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Database: PDB
Entry: 3CQG
LinkDB: 3CQG
Original site: 3CQG 
HEADER    PROTEIN TRANSPORT                       02-APR-08   3CQG              
TITLE     NUCLEOPORIN NUP107/NUP133 INTERACTION COMPLEX, DELTA FINGER MUTANT    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEAR PORE COMPLEX PROTEIN NUP107;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 658-771, 802-925, CONNECTED BY LINKER GGSGGS;     
COMPND   5 SYNONYM: NUCLEOPORIN NUP107, 107 KDA NUCLEOPORIN, RESIDUES 658-771 + 
COMPND   6 LINKER GGSGGS + RESIDUES 802-925;                                    
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: NUCLEAR PORE COMPLEX PROTEIN NUP133;                       
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: RESIDUES 935-1156;                                         
COMPND  12 SYNONYM: NUCLEOPORIN NUP133, 133 KDA NUCLEOPORIN;                    
COMPND  13 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: NUP107;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-DUET1;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: NUP133;                                                        
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET-DUET1                                 
KEYWDS    NUCLEOPORINS, NUCLEAR PORE COMPLEX, MRNA TRANSPORT, NUCLEUS,          
KEYWDS   2 PHOSPHOPROTEIN, PROTEIN TRANSPORT, TRANSLOCATION                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.JEUDY,T.BOEHMER,I.BERKE,T.U.SCHWARTZ                                
REVDAT   4   23-AUG-17 3CQG    1       SOURCE                                   
REVDAT   3   23-JAN-13 3CQG    1       JRNL   VERSN                             
REVDAT   2   24-FEB-09 3CQG    1       VERSN                                    
REVDAT   1   01-JUL-08 3CQG    0                                                
JRNL        AUTH   T.BOEHMER,S.JEUDY,I.C.BERKE,T.U.SCHWARTZ                     
JRNL        TITL   STRUCTURAL AND FUNCTIONAL STUDIES OF NUP107/NUP133           
JRNL        TITL 2 INTERACTION AND ITS IMPLICATIONS FOR THE ARCHITECTURE OF THE 
JRNL        TITL 3 NUCLEAR PORE COMPLEX.                                        
JRNL        REF    MOL.CELL                      V.  30   721 2008              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   18570875                                                     
JRNL        DOI    10.1016/J.MOLCEL.2008.04.022                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12548                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.243                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1004                            
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  3.1400 -  3.0000    0.95        0   134  0.2860 0.3290        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 74.90                          
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      :  0.011           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3CQG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047088.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
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) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
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   : 12599                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.52400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-27% PEG 2000 MME, 500MM KSCN, 0.1M    
REMARK 280  HEPES, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       23.82750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       96.61500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.76650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       96.61500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.82750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.76650            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.1 KCAL/MOL                        
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 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   656                                                      
REMARK 465     SER A   657                                                      
REMARK 465     PRO A   658                                                      
REMARK 465     ALA A   659                                                      
REMARK 465     LEU A   660                                                      
REMARK 465     ASP A   661                                                      
REMARK 465     THR A   662                                                      
REMARK 465     GLY A   663                                                      
REMARK 465     THR A   664                                                      
REMARK 465     THR A   665                                                      
REMARK 465     GLN A   730                                                      
REMARK 465     GLY A   731                                                      
REMARK 465     MET A   732                                                      
REMARK 465     GLU A   733                                                      
REMARK 465     SER A   734                                                      
REMARK 465     PRO A   735                                                      
REMARK 465     GLY A   796                                                      
REMARK 465     GLY A   797                                                      
REMARK 465     SER A   798                                                      
REMARK 465     GLY A   799                                                      
REMARK 465     LEU A   925                                                      
REMARK 465     MET B   930                                                      
REMARK 465     ALA B   931                                                      
REMARK 465     SER B   932                                                      
REMARK 465     HIS B   933                                                      
REMARK 465     HIS B   934                                                      
REMARK 465     GLU B  1061                                                      
REMARK 465     GLU B  1062                                                      
REMARK 465     ASP B  1063                                                      
REMARK 465     ILE B  1064                                                      
REMARK 465     SER B  1084                                                      
REMARK 465     SER B  1085                                                      
REMARK 465     SER B  1086                                                      
REMARK 465     ASP B  1087                                                      
REMARK 465     GLY B  1088                                                      
REMARK 465     LYS B  1089                                                      
REMARK 465     ASP B  1090                                                      
REMARK 465     ASP B  1091                                                      
REMARK 465     PRO B  1092                                                      
REMARK 465     ILE B  1093                                                      
REMARK 465     GLU B  1094                                                      
REMARK 465     GLN B  1106                                                      
REMARK 465     LYS B  1107                                                      
REMARK 465     LEU B  1108                                                      
REMARK 465     LEU B  1109                                                      
REMARK 465     LYS B  1110                                                      
REMARK 465     ASP B  1111                                                      
REMARK 465     GLY B  1112                                                      
REMARK 465     ILE B  1113                                                      
REMARK 465     GLN B  1114                                                      
REMARK 465     LEU B  1115                                                      
REMARK 465     SER B  1116                                                      
REMARK 465     GLU B  1117                                                      
REMARK 465     TYR B  1118                                                      
REMARK 465     GLN B  1130                                                      
REMARK 465     LEU B  1131                                                      
REMARK 465     GLY B  1132                                                      
REMARK 465     SER B  1133                                                      
REMARK 465     LEU B  1134                                                      
REMARK 465     LYS B  1135                                                      
REMARK 465     SER B  1136                                                      
REMARK 465     ASN B  1137                                                      
REMARK 465     PRO B  1138                                                      
REMARK 465     TYR B  1139                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 666    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 667    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 668    CG   OD1  OD2                                       
REMARK 470     ARG A 669    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 684    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 924    CG   CD   OE1  NE2                                  
REMARK 470     LYS B1097    CG   CD   CE   NZ                                   
REMARK 470     LYS B1103    CG   CD   CE   NZ                                   
REMARK 470     LYS B1123    CG   CD   CE   NZ                                   
REMARK 470     LEU B1125    CG   CD1  CD2                                       
REMARK 470     LEU B1126    CG   CD1  CD2                                       
REMARK 470     PHE B1140    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     GLU B1141    CG   CD   OE1  OE2                                  
REMARK 470     PHE B1142    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B1144    CG   CD1  CD2                                       
REMARK 470     LYS B1145    CG   CD   CE   NZ                                   
REMARK 470     TYR B1148    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B1149    CG   CD   OE1  OE2                                  
REMARK 470     TYR B1150    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR B1151    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B1153    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A 684       57.79   -116.36                                   
REMARK 500    PRO A 716       14.35    -59.95                                   
REMARK 500    ASP A 718        6.65   -151.17                                   
REMARK 500    CYS A 727      -97.22   -115.42                                   
REMARK 500    TRP A 802      -71.95    -74.66                                   
REMARK 500    LEU A 822       54.19   -114.91                                   
REMARK 500    THR A 863      -72.24    -42.58                                   
REMARK 500    SER A 867      -19.35    -47.95                                   
REMARK 500    GLN A 870       53.41    -92.28                                   
REMARK 500    ASP A 913       -6.91    -57.02                                   
REMARK 500    THR B 961      -15.04   -147.60                                   
REMARK 500    ASN B1019      103.43    -49.20                                   
REMARK 500    LEU B1020      -49.05    -12.89                                   
REMARK 500    SER B1021       60.83   -151.89                                   
REMARK 500    ARG B1042       13.45    -68.06                                   
REMARK 500    ASP B1059       72.31     58.40                                   
REMARK 500    PRO B1120       10.75    -59.95                                   
REMARK 500    ASP B1124      -85.68   -129.42                                   
REMARK 500    TYR B1148        4.74    -68.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CQC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NUCLEOPORINS                                    
DBREF  3CQG A  658   771  UNP    P57740   NU107_HUMAN    658    771             
DBREF  3CQG A  802   925  UNP    P57740   NU107_HUMAN    802    925             
DBREF  3CQG B  934  1156  UNP    Q8WUM0   NU133_HUMAN    934   1156             
SEQADV 3CQG GLY A  656  UNP  P57740              EXPRESSION TAG                 
SEQADV 3CQG SER A  657  UNP  P57740              EXPRESSION TAG                 
SEQADV 3CQG GLY A  796  UNP  P57740              LINKER                         
SEQADV 3CQG GLY A  797  UNP  P57740              LINKER                         
SEQADV 3CQG SER A  798  UNP  P57740              LINKER                         
SEQADV 3CQG GLY A  799  UNP  P57740              LINKER                         
SEQADV 3CQG GLY A  800  UNP  P57740              LINKER                         
SEQADV 3CQG SER A  801  UNP  P57740              LINKER                         
SEQADV 3CQG MET B  930  UNP  Q8WUM0              EXPRESSION TAG                 
SEQADV 3CQG ALA B  931  UNP  Q8WUM0              EXPRESSION TAG                 
SEQADV 3CQG SER B  932  UNP  Q8WUM0              EXPRESSION TAG                 
SEQADV 3CQG HIS B  933  UNP  Q8WUM0              EXPRESSION TAG                 
SEQRES   1 A  246  GLY SER PRO ALA LEU ASP THR GLY THR THR GLU GLU ASP          
SEQRES   2 A  246  ARG LEU LYS ILE ASP VAL ILE ASP TRP LEU VAL PHE ASP          
SEQRES   3 A  246  PRO ALA GLN ARG ALA GLU ALA LEU LYS GLN GLY ASN ALA          
SEQRES   4 A  246  ILE MET ARG LYS PHE LEU ALA SER LYS LYS HIS GLU ALA          
SEQRES   5 A  246  ALA LYS GLU VAL PHE VAL LYS ILE PRO GLN ASP SER ILE          
SEQRES   6 A  246  ALA GLU ILE TYR ASN GLN CYS GLU GLU GLN GLY MET GLU          
SEQRES   7 A  246  SER PRO LEU PRO ALA GLU ASP ASP ASN ALA ILE ARG GLU          
SEQRES   8 A  246  HIS LEU CYS ILE ARG ALA TYR LEU GLU ALA HIS GLU THR          
SEQRES   9 A  246  PHE ASN GLU TRP PHE LYS HIS MET ASN SER VAL PRO GLY          
SEQRES  10 A  246  GLY SER GLY GLY SER TRP LYS GLY HIS LEU ASP ALA LEU          
SEQRES  11 A  246  THR ALA ASP VAL LYS GLU LYS MET TYR ASN VAL LEU LEU          
SEQRES  12 A  246  PHE VAL ASP GLY GLY TRP MET VAL ASP VAL ARG GLU ASP          
SEQRES  13 A  246  ALA LYS GLU ASP HIS GLU ARG THR HIS GLN MET VAL LEU          
SEQRES  14 A  246  LEU ARG LYS LEU CYS LEU PRO MET LEU CYS PHE LEU LEU          
SEQRES  15 A  246  HIS THR ILE LEU HIS SER THR GLY GLN TYR GLN GLU CYS          
SEQRES  16 A  246  LEU GLN LEU ALA ASP MET VAL SER SER GLU ARG HIS LYS          
SEQRES  17 A  246  LEU TYR LEU VAL PHE SER LYS GLU GLU LEU ARG LYS LEU          
SEQRES  18 A  246  LEU GLN LYS LEU ARG GLU SER SER LEU MET LEU LEU ASP          
SEQRES  19 A  246  GLN GLY LEU ASP PRO LEU GLY TYR GLU ILE GLN LEU              
SEQRES   1 B  227  MET ALA SER HIS HIS LEU SER TRP LEU HIS GLU ILE ASN          
SEQRES   2 B  227  SER GLN GLU LEU GLU LYS ALA HIS ALA THR LEU LEU GLY          
SEQRES   3 B  227  LEU ALA ASN MET GLU THR ARG TYR PHE ALA LYS LYS LYS          
SEQRES   4 B  227  THR LEU LEU GLY LEU SER LYS LEU ALA ALA LEU ALA SER          
SEQRES   5 B  227  ASP PHE SER GLU ASP MET LEU GLN GLU LYS ILE GLU GLU          
SEQRES   6 B  227  MET ALA GLU GLN GLU ARG PHE LEU LEU HIS GLN GLU THR          
SEQRES   7 B  227  LEU PRO GLU GLN LEU LEU ALA GLU LYS GLN LEU ASN LEU          
SEQRES   8 B  227  SER ALA MET PRO VAL LEU THR ALA PRO GLN LEU ILE GLY          
SEQRES   9 B  227  LEU TYR ILE CYS GLU GLU ASN ARG ARG ALA ASN GLU TYR          
SEQRES  10 B  227  ASP PHE LYS LYS ALA LEU ASP LEU LEU GLU TYR ILE ASP          
SEQRES  11 B  227  GLU GLU GLU ASP ILE ASN ILE ASN ASP LEU LYS LEU GLU          
SEQRES  12 B  227  ILE LEU CYS LYS ALA LEU GLN ARG ASP ASN TRP SER SER          
SEQRES  13 B  227  SER ASP GLY LYS ASP ASP PRO ILE GLU VAL SER LYS ASP          
SEQRES  14 B  227  SER ILE PHE VAL LYS ILE LEU GLN LYS LEU LEU LYS ASP          
SEQRES  15 B  227  GLY ILE GLN LEU SER GLU TYR LEU PRO GLU VAL LYS ASP          
SEQRES  16 B  227  LEU LEU GLN ALA ASP GLN LEU GLY SER LEU LYS SER ASN          
SEQRES  17 B  227  PRO TYR PHE GLU PHE VAL LEU LYS ALA ASN TYR GLU TYR          
SEQRES  18 B  227  TYR VAL GLN GLY GLN ILE                                      
FORMUL   3  HOH   *34(H2 O)                                                     
HELIX    1   1 GLU A  666  VAL A  679  1                                  14    
HELIX    2   2 ASP A  681  ALA A  683  5                                   3    
HELIX    3   3 GLN A  684  SER A  702  1                                  19    
HELIX    4   4 LYS A  704  LYS A  714  1                                  11    
HELIX    5   5 ASP A  718  GLN A  726  1                                   9    
HELIX    6   6 PRO A  737  VAL A  770  1                                  34    
HELIX    7   7 GLY A  800  LEU A  822  1                                  23    
HELIX    8   8 ASP A  839  SER A  867  1                                  29    
HELIX    9   9 GLN A  870  GLN A  876  1                                   7    
HELIX   10  10 GLN A  876  SER A  883  1                                   8    
HELIX   11  11 LYS A  887  PHE A  892  5                                   6    
HELIX   12  12 SER A  893  ASP A  913  1                                  21    
HELIX   13  13 SER B  936  SER B  943  1                                   8    
HELIX   14  14 GLU B  945  GLU B  960  1                                  16    
HELIX   15  15 TYR B  963  SER B  981  1                                  19    
HELIX   16  16 SER B  984  ARG B 1000  1                                  17    
HELIX   17  17 PHE B 1001  THR B 1007  1                                   7    
HELIX   18  18 PRO B 1009  LYS B 1016  1                                   8    
HELIX   19  19 THR B 1027  CYS B 1037  1                                  11    
HELIX   20  20 ASN B 1044  LEU B 1054  1                                  11    
HELIX   21  21 LEU B 1055  ILE B 1058  5                                   4    
HELIX   22  22 ASN B 1065  ASN B 1082  1                                  18    
HELIX   23  23 VAL B 1095  LEU B 1105  1                                  11    
HELIX   24  24 ASP B 1124  ASP B 1129  1                                   6    
HELIX   25  25 PHE B 1140  ILE B 1156  1                                  17    
CRYST1   47.655   65.533  193.230  90.00  90.00  90.00 P 21 21 21    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      0.020984  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015259  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005175        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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