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Database: PDB
Entry: 5B56
LinkDB: 5B56
Original site: 5B56 
HEADER    PROTEIN TRANSPORT/VIRAL PROTEIN         25-APR-16   5B56              
TITLE     CRYSTAL STRUCTURE OF HIV-1 VPR C-TERMINAL DOMAIN AND DIBB-M-IMPORTIN- 
TITLE    2 ALPHA2 COMPLEX                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IMPORTIN SUBUNIT ALPHA-1;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 70-529;                                       
COMPND   5 SYNONYM: IMPORTIN ALPHA P1,KARYOPHERIN SUBUNIT ALPHA-2,PENDULIN,PORE 
COMPND   6 TARGETING COMPLEX 58 KDA SUBUNIT,PTAC58,RAG COHORT PROTEIN 1,SRP1-   
COMPND   7 ALPHA;                                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PROTEIN VPR;                                               
COMPND  11 CHAIN: C, D, E, F;                                                   
COMPND  12 FRAGMENT: C-TERMINAL DOMAIN, UNP RESIDUES 85-96;                     
COMPND  13 SYNONYM: R ORF PROTEIN,VIRAL PROTEIN R;                              
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: KPNA2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HIV-1 M:B_89.6;                                 
SOURCE  11 ORGANISM_COMMON: HIV-1;                                              
SOURCE  12 ORGANISM_TAXID: 401671;                                              
SOURCE  13 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    ARM REPEAT, ALL ALPHA PROTEIN, NUCLEAR IMPORT, IMPORTIN-BETA, NLS-    
KEYWDS   2 CARGO, PROTEIN TRANSPORT-VIRAL PROTEIN COMPLEX                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.MIYATAKE,A.SANJOH,G.MATUSDA,T.MURAKAMI,H.MURAKAMI,K.HAGIWARA,       
AUTHOR   2 M.YOKOYAMA,H.SATO,Y.MIYAMOTO,N.DOHMAE,Y.AIDA                         
REVDAT   4   08-NOV-23 5B56    1       REMARK                                   
REVDAT   3   26-FEB-20 5B56    1       JRNL   REMARK                            
REVDAT   2   29-JUN-16 5B56    1       JRNL                                     
REVDAT   1   01-JUN-16 5B56    0                                                
JRNL        AUTH   H.MIYATAKE,A.SANJOH,T.MURAKAMI,H.MURAKAMI,G.MATSUDA,         
JRNL        AUTH 2 K.HAGIWARA,M.YOKOYAMA,H.SATO,Y.MIYAMOTO,N.DOHMAE,Y.AIDA      
JRNL        TITL   MOLECULAR MECHANISM OF HIV-1 VPR FOR BINDING TO              
JRNL        TITL 2 IMPORTIN-ALPHA                                               
JRNL        REF    J.MOL.BIOL.                   V. 428  2744 2016              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   27181198                                                     
JRNL        DOI    10.1016/J.JMB.2016.05.003                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.210                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 57284                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2906                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.4064 -  6.3342    0.98     2989   174  0.1544 0.1867        
REMARK   3     2  6.3342 -  5.0301    0.99     2962   168  0.1811 0.2278        
REMARK   3     3  5.0301 -  4.3949    0.99     2987   159  0.1377 0.1727        
REMARK   3     4  4.3949 -  3.9934    0.99     3002   136  0.1331 0.1480        
REMARK   3     5  3.9934 -  3.7074    0.98     2899   161  0.1401 0.1997        
REMARK   3     6  3.7074 -  3.4889    0.98     2921   157  0.1592 0.2229        
REMARK   3     7  3.4889 -  3.3142    0.98     2910   164  0.1831 0.2200        
REMARK   3     8  3.3142 -  3.1700    0.96     2863   145  0.1943 0.2402        
REMARK   3     9  3.1700 -  3.0480    0.95     2845   151  0.1969 0.2535        
REMARK   3    10  3.0480 -  2.9428    0.92     2744   141  0.1952 0.2369        
REMARK   3    11  2.9428 -  2.8508    0.90     2660   146  0.2044 0.2680        
REMARK   3    12  2.8508 -  2.7694    0.89     2659   121  0.2184 0.2790        
REMARK   3    13  2.7694 -  2.6965    0.88     2584   142  0.2226 0.2863        
REMARK   3    14  2.6965 -  2.6307    0.86     2530   128  0.2372 0.2743        
REMARK   3    15  2.6307 -  2.5709    0.83     2502   120  0.2532 0.3171        
REMARK   3    16  2.5709 -  2.5162    0.79     2327   123  0.2723 0.3254        
REMARK   3    17  2.5162 -  2.4659    0.76     2239   112  0.2939 0.3302        
REMARK   3    18  2.4659 -  2.4193    0.75     2229   130  0.3007 0.3364        
REMARK   3    19  2.4193 -  2.3761    0.71     2100   120  0.3081 0.3318        
REMARK   3    20  2.3761 -  2.3359    0.66     1911   121  0.3236 0.3302        
REMARK   3    21  2.3359 -  2.2982    0.51     1515    87  0.3438 0.4092        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.360           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.74                          
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      :  0.003           7063                                  
REMARK   3   ANGLE     :  0.724           9601                                  
REMARK   3   CHIRALITY :  0.028           1147                                  
REMARK   3   PLANARITY :  0.003           1239                                  
REMARK   3   DIHEDRAL  : 14.235           2610                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 70:133)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  68.1292 -16.2423  45.5953              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7096 T22:   0.7267                                     
REMARK   3      T33:   0.6193 T12:  -0.0642                                     
REMARK   3      T13:   0.0876 T23:   0.1212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3210 L22:   1.4479                                     
REMARK   3      L33:   1.1499 L12:   0.5620                                     
REMARK   3      L13:  -0.4905 L23:   0.9592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0760 S12:   0.4480 S13:   0.1265                       
REMARK   3      S21:  -0.7355 S22:   0.0048 S23:  -0.5473                       
REMARK   3      S31:  -0.1383 S32:   0.9289 S33:   0.0025                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 134:362)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  38.2426  -8.6729  55.7619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3233 T22:   0.3649                                     
REMARK   3      T33:   0.5425 T12:  -0.0352                                     
REMARK   3      T13:  -0.0499 T23:   0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8931 L22:   0.8217                                     
REMARK   3      L33:  -0.0197 L12:  -2.4870                                     
REMARK   3      L13:   0.6370 L23:  -0.6147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1173 S12:  -0.2569 S13:   0.0103                       
REMARK   3      S21:   0.1165 S22:   0.0640 S23:   0.0282                       
REMARK   3      S31:  -0.0630 S32:  -0.0191 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 363:498)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6151   0.2210  36.6654              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4564 T22:   0.4634                                     
REMARK   3      T33:   0.3729 T12:  -0.0534                                     
REMARK   3      T13:  -0.0307 T23:  -0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2438 L22:   2.9220                                     
REMARK   3      L33:   2.1954 L12:  -0.7699                                     
REMARK   3      L13:  -0.0816 L23:  -0.6420                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2367 S12:   0.5257 S13:  -0.2270                       
REMARK   3      S21:  -0.7650 S22:  -0.0483 S23:   0.2095                       
REMARK   3      S31:   0.4872 S32:  -0.2497 S33:   0.0006                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 71:222)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8855 -20.2957 -19.6548              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4806 T22:   0.4391                                     
REMARK   3      T33:   0.3429 T12:   0.0514                                     
REMARK   3      T13:   0.0003 T23:  -0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4582 L22:   3.8553                                     
REMARK   3      L33:   3.9949 L12:  -0.3580                                     
REMARK   3      L13:  -0.1811 L23:  -0.4060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1707 S12:   0.2184 S13:  -0.2129                       
REMARK   3      S21:  -0.1322 S22:  -0.0030 S23:  -0.4563                       
REMARK   3      S31:   0.2622 S32:   0.4060 S33:   0.0017                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 223:481)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.2397 -33.8352  19.7313              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5467 T22:   0.4025                                     
REMARK   3      T33:   0.3830 T12:   0.0736                                     
REMARK   3      T13:   0.0409 T23:  -0.0369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0239 L22:   2.1497                                     
REMARK   3      L33:   4.4367 L12:  -0.9219                                     
REMARK   3      L13:   0.8374 L23:  -2.1353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2064 S12:  -0.0929 S13:   0.0764                       
REMARK   3      S21:   0.1894 S22:   0.2366 S23:  -0.0667                       
REMARK   3      S31:  -0.3974 S32:  -0.1731 S33:  -0.0016                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 482:502)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8747 -30.5366  48.1630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7336 T22:   0.9896                                     
REMARK   3      T33:   1.1026 T12:  -0.0764                                     
REMARK   3      T13:  -0.1562 T23:  -0.3103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7085 L22:   2.4465                                     
REMARK   3      L33:   1.9851 L12:   0.2641                                     
REMARK   3      L13:  -0.2106 L23:  -1.0138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4752 S12:  -0.5301 S13:   0.3854                       
REMARK   3      S21:  -0.0271 S22:  -0.1735 S23:  -1.4478                       
REMARK   3      S31:  -0.8843 S32:   1.5862 S33:  -0.1377                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN C AND (RESID 85:96)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  17.1867 -11.9217  45.2395              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8831 T22:   0.5138                                     
REMARK   3      T33:   0.9397 T12:   0.0010                                     
REMARK   3      T13:   0.0700 T23:  -0.0569                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1382 L22:   0.0768                                     
REMARK   3      L33:   1.0367 L12:   0.0854                                     
REMARK   3      L13:  -0.2858 L23:  -0.2452                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3716 S12:  -0.0426 S13:  -1.4077                       
REMARK   3      S21:  -0.2659 S22:  -0.3698 S23:   0.1514                       
REMARK   3      S31:   1.3266 S32:   0.2081 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 85:96)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.9276 -24.0354  22.2413              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1937 T22:   0.6849                                     
REMARK   3      T33:   0.6920 T12:   0.1004                                     
REMARK   3      T13:  -0.0511 T23:   0.0534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1988 L22:   0.4367                                     
REMARK   3      L33:   0.2383 L12:   0.0124                                     
REMARK   3      L13:   0.1611 L23:  -0.1466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0224 S12:   0.2800 S13:   0.7450                       
REMARK   3      S21:   0.5575 S22:   0.0749 S23:  -0.3470                       
REMARK   3      S31:  -0.9015 S32:  -0.2976 S33:   0.0091                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN E AND (RESID 85:96)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  49.9768  -7.4701  46.0297              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3162 T22:   0.7493                                     
REMARK   3      T33:   1.5097 T12:  -0.0974                                     
REMARK   3      T13:  -0.1018 T23:   0.0946                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5742 L22:   0.2846                                     
REMARK   3      L33:   0.0340 L12:   0.3031                                     
REMARK   3      L13:   0.2020 L23:  -0.0115                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0032 S12:   0.1295 S13:   0.4696                       
REMARK   3      S21:  -0.5145 S22:  -0.1584 S23:  -0.0898                       
REMARK   3      S31:  -0.3631 S32:   0.1147 S33:   0.0079                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN F AND (RESID 85:96)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9659 -28.2288  -1.0976              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8033 T22:   1.1848                                     
REMARK   3      T33:   1.0256 T12:  -0.0188                                     
REMARK   3      T13:   0.0180 T23:  -0.0774                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0890 L22:   0.2337                                     
REMARK   3      L33:   0.9740 L12:   0.0689                                     
REMARK   3      L13:   0.2646 L23:   0.4073                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2277 S12:  -0.9824 S13:  -0.1572                       
REMARK   3      S21:   1.3303 S22:  -0.3231 S23:  -0.0930                       
REMARK   3      S31:  -0.1207 S32:  -0.2257 S33:   0.0116                       
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 5B56 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300000549.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN A200                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57284                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.298                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.523                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY                : 8.700                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.7000                            
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) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 51.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.8.1_1168                                     
REMARK 200 STARTING MODEL: 3KND                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES, 100MM AMMONIUM SULFATE, 10MM   
REMARK 280  MGCL2, 20-23%(W/V) PEG8000, 5MM DTT, PH 6.2, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.77750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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     GLU A   499                                                      
REMARK 465     GLU A   500                                                      
REMARK 465     GLU A   501                                                      
REMARK 465     GLU A   502                                                      
REMARK 465     ASP A   503                                                      
REMARK 465     GLN A   504                                                      
REMARK 465     ASN A   505                                                      
REMARK 465     VAL A   506                                                      
REMARK 465     VAL A   507                                                      
REMARK 465     PRO A   508                                                      
REMARK 465     GLU A   509                                                      
REMARK 465     THR A   510                                                      
REMARK 465     THR A   511                                                      
REMARK 465     SER A   512                                                      
REMARK 465     GLU A   513                                                      
REMARK 465     GLY A   514                                                      
REMARK 465     PHE A   515                                                      
REMARK 465     ALA A   516                                                      
REMARK 465     PHE A   517                                                      
REMARK 465     GLN A   518                                                      
REMARK 465     VAL A   519                                                      
REMARK 465     GLN A   520                                                      
REMARK 465     ASP A   521                                                      
REMARK 465     GLY A   522                                                      
REMARK 465     ALA A   523                                                      
REMARK 465     PRO A   524                                                      
REMARK 465     GLY A   525                                                      
REMARK 465     THR A   526                                                      
REMARK 465     PHE A   527                                                      
REMARK 465     ASN A   528                                                      
REMARK 465     PHE A   529                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     ASP B   503                                                      
REMARK 465     GLN B   504                                                      
REMARK 465     ASN B   505                                                      
REMARK 465     VAL B   506                                                      
REMARK 465     VAL B   507                                                      
REMARK 465     PRO B   508                                                      
REMARK 465     GLU B   509                                                      
REMARK 465     THR B   510                                                      
REMARK 465     THR B   511                                                      
REMARK 465     SER B   512                                                      
REMARK 465     GLU B   513                                                      
REMARK 465     GLY B   514                                                      
REMARK 465     PHE B   515                                                      
REMARK 465     ALA B   516                                                      
REMARK 465     PHE B   517                                                      
REMARK 465     GLN B   518                                                      
REMARK 465     VAL B   519                                                      
REMARK 465     GLN B   520                                                      
REMARK 465     ASP B   521                                                      
REMARK 465     GLY B   522                                                      
REMARK 465     ALA B   523                                                      
REMARK 465     PRO B   524                                                      
REMARK 465     GLY B   525                                                      
REMARK 465     THR B   526                                                      
REMARK 465     PHE B   527                                                      
REMARK 465     ASN B   528                                                      
REMARK 465     PHE B   529                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY A   150     NH1  ARG E    87              2.08            
REMARK 500   O    HOH A   640     O    HOH A   703              2.11            
REMARK 500   OE1  GLU A   250     O    HOH A   601              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  71      166.09     62.45                                   
REMARK 500    ASN A  75       67.45     61.88                                   
REMARK 500    ASN A 239      155.73     72.66                                   
REMARK 500    LYS A 432       55.36    -90.09                                   
REMARK 500    GLU A 456       39.24   -140.96                                   
REMARK 500    ARG A 478       50.62    -97.22                                   
REMARK 500    THR B  73     -153.10   -171.14                                   
REMARK 500    VAL B  74     -153.89     88.09                                   
REMARK 500    ASN B  75      174.06    106.25                                   
REMARK 500    LYS B 108     -154.99   -152.78                                   
REMARK 500    CYS B 133       88.64   -162.58                                   
REMARK 500    ASN B 239      159.64     70.87                                   
REMARK 500    ARG B 478     -138.29    -88.17                                   
REMARK 500    HIS B 479      150.37     67.28                                   
REMARK 500    GLU B 480     -175.75    -66.31                                   
REMARK 500    ASN B 481      148.65     69.34                                   
REMARK 500    TYR B 485      -70.48    -55.53                                   
REMARK 500    PHE B 496     -107.02   -129.54                                   
REMARK 500    SER B 497     -147.32     60.42                                   
REMARK 500    VAL B 498     -122.47     67.94                                   
REMARK 500    GLU B 500      -37.35   -166.88                                   
REMARK 500    GLU B 501      142.68    168.50                                   
REMARK 500    GLN C  86      115.14   -162.39                                   
REMARK 500    ALA C  93      -94.87    -91.39                                   
REMARK 500    SER C  94      145.05   -175.58                                   
REMARK 500    ALA D  93      -90.75    -71.16                                   
REMARK 500    SER D  94      157.50    175.50                                   
REMARK 500    LYS D  95      -71.62   -109.81                                   
REMARK 500    ASN E  91      -55.91   -135.70                                   
REMARK 500    ALA E  93      122.14    168.48                                   
REMARK 500    SER E  94     -120.90   -147.95                                   
REMARK 500    LYS E  95      127.35   -178.70                                   
REMARK 500    GLN F  86      129.75     63.42                                   
REMARK 500    ARG F  87     -145.42    -98.68                                   
REMARK 500    ARG F  88       96.08     63.51                                   
REMARK 500    ARG F  90       74.64   -176.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 864        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A 865        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH A 866        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH A 867        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH A 868        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A 869        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH A 870        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH A 871        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH A 872        DISTANCE =  7.31 ANGSTROMS                       
REMARK 525    HOH A 873        DISTANCE =  7.74 ANGSTROMS                       
REMARK 525    HOH A 874        DISTANCE =  8.19 ANGSTROMS                       
REMARK 525    HOH A 875        DISTANCE =  8.68 ANGSTROMS                       
REMARK 525    HOH B 803        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH B 804        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH B 805        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH B 806        DISTANCE =  6.70 ANGSTROMS                       
REMARK 525    HOH B 807        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH B 808        DISTANCE =  7.59 ANGSTROMS                       
REMARK 525    HOH B 809        DISTANCE =  7.70 ANGSTROMS                       
REMARK 525    HOH B 810        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH B 811        DISTANCE =  8.44 ANGSTROMS                       
REMARK 525    HOH B 812        DISTANCE =  8.62 ANGSTROMS                       
REMARK 525    HOH B 813        DISTANCE =  9.59 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WPT   RELATED DB: PDB                                   
REMARK 900 3WPT CONTAINS HOMODIMERIC STRUCTURE OF DIBB-HUMAN-IMPORTIN-ALPHA1.   
DBREF  5B56 A   70   529  UNP    P52293   IMA1_MOUSE      70    529             
DBREF  5B56 B   70   529  UNP    P52293   IMA1_MOUSE      70    529             
DBREF  5B56 C   85    96  UNP    Q73369   VPR_HV1B9       85     96             
DBREF  5B56 D   85    96  UNP    Q73369   VPR_HV1B9       85     96             
DBREF  5B56 E   85    96  UNP    Q73369   VPR_HV1B9       85     96             
DBREF  5B56 F   85    96  UNP    Q73369   VPR_HV1B9       85     96             
SEQRES   1 A  460  ASN GLN GLY THR VAL ASN TRP SER VAL GLU ASP ILE VAL          
SEQRES   2 A  460  LYS GLY ILE ASN SER ASN ASN LEU GLU SER GLN LEU GLN          
SEQRES   3 A  460  ALA THR GLN ALA ALA ARG LYS LEU LEU SER ARG GLU LYS          
SEQRES   4 A  460  GLN PRO PRO ILE ASP ASN ILE ILE ARG ALA GLY LEU ILE          
SEQRES   5 A  460  PRO LYS PHE VAL SER PHE LEU GLY LYS THR ASP CYS SER          
SEQRES   6 A  460  PRO ILE GLN PHE GLU SER ALA TRP ALA LEU THR ASN ILE          
SEQRES   7 A  460  ALA SER GLY THR SER GLU GLN THR LYS ALA VAL VAL ASP          
SEQRES   8 A  460  GLY GLY ALA ILE PRO ALA PHE ILE SER LEU LEU ALA SER          
SEQRES   9 A  460  PRO HIS ALA HIS ILE SER GLU GLN ALA VAL TRP ALA LEU          
SEQRES  10 A  460  GLY ASN ILE ALA GLY ASP GLY SER ALA PHE ARG ASP LEU          
SEQRES  11 A  460  VAL ILE LYS HIS GLY ALA ILE ASP PRO LEU LEU ALA LEU          
SEQRES  12 A  460  LEU ALA VAL PRO ASP LEU SER THR LEU ALA CYS GLY TYR          
SEQRES  13 A  460  LEU ARG ASN LEU THR TRP THR LEU SER ASN LEU CYS ARG          
SEQRES  14 A  460  ASN LYS ASN PRO ALA PRO PRO LEU ASP ALA VAL GLU GLN          
SEQRES  15 A  460  ILE LEU PRO THR LEU VAL ARG LEU LEU HIS HIS ASN ASP          
SEQRES  16 A  460  PRO GLU VAL LEU ALA ASP SER CYS TRP ALA ILE SER TYR          
SEQRES  17 A  460  LEU THR ASP GLY PRO ASN GLU ARG ILE GLU MET VAL VAL          
SEQRES  18 A  460  LYS LYS GLY VAL VAL PRO GLN LEU VAL LYS LEU LEU GLY          
SEQRES  19 A  460  ALA THR GLU LEU PRO ILE VAL THR PRO ALA LEU ARG ALA          
SEQRES  20 A  460  ILE GLY ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN          
SEQRES  21 A  460  LYS VAL ILE ASP ALA GLY ALA LEU ALA VAL PHE PRO SER          
SEQRES  22 A  460  LEU LEU THR ASN PRO LYS THR ASN ILE GLN LYS GLU ALA          
SEQRES  23 A  460  THR TRP THR MET SER ASN ILE THR ALA GLY ARG GLN ASP          
SEQRES  24 A  460  GLN ILE GLN GLN VAL VAL ASN HIS GLY LEU VAL PRO PHE          
SEQRES  25 A  460  LEU VAL GLY VAL LEU SER LYS ALA ASP PHE LYS THR GLN          
SEQRES  26 A  460  LYS GLU ALA ALA TRP ALA ILE THR ASN TYR THR SER GLY          
SEQRES  27 A  460  GLY THR VAL GLU GLN ILE VAL TYR LEU VAL HIS CYS GLY          
SEQRES  28 A  460  ILE ILE GLU PRO LEU MET ASN LEU LEU SER ALA LYS ASP          
SEQRES  29 A  460  THR LYS ILE ILE GLN VAL ILE LEU ASP ALA ILE SER ASN          
SEQRES  30 A  460  ILE PHE GLN ALA ALA GLU LYS LEU GLY GLU THR GLU LYS          
SEQRES  31 A  460  LEU SER ILE MET ILE GLU GLU CYS GLY GLY LEU ASP LYS          
SEQRES  32 A  460  ILE GLU ALA LEU GLN ARG HIS GLU ASN GLU SER VAL TYR          
SEQRES  33 A  460  LYS ALA SER LEU ASN LEU ILE GLU LYS TYR PHE SER VAL          
SEQRES  34 A  460  GLU GLU GLU GLU ASP GLN ASN VAL VAL PRO GLU THR THR          
SEQRES  35 A  460  SER GLU GLY PHE ALA PHE GLN VAL GLN ASP GLY ALA PRO          
SEQRES  36 A  460  GLY THR PHE ASN PHE                                          
SEQRES   1 B  460  ASN GLN GLY THR VAL ASN TRP SER VAL GLU ASP ILE VAL          
SEQRES   2 B  460  LYS GLY ILE ASN SER ASN ASN LEU GLU SER GLN LEU GLN          
SEQRES   3 B  460  ALA THR GLN ALA ALA ARG LYS LEU LEU SER ARG GLU LYS          
SEQRES   4 B  460  GLN PRO PRO ILE ASP ASN ILE ILE ARG ALA GLY LEU ILE          
SEQRES   5 B  460  PRO LYS PHE VAL SER PHE LEU GLY LYS THR ASP CYS SER          
SEQRES   6 B  460  PRO ILE GLN PHE GLU SER ALA TRP ALA LEU THR ASN ILE          
SEQRES   7 B  460  ALA SER GLY THR SER GLU GLN THR LYS ALA VAL VAL ASP          
SEQRES   8 B  460  GLY GLY ALA ILE PRO ALA PHE ILE SER LEU LEU ALA SER          
SEQRES   9 B  460  PRO HIS ALA HIS ILE SER GLU GLN ALA VAL TRP ALA LEU          
SEQRES  10 B  460  GLY ASN ILE ALA GLY ASP GLY SER ALA PHE ARG ASP LEU          
SEQRES  11 B  460  VAL ILE LYS HIS GLY ALA ILE ASP PRO LEU LEU ALA LEU          
SEQRES  12 B  460  LEU ALA VAL PRO ASP LEU SER THR LEU ALA CYS GLY TYR          
SEQRES  13 B  460  LEU ARG ASN LEU THR TRP THR LEU SER ASN LEU CYS ARG          
SEQRES  14 B  460  ASN LYS ASN PRO ALA PRO PRO LEU ASP ALA VAL GLU GLN          
SEQRES  15 B  460  ILE LEU PRO THR LEU VAL ARG LEU LEU HIS HIS ASN ASP          
SEQRES  16 B  460  PRO GLU VAL LEU ALA ASP SER CYS TRP ALA ILE SER TYR          
SEQRES  17 B  460  LEU THR ASP GLY PRO ASN GLU ARG ILE GLU MET VAL VAL          
SEQRES  18 B  460  LYS LYS GLY VAL VAL PRO GLN LEU VAL LYS LEU LEU GLY          
SEQRES  19 B  460  ALA THR GLU LEU PRO ILE VAL THR PRO ALA LEU ARG ALA          
SEQRES  20 B  460  ILE GLY ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN          
SEQRES  21 B  460  LYS VAL ILE ASP ALA GLY ALA LEU ALA VAL PHE PRO SER          
SEQRES  22 B  460  LEU LEU THR ASN PRO LYS THR ASN ILE GLN LYS GLU ALA          
SEQRES  23 B  460  THR TRP THR MET SER ASN ILE THR ALA GLY ARG GLN ASP          
SEQRES  24 B  460  GLN ILE GLN GLN VAL VAL ASN HIS GLY LEU VAL PRO PHE          
SEQRES  25 B  460  LEU VAL GLY VAL LEU SER LYS ALA ASP PHE LYS THR GLN          
SEQRES  26 B  460  LYS GLU ALA ALA TRP ALA ILE THR ASN TYR THR SER GLY          
SEQRES  27 B  460  GLY THR VAL GLU GLN ILE VAL TYR LEU VAL HIS CYS GLY          
SEQRES  28 B  460  ILE ILE GLU PRO LEU MET ASN LEU LEU SER ALA LYS ASP          
SEQRES  29 B  460  THR LYS ILE ILE GLN VAL ILE LEU ASP ALA ILE SER ASN          
SEQRES  30 B  460  ILE PHE GLN ALA ALA GLU LYS LEU GLY GLU THR GLU LYS          
SEQRES  31 B  460  LEU SER ILE MET ILE GLU GLU CYS GLY GLY LEU ASP LYS          
SEQRES  32 B  460  ILE GLU ALA LEU GLN ARG HIS GLU ASN GLU SER VAL TYR          
SEQRES  33 B  460  LYS ALA SER LEU ASN LEU ILE GLU LYS TYR PHE SER VAL          
SEQRES  34 B  460  GLU GLU GLU GLU ASP GLN ASN VAL VAL PRO GLU THR THR          
SEQRES  35 B  460  SER GLU GLY PHE ALA PHE GLN VAL GLN ASP GLY ALA PRO          
SEQRES  36 B  460  GLY THR PHE ASN PHE                                          
SEQRES   1 C   12  GLN GLN ARG ARG THR ARG ASN GLY ALA SER LYS SER              
SEQRES   1 D   12  GLN GLN ARG ARG THR ARG ASN GLY ALA SER LYS SER              
SEQRES   1 E   12  GLN GLN ARG ARG THR ARG ASN GLY ALA SER LYS SER              
SEQRES   1 F   12  GLN GLN ARG ARG THR ARG ASN GLY ALA SER LYS SER              
FORMUL   7  HOH   *512(H2 O)                                                    
HELIX    1 AA1 SER A   77  ASN A   86  1                                  10    
HELIX    2 AA2 ASN A   89  SER A  105  1                                  17    
HELIX    3 AA3 PRO A  111  ALA A  118  1                                   8    
HELIX    4 AA4 LEU A  120  GLY A  129  1                                  10    
HELIX    5 AA5 CYS A  133  GLY A  150  1                                  18    
HELIX    6 AA6 THR A  151  GLY A  161  1                                  11    
HELIX    7 AA7 GLY A  162  LEU A  171  1                                  10    
HELIX    8 AA8 HIS A  175  ASP A  192  1                                  18    
HELIX    9 AA9 GLY A  193  HIS A  203  1                                  11    
HELIX   10 AB1 ALA A  205  ALA A  214  1                                  10    
HELIX   11 AB2 ASP A  217  LEU A  221  5                                   5    
HELIX   12 AB3 ALA A  222  LEU A  236  1                                  15    
HELIX   13 AB4 PRO A  245  HIS A  261  1                                  17    
HELIX   14 AB5 ASP A  264  ASP A  280  1                                  17    
HELIX   15 AB6 PRO A  282  LYS A  291  1                                  10    
HELIX   16 AB7 VAL A  294  GLY A  303  1                                  10    
HELIX   17 AB8 GLU A  306  VAL A  321  1                                  16    
HELIX   18 AB9 THR A  324  ALA A  334  1                                  11    
HELIX   19 AC1 GLY A  335  ALA A  338  5                                   4    
HELIX   20 AC2 VAL A  339  THR A  345  1                                   7    
HELIX   21 AC3 LYS A  348  THR A  363  1                                  16    
HELIX   22 AC4 ARG A  366  HIS A  376  1                                  11    
HELIX   23 AC5 LEU A  378  ALA A  389  1                                  12    
HELIX   24 AC6 ASP A  390  GLY A  408  1                                  19    
HELIX   25 AC7 THR A  409  CYS A  419  1                                  11    
HELIX   26 AC8 ILE A  421  LEU A  428  1                                   8    
HELIX   27 AC9 LEU A  429  ALA A  431  5                                   3    
HELIX   28 AD1 ASP A  433  GLY A  455  1                                  23    
HELIX   29 AD2 GLU A  456  CYS A  467  1                                  12    
HELIX   30 AD3 GLY A  468  LEU A  476  1                                   9    
HELIX   31 AD4 GLN A  477  HIS A  479  5                                   3    
HELIX   32 AD5 ASN A  481  PHE A  496  1                                  16    
HELIX   33 AD6 SER B   77  ASN B   86  1                                  10    
HELIX   34 AD7 ASN B   89  ARG B  106  1                                  18    
HELIX   35 AD8 PRO B  111  ALA B  118  1                                   8    
HELIX   36 AD9 LEU B  120  LEU B  128  1                                   9    
HELIX   37 AE1 CYS B  133  SER B  149  1                                  17    
HELIX   38 AE2 THR B  151  GLY B  161  1                                  11    
HELIX   39 AE3 GLY B  162  LEU B  171  1                                  10    
HELIX   40 AE4 HIS B  175  GLY B  191  1                                  17    
HELIX   41 AE5 GLY B  193  HIS B  203  1                                  11    
HELIX   42 AE6 ALA B  205  ALA B  214  1                                  10    
HELIX   43 AE7 ASP B  217  LEU B  221  5                                   5    
HELIX   44 AE8 ALA B  222  CYS B  237  1                                  16    
HELIX   45 AE9 PRO B  245  LEU B  260  1                                  16    
HELIX   46 AF1 ASP B  264  THR B  279  1                                  16    
HELIX   47 AF2 PRO B  282  LYS B  291  1                                  10    
HELIX   48 AF3 VAL B  294  GLY B  303  1                                  10    
HELIX   49 AF4 GLU B  306  THR B  322  1                                  17    
HELIX   50 AF5 THR B  324  ALA B  334  1                                  11    
HELIX   51 AF6 GLY B  335  ALA B  338  5                                   4    
HELIX   52 AF7 VAL B  339  THR B  345  1                                   7    
HELIX   53 AF8 LYS B  348  THR B  363  1                                  16    
HELIX   54 AF9 ARG B  366  HIS B  376  1                                  11    
HELIX   55 AG1 LEU B  378  LYS B  388  1                                  11    
HELIX   56 AG2 ASP B  390  GLY B  408  1                                  19    
HELIX   57 AG3 THR B  409  CYS B  419  1                                  11    
HELIX   58 AG4 ILE B  421  LEU B  428  1                                   8    
HELIX   59 AG5 LEU B  429  ALA B  431  5                                   3    
HELIX   60 AG6 ASP B  433  LYS B  453  1                                  21    
HELIX   61 AG7 GLU B  456  GLU B  466  1                                  11    
HELIX   62 AG8 GLY B  468  LEU B  476  1                                   9    
HELIX   63 AG9 GLU B  482  PHE B  496  1                                  15    
CISPEP   1 ASN A  241    PRO A  242          0        -1.76                     
CISPEP   2 GLN B   71    GLY B   72          0        -1.90                     
CISPEP   3 GLU B  107    LYS B  108          0         1.37                     
CISPEP   4 ASN B  241    PRO B  242          0        -1.63                     
CISPEP   5 ASN E   91    GLY E   92          0        -5.19                     
CRYST1   91.021   81.555  101.545  90.00  97.78  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010986  0.000000  0.001501        0.00000                         
SCALE2      0.000000  0.012262  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009939        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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