                      
    REMARK 465     GLY B   457                                                      
    REMARK 465     ARG B   458                                                      
    REMARK 465     VAL B   459                                                      
    REMARK 465     GLU B   460                                                      
    REMARK 465     GLU B   461                                                      
    REMARK 465     LYS B   462                                                      
    REMARK 465     PRO B   463                                                      
    REMARK 465     PRO B   464                                                      
    REMARK 465     ASN B   465                                                      
    REMARK 465     PRO B   466                                                      
    REMARK 465     MET B   467                                                      
    REMARK 465     GLU B   468                                                      
    REMARK 465     GLY B   469                                                      
    REMARK 465     MET B   470                                                      
    REMARK 465     THR B   471                                                      
    REMARK 465     GLU B   472                                                      
    REMARK 465     GLU B   473                                                      
    REMARK 465     GLN B   474                                                      
    REMARK 465     LYS B   475                                                      
    REMARK 465     GLU B   476                                                      
    REMARK 465     HIS B   477                                                      
    REMARK 465     GLU B   478                                                      
    REMARK 465     ALA B   479                                                      
    REMARK 465     MET B   480                                                      
    REMARK 465     LYS B   481                                                      
    REMARK 465     LEU B   482                                                      
    REMARK 465     VAL B   483                                                      
    REMARK 465     ASN B   484                                                      
    REMARK 465     MET B   485                                                      
    REMARK 465     PHE B   486                                                      
    REMARK 465     ASP B   487                                                      
    REMARK 465     LYS B   488                                                      
    REMARK 465     LEU B   489                                                      
    REMARK 465     SER B   490                                                      
    REMARK 465     ARG B   491                                                      
    REMARK 465     HIS B   492                                                      
    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 B  14     -157.09    -82.49                                   
    REMARK 500    GLN B  39       31.28    -98.27                                   
    REMARK 500    ARG B  63      -49.58   -136.37                                   
    REMARK 500    LEU B 150      -72.59    -50.99                                   
    REMARK 500    CYS B 151      -46.99     62.09                                   
    REMARK 500    ARG B 152      -70.13    -81.44                                   
    REMARK 500    SER B 155       31.38    -93.98                                   
    REMARK 500    PHE B 232      -25.51   -162.83                                   
    REMARK 500                                                                      
    REMARK 500 REMARK: NULL                                                         
    DBREF  6N86 B    1   492  UNP    Q5E9J8   RIC8A_BOVIN      1    492             
    SEQADV 6N86 MET B  -19  UNP  Q5E9J8              INITIATING METHIONINE          
    SEQADV 6N86 GLY B  -18  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 SER B  -17  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 SER B  -16  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 HIS B  -15  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 HIS B  -14  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 HIS B  -13  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 HIS B  -12  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 HIS B  -11  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 HIS B  -10  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 SER B   -9  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 SER B   -8  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 GLY B   -7  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 LEU B   -6  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 VAL B   -5  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 PRO B   -4  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 ARG B   -3  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 GLY B   -2  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 SER B   -1  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQADV 6N86 HIS B    0  UNP  Q5E9J8              EXPRESSION TAG                 
    SEQRES   1 B  512  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
    SEQRES   2 B  512  LEU VAL PRO ARG GLY SER HIS MET GLU PRO ARG ALA VAL          
    SEQRES   3 B  512  ALA ASP ALA LEU GLU THR GLY GLU GLU ASP VAL VAL MET          
    SEQRES   4 B  512  GLU ALA LEU ARG ALA TYR ASN ARG GLU ASN SER GLN SER          
    SEQRES   5 B  512  PHE THR PHE ASP ASP ALA GLN GLN GLU ASP ARG LYS ARG          
    SEQRES   6 B  512  LEU ALA LYS LEU LEU VAL SER VAL LEU GLU GLN GLY LEU          
    SEQRES   7 B  512  PRO PRO SER ARG ARG VAL ILE TRP LEU GLN SER ILE ARG          
    SEQRES   8 B  512  ILE LEU SER ARG ASP ARG SER CYS LEU ASP SER PHE THR          
    SEQRES   9 B  512  SER ARG ARG SER LEU GLN ALA LEU ALA CYS TYR ALA GLY          
    SEQRES  10 B  512  ILE SER ALA SER GLN GLY SER VAL PRO GLU PRO LEU ASN          
    SEQRES  11 B  512  MET ASP VAL VAL LEU GLU SER LEU LYS CYS LEU CYS ASN          
    SEQRES  12 B  512  LEU VAL LEU SER SER PRO VAL ALA GLN ALA LEU ALA ALA          
    SEQRES  13 B  512  GLU ALA GLY LEU VAL VAL ARG LEU ALA GLU ARG VAL GLY          
    SEQRES  14 B  512  LEU CYS ARG GLN SER SER PHE PRO HIS ASP VAL GLN PHE          
    SEQRES  15 B  512  PHE ASP LEU ARG LEU LEU PHE LEU LEU THR ALA LEU ARG          
    SEQRES  16 B  512  THR ASP VAL ARG GLN GLN LEU PHE GLN GLU LEU GLN GLY          
    SEQRES  17 B  512  VAL ARG LEU LEU THR ARG ALA LEU GLU LEU THR LEU GLY          
    SEQRES  18 B  512  MET THR GLU GLY GLU ARG HIS PRO GLU LEU LEU PRO PRO          
    SEQRES  19 B  512  GLN GLU THR GLU ARG ALA MET GLU ILE LEU LYS VAL LEU          
    SEQRES  20 B  512  PHE ASN ILE THR PHE ASP SER ILE LYS ARG GLU VAL ASP          
    SEQRES  21 B  512  GLU GLU ASP ALA ALA LEU TYR ARG HIS LEU GLY THR LEU          
    SEQRES  22 B  512  LEU ARG HIS CYS VAL MET LEU ALA ALA ALA GLY ASP ARG          
    SEQRES  23 B  512  THR GLU GLU LEU HIS GLY HIS ALA VAL ASN LEU LEU GLY          
    SEQRES  24 B  512  ASN LEU PRO VAL LYS CYS LEU ASP VAL LEU LEU THR LEU          
    SEQRES  25 B  512  GLU PRO HIS GLU GLY SER LEU GLU PHE LEU GLY VAL ASN          
    SEQRES  26 B  512  MET ASP VAL ILE ARG VAL LEU LEU SER PHE MET GLU LYS          
    SEQRES  27 B  512  ARG LEU HIS GLN THR HIS ARG LEU LYS GLU SER VAL ALA          
    SEQRES  28 B  512  PRO VAL LEU SER VAL LEU THR GLU CYS ALA ARG MET HIS          
    SEQRES  29 B  512  ARG PRO ALA ARG LYS PHE LEU LYS ALA GLN VAL LEU PRO          
    SEQRES  30 B  512  PRO LEU ARG ASP VAL ARG THR ARG PRO GLU VAL GLY GLU          
    SEQRES  31 B  512  LEU LEU ARG ASN LYS LEU VAL ARG LEU MET THR HIS LEU          
    SEQRES  32 B  512  ASP THR ASP VAL LYS ARG VAL ALA ALA GLU PHE LEU PHE          
    SEQRES  33 B  512  VAL LEU CYS SER GLU SER VAL PRO ARG PHE ILE LYS TYR          
    SEQRES  34 B  512  THR GLY TYR GLY ASN ALA ALA GLY LEU LEU ALA ALA ARG          
    SEQRES  35 B  512  GLY LEU MET ALA GLY GLY ARG PRO GLU GLY GLN TYR SER          
    SEQRES  36 B  512  GLU ASP GLU ASP THR ASP THR ASP GLU TYR LYS GLU ALA          
    SEQRES  37 B  512  LYS ALA SER ILE ASN PRO VAL THR GLY ARG VAL GLU GLU          
    SEQRES  38 B  512  LYS PRO PRO ASN PRO MET GLU GLY MET THR GLU GLU GLN          
    SEQRES  39 B  512  LYS GLU HIS GLU ALA MET LYS LEU VAL ASN MET PHE ASP          
    SEQRES  40 B  512  LYS LEU SER ARG HIS                                          
    HELIX    1 AA1 GLU B    2  THR B   12  1                                  11    
    HELIX    2 AA2 GLU B   14  ASN B   29  1                                  16    
    HELIX    3 AA3 GLN B   39  GLY B   57  1                                  19    
    HELIX    4 AA4 ARG B   63  ARG B   75  1                                  13    
    HELIX    5 AA5 ASP B   76  THR B   84  1                                   9    
    HELIX    6 AA6 SER B   85  ALA B   96  1                                  12    
    HELIX    7 AA7 ASN B  110  SER B  128  1                                  19    
    HELIX    8 AA8 SER B  128  GLY B  139  1                                  12    
    HELIX    9 AA9 GLY B  139  CYS B  151  1                                  13    
    HELIX   10 AB1 PRO B  157  ARG B  175  1                                  19    
    HELIX   11 AB2 ARG B  175  GLN B  184  1                                  10    
    HELIX   12 AB3 GLN B  187  GLY B  201  1                                  15    
    HELIX   13 AB4 PRO B  213  THR B  231  1                                  19    
    HELIX   14 AB5 ASP B  240  MET B  259  1                                  20    
    HELIX   15 AB6 ARG B  266  GLY B  279  1                                  14    
    HELIX   16 AB7 VAL B  283  LEU B  290  5                                   8    
    HELIX   17 AB8 MET B  306  LEU B  320  1                                  15    
    HELIX   18 AB9 ARG B  325  HIS B  344  1                                  20    
    HELIX   19 AC1 HIS B  344  LEU B  356  1                                  13    
    HELIX   20 AC2 LEU B  371  MET B  380  1                                  10    
    HELIX   21 AC3 ASP B  384  CYS B  399  1                                  16    
    HELIX   22 AC4 SER B  402  GLY B  411  1                                  10    
    HELIX   23 AC5 GLY B  411  ARG B  422  1                                  12    
    SHEET    1 AA1 2 LEU B 211  LEU B 212  0                                        
    SHEET    2 AA1 2 ALA B 261  ALA B 262  1  O  ALA B 261   N  LEU B 212           
    CRYST1   95.150  134.340  221.750  90.00  90.00  90.00 F 2 2 2      16          
    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      0.010510  0.000000  0.000000        0.00000                         
    SCALE2      0.000000  0.007444  0.000000        0.00000                         
    SCALE3      0.000000  0.000000  0.004510        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 : pdb6n86.ent

    Chains and HETATMs selected: 
      ATOM        B

    The following atoms are removed from PDB data on concern that they may have 
    abnormally large fluctuations, because they interact with few atoms.
      ATOM      6  CG  MET B   1     -52.455  24.355  18.887  1.00265.04           C  
      ATOM      7  SD  MET B   1     -53.180  23.236  17.672  1.00273.56           S  
      ATOM      8  CE  MET B   1     -54.423  24.295  16.936  1.00275.26           C  
      ATOM    620  CG  ARG B  77     -40.037  33.265  -0.623  1.00210.97           C  
      ATOM    621  CD  ARG B  77     -40.658  34.041  -1.772  1.00226.03           C  
      ATOM    622  NE  ARG B  77     -39.811  35.150  -2.201  1.00240.41           N  
      ATOM    623  CZ  ARG B  77     -40.132  36.004  -3.167  1.00249.47           C  
      ATOM    624  NH1 ARG B  77     -41.285  35.878  -3.811  1.00249.36           N  
      ATOM    625  NH2 ARG B  77     -39.300  36.985  -3.491  1.00251.94           N  
      ATOM   1776  CG  LYS B 236     -14.034  23.213 -27.432  1.00272.20           C  
      ATOM   1777  CD  LYS B 236     -12.515  23.214 -27.499  1.00283.53           C  
      ATOM   1778  CE  LYS B 236     -11.901  23.958 -26.323  1.00292.93           C  
      ATOM   1779  NZ  LYS B 236     -10.413  23.975 -26.402  1.00301.82           N  
      ATOM   1785  CG  ARG B 237     -17.177  24.354 -33.306  1.00251.24           C  
      ATOM   1786  CD  ARG B 237     -16.909  25.296 -34.468  1.00248.23           C  
      ATOM   1787  NE  ARG B 237     -17.636  26.554 -34.329  1.00242.09           N  
      ATOM   1788  CZ  ARG B 237     -17.615  27.532 -35.228  1.00240.38           C  
      ATOM   1789  NH1 ARG B 237     -16.902  27.401 -36.338  1.00241.46           N  
      ATOM   1790  NH2 ARG B 237     -18.309  28.643 -35.018  1.00238.20           N  
      ATOM   2147  CG  LYS B 284     -18.792  14.826 -36.774  1.00246.12           C  
      ATOM   2148  CD  LYS B 284     -17.274  14.777 -36.684  1.00250.24           C  
      ATOM   2149  CE  LYS B 284     -16.628  15.751 -37.657  1.00249.40           C  
      ATOM   2150  NZ  LYS B 284     -15.141  15.693 -37.594  1.00247.49           N  
      ATOM   2706  CG  ARG B 365     -51.621  29.849 -52.625  1.00279.97           C  
      ATOM   2707  CD  ARG B 365     -52.067  31.203 -52.093  1.00279.49           C  
      ATOM   2708  NE  ARG B 365     -52.513  32.092 -53.162  1.00281.30           N  
      ATOM   2709  CZ  ARG B 365     -53.003  33.312 -52.964  1.00281.44           C  
      ATOM   2710  NH1 ARG B 365     -53.114  33.790 -51.733  1.00279.97           N  
      ATOM   2711  NH2 ARG B 365     -53.384  34.053 -53.996  1.00282.57           N  

    = 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       20.00
        1-5             1.00    5.00       20.00
        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