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Database: PDB
Entry: 4W5V
LinkDB: 4W5V
Original site: 4W5V 
HEADER    LIGASE                                  19-AUG-14   4W5V              
TITLE     CRYSTAL STRUCTURE OF HUMAN SUMO E2-CONJUGATING ENZYME (UBC9) IN       
TITLE    2 COMPLEX WITH E1-ACTIVATING ENZYME (UBA2) UBIQUITIN FOLD DOMAIN (UFD) 
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,UBIQUITIN   
COMPND   5 CARRIER PROTEIN I,UBIQUITIN-CONJUGATING ENZYME E2 I,UBIQUITIN-PROTEIN
COMPND   6 LIGASE I,P18;                                                        
COMPND   7 EC: 6.3.2.-;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: SUMO-ACTIVATING ENZYME SUBUNIT 2;                          
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 445-561;                                      
COMPND  13 SYNONYM: ANTHRACYCLINE-ASSOCIATED RESISTANCE ARX,UBIQUITIN-LIKE 1-   
COMPND  14 ACTIVATING ENZYME E1B,UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 2;   
COMPND  15 EC: 6.3.2.-;                                                         
COMPND  16 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: UBE2I, UBC9, UBCE9;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: UBA2, SAE2, UBLE1B, HRIHFB2115;                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SUMO, E2-ACTIVATING ENZYME, UBC9, E1-CONJUGATING ENZYME, UBA2,        
KEYWDS   2 UBIQUITIN FOLD DOMAIN, UFD, UBIQUITIN, LIGASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.E.BOUCHER,K.H.REITER,M.J.MATUNIS,J.BOSCH                            
REVDAT   3   25-DEC-19 4W5V    1       REMARK                                   
REVDAT   2   06-SEP-17 4W5V    1       REMARK                                   
REVDAT   1   09-SEP-15 4W5V    0                                                
JRNL        AUTH   K.H.REITER,L.E.BOUCHER,J.BOSCH,M.J.MATUNIS                   
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN SUMO COMPLEX                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 10631                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 553                             
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 44.7118 -  3.9678    0.93     2663   149  0.1792 0.2512        
REMARK   3     2  3.9678 -  3.1497    0.92     2541   142  0.2384 0.2890        
REMARK   3     3  3.1497 -  2.7516    0.92     2512   135  0.3213 0.3734        
REMARK   3     4  2.7516 -  2.5000    0.87     2362   127  0.4136 0.4135        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.540            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.180           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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      :  0.002           2148                                  
REMARK   3   ANGLE     :  0.500           2903                                  
REMARK   3   CHIRALITY :  0.022            317                                  
REMARK   3   PLANARITY :  0.003            379                                  
REMARK   3   DIHEDRAL  :  8.261            821                                  
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 4W5V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203215.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JAN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97945                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, XSCALE                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10654                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3ONG, 1U9B                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS, PH 8.0, 20% PEG MME 550,    
REMARK 280  200 MM POTASSIUM FORMATE, 20% GLYCEROL; SEEDED, VAPOR DIFFUSION,    
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       80.63650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       17.63600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       80.63650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       17.63600            
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: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     GLY B   440                                                      
REMARK 465     PRO B   441                                                      
REMARK 465     LEU B   442                                                      
REMARK 465     GLY B   443                                                      
REMARK 465     ALA B   550                                                      
REMARK 465     PRO B   551                                                      
REMARK 465     GLU B   552                                                      
REMARK 465     LYS B   553                                                      
REMARK 465     VAL B   554                                                      
REMARK 465     GLY B   555                                                      
REMARK 465     PRO B   556                                                      
REMARK 465     LYS B   557                                                      
REMARK 465     GLN B   558                                                      
REMARK 465     ALA B   559                                                      
REMARK 465     GLU B   560                                                      
REMARK 465     ASP B   561                                                      
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 139      -93.56   -120.37                                   
REMARK 500    PHE A 155       38.46    -96.83                                   
REMARK 500    ILE B 468      -67.83    -92.84                                   
REMARK 500    GLU B 483       92.01    -69.47                                   
REMARK 500    ARG B 512     -167.77   -126.95                                   
REMARK 500    ASP B 525       75.06    -69.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 721        DISTANCE =  7.17 ANGSTROMS                       
REMARK 525    HOH B 730        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH B 733        DISTANCE =  7.52 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 602   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 499   O                                                      
REMARK 620 2 HOH B 729   O   123.9                                              
REMARK 620 3 HOH B 731   O   134.4  84.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 602                   
DBREF  4W5V A    1   158  UNP    P63279   UBC9_HUMAN       1    158             
DBREF  4W5V B  445   561  UNP    Q9UBT2   SAE2_HUMAN     445    561             
SEQADV 4W5V GLY A   -4  UNP  P63279              EXPRESSION TAG                 
SEQADV 4W5V PRO A   -3  UNP  P63279              EXPRESSION TAG                 
SEQADV 4W5V LEU A   -2  UNP  P63279              EXPRESSION TAG                 
SEQADV 4W5V GLY A   -1  UNP  P63279              EXPRESSION TAG                 
SEQADV 4W5V SER A    0  UNP  P63279              EXPRESSION TAG                 
SEQADV 4W5V GLY B  440  UNP  Q9UBT2              EXPRESSION TAG                 
SEQADV 4W5V PRO B  441  UNP  Q9UBT2              EXPRESSION TAG                 
SEQADV 4W5V LEU B  442  UNP  Q9UBT2              EXPRESSION TAG                 
SEQADV 4W5V GLY B  443  UNP  Q9UBT2              EXPRESSION TAG                 
SEQADV 4W5V SER B  444  UNP  Q9UBT2              EXPRESSION TAG                 
SEQRES   1 A  163  GLY PRO LEU GLY SER MET SER GLY ILE ALA LEU SER ARG          
SEQRES   2 A  163  LEU ALA GLN GLU ARG LYS ALA TRP ARG LYS ASP HIS PRO          
SEQRES   3 A  163  PHE GLY PHE VAL ALA VAL PRO THR LYS ASN PRO ASP GLY          
SEQRES   4 A  163  THR MET ASN LEU MET ASN TRP GLU CYS ALA ILE PRO GLY          
SEQRES   5 A  163  LYS LYS GLY THR PRO TRP GLU GLY GLY LEU PHE LYS LEU          
SEQRES   6 A  163  ARG MET LEU PHE LYS ASP ASP TYR PRO SER SER PRO PRO          
SEQRES   7 A  163  LYS CYS LYS PHE GLU PRO PRO LEU PHE HIS PRO ASN VAL          
SEQRES   8 A  163  TYR PRO SER GLY THR VAL CYS LEU SER ILE LEU GLU GLU          
SEQRES   9 A  163  ASP LYS ASP TRP ARG PRO ALA ILE THR ILE LYS GLN ILE          
SEQRES  10 A  163  LEU LEU GLY ILE GLN GLU LEU LEU ASN GLU PRO ASN ILE          
SEQRES  11 A  163  GLN ASP PRO ALA GLN ALA GLU ALA TYR THR ILE TYR CYS          
SEQRES  12 A  163  GLN ASN ARG VAL GLU TYR GLU LYS ARG VAL ARG ALA GLN          
SEQRES  13 A  163  ALA LYS LYS PHE ALA PRO SER                                  
SEQRES   1 B  122  GLY PRO LEU GLY SER ALA SER LYS PRO GLU VAL THR VAL          
SEQRES   2 B  122  ARG LEU ASN VAL HIS LYS VAL THR VAL LEU THR LEU GLN          
SEQRES   3 B  122  ASP LYS ILE VAL LYS GLU LYS PHE ALA MET VAL ALA PRO          
SEQRES   4 B  122  ASP VAL GLN ILE GLU ASP GLY LYS GLY THR ILE LEU ILE          
SEQRES   5 B  122  SER SER GLU GLU GLY GLU THR GLU ALA ASN ASN HIS LYS          
SEQRES   6 B  122  LYS LEU SER GLU PHE GLY ILE ARG ASN GLY SER ARG LEU          
SEQRES   7 B  122  GLN ALA ASP ASP PHE LEU GLN ASP TYR THR LEU LEU ILE          
SEQRES   8 B  122  ASN ILE LEU HIS SER GLU ASP LEU GLY LYS ASP VAL GLU          
SEQRES   9 B  122  PHE GLU VAL VAL GLY ASP ALA PRO GLU LYS VAL GLY PRO          
SEQRES  10 B  122  LYS GLN ALA GLU ASP                                          
HET    FMT  A 201       3                                                       
HET    GOL  B 601       6                                                       
HET      K  B 602       1                                                       
HETNAM     FMT FORMIC ACID                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM       K POTASSIUM ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  FMT    C H2 O2                                                      
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5    K    K 1+                                                         
FORMUL   6  HOH   *74(H2 O)                                                     
HELIX    1 AA1 MET A    1  ASP A   19  1                                  19    
HELIX    2 AA2 LEU A   94  GLU A   98  5                                   5    
HELIX    3 AA3 THR A  108  GLU A  122  1                                  15    
HELIX    4 AA4 GLN A  130  GLN A  139  1                                  10    
HELIX    5 AA5 ASN A  140  PHE A  155  1                                  16    
HELIX    6 AA6 THR B  460  ASP B  466  1                                   7    
HELIX    7 AA7 LYS B  505  GLY B  510  5                                   6    
SHEET    1 AA1 4 VAL A  25  LYS A  30  0                                        
SHEET    2 AA1 4 MET A  36  PRO A  46 -1  O  GLU A  42   N  VAL A  27           
SHEET    3 AA1 4 LEU A  57  LEU A  63 -1  O  PHE A  58   N  ILE A  45           
SHEET    4 AA1 4 LYS A  74  PHE A  77 -1  O  LYS A  76   N  ARG A  61           
SHEET    1 AA2 8 VAL A  25  LYS A  30  0                                        
SHEET    2 AA2 8 MET A  36  PRO A  46 -1  O  GLU A  42   N  VAL A  27           
SHEET    3 AA2 8 THR B 488  ILE B 491 -1  O  ILE B 489   N  MET A  36           
SHEET    4 AA2 8 PRO B 478  ILE B 482 -1  N  ILE B 482   O  THR B 488           
SHEET    5 AA2 8 ARG B 516  ASP B 521 -1  O  GLN B 518   N  GLN B 481           
SHEET    6 AA2 8 THR B 527  HIS B 534 -1  O  ILE B 530   N  LEU B 517           
SHEET    7 AA2 8 GLU B 449  LEU B 454  1  N  VAL B 452   O  ASN B 531           
SHEET    8 AA2 8 PHE B 544  VAL B 547 -1  O  VAL B 547   N  THR B 451           
LINK         O   GLU B 499                 K     K B 602     1555   1555  3.33  
LINK         K     K B 602                 O   HOH B 729     1555   1555  3.16  
LINK         K     K B 602                 O   HOH B 731     1555   1555  2.87  
CISPEP   1 TYR A   68    PRO A   69          0         2.09                     
CISPEP   2 GLU A   78    PRO A   79          0         0.23                     
CISPEP   3 SER B  444    ALA B  445          0        -1.00                     
CISPEP   4 LYS B  540    ASP B  541          0         3.41                     
CISPEP   5 VAL B  547    GLY B  548          0        -4.49                     
CISPEP   6 GLY B  548    ASP B  549          0        -1.02                     
SITE     1 AC1  2 TYR A 134  ALA B 445                                          
SITE     1 AC2  2 PHE B 473  TYR B 526                                          
SITE     1 AC3  2 GLU B 499  HOH B 731                                          
CRYST1  161.273   35.272   58.672  90.00  96.69  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006201  0.000000  0.000728        0.00000                         
SCALE2      0.000000  0.028351  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017161        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system