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Database: PDB
Entry: 3GJ6
LinkDB: 3GJ6
Original site: 3GJ6 
HEADER    TRANSPORT PROTEIN                       07-MAR-09   3GJ6              
TITLE     CRYSTAL STRUCTURE OF HUMAN RANGDP-NUP153ZNF1 COMPLEX                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTP-BINDING NUCLEAR PROTEIN RAN;                           
COMPND   3 CHAIN: A;                                                            
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;                                                            
COMPND  11 FRAGMENT: NUP153 - ZINC FINGER MODULE 1: UNP RESIDUES 658-           
COMPND  12 686;                                                                 
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, NUCLEAR PORE, NUP153, 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 3GJ6    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.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 7461                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 12.570                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 938                             
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 36.1194 -  5.1625    0.99     1029   138  0.1976 0.2713        
REMARK   3     2  5.1625 -  4.0994    1.00      956   149  0.1607 0.2110        
REMARK   3     3  4.0994 -  3.5818    0.98      922   138  0.1940 0.2592        
REMARK   3     4  3.5818 -  3.2545    0.99      940   134  0.1979 0.3270        
REMARK   3     5  3.2545 -  3.0214    1.00      916   147  0.2101 0.2695        
REMARK   3     6  3.0214 -  2.8433    0.97      933   115  0.2370 0.3566        
REMARK   3     7  2.8433 -  2.7000    0.90      827   117  0.2823 0.3766        
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              : 0.25                                          
REMARK   3   B_SOL              : 48.93                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.810            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.100           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.33                          
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      :  0.008           1892                                  
REMARK   3   ANGLE     :  1.138           2570                                  
REMARK   3   CHIRALITY :  0.074            286                                  
REMARK   3   PLANARITY :  0.004            323                                  
REMARK   3   DIHEDRAL  : 16.536            690                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.4270  26.9383  13.7668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1650 T22:   0.1924                                     
REMARK   3      T33:   0.2547 T12:  -0.0331                                     
REMARK   3      T13:  -0.0471 T23:  -0.0811                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9077 L22:   2.1367                                     
REMARK   3      L33:   1.3794 L12:   0.1912                                     
REMARK   3      L13:   0.0684 L23:  -0.3487                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0926 S12:   0.1424 S13:  -0.4817                       
REMARK   3      S21:  -0.1938 S22:   0.1788 S23:   0.0750                       
REMARK   3      S31:   0.0684 S32:  -0.0137 S33:  -0.0688                       
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 3GJ6 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 RCSB051926.                                      
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   : 7528                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
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     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.70000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.620                              
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 ENTRY 3GJ3                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M 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 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       30.06600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.15250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.06600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.15250            
REMARK 290   SMTRY3   4  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: 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 234  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     LEU A   209                                                      
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   653                                                      
REMARK 465     PRO B   654                                                      
REMARK 465     LEU B   655                                                      
REMARK 465     GLY B   656                                                      
REMARK 465     SER B   657                                                      
REMARK 465     ALA B   658                                                      
REMARK 465     GLY B   659                                                      
REMARK 465     SER B   660                                                      
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    LEU A  43       -5.82   -140.27                                   
REMARK 500    ALA A  67       34.76    -92.90                                   
REMARK 500    GLN A  82       12.04     48.81                                   
REMARK 500    CYS A  85      168.12    178.02                                   
REMARK 500    LEU A 108      -65.19    -90.30                                   
REMARK 500    ASN A 114       75.20     44.81                                   
REMARK 500    VAL A 137      -20.20   -142.92                                   
REMARK 500    LYS A 142     -131.73     69.59                                   
REMARK 500    ASN A 143       54.73   -141.74                                   
REMARK 500    VAL A 203       12.85    -64.25                                   
REMARK 500    THR A 207      -66.16   -123.13                                   
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 HOH A 217   O   109.4                                              
REMARK 620 3 HOH A 220   O    99.3 126.5                                        
REMARK 620 4 HOH A 218   O   161.4  74.2  65.9                                  
REMARK 620 5 HOH A 219   O   108.2 112.2  99.5  86.3                            
REMARK 620 N                    1     2     3     4                             
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 664   SG                                                     
REMARK 620 2 CYS B 667   SG  118.2                                              
REMARK 620 3 CYS B 678   SG  100.0 107.1                                        
REMARK 620 N                    1     2                                         
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 ZN B 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: 3GJ7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN                
REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 12                          
REMARK 900 RELATED ID: 3GJ8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN                
REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 34                          
DBREF  3GJ6 A    2   216  UNP    P62826   RAN_HUMAN        2    216             
DBREF  3GJ6 B  658   686  UNP    P49791   NU153_RAT      658    686             
SEQADV 3GJ6 GLY A   -4  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ6 PRO A   -3  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ6 HIS A   -2  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ6 MET A   -1  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ6 ALA A    0  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ6 SER A    1  UNP  P62826              EXPRESSION TAG                 
SEQADV 3GJ6 SER A   35  UNP  P62826    PHE    35 ENGINEERED                     
SEQADV 3GJ6 GLY B  653  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ6 PRO B  654  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ6 LEU B  655  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ6 GLY B  656  UNP  P49791              EXPRESSION TAG                 
SEQADV 3GJ6 SER B  657  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   34  GLY PRO LEU GLY SER ALA GLY SER SER TRP GLN CYS ASP          
SEQRES   2 B   34  THR CYS LEU LEU GLN ASN LYS VAL THR ASP ASN LYS CYS          
SEQRES   3 B   34  ILE ALA CYS GLN ALA ALA LYS LEU                              
HET     MG  A 301       1                                                       
HET    GDP  A 302      28                                                       
HET     ZN  B 300       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM      ZN ZINC ION                                                         
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  GDP    C10 H15 N5 O11 P2                                            
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6  HOH   *34(H2 O)                                                     
HELIX    1   1 GLY A   22  LYS A   28  1                                   7    
HELIX    2   2 HIS A   30  LYS A   37  1                                   8    
HELIX    3   3 GLY A   68  GLY A   73  5                                   6    
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  ARG A  110  1                                  11    
HELIX    7   7 LYS A  132  ILE A  136  5                                   5    
HELIX    8   8 VAL A  137  LYS A  141  5                                   5    
HELIX    9   9 SER A  150  ASN A  154  5                                   5    
HELIX   10  10 GLU A  158  GLY A  170  1                                  13    
HELIX   11  11 ASP A  190  THR A  206  1                                  17    
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  47   N  LYS A  38           
SHEET    3   A 7 GLY A  57  THR A  66 -1  O  GLY A  57   N  THR A  54           
SHEET    4   A 7 GLN A  10  GLY A  17  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  CYS A 120   N  ILE A  88           
SHEET    7   A 7 LEU A 144  ASP A 148  1  O  GLN A 145   N  LEU A 119           
SHEET    1   B 3 LYS A  38  VAL A  40  0                                        
SHEET    2   B 3 VAL A  45  THR A  54 -1  O  VAL A  47   N  LYS A  38           
SHEET    3   B 3 PHE A 176  ALA A 178 -1  O  VAL A 177   N  HIS A  53           
LINK         OG1 THR A  24                MG    MG A 301     1555   1555  2.28  
LINK         SG  CYS B 664                ZN    ZN B 300     1555   1555  2.81  
LINK         SG  CYS B 667                ZN    ZN B 300     1555   1555  2.58  
LINK         SG  CYS B 678                ZN    ZN B 300     1555   1555  2.62  
LINK        MG    MG A 301                 O   HOH A 217     1555   1555  2.45  
LINK        MG    MG A 301                 O   HOH A 220     1555   1555  2.35  
LINK        MG    MG A 301                 O   HOH A 218     1555   1555  2.48  
LINK        MG    MG A 301                 O   HOH A 219     1555   1555  2.42  
SITE     1 AC1  7 THR A  24  THR A  66  HOH A 217  HOH A 218                    
SITE     2 AC1  7 HOH A 219  HOH A 220  GDP A 302                               
SITE     1 AC2 19 GLY A  20  THR A  21  GLY A  22  LYS A  23                    
SITE     2 AC2 19 THR A  24  THR A  25  ASN A 122  LYS A 123                    
SITE     3 AC2 19 ASP A 125  ILE A 126  SER A 150  ALA A 151                    
SITE     4 AC2 19 LYS A 152  HOH A 217  HOH A 218  HOH A 220                    
SITE     5 AC2 19 HOH A 226   MG A 301  LYS B 672                               
SITE     1 AC3  4 CYS B 664  CYS B 667  CYS B 678  CYS B 681                    
CRYST1   60.132   80.305   54.634  90.00  90.00  90.00 P 21 21 2     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      0.016630  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012453  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018304        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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