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Database: PDB
Entry: 3GJ8
LinkDB: 3GJ8
Original site: 3GJ8 
HEADER    TRANSPORT PROTEIN                       07-MAR-09   3GJ8              
TITLE     CRYSTAL STRUCTURE OF HUMAN RANGDP-NUP153ZNF34 COMPLEX                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTP-BINDING NUCLEAR PROTEIN RAN;                           
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: GTPASE RAN, RAS-RELATED NUCLEAR PROTEIN, RAS-LIKE           
COMPND   5 PROTEIN TC4, ANDROGEN RECEPTOR-ASSOCIATED PROTEIN 24;                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: NUCLEAR PORE COMPLEX PROTEIN NUP153;                       
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: NUP153 - ZINC FINGER MODULE 34: UNP RESIDUES 790-          
COMPND  12 876;                                                                 
COMPND  13 SYNONYM: NUCLEOPORIN NUP153, 153 KDA NUCLEOPORIN;                    
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RAN, ARA24, OK/SW-CL.81;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: BL21(DE3)-RIL;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  13 ORGANISM_COMMON: RAT;                                                
SOURCE  14 ORGANISM_TAXID: 10116;                                               
SOURCE  15 GENE: NUP153;                                                        
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_VARIANT: BL21(DE3)-RIL;                            
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1                                  
KEYWDS    G PROTEIN, GDP, RAN, NUP153, NUCLEAR PORE, ZINC FINGER,               
KEYWDS   2 ACETYLATION, CYTOPLASM, GTP-BINDING, HOST-VIRUS                      
KEYWDS   3 INTERACTION, ISOPEPTIDE BOND, NUCLEOTIDE-BINDING, NUCLEUS,           
KEYWDS   4 PHOSPHOPROTEIN, POLYMORPHISM, PROTEIN TRANSPORT, TRANSPORT,          
KEYWDS   5 UBL CONJUGATION, DNA-BINDING, METAL-BINDING, MRNA                    
KEYWDS   6 TRANSPORT, NUCLEAR PORE COMPLEX, TRANSLOCATION, ZINC, ZINC-          
KEYWDS   7 FINGER, TRANSPORT PROTEIN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.PARTRIDGE,T.U.SCHWARTZ                                            
REVDAT   1   04-AUG-09 3GJ8    0                                                
JRNL        AUTH   J.R.PARTRIDGE,T.U.SCHWARTZ                                   
JRNL        TITL   CRYSTALLOGRAPHIC AND BIOCHEMICAL ANALYSIS OF THE             
JRNL        TITL 2 RAN-BINDING ZINC FINGER DOMAIN.                              
JRNL        REF    J.MOL.BIOL.                   V. 391   375 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19505478                                                     
JRNL        DOI    10.1016/J.JMB.2009.06.011                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 52792                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2688                            
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 33.7601 -  4.8494    0.96     2657   138  0.1651 0.1795        
REMARK   3     2  4.8494 -  3.8509    0.98     2620   143  0.1382 0.1599        
REMARK   3     3  3.8509 -  3.3646    0.99     2665   129  0.1569 0.1553        
REMARK   3     4  3.3646 -  3.0572    0.99     2673   141  0.1681 0.2369        
REMARK   3     5  3.0572 -  2.8382    0.99     2607   156  0.1758 0.2135        
REMARK   3     6  2.8382 -  2.6709    1.00     2688   121  0.1768 0.2305        
REMARK   3     7  2.6709 -  2.5372    1.00     2605   168  0.1751 0.2186        
REMARK   3     8  2.5372 -  2.4268    1.00     2670   149  0.1681 0.1901        
REMARK   3     9  2.4268 -  2.3334    1.00     2648   136  0.1766 0.2291        
REMARK   3    10  2.3334 -  2.2529    1.00     2626   143  0.1670 0.1913        
REMARK   3    11  2.2529 -  2.1825    1.00     2614   153  0.1659 0.2360        
REMARK   3    12  2.1825 -  2.1201    1.00     2651   136  0.1676 0.1860        
REMARK   3    13  2.1201 -  2.0643    1.00     2646   137  0.1710 0.2134        
REMARK   3    14  2.0643 -  2.0139    1.00     2662   130  0.1753 0.2061        
REMARK   3    15  2.0139 -  1.9682    1.00     2646   129  0.1779 0.2499        
REMARK   3    16  1.9682 -  1.9263    1.00     2641   149  0.1943 0.2365        
REMARK   3    17  1.9263 -  1.8878    1.00     2639   141  0.2023 0.2090        
REMARK   3    18  1.8878 -  1.8521    1.00     2617   150  0.2279 0.2554        
REMARK   3    19  1.8521 -  1.8200    0.96     2529   139  0.2477 0.2695        
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              : 0.34                                          
REMARK   3   B_SOL              : 58.19                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.490            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.430           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.31                          
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      :  0.005           3796                                  
REMARK   3   ANGLE     :  0.943           5157                                  
REMARK   3   CHIRALITY :  0.062            572                                  
REMARK   3   PLANARITY :  0.003            649                                  
REMARK   3   DIHEDRAL  : 14.714           1385                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  52.4465  -4.3495  -3.9274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0934 T22:   0.0202                                     
REMARK   3      T33:   0.0373 T12:   0.0084                                     
REMARK   3      T13:  -0.0553 T23:  -0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1836 L22:   0.3288                                     
REMARK   3      L33:   0.5969 L12:  -0.3351                                     
REMARK   3      L13:   0.2717 L23:   0.1893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1049 S12:  -0.1273 S13:   0.0880                       
REMARK   3      S21:   0.0268 S22:   0.0375 S23:  -0.0363                       
REMARK   3      S31:  -0.0393 S32:  -0.0350 S33:   0.0576                       
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 3GJ8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051928.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-AUG-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52824                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.56000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.970                              
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: PDB ENTRU 3GJ3                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5, 18-20% PEG         
REMARK 280  3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K               
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       30.85650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     GLY A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     MET A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     PRO A   210                                                      
REMARK 465     ASP A   211                                                      
REMARK 465     GLU A   212                                                      
REMARK 465     ASP A   213                                                      
REMARK 465     ASP A   214                                                      
REMARK 465     ASP A   215                                                      
REMARK 465     LEU A   216                                                      
REMARK 465     GLY B   785                                                      
REMARK 465     PRO B   786                                                      
REMARK 465     LEU B   787                                                      
REMARK 465     GLY B   788                                                      
REMARK 465     SER B   789                                                      
REMARK 465     VAL B   790                                                      
REMARK 465     GLY B   791                                                      
REMARK 465     SER B   792                                                      
REMARK 465     TRP B   793                                                      
REMARK 465     GLU B   794                                                      
REMARK 465     CYS B   795                                                      
REMARK 465     PRO B   796                                                      
REMARK 465     VAL B   797                                                      
REMARK 465     CYS B   798                                                      
REMARK 465     CYS B   799                                                      
REMARK 465     VAL B   800                                                      
REMARK 465     SER B   801                                                      
REMARK 465     ASN B   802                                                      
REMARK 465     LYS B   803                                                      
REMARK 465     ALA B   804                                                      
REMARK 465     GLU B   805                                                      
REMARK 465     ASP B   806                                                      
REMARK 465     SER B   807                                                      
REMARK 465     ARG B   808                                                      
REMARK 465     CYS B   809                                                      
REMARK 465     VAL B   810                                                      
REMARK 465     SER B   811                                                      
REMARK 465     CYS B   812                                                      
REMARK 465     THR B   813                                                      
REMARK 465     SER B   814                                                      
REMARK 465     GLU B   815                                                      
REMARK 465     LYS B   816                                                      
REMARK 465     PRO B   817                                                      
REMARK 465     GLY B   818                                                      
REMARK 465     LEU B   819                                                      
REMARK 465     VAL B   820                                                      
REMARK 465     SER B   821                                                      
REMARK 465     ALA B   822                                                      
REMARK 465     SER B   823                                                      
REMARK 465     SER B   824                                                      
REMARK 465     SER B   825                                                      
REMARK 465     ASN B   826                                                      
REMARK 465     SER B   827                                                      
REMARK 465     VAL B   828                                                      
REMARK 465     PRO B   829                                                      
REMARK 465     VAL B   830                                                      
REMARK 465     SER B   831                                                      
REMARK 465     LEU B   832                                                      
REMARK 465     PRO B   833                                                      
REMARK 465     SER B   834                                                      
REMARK 465     GLY B   835                                                      
REMARK 465     GLY B   836                                                      
REMARK 465     CYS B   837                                                      
REMARK 465     LEU B   838                                                      
REMARK 465     GLY B   839                                                      
REMARK 465     LEU B   840                                                      
REMARK 465     ASP B   841                                                      
REMARK 465     LYS B   842                                                      
REMARK 465     PHE B   843                                                      
REMARK 465     LYS B   844                                                      
REMARK 465     LYS B   845                                                      
REMARK 465     PRO B   846                                                      
REMARK 465     GLU B   847                                                      
REMARK 465     GLY B   875                                                      
REMARK 465     THR B   876                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     PRO C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     PRO C   210                                                      
REMARK 465     ASP C   211                                                      
REMARK 465     GLU C   212                                                      
REMARK 465     ASP C   213                                                      
REMARK 465     ASP C   214                                                      
REMARK 465     ASP C   215                                                      
REMARK 465     LEU C   216                                                      
REMARK 465     GLY D   785                                                      
REMARK 465     PRO D   786                                                      
REMARK 465     LEU D   787                                                      
REMARK 465     GLY D   788                                                      
REMARK 465     SER D   789                                                      
REMARK 465     VAL D   790                                                      
REMARK 465     GLY D   791                                                      
REMARK 465     SER D   792                                                      
REMARK 465     TRP D   793                                                      
REMARK 465     GLU D   794                                                      
REMARK 465     CYS D   795                                                      
REMARK 465     PRO D   796                                                      
REMARK 465     VAL D   797                                                      
REMARK 465     CYS D   798                                                      
REMARK 465     CYS D   799                                                      
REMARK 465     VAL D   800                                                      
REMARK 465     SER D   801                                                      
REMARK 465     ASN D   802                                                      
REMARK 465     LYS D   803                                                      
REMARK 465     ALA D   804                                                      
REMARK 465     GLU D   805                                                      
REMARK 465     ASP D   806                                                      
REMARK 465     SER D   807                                                      
REMARK 465     ARG D   808                                                      
REMARK 465     CYS D   809                                                      
REMARK 465     VAL D   810                                                      
REMARK 465     SER D   811                                                      
REMARK 465     CYS D   812                                                      
REMARK 465     THR D   813                                                      
REMARK 465     SER D   814                                                      
REMARK 465     GLU D   815                                                      
REMARK 465     LYS D   816                                                      
REMARK 465     PRO D   817                                                      
REMARK 465     GLY D   818                                                      
REMARK 465     LEU D   819                                                      
REMARK 465     VAL D   820                                                      
REMARK 465     SER D   821                                                      
REMARK 465     ALA D   822                                                      
REMARK 465     SER D   823                                                      
REMARK 465     SER D   824                                                      
REMARK 465     SER D   825                                                      
REMARK 465     ASN D   826                                                      
REMARK 465     SER D   827                                                      
REMARK 465     VAL D   828                                                      
REMARK 465     PRO D   829                                                      
REMARK 465     VAL D   830                                                      
REMARK 465     SER D   831                                                      
REMARK 465     LEU D   832                                                      
REMARK 465     PRO D   833                                                      
REMARK 465     SER D   834                                                      
REMARK 465     GLY D   835                                                      
REMARK 465     GLY D   836                                                      
REMARK 465     CYS D   837                                                      
REMARK 465     LEU D   838                                                      
REMARK 465     GLY D   839                                                      
REMARK 465     LEU D   840                                                      
REMARK 465     ASP D   841                                                      
REMARK 465     LYS D   842                                                      
REMARK 465     PHE D   843                                                      
REMARK 465     LYS D   844                                                      
REMARK 465     LYS D   845                                                      
REMARK 465     PRO D   846                                                      
REMARK 465     GLU D   847                                                      
REMARK 465     GLY D   848                                                      
REMARK 465     GLY D   875                                                      
REMARK 465     THR D   876                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 113     -138.73     66.74                                   
REMARK 500    ASN A 114       59.93    -92.17                                   
REMARK 500    LYS A 123       33.68     75.62                                   
REMARK 500    ASN A 143        4.71     83.95                                   
REMARK 500    ALA B 868      -61.89    -90.09                                   
REMARK 500    GLU C 113     -141.95     68.48                                   
REMARK 500    LYS C 123       30.88     76.22                                   
REMARK 500    ASN C 143       12.26     82.14                                   
REMARK 500    ALA D 868      -64.02    -91.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  24   OG1                                                    
REMARK 620 2 GDP A 302   O1B  91.6                                              
REMARK 620 3 HOH A 479   O    91.5  86.4                                        
REMARK 620 4 HOH A 480   O    84.9 174.4  89.4                                  
REMARK 620 5 HOH A 481   O    87.3  97.0 176.5  87.2                            
REMARK 620 6 HOH A 482   O   174.3  93.9  90.6  89.8  90.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 852   SG                                                     
REMARK 620 2 CYS B 855   SG  115.4                                              
REMARK 620 3 CYS B 866   SG  108.8 104.2                                        
REMARK 620 4 CYS B 869   SG   99.9 116.4 112.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C  24   OG1                                                    
REMARK 620 2 GDP C 302   O1B  91.4                                              
REMARK 620 3 HOH C 475   O    86.5  95.6                                        
REMARK 620 4 HOH C 476   O   176.8  90.6  90.8                                  
REMARK 620 5 HOH C 477   O    85.2 174.3  88.8  93.0                            
REMARK 620 6 HOH C 478   O    93.2  83.7 179.2  89.6  91.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 852   SG                                                     
REMARK 620 2 CYS D 855   SG  114.4                                              
REMARK 620 3 CYS D 866   SG  107.7 103.7                                        
REMARK 620 4 CYS D 869   SG  100.0 118.5 112.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 302                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 303                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 300                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 303                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 301                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 302                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 300                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CH5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE RANGDP-NUP153ZNF2 COMPLEX                   
REMARK 900 RELATED ID: 2GQE   RELATED DB: PDB                                   
REMARK 900 MOLECULAR CHARACTERIZATION OF THE RAN BINDING ZINC FINGER            
REMARK 900 DOMAIN                                                               
REMARK 900 RELATED ID: 1BYU   RELATED DB: PDB                                   
REMARK 900 CANINE GDP-RAN                                                       
REMARK 900 RELATED ID: 3GJ0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN                               
REMARK 900 RELATED ID: 3GJ3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN IN COMPLEX WITH               
REMARK 900 NUP153 - ZINC FINGER MODULE 2                                        
REMARK 900 RELATED ID: 3GJ4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN IN COMPLEX WITH               
REMARK 900 NUP153 - ZINC FINGER MODULE 3                                        
REMARK 900 RELATED ID: 3GJ5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN                
REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 4                           
REMARK 900 RELATED ID: 3GJ6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN                
REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 1                           
REMARK 900 RELATED ID: 3GJ7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN                
REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 12                          
DBREF  3GJ8 A    2   216  UNP    P62826   RAN_HUMAN        2    216             
DBREF  3GJ8 B  790   876  UNP    P49791   NU153_RAT      790    876             
DBREF  3GJ8 C    2   216  UNP    P62826   RAN_HUMAN        2    216             
DBREF  3GJ8 D  790   876  UNP    P49791   NU153_RAT      790    876             
SEQADV 3GJ8 GLY A   -4  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 PRO A   -3  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 HIS A   -2  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 MET A   -1  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 ALA A    0  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 SER A    1  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 SER A   35  UNP  P62826    PHE    35 ENGINEERED                     
SEQADV 3GJ8 GLY B  785  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ8 PRO B  786  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ8 LEU B  787  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ8 GLY B  788  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ8 SER B  789  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ8 GLY C   -4  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 PRO C   -3  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 HIS C   -2  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 MET C   -1  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 ALA C    0  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 SER C    1  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ8 SER C   35  UNP  P62826    PHE    35 ENGINEERED                     
SEQADV 3GJ8 GLY D  785  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ8 PRO D  786  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ8 LEU D  787  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ8 GLY D  788  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ8 SER D  789  UNP  P49791              EXPRESSION TAG                 
SEQRES   1 A  221  GLY PRO HIS MET ALA SER ALA ALA GLN GLY GLU PRO GLN          
SEQRES   2 A  221  VAL GLN PHE LYS LEU VAL LEU VAL GLY ASP GLY GLY THR          
SEQRES   3 A  221  GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR GLY GLU          
SEQRES   4 A  221  SER GLU LYS LYS TYR VAL ALA THR LEU GLY VAL GLU VAL          
SEQRES   5 A  221  HIS PRO LEU VAL PHE HIS THR ASN ARG GLY PRO ILE LYS          
SEQRES   6 A  221  PHE ASN VAL TRP ASP THR ALA GLY GLN GLU LYS PHE GLY          
SEQRES   7 A  221  GLY LEU ARG ASP GLY TYR TYR ILE GLN ALA GLN CYS ALA          
SEQRES   8 A  221  ILE ILE MET PHE ASP VAL THR SER ARG VAL THR TYR LYS          
SEQRES   9 A  221  ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG VAL CYS          
SEQRES  10 A  221  GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS VAL ASP          
SEQRES  11 A  221  ILE LYS ASP ARG LYS VAL LYS ALA LYS SER ILE VAL PHE          
SEQRES  12 A  221  HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE SER ALA          
SEQRES  13 A  221  LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU TRP LEU          
SEQRES  14 A  221  ALA ARG LYS LEU ILE GLY ASP PRO ASN LEU GLU PHE VAL          
SEQRES  15 A  221  ALA MET PRO ALA LEU ALA PRO PRO GLU VAL VAL MET ASP          
SEQRES  16 A  221  PRO ALA LEU ALA ALA GLN TYR GLU HIS ASP LEU GLU VAL          
SEQRES  17 A  221  ALA GLN THR THR ALA LEU PRO ASP GLU ASP ASP ASP LEU          
SEQRES   1 B   92  GLY PRO LEU GLY SER VAL GLY SER TRP GLU CYS PRO VAL          
SEQRES   2 B   92  CYS CYS VAL SER ASN LYS ALA GLU ASP SER ARG CYS VAL          
SEQRES   3 B   92  SER CYS THR SER GLU LYS PRO GLY LEU VAL SER ALA SER          
SEQRES   4 B   92  SER SER ASN SER VAL PRO VAL SER LEU PRO SER GLY GLY          
SEQRES   5 B   92  CYS LEU GLY LEU ASP LYS PHE LYS LYS PRO GLU GLY SER          
SEQRES   6 B   92  TRP ASP CYS GLU VAL CYS LEU VAL GLN ASN LYS ALA ASP          
SEQRES   7 B   92  SER THR LYS CYS ILE ALA CYS GLU SER ALA LYS PRO GLY          
SEQRES   8 B   92  THR                                                          
SEQRES   1 C  221  GLY PRO HIS MET ALA SER ALA ALA GLN GLY GLU PRO GLN          
SEQRES   2 C  221  VAL GLN PHE LYS LEU VAL LEU VAL GLY ASP GLY GLY THR          
SEQRES   3 C  221  GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR GLY GLU          
SEQRES   4 C  221  SER GLU LYS LYS TYR VAL ALA THR LEU GLY VAL GLU VAL          
SEQRES   5 C  221  HIS PRO LEU VAL PHE HIS THR ASN ARG GLY PRO ILE LYS          
SEQRES   6 C  221  PHE ASN VAL TRP ASP THR ALA GLY GLN GLU LYS PHE GLY          
SEQRES   7 C  221  GLY LEU ARG ASP GLY TYR TYR ILE GLN ALA GLN CYS ALA          
SEQRES   8 C  221  ILE ILE MET PHE ASP VAL THR SER ARG VAL THR TYR LYS          
SEQRES   9 C  221  ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG VAL CYS          
SEQRES  10 C  221  GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS VAL ASP          
SEQRES  11 C  221  ILE LYS ASP ARG LYS VAL LYS ALA LYS SER ILE VAL PHE          
SEQRES  12 C  221  HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE SER ALA          
SEQRES  13 C  221  LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU TRP LEU          
SEQRES  14 C  221  ALA ARG LYS LEU ILE GLY ASP PRO ASN LEU GLU PHE VAL          
SEQRES  15 C  221  ALA MET PRO ALA LEU ALA PRO PRO GLU VAL VAL MET ASP          
SEQRES  16 C  221  PRO ALA LEU ALA ALA GLN TYR GLU HIS ASP LEU GLU VAL          
SEQRES  17 C  221  ALA GLN THR THR ALA LEU PRO ASP GLU ASP ASP ASP LEU          
SEQRES   1 D   92  GLY PRO LEU GLY SER VAL GLY SER TRP GLU CYS PRO VAL          
SEQRES   2 D   92  CYS CYS VAL SER ASN LYS ALA GLU ASP SER ARG CYS VAL          
SEQRES   3 D   92  SER CYS THR SER GLU LYS PRO GLY LEU VAL SER ALA SER          
SEQRES   4 D   92  SER SER ASN SER VAL PRO VAL SER LEU PRO SER GLY GLY          
SEQRES   5 D   92  CYS LEU GLY LEU ASP LYS PHE LYS LYS PRO GLU GLY SER          
SEQRES   6 D   92  TRP ASP CYS GLU VAL CYS LEU VAL GLN ASN LYS ALA ASP          
SEQRES   7 D   92  SER THR LYS CYS ILE ALA CYS GLU SER ALA LYS PRO GLY          
SEQRES   8 D   92  THR                                                          
HET     MG  A 301       1                                                       
HET    GDP  A 302      28                                                       
HET     MG  A 303       1                                                       
HET     ZN  B 300       1                                                       
HET     MG  C 303       1                                                       
HET     MG  C 301       1                                                       
HET    GDP  C 302      28                                                       
HET     ZN  D 300       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM      ZN ZINC ION                                                         
FORMUL   5   MG    4(MG 2+)                                                     
FORMUL   6  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   8   ZN    2(ZN 2+)                                                     
FORMUL  13  HOH   *548(H2 O)                                                    
HELIX    1   1 GLY A   22  LYS A   28  1                                   7    
HELIX    2   2 HIS A   30  GLU A   36  1                                   7    
HELIX    3   3 GLY A   68  PHE A   72  5                                   5    
HELIX    4   4 ARG A   76  ILE A   81  1                                   6    
HELIX    5   5 SER A   94  ASN A  100  1                                   7    
HELIX    6   6 ASN A  100  GLU A  113  1                                  14    
HELIX    7   7 LYS A  132  ILE A  136  5                                   5    
HELIX    8   8 GLU A  158  GLY A  170  1                                  13    
HELIX    9   9 ASP A  190  THR A  207  1                                  18    
HELIX   10  10 GLY C   22  LYS C   28  1                                   7    
HELIX   11  11 HIS C   30  GLU C   36  1                                   7    
HELIX   12  12 GLY C   68  GLY C   73  5                                   6    
HELIX   13  13 ARG C   76  ILE C   81  1                                   6    
HELIX   14  14 SER C   94  ASN C  100  1                                   7    
HELIX   15  15 ASN C  100  GLU C  113  1                                  14    
HELIX   16  16 LYS C  132  ILE C  136  5                                   5    
HELIX   17  17 VAL C  137  ASN C  143  1                                   7    
HELIX   18  18 GLU C  158  GLY C  170  1                                  13    
HELIX   19  19 ASP C  190  THR C  207  1                                  18    
SHEET    1   A 7 LYS A  38  VAL A  40  0                                        
SHEET    2   A 7 VAL A  45  THR A  54 -1  O  VAL A  45   N  VAL A  40           
SHEET    3   A 7 GLY A  57  THR A  66 -1  O  PHE A  61   N  LEU A  50           
SHEET    4   A 7 GLN A  10  VAL A  16  1  N  PHE A  11   O  ASN A  62           
SHEET    5   A 7 CYS A  85  ASP A  91  1  O  MET A  89   N  VAL A  16           
SHEET    6   A 7 ILE A 117  ASN A 122  1  O  ASN A 122   N  PHE A  90           
SHEET    7   A 7 GLN A 145  ASP A 148  1  O  GLN A 145   N  LEU A 119           
SHEET    1   B 2 TRP B 850  ASP B 851  0                                        
SHEET    2   B 2 GLN B 858  ASN B 859 -1  O  ASN B 859   N  TRP B 850           
SHEET    1   C 7 LYS C  38  VAL C  40  0                                        
SHEET    2   C 7 VAL C  45  THR C  54 -1  O  VAL C  45   N  VAL C  40           
SHEET    3   C 7 GLY C  57  THR C  66 -1  O  PHE C  61   N  LEU C  50           
SHEET    4   C 7 GLN C  10  VAL C  16  1  N  PHE C  11   O  ASN C  62           
SHEET    5   C 7 CYS C  85  ASP C  91  1  O  MET C  89   N  VAL C  16           
SHEET    6   C 7 ILE C 117  ASN C 122  1  O  ASN C 122   N  PHE C  90           
SHEET    7   C 7 GLN C 145  ASP C 148  1  O  GLN C 145   N  LEU C 119           
SHEET    1   D 2 TRP D 850  ASP D 851  0                                        
SHEET    2   D 2 GLN D 858  ASN D 859 -1  O  ASN D 859   N  TRP D 850           
LINK         OG1 THR A  24                MG    MG A 301     1555   1555  2.16  
LINK         SG  CYS B 852                ZN    ZN B 300     1555   1555  2.46  
LINK         SG  CYS B 855                ZN    ZN B 300     1555   1555  2.29  
LINK         SG  CYS B 866                ZN    ZN B 300     1555   1555  2.36  
LINK         SG  CYS B 869                ZN    ZN B 300     1555   1555  2.40  
LINK         OG1 THR C  24                MG    MG C 301     1555   1555  2.17  
LINK         SG  CYS D 852                ZN    ZN D 300     1555   1555  2.43  
LINK         SG  CYS D 855                ZN    ZN D 300     1555   1555  2.25  
LINK         SG  CYS D 866                ZN    ZN D 300     1555   1555  2.38  
LINK         SG  CYS D 869                ZN    ZN D 300     1555   1555  2.41  
LINK        MG    MG A 301                 O1B GDP A 302     1555   1555  2.13  
LINK        MG    MG C 301                 O1B GDP C 302     1555   1555  2.17  
LINK        MG    MG A 301                 O   HOH A 479     1555   1555  2.21  
LINK        MG    MG A 301                 O   HOH A 480     1555   1555  2.29  
LINK        MG    MG A 301                 O   HOH A 481     1555   1555  2.29  
LINK        MG    MG A 301                 O   HOH A 482     1555   1555  2.24  
LINK        MG    MG C 301                 O   HOH C 475     1555   1555  2.25  
LINK        MG    MG C 301                 O   HOH C 476     1555   1555  2.25  
LINK        MG    MG C 301                 O   HOH C 477     1555   1555  2.30  
LINK        MG    MG C 301                 O   HOH C 478     1555   1555  2.27  
SITE     1 AC1  6 THR A  24  GDP A 302  HOH A 479  HOH A 480                    
SITE     2 AC1  6 HOH A 481  HOH A 482                                          
SITE     1 AC2 23 GLY A  20  THR A  21  GLY A  22  LYS A  23                    
SITE     2 AC2 23 THR A  24  THR A  25  ASN A 122  LYS A 123                    
SITE     3 AC2 23 ASP A 125  ILE A 126  SER A 150  ALA A 151                    
SITE     4 AC2 23 LYS A 152  HOH A 240  HOH A 254  HOH A 279                    
SITE     5 AC2 23  MG A 301  HOH A 336  HOH A 350  HOH A 404                    
SITE     6 AC2 23 HOH A 417  HOH A 479  HOH A 482                               
SITE     1 AC3  4 PRO A 180  ALA A 181  HOH A 322   MG C 303                    
SITE     1 AC4  4 CYS B 852  CYS B 855  CYS B 866  CYS B 869                    
SITE     1 AC5  5  MG A 303  PRO C 180  ALA C 181  HOH C 243                    
SITE     2 AC5  5 HOH C 341                                                     
SITE     1 AC6  6 THR C  24  GDP C 302  HOH C 475  HOH C 476                    
SITE     2 AC6  6 HOH C 477  HOH C 478                                          
SITE     1 AC7 24 GLY C  20  THR C  21  GLY C  22  LYS C  23                    
SITE     2 AC7 24 THR C  24  THR C  25  ASN C 122  LYS C 123                    
SITE     3 AC7 24 ASP C 125  ILE C 126  SER C 150  ALA C 151                    
SITE     4 AC7 24 LYS C 152  HOH C 219  HOH C 249  HOH C 274                    
SITE     5 AC7 24  MG C 301  HOH C 310  HOH C 373  HOH C 476                    
SITE     6 AC7 24 HOH C 478  HOH C 499  HOH C 540  HOH C 541                    
SITE     1 AC8  4 CYS D 852  CYS D 855  CYS D 866  CYS D 869                    
CRYST1   74.257   61.713   70.635  90.00 112.31  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013467  0.000000  0.005526        0.00000                         
SCALE2      0.000000  0.016204  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015303        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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