GenomeNet

Database: PDB
Entry: 5FQ2
LinkDB: 5FQ2
Original site: 5FQ2 
HEADER    LIGASE                                  04-DEC-15   5FQ2              
TITLE     CRYSTAL STRUCTURE OF HUMAN SUMO E1 UFD DOMAIN IN COMPLEX              
TITLE    2 WITH UBC9 IN A P422 SPACE GROUP.                                     
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, SUMO E2-CONJUGATING ENZYME;       
COMPND   7 EC: 6.3.2.-;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: LYSINE METHYLATION AT LYS110;                         
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: SUMO-ACTIVATING ENZYME SUBUNIT 2;                          
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: UBIQUITIN FOLD DOMAIN, UNP RESIDUES 446-547;               
COMPND  14 SYNONYM: ANTHRACYCLINE-ASSOCIATED RESISTANCE ARX, UBIQUITIN-LIKE     
COMPND  15  1-ACTIVATING ENZYME E1B, UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME  
COMPND  16  2, SUMO E1 ACTIVATING ENZYME;                                       
COMPND  17 EC: 6.3.2.-;                                                         
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 OTHER_DETAILS: LYSINE METHYLATION AT LYS505                          
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: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET28;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: PET28                                      
KEYWDS    LIGASE, ACTIVATING ENZYME, CONJUGATING ENZYME, SUMO                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.LIU,L.CASTANO,M.LOIS,D.REVERTER                                     
REVDAT   1   16-NOV-16 5FQ2    0                                                
JRNL        AUTH   B.LIU,L.CASTANO,M.LOIS,D.REVERTER                            
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN SUMO E1 UFD DOMAIN IN COMPLEX     
JRNL        TITL 2 WITH UBC9.                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-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) : 2.201                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.439                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.33                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.75                          
REMARK   3   NUMBER OF REFLECTIONS             : 29254                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2303                          
REMARK   3   R VALUE            (WORKING SET) : 0.2293                          
REMARK   3   FREE R VALUE                     : 0.2489                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1488                            
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 46.4493 -  4.8931    1.00     2739   130  0.2228 0.2317        
REMARK   3     2  4.8931 -  3.8844    1.00     2592   126  0.1981 0.2188        
REMARK   3     3  3.8844 -  3.3936    1.00     2529   144  0.2244 0.2485        
REMARK   3     4  3.3936 -  3.0834    1.00     2530   135  0.2524 0.2841        
REMARK   3     5  3.0834 -  2.8624    1.00     2508   141  0.2558 0.2553        
REMARK   3     6  2.8624 -  2.6937    1.00     2502   132  0.2600 0.2630        
REMARK   3     7  2.6937 -  2.5588    1.00     2506   129  0.2604 0.2986        
REMARK   3     8  2.5588 -  2.4474    1.00     2494   139  0.2431 0.2482        
REMARK   3     9  2.4474 -  2.3532    1.00     2479   140  0.2554 0.3334        
REMARK   3    10  2.3532 -  2.2720    1.00     2479   127  0.2583 0.2703        
REMARK   3    11  2.2720 -  2.2009    0.97     2408   145  0.2633 0.3149        
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)     : 0.22             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.82            
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      :  0.008           2108                                  
REMARK   3   ANGLE     :  1.114           2853                                  
REMARK   3   CHIRALITY :  0.048            312                                  
REMARK   3   PLANARITY :  0.005            373                                  
REMARK   3   DIHEDRAL  : 14.191            808                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6666 124.7904  13.2245              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4080 T22:   0.4243                                     
REMARK   3      T33:   0.4343 T12:  -0.0283                                     
REMARK   3      T13:   0.0617 T23:  -0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6376 L22:   5.0730                                     
REMARK   3      L33:   0.3453 L12:  -1.8015                                     
REMARK   3      L13:   0.1082 L23:   0.1130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0723 S12:  -0.0809 S13:  -0.0548                       
REMARK   3      S21:   0.0106 S22:   0.0570 S23:   0.1050                       
REMARK   3      S31:  -0.0032 S32:   0.0477 S33:   0.0253                       
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 5FQ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-DEC-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-65708.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29309                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.44                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 10.9                               
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.40                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11                                 
REMARK 200  R MERGE FOR SHELL          (I) : 0.60                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.30                               
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: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       33.28900            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       64.80700            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       64.80700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       49.93350            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       64.80700            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       64.80700            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       16.64450            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       64.80700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       64.80700            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       49.93350            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       64.80700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       64.80700            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       16.64450            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       33.28900            
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.4 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    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY B   443                                                      
REMARK 465     SER B   444                                                      
REMARK 465     HIS B   445                                                      
REMARK 465     SER B   446                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN B   501     O    HOH A  2008              2.14            
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    ASP A  19      107.34   -166.68                                   
REMARK 500    HIS A  83      136.75   -171.50                                   
REMARK 500    LYS A 101     -107.57   -120.18                                   
REMARK 500    ILE B 468      -60.91    -91.70                                   
REMARK 500    TYR B 526      104.98   -165.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 LYSINE METHYLATION AT POSITION LYS110                                
REMARK 999 LYSINE METHYLATION AT POSITION LYS505                                
DBREF  5FQ2 A    1   158  UNP    P63279   UBC9_HUMAN       1    158             
DBREF  5FQ2 B  446   547  UNP    Q9UBT2   SAE2_HUMAN     446    547             
SEQADV 5FQ2 GLY A   -2  UNP  P63279              EXPRESSION TAG                 
SEQADV 5FQ2 SER A   -1  UNP  P63279              EXPRESSION TAG                 
SEQADV 5FQ2 HIS A    0  UNP  P63279              EXPRESSION TAG                 
SEQADV 5FQ2 GLY B  443  UNP  Q9UBT2              EXPRESSION TAG                 
SEQADV 5FQ2 SER B  444  UNP  Q9UBT2              EXPRESSION TAG                 
SEQADV 5FQ2 HIS B  445  UNP  Q9UBT2              EXPRESSION TAG                 
SEQRES   1 A  161  GLY SER HIS MET SER GLY ILE ALA LEU SER ARG LEU ALA          
SEQRES   2 A  161  GLN GLU ARG LYS ALA TRP ARG LYS ASP HIS PRO PHE GLY          
SEQRES   3 A  161  PHE VAL ALA VAL PRO THR LYS ASN PRO ASP GLY THR MET          
SEQRES   4 A  161  ASN LEU MET ASN TRP GLU CYS ALA ILE PRO GLY LYS LYS          
SEQRES   5 A  161  GLY THR PRO TRP GLU GLY GLY LEU PHE LYS LEU ARG MET          
SEQRES   6 A  161  LEU PHE LYS ASP ASP TYR PRO SER SER PRO PRO LYS CYS          
SEQRES   7 A  161  LYS PHE GLU PRO PRO LEU PHE HIS PRO ASN VAL TYR PRO          
SEQRES   8 A  161  SER GLY THR VAL CYS LEU SER ILE LEU GLU GLU ASP LYS          
SEQRES   9 A  161  ASP TRP ARG PRO ALA ILE THR ILE LDH GLN ILE LEU LEU          
SEQRES  10 A  161  GLY ILE GLN GLU LEU LEU ASN GLU PRO ASN ILE GLN ASP          
SEQRES  11 A  161  PRO ALA GLN ALA GLU ALA TYR THR ILE TYR CYS GLN ASN          
SEQRES  12 A  161  ARG VAL GLU TYR GLU LYS ARG VAL ARG ALA GLN ALA LYS          
SEQRES  13 A  161  LYS PHE ALA PRO SER                                          
SEQRES   1 B  105  GLY SER HIS SER LYS PRO GLU VAL THR VAL ARG LEU ASN          
SEQRES   2 B  105  VAL HIS LYS VAL THR VAL LEU THR LEU GLN ASP LYS ILE          
SEQRES   3 B  105  VAL LYS GLU LYS PHE ALA MET VAL ALA PRO ASP VAL GLN          
SEQRES   4 B  105  ILE GLU ASP GLY LYS GLY THR ILE LEU ILE SER SER GLU          
SEQRES   5 B  105  GLU GLY GLU THR GLU ALA ASN ASN HIS LYS MLZ LEU SER          
SEQRES   6 B  105  GLU PHE GLY ILE ARG ASN GLY SER ARG LEU GLN ALA ASP          
SEQRES   7 B  105  ASP PHE LEU GLN ASP TYR THR LEU LEU ILE ASN ILE LEU          
SEQRES   8 B  105  HIS SER GLU ASP LEU GLY LYS ASP VAL GLU PHE GLU VAL          
SEQRES   9 B  105  VAL                                                          
MODRES 5FQ2 LDH A  110  LYS  N~6~-ETHYL-L-LYSINE                                
MODRES 5FQ2 MLZ B  505  LYS  N-METHYL-LYSINE                                    
HET    LDH  A 110      11                                                       
HET    MLZ  B 505      10                                                       
HETNAM     LDH N~6~-ETHYL-L-LYSINE                                              
HETNAM     MLZ N-METHYL-LYSINE                                                  
FORMUL   1  LDH    C8 H18 N2 O2                                                 
FORMUL   2  MLZ    C7 H16 N2 O2                                                 
FORMUL   3  HOH   *38(H2 O)                                                     
HELIX    1   1 SER A    2  ASP A   19  1                                  18    
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  460  LYS B  467  1                                   8    
HELIX    7   7 ILE B  468  PHE B  473  1                                   6    
HELIX    8   8 THR B  498  ASN B  502  5                                   5    
HELIX    9   9 LEU B  506  GLY B  510  5                                   5    
SHEET    1  AA 2 VAL A  25  LYS A  30  0                                        
SHEET    2  AA 2 MET A  36  PRO A  46 -1  N  ASN A  37   O  THR A  29           
SHEET    1  AB 9 LYS A  74  PHE A  77  0                                        
SHEET    2  AB 9 LEU A  57  LEU A  63 -1  O  ARG A  61   N  LYS A  76           
SHEET    3  AB 9 MET A  36  PRO A  46  1  O  TRP A  41   N  MET A  62           
SHEET    4  AB 9 THR B 488  ILE B 491 -1  O  ILE B 489   N  MET A  36           
SHEET    5  AB 9 PRO B 478  ILE B 482 -1  O  VAL B 480   N  LEU B 490           
SHEET    6  AB 9 ARG B 516  ASP B 521 -1  O  GLN B 518   N  GLN B 481           
SHEET    7  AB 9 THR B 527  HIS B 534 -1  O  LEU B 528   N  ALA B 519           
SHEET    8  AB 9 GLU B 449  LEU B 454  1  O  VAL B 450   N  ASN B 531           
SHEET    9  AB 9 PHE B 544  VAL B 546 -1  O  GLU B 545   N  ARG B 453           
SHEET    1  AC 4 LYS A  74  PHE A  77  0                                        
SHEET    2  AC 4 LEU A  57  LEU A  63 -1  O  ARG A  61   N  LYS A  76           
SHEET    3  AC 4 MET A  36  PRO A  46  1  O  TRP A  41   N  MET A  62           
SHEET    4  AC 4 VAL A  25  LYS A  30 -1  O  VAL A  25   N  ALA A  44           
LINK         C   ILE A 109                 N   LDH A 110     1555   1555  1.32  
LINK         C   LDH A 110                 N   GLN A 111     1555   1555  1.33  
LINK         C   LYS B 504                 N   MLZ B 505     1555   1555  1.34  
LINK         C   MLZ B 505                 N   LEU B 506     1555   1555  1.33  
CISPEP   1 TYR A   68    PRO A   69          0         7.21                     
CISPEP   2 GLU A   78    PRO A   79          0         1.10                     
CISPEP   3 GLU B  495    GLY B  496          0        -6.08                     
CRYST1  129.614  129.614   66.578  90.00  90.00  90.00 P 43 21 2     8          
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      0.007715  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007715  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015020        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system