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Database: PDB
Entry: 2XWU
LinkDB: 2XWU
Original site: 2XWU 
HEADER    LIGASE/NUCLEAR PROTEIN                  05-NOV-10   2XWU              
TITLE     CRYSTAL STRUCTURE OF IMPORTIN 13 - UBC9 COMPLEX                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUMO-CONJUGATING ENZYME UBC9;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SUMO-PROTEIN LIGASE, UBIQUITIN CARRIER PROTEIN 9,           
COMPND   5  UBIQUITIN CARRIER PROTEIN I, UBIQUITIN-CONJUGATING ENZYME E2 I,     
COMPND   6  UBIQUITIN-PROTEIN LIGASE I, P18, UBC9;                              
COMPND   7 EC: 6.3.2.19;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: IMPORTIN13;                                                
COMPND  11 CHAIN: B;                                                            
COMPND  12 SYNONYM: IMP13, KARYOPHERIN-13, KAP13, RAN-BINDING PROTEIN 13,       
COMPND  13  RANBP13;                                                            
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    LIGASE-NUCLEAR PROTEIN COMPLEX, NUCLEAR IMPORT                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GRUENWALD,F.BONO                                                    
REVDAT   2   06-APR-11 2XWU    1       JRNL   REMARK                            
REVDAT   1   29-DEC-10 2XWU    0                                                
JRNL        AUTH   M.GRUENWALD,F.BONO                                           
JRNL        TITL   STRUCTURE OF IMPORTIN13-UBC9 COMPLEX: NUCLEAR IMPORT AND     
JRNL        TITL 2 RELEASE OF A KEY REGULATOR OF SUMOYLATION.                   
JRNL        REF    EMBO J.                       V.  30   427 2011              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   21139563                                                     
JRNL        DOI    10.1038/EMBOJ.2010.320                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3441228.86                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 31.200000                      
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 40230                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2005                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.8                          
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8098                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 36                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.9                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.40                                                 
REMARK   3    B22 (A**2) : 2.92                                                 
REMARK   3    B33 (A**2) : -3.32                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.52                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.45                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.53                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.405                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : CNS BULK SOLVENT MODEL USED                          
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 62.8192                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2XWU COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-NOV-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-46109.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUL-09                          
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               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9997                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40287                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.49                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.68                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.37                               
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 ENTRIES 2X19 AND 1U9A                            
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.3                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES PH 6.5 25% PEG 300             
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       34.35000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       92.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.40000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       92.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.35000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.40000            
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: 2650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.3 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     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     PRO B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     GLU B   153                                                      
REMARK 465     ASP B   154                                                      
REMARK 465     SER B   155                                                      
REMARK 465     SER B   457                                                      
REMARK 465     GLU B   458                                                      
REMARK 465     GLU B   459                                                      
REMARK 465     PRO B   460                                                      
REMARK 465     HIS B   656                                                      
REMARK 465     GLU B   657                                                      
REMARK 465     ASP B   658                                                      
REMARK 465     ASP B   659                                                      
REMARK 465     HIS B   660                                                      
REMARK 465     GLU B   661                                                      
REMARK 465     GLY B   662                                                      
REMARK 465     PRO B   663                                                      
REMARK 465     GLU B   664                                                      
REMARK 465     LEU B   665                                                      
REMARK 465     ARG B   666                                                      
REMARK 465     LYS B   667                                                      
REMARK 465     LEU B   668                                                      
REMARK 465     PRO B   669                                                      
REMARK 465     VAL B   670                                                      
REMARK 465     PRO B   671                                                      
REMARK 465     GLN B   672                                                      
REMARK 465     GLY B   673                                                      
REMARK 465     HIS B   955                                                      
REMARK 465     GLY B   956                                                      
REMARK 465     THR B   957                                                      
REMARK 465     ASP B   958                                                      
REMARK 465     TYR B   959                                                      
REMARK 465     THR B   960                                                      
REMARK 465     ALA B   961                                                      
REMARK 465     ASP B   962                                                      
REMARK 465     TYR B   963                                                      
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     ILE A   4    CG1  CG2  CD1                                       
REMARK 470     LYS A  14    CG   CD   CE   NZ                                   
REMARK 470     LYS A  30    CG   CD   CE   NZ                                   
REMARK 470     ASP A  33    CG   OD1  OD2                                       
REMARK 470     THR A  35    OG1  CG2                                            
REMARK 470     LYS A  49    CG   CD   CE   NZ                                   
REMARK 470     LYS A  65    CG   CD   CE   NZ                                   
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     LYS A  76    CG   CD   CE   NZ                                   
REMARK 470     SER A  95    OG                                                  
REMARK 470     GLN A 126    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     SER A 158    OG                                                  
REMARK 470     LEU B  19    CG   CD1  CD2                                       
REMARK 470     ASP B  20    CG   OD1  OD2                                       
REMARK 470     LYS B  28    CG   CD   CE   NZ                                   
REMARK 470     GLN B  32    CG   CD   OE1  NE2                                  
REMARK 470     ILE B  39    CG1  CG2  CD1                                       
REMARK 470     GLU B  40    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  47    CG   CD   CE   NZ                                   
REMARK 470     GLN B  51    CG   CD   OE1  NE2                                  
REMARK 470     SER B  91    OG                                                  
REMARK 470     SER B 100    OG                                                  
REMARK 470     GLN B 104    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 117    CG   CD   CE   NZ                                   
REMARK 470     PRO B 156    CG   CD                                             
REMARK 470     VAL B 157    CG1  CG2                                            
REMARK 470     ARG B 162    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 180    OG                                                  
REMARK 470     GLN B 184    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 185    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     LEU B 189    CG   CD1  CD2                                       
REMARK 470     SER B 193    OG                                                  
REMARK 470     GLN B 210    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 211    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 220    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 251    CG   CD   OE1  NE2                                  
REMARK 470     SER B 253    OG                                                  
REMARK 470     GLU B 254    CG   CD   OE1  OE2                                  
REMARK 470     SER B 258    OG                                                  
REMARK 470     GLN B 273    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 274    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 276    CG1  CG2                                            
REMARK 470     GLN B 295    CG   CD   OE1  NE2                                  
REMARK 470     SER B 320    OG                                                  
REMARK 470     GLU B 328    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 368    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 375    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 377    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 384    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 407    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 408    CG   CD   OE1  OE2                                  
REMARK 470     SER B 414    OG                                                  
REMARK 470     GLU B 441    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 456    OG                                                  
REMARK 470     TYR B 461    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER B 485    OG                                                  
REMARK 470     SER B 499    OG                                                  
REMARK 470     SER B 529    OG                                                  
REMARK 470     SER B 585    OG                                                  
REMARK 470     GLN B 602    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 603    CG1  CG2                                            
REMARK 470     GLU B 604    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 608    CG   CD   CE   NZ                                   
REMARK 470     SER B 615    OG                                                  
REMARK 470     ILE B 618    CG1  CG2  CD1                                       
REMARK 470     GLN B 619    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 624    CG   CD1  CD2                                       
REMARK 470     GLU B 626    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 628    CG1  CG2  CD1                                       
REMARK 470     LYS B 634    CG   CD   CE   NZ                                   
REMARK 470     ILE B 637    CG1  CG2  CD1                                       
REMARK 470     SER B 654    OG                                                  
REMARK 470     HIS B 655    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN B 675    CG   OD1  ND2                                       
REMARK 470     GLN B 682    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 686    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 687    CG   CD1  CD2                                       
REMARK 470     ILE B 688    CG1  CG2  CD1                                       
REMARK 470     LYS B 690    CG   CD   CE   NZ                                   
REMARK 470     LYS B 694    CG   CD   CE   NZ                                   
REMARK 470     VAL B 702    CG1  CG2                                            
REMARK 470     ARG B 733    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 749    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 757    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 765    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 804    CG   CD   CE   NZ                                   
REMARK 470     GLU B 811    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 812    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 827    CG   CD   CE   NZ                                   
REMARK 470     GLU B 852    CG   CD   OE1  OE2                                  
REMARK 470     SER B 853    OG                                                  
REMARK 470     LYS B 856    CG   CD   CE   NZ                                   
REMARK 470     GLN B 859    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 863    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 878    OG                                                  
REMARK 470     SER B 880    OG                                                  
REMARK 470     SER B 901    OG                                                  
REMARK 470     ILE B 904    CG1  CG2  CD1                                       
REMARK 470     LYS B 905    CG   CD   CE   NZ                                   
REMARK 470     GLN B 909    CG   CD   OE1  NE2                                  
REMARK 470     SER B 919    OG                                                  
REMARK 470     GLU B 921    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 924    CG   OD1  OD2                                       
REMARK 470     GLN B 928    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 933    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 934    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 938    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 939    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 946    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 954    CA   C    O    CB   CG   CD1  CD2                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR B 565   CD1   TYR B 565   CE1    -0.158                       
REMARK 500    TYR B 565   CD2   TYR B 565   CE2    -0.157                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 156   N   -  CA  -  CB  ANGL. DEV. =   7.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  83      137.88   -177.51                                   
REMARK 500    LYS A 101      -71.09   -115.92                                   
REMARK 500    TYR B  89       67.70   -114.63                                   
REMARK 500    TYR B 275       73.65   -110.89                                   
REMARK 500    TRP B 330      -36.69    -39.01                                   
REMARK 500    ALA B 376     -130.49     60.63                                   
REMARK 500    PRO B 496       -1.83    -59.57                                   
REMARK 500    LEU B 717     -118.87     62.77                                   
REMARK 500    ALA B 721      -39.71    -34.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B 365         0.07    SIDE CHAIN                              
REMARK 500    TYR B 484         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2GRO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN RANGAP1-UBC9-N85Q                        
REMARK 900 RELATED ID: 2GRR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN RANGAP1-UBC9-D127S                       
REMARK 900 RELATED ID: 1KPS   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR E2-MEDIATED SUMO CONJUGATION                   
REMARK 900  REVEALEDBY A COMPLEX BETWEEN UBIQUITIN CONJUGATING ENZYME           
REMARK 900   UBC9 ANDRANGAP1                                                    
REMARK 900 RELATED ID: 2GRP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN RANGAP1-UBC9-Y87A                        
REMARK 900 RELATED ID: 1Z5S   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF A COMPLEX BETWEEN UBC9, SUMO-1,                
REMARK 900  RANGAP1 AND NUP358/RANBP2                                           
REMARK 900 RELATED ID: 2X19   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF IMPORTIN13 - RANGTP COMPLEX                    
REMARK 900 RELATED ID: 2GRQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN RANGAP1-UBC9-D127A                       
REMARK 900 RELATED ID: 1A3S   RELATED DB: PDB                                   
REMARK 900  HUMAN UBC9                                                          
REMARK 900 RELATED ID: 2GRN   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN RANGAP1-UBC9                             
DBREF  2XWU A    1   158  UNP    P63279   UBC9_HUMAN       1    158             
DBREF  2XWU B    1   963  UNP    O94829   IPO13_HUMAN      1    963             
SEQRES   1 A  158  MET SER GLY ILE ALA LEU SER ARG LEU ALA GLN GLU ARG          
SEQRES   2 A  158  LYS ALA TRP ARG LYS ASP HIS PRO PHE GLY PHE VAL ALA          
SEQRES   3 A  158  VAL PRO THR LYS ASN PRO ASP GLY THR MET ASN LEU MET          
SEQRES   4 A  158  ASN TRP GLU CYS ALA ILE PRO GLY LYS LYS GLY THR PRO          
SEQRES   5 A  158  TRP GLU GLY GLY LEU PHE LYS LEU ARG MET LEU PHE LYS          
SEQRES   6 A  158  ASP ASP TYR PRO SER SER PRO PRO LYS CYS LYS PHE GLU          
SEQRES   7 A  158  PRO PRO LEU PHE HIS PRO ASN VAL TYR PRO SER GLY THR          
SEQRES   8 A  158  VAL CYS LEU SER ILE LEU GLU GLU ASP LYS ASP TRP ARG          
SEQRES   9 A  158  PRO ALA ILE THR ILE LYS GLN ILE LEU LEU GLY ILE GLN          
SEQRES  10 A  158  GLU LEU LEU ASN GLU PRO ASN ILE GLN ASP PRO ALA GLN          
SEQRES  11 A  158  ALA GLU ALA TYR THR ILE TYR CYS GLN ASN ARG VAL GLU          
SEQRES  12 A  158  TYR GLU LYS ARG VAL ARG ALA GLN ALA LYS LYS PHE ALA          
SEQRES  13 A  158  PRO SER                                                      
SEQRES   1 B  963  MET GLU ARG ARG GLU GLU GLN PRO GLY ALA ALA GLY ALA          
SEQRES   2 B  963  GLY ALA ALA PRO ALA LEU ASP PHE THR VAL GLU ASN VAL          
SEQRES   3 B  963  GLU LYS ALA LEU HIS GLN LEU TYR TYR ASP PRO ASN ILE          
SEQRES   4 B  963  GLU ASN LYS ASN LEU ALA GLN LYS TRP LEU MET GLN ALA          
SEQRES   5 B  963  GLN VAL SER PRO GLN ALA TRP HIS PHE SER TRP GLN LEU          
SEQRES   6 B  963  LEU GLN PRO ASP LYS VAL PRO GLU ILE GLN TYR PHE GLY          
SEQRES   7 B  963  ALA SER ALA LEU HIS ILE LYS ILE SER ARG TYR TRP SER          
SEQRES   8 B  963  ASP ILE PRO THR ASP GLN TYR GLU SER LEU LYS ALA GLN          
SEQRES   9 B  963  LEU PHE THR GLN ILE THR ARG PHE ALA SER GLY SER LYS          
SEQRES  10 B  963  ILE VAL LEU THR ARG LEU CYS VAL ALA LEU ALA SER LEU          
SEQRES  11 B  963  ALA LEU SER MET MET PRO ASP ALA TRP PRO CYS ALA VAL          
SEQRES  12 B  963  ALA ASP MET VAL ARG LEU PHE GLN ALA GLU ASP SER PRO          
SEQRES  13 B  963  VAL ASP GLY GLN GLY ARG CYS LEU ALA LEU LEU GLU LEU          
SEQRES  14 B  963  LEU THR VAL LEU PRO GLU GLU PHE GLN THR SER ARG LEU          
SEQRES  15 B  963  PRO GLN TYR ARG LYS GLY LEU VAL ARG THR SER LEU ALA          
SEQRES  16 B  963  VAL GLU CYS GLY ALA VAL PHE PRO LEU LEU GLU GLN LEU          
SEQRES  17 B  963  LEU GLN GLN PRO SER SER PRO SER CYS VAL ARG GLN LYS          
SEQRES  18 B  963  VAL LEU LYS CYS PHE SER SER TRP VAL GLN LEU GLU VAL          
SEQRES  19 B  963  PRO LEU GLN ASP CYS GLU ALA LEU ILE GLN ALA ALA PHE          
SEQRES  20 B  963  ALA ALA LEU GLN ASP SER GLU LEU PHE ASP SER SER VAL          
SEQRES  21 B  963  GLU ALA ILE VAL ASN ALA ILE SER GLN PRO ASP ALA GLN          
SEQRES  22 B  963  ARG TYR VAL ASN THR LEU LEU LYS LEU ILE PRO LEU VAL          
SEQRES  23 B  963  LEU GLY LEU GLN GLU GLN LEU ARG GLN ALA VAL GLN ASN          
SEQRES  24 B  963  GLY ASP MET GLU THR SER HIS GLY ILE CYS ARG ILE ALA          
SEQRES  25 B  963  VAL ALA LEU GLY GLU ASN HIS SER ARG ALA LEU LEU ASP          
SEQRES  26 B  963  GLN VAL GLU HIS TRP GLN SER PHE LEU ALA LEU VAL ASN          
SEQRES  27 B  963  MET ILE MET PHE CYS THR GLY ILE PRO GLY HIS TYR PRO          
SEQRES  28 B  963  VAL ASN GLU THR THR SER SER LEU THR LEU THR PHE TRP          
SEQRES  29 B  963  TYR THR LEU GLN ASP ASP ILE LEU SER PHE GLU ALA GLU          
SEQRES  30 B  963  LYS GLN ALA VAL TYR GLN GLN VAL TYR ARG PRO VAL TYR          
SEQRES  31 B  963  PHE GLN LEU VAL ASP VAL LEU LEU HIS LYS ALA GLN PHE          
SEQRES  32 B  963  PRO SER ASP GLU GLU TYR GLY PHE TRP SER SER ASP GLU          
SEQRES  33 B  963  LYS GLU GLN PHE ARG ILE TYR ARG VAL ASP ILE SER ASP          
SEQRES  34 B  963  THR LEU MET TYR VAL TYR GLU MET LEU GLY ALA GLU LEU          
SEQRES  35 B  963  LEU SER ASN LEU TYR ASP LYS LEU GLY ARG LEU LEU THR          
SEQRES  36 B  963  SER SER GLU GLU PRO TYR SER TRP GLN HIS THR GLU ALA          
SEQRES  37 B  963  LEU LEU TYR GLY PHE GLN SER ILE ALA GLU THR ILE ASP          
SEQRES  38 B  963  VAL ASN TYR SER ASP VAL VAL PRO GLY LEU ILE GLY LEU          
SEQRES  39 B  963  ILE PRO ARG ILE SER ILE SER ASN VAL GLN LEU ALA ASP          
SEQRES  40 B  963  THR VAL MET PHE THR ILE GLY ALA LEU SER GLU TRP LEU          
SEQRES  41 B  963  ALA ASP HIS PRO VAL MET ILE ASN SER VAL LEU PRO LEU          
SEQRES  42 B  963  VAL LEU HIS ALA LEU GLY ASN PRO GLU LEU SER VAL SER          
SEQRES  43 B  963  SER VAL SER THR LEU LYS LYS ILE CYS ARG GLU CYS LYS          
SEQRES  44 B  963  TYR ASP LEU PRO PRO TYR ALA ALA ASN ILE VAL ALA VAL          
SEQRES  45 B  963  SER GLN ASP VAL LEU MET LYS GLN ILE HIS LYS THR SER          
SEQRES  46 B  963  GLN CYS MET TRP LEU MET GLN ALA LEU GLY PHE LEU LEU          
SEQRES  47 B  963  SER ALA LEU GLN VAL GLU GLU ILE LEU LYS ASN LEU HIS          
SEQRES  48 B  963  SER LEU ILE SER PRO TYR ILE GLN GLN LEU GLU LYS LEU          
SEQRES  49 B  963  ALA GLU GLU ILE PRO ASN PRO SER ASN LYS LEU ALA ILE          
SEQRES  50 B  963  VAL HIS ILE LEU GLY LEU LEU SER ASN LEU PHE THR THR          
SEQRES  51 B  963  LEU ASP ILE SER HIS HIS GLU ASP ASP HIS GLU GLY PRO          
SEQRES  52 B  963  GLU LEU ARG LYS LEU PRO VAL PRO GLN GLY PRO ASN PRO          
SEQRES  53 B  963  VAL VAL VAL VAL LEU GLN GLN VAL PHE GLN LEU ILE GLN          
SEQRES  54 B  963  LYS VAL LEU SER LYS TRP LEU ASN ASP ALA GLN VAL VAL          
SEQRES  55 B  963  GLU ALA VAL CYS ALA ILE PHE GLU LYS SER VAL LYS THR          
SEQRES  56 B  963  LEU LEU ASP ASP PHE ALA PRO MET VAL PRO GLN LEU CYS          
SEQRES  57 B  963  GLU MET LEU GLY ARG MET TYR SER THR ILE PRO GLN ALA          
SEQRES  58 B  963  SER ALA LEU ASP LEU THR ARG GLN LEU VAL HIS ILE PHE          
SEQRES  59 B  963  ALA HIS GLU PRO ALA HIS PHE PRO PRO ILE GLU ALA LEU          
SEQRES  60 B  963  PHE LEU LEU VAL THR SER VAL THR LEU THR LEU PHE GLN          
SEQRES  61 B  963  GLN GLY PRO ARG ASP HIS PRO ASP ILE VAL ASP SER PHE          
SEQRES  62 B  963  MET GLN LEU LEU ALA GLN ALA LEU LYS ARG LYS PRO ASP          
SEQRES  63 B  963  LEU PHE LEU CYS GLU ARG LEU ASP VAL LYS ALA VAL PHE          
SEQRES  64 B  963  GLN CYS ALA VAL LEU ALA LEU LYS PHE PRO GLU ALA PRO          
SEQRES  65 B  963  THR VAL LYS ALA SER CYS GLY PHE PHE THR GLU LEU LEU          
SEQRES  66 B  963  PRO ARG CYS GLY GLU VAL GLU SER VAL GLY LYS VAL VAL          
SEQRES  67 B  963  GLN GLU ASP GLY ARG MET LEU LEU ILE ALA VAL LEU GLU          
SEQRES  68 B  963  ALA ILE GLY GLY GLN ALA SER ARG SER LEU MET ASP CYS          
SEQRES  69 B  963  PHE ALA ASP ILE LEU PHE ALA LEU ASN LYS HIS CYS PHE          
SEQRES  70 B  963  SER LEU LEU SER MET TRP ILE LYS GLU ALA LEU GLN PRO          
SEQRES  71 B  963  PRO GLY PHE PRO SER ALA ARG LEU SER PRO GLU GLN LYS          
SEQRES  72 B  963  ASP THR PHE SER GLN GLN ILE LEU ARG GLU ARG VAL ASN          
SEQRES  73 B  963  LYS ARG ARG VAL LYS GLU MET VAL LYS GLU PHE THR LEU          
SEQRES  74 B  963  LEU CYS ARG GLY LEU HIS GLY THR ASP TYR THR ALA ASP          
SEQRES  75 B  963  TYR                                                          
FORMUL   3  HOH   *36(H2 O)                                                     
HELIX    1   1 MET A    1  ASP A   19  1                                  19    
HELIX    2   2 LEU A   94  GLU A   98  5                                   5    
HELIX    3   3 THR A  108  GLU A  122  1                                  15    
HELIX    4   4 GLN A  130  ASN A  140  1                                  11    
HELIX    5   5 ASN A  140  PHE A  155  1                                  16    
HELIX    6   6 THR B   22  ASP B   36  1                                  15    
HELIX    7   7 ASN B   38  SER B   55  1                                  18    
HELIX    8   8 GLN B   57  LEU B   65  1                                   9    
HELIX    9   9 VAL B   71  TYR B   89  1                                  19    
HELIX   10  10 TRP B   90  ILE B   93  5                                   4    
HELIX   11  11 PRO B   94  ASP B   96  5                                   3    
HELIX   12  12 GLN B   97  PHE B  112  1                                  16    
HELIX   13  13 SER B  116  MET B  135  1                                  20    
HELIX   14  14 CYS B  141  ALA B  152  1                                  12    
HELIX   15  15 ASP B  158  SER B  180  1                                  23    
HELIX   16  16 PRO B  183  GLN B  211  1                                  29    
HELIX   17  17 PRO B  215  GLN B  231  1                                  17    
HELIX   18  18 PRO B  235  LEU B  250  1                                  16    
HELIX   19  19 LEU B  255  SER B  268  1                                  14    
HELIX   20  20 ASP B  271  ARG B  274  5                                   4    
HELIX   21  21 TYR B  275  GLY B  288  1                                  14    
HELIX   22  22 LEU B  289  GLY B  300  1                                  12    
HELIX   23  23 ASP B  301  HIS B  319  1                                  19    
HELIX   24  24 HIS B  319  GLN B  326  1                                   8    
HELIX   25  25 HIS B  329  GLY B  345  1                                  17    
HELIX   26  26 THR B  356  LEU B  359  5                                   4    
HELIX   27  27 THR B  360  PHE B  374  1                                  15    
HELIX   28  28 ALA B  376  ALA B  401  1                                  26    
HELIX   29  29 SER B  405  PHE B  411  1                                   7    
HELIX   30  30 SER B  413  GLY B  439  1                                  27    
HELIX   31  31 GLY B  439  SER B  456  1                                  18    
HELIX   32  32 SER B  462  GLU B  478  1                                  17    
HELIX   33  33 ASP B  486  ILE B  495  1                                  10    
HELIX   34  34 PRO B  496  ILE B  498  5                                   3    
HELIX   35  35 ASN B  502  LEU B  516  1                                  15    
HELIX   36  36 LEU B  516  HIS B  523  1                                   8    
HELIX   37  37 MET B  526  LEU B  538  1                                  13    
HELIX   38  38 ASN B  540  GLU B  542  5                                   3    
HELIX   39  39 LEU B  543  CYS B  558  1                                  16    
HELIX   40  40 LYS B  559  LEU B  562  5                                   4    
HELIX   41  41 TYR B  565  LYS B  579  1                                  15    
HELIX   42  42 LYS B  583  ALA B  600  1                                  18    
HELIX   43  43 GLN B  602  GLU B  626  1                                  25    
HELIX   44  44 ASN B  630  LEU B  651  1                                  22    
HELIX   45  45 ASN B  675  LEU B  696  1                                  22    
HELIX   46  46 ASP B  698  LEU B  717  1                                  20    
HELIX   47  47 ASP B  718  PRO B  722  5                                   5    
HELIX   48  48 MET B  723  ILE B  738  1                                  16    
HELIX   49  49 GLN B  740  ALA B  755  1                                  16    
HELIX   50  50 PHE B  761  GLY B  782  1                                  22    
HELIX   51  51 HIS B  786  LYS B  804  1                                  19    
HELIX   52  52 PRO B  805  CYS B  810  5                                   6    
HELIX   53  53 ASP B  814  LEU B  826  1                                  13    
HELIX   54  54 GLU B  830  LEU B  845  1                                  16    
HELIX   55  55 VAL B  851  GLY B  875  1                                  25    
HELIX   56  56 SER B  878  SER B  880  5                                   3    
HELIX   57  57 LEU B  881  CYS B  896  1                                  16    
HELIX   58  58 CYS B  896  GLN B  909  1                                  14    
HELIX   59  59 SER B  919  LEU B  931  1                                  13    
HELIX   60  60 ASN B  936  GLY B  953  1                                  18    
SHEET    1  AA 4 VAL A  25  LYS A  30  0                                        
SHEET    2  AA 4 MET A  36  PRO A  46 -1  O  ASN A  37   N  THR A  29           
SHEET    3  AA 4 LEU A  57  LEU A  63 -1  O  PHE A  58   N  ILE A  45           
SHEET    4  AA 4 LYS A  74  PHE A  77 -1  O  LYS A  74   N  LEU A  63           
CISPEP   1 TYR A   68    PRO A   69          0         1.29                     
CISPEP   2 GLU A   78    PRO A   79          0         2.07                     
CISPEP   3 MET B  135    PRO B  136          0         0.88                     
CISPEP   4 TYR B  350    PRO B  351          0        -0.29                     
CISPEP   5 PHE B  913    PRO B  914          0         1.62                     
CRYST1   68.700  126.800  184.000  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      0.014556  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007886  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005435        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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