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Database: PDB
Entry: 1QWI
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Original site: 1QWI 
HEADER    HYDROPEROXIDE REDUCTASE                 02-SEP-03   1QWI              
TITLE     CRYSTAL STRUCTURE OF E. COLI OSMC                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OSMOTICALLY INDUCIBLE PROTEIN;                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: OSMC;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: 0157:H7 EDL399;                                              
SOURCE   5 GENE: OSMC;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROPEROXIDE RESISTANCE, HYDROPEROXIDE REDUCTASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LESNIAK,W.A.BARTON,D.B.NIKOLOV                                      
REVDAT   2   24-FEB-09 1QWI    1       VERSN                                    
REVDAT   1   16-DEC-03 1QWI    0                                                
JRNL        AUTH   J.LESNIAK,W.A.BARTON,D.B.NIKOLOV                             
JRNL        TITL   STRUCTURAL AND FUNCTIONAL FEATURES OF THE                    
JRNL        TITL 2 ESCHERICHIA COLI HYDROPEROXIDE RESISTANCE PROTEIN            
JRNL        TITL 3 OSMC                                                         
JRNL        REF    PROTEIN SCI.                  V.  12  2838 2003              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   14627744                                                     
JRNL        DOI    10.1110/PS.03375603                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 98304                          
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) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4810                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
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) : NULL                         
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            : 4152                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 504                                     
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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 : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: FREIDEL PAIRS WERE USED IN                
REMARK   3  REFINEMENT.                                                         
REMARK   4                                                                      
REMARK   4 1QWI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020152.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795, 0.9793, 0.9770             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48947                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : 0.04500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.8                               
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: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000 MME, 0.2M AMMONIUM              
REMARK 280  SULFATE, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  297K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       32.11450            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 6000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 6000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     MSE A     1                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     MSE D     1                                                      
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     LYS A  16    CB   CG   CD   CE   NZ                              
REMARK 470     ARG A  17    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     THR A  74    CB   OG1  CG2                                       
REMARK 470     LYS B  16    CB   CG   CD   CE   NZ                              
REMARK 470     ARG B  17    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     THR B  74    CB   OG1  CG2                                       
REMARK 470     LYS C  16    CB   CG   CD   CE   NZ                              
REMARK 470     ARG C  17    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     THR C  74    CB   OG1  CG2                                       
REMARK 470     LYS D  16    CB   CG   CD   CE   NZ                              
REMARK 470     ARG D  17    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     THR D  74    CB   OG1  CG2                                       
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    SER A  13     -169.72     67.91                                   
REMARK 500    ASP A  14     -166.77    -73.25                                   
REMARK 500    SER B  13     -166.06     76.43                                   
REMARK 500    ASP B  14     -169.11    -79.41                                   
REMARK 500    SER C  13     -169.24     71.51                                   
REMARK 500    SER D  13     -167.37     69.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1N2F   RELATED DB: PDB                                   
REMARK 900 OHR                                                                  
DBREF  1QWI A    1   143  UNP    P0C0L2   OSMC_ECOLI       1    143             
DBREF  1QWI B    1   143  UNP    P0C0L2   OSMC_ECOLI       1    143             
DBREF  1QWI C    1   143  UNP    P0C0L2   OSMC_ECOLI       1    143             
DBREF  1QWI D    1   143  UNP    P0C0L2   OSMC_ECOLI       1    143             
SEQADV 1QWI MSE A    1  UNP  P0C0L2    MET     1 MODIFIED RESIDUE               
SEQADV 1QWI MSE A   62  UNP  P0C0L2    MET    62 MODIFIED RESIDUE               
SEQADV 1QWI MSE A   67  UNP  P0C0L2    MET    67 MODIFIED RESIDUE               
SEQADV 1QWI MSE B    1  UNP  P0C0L2    MET     1 MODIFIED RESIDUE               
SEQADV 1QWI MSE B   62  UNP  P0C0L2    MET    62 MODIFIED RESIDUE               
SEQADV 1QWI MSE B   67  UNP  P0C0L2    MET    67 MODIFIED RESIDUE               
SEQADV 1QWI MSE C    1  UNP  P0C0L2    MET     1 MODIFIED RESIDUE               
SEQADV 1QWI MSE C   62  UNP  P0C0L2    MET    62 MODIFIED RESIDUE               
SEQADV 1QWI MSE C   67  UNP  P0C0L2    MET    67 MODIFIED RESIDUE               
SEQADV 1QWI MSE D    1  UNP  P0C0L2    MET     1 MODIFIED RESIDUE               
SEQADV 1QWI MSE D   62  UNP  P0C0L2    MET    62 MODIFIED RESIDUE               
SEQADV 1QWI MSE D   67  UNP  P0C0L2    MET    67 MODIFIED RESIDUE               
SEQRES   1 A  143  MSE THR ILE HIS LYS LYS GLY GLN ALA HIS TRP GLU SER          
SEQRES   2 A  143  ASP ILE LYS ARG GLY LYS GLY THR VAL SER THR GLU SER          
SEQRES   3 A  143  GLY VAL LEU ASN GLN GLN PRO TYR GLY PHE ASN THR ARG          
SEQRES   4 A  143  PHE GLU GLY GLU LYS GLY THR ASN PRO GLU GLU LEU ILE          
SEQRES   5 A  143  GLY ALA ALA HIS ALA ALA CYS PHE SER MSE ALA LEU SER          
SEQRES   6 A  143  LEU MSE LEU GLY GLU ALA GLY PHE THR PRO THR SER ILE          
SEQRES   7 A  143  ASP THR THR ALA ASP VAL SER LEU ASP LYS VAL ASP ALA          
SEQRES   8 A  143  GLY PHE ALA ILE THR LYS ILE ALA LEU LYS SER GLU VAL          
SEQRES   9 A  143  ALA VAL PRO GLY ILE ASP ALA SER THR PHE ASP GLY ILE          
SEQRES  10 A  143  ILE GLN LYS ALA LYS ALA GLY CYS PRO VAL SER GLN VAL          
SEQRES  11 A  143  LEU LYS ALA GLU ILE THR LEU ASP TYR GLN LEU LYS SER          
SEQRES   1 B  143  MSE THR ILE HIS LYS LYS GLY GLN ALA HIS TRP GLU SER          
SEQRES   2 B  143  ASP ILE LYS ARG GLY LYS GLY THR VAL SER THR GLU SER          
SEQRES   3 B  143  GLY VAL LEU ASN GLN GLN PRO TYR GLY PHE ASN THR ARG          
SEQRES   4 B  143  PHE GLU GLY GLU LYS GLY THR ASN PRO GLU GLU LEU ILE          
SEQRES   5 B  143  GLY ALA ALA HIS ALA ALA CYS PHE SER MSE ALA LEU SER          
SEQRES   6 B  143  LEU MSE LEU GLY GLU ALA GLY PHE THR PRO THR SER ILE          
SEQRES   7 B  143  ASP THR THR ALA ASP VAL SER LEU ASP LYS VAL ASP ALA          
SEQRES   8 B  143  GLY PHE ALA ILE THR LYS ILE ALA LEU LYS SER GLU VAL          
SEQRES   9 B  143  ALA VAL PRO GLY ILE ASP ALA SER THR PHE ASP GLY ILE          
SEQRES  10 B  143  ILE GLN LYS ALA LYS ALA GLY CYS PRO VAL SER GLN VAL          
SEQRES  11 B  143  LEU LYS ALA GLU ILE THR LEU ASP TYR GLN LEU LYS SER          
SEQRES   1 C  143  MSE THR ILE HIS LYS LYS GLY GLN ALA HIS TRP GLU SER          
SEQRES   2 C  143  ASP ILE LYS ARG GLY LYS GLY THR VAL SER THR GLU SER          
SEQRES   3 C  143  GLY VAL LEU ASN GLN GLN PRO TYR GLY PHE ASN THR ARG          
SEQRES   4 C  143  PHE GLU GLY GLU LYS GLY THR ASN PRO GLU GLU LEU ILE          
SEQRES   5 C  143  GLY ALA ALA HIS ALA ALA CYS PHE SER MSE ALA LEU SER          
SEQRES   6 C  143  LEU MSE LEU GLY GLU ALA GLY PHE THR PRO THR SER ILE          
SEQRES   7 C  143  ASP THR THR ALA ASP VAL SER LEU ASP LYS VAL ASP ALA          
SEQRES   8 C  143  GLY PHE ALA ILE THR LYS ILE ALA LEU LYS SER GLU VAL          
SEQRES   9 C  143  ALA VAL PRO GLY ILE ASP ALA SER THR PHE ASP GLY ILE          
SEQRES  10 C  143  ILE GLN LYS ALA LYS ALA GLY CYS PRO VAL SER GLN VAL          
SEQRES  11 C  143  LEU LYS ALA GLU ILE THR LEU ASP TYR GLN LEU LYS SER          
SEQRES   1 D  143  MSE THR ILE HIS LYS LYS GLY GLN ALA HIS TRP GLU SER          
SEQRES   2 D  143  ASP ILE LYS ARG GLY LYS GLY THR VAL SER THR GLU SER          
SEQRES   3 D  143  GLY VAL LEU ASN GLN GLN PRO TYR GLY PHE ASN THR ARG          
SEQRES   4 D  143  PHE GLU GLY GLU LYS GLY THR ASN PRO GLU GLU LEU ILE          
SEQRES   5 D  143  GLY ALA ALA HIS ALA ALA CYS PHE SER MSE ALA LEU SER          
SEQRES   6 D  143  LEU MSE LEU GLY GLU ALA GLY PHE THR PRO THR SER ILE          
SEQRES   7 D  143  ASP THR THR ALA ASP VAL SER LEU ASP LYS VAL ASP ALA          
SEQRES   8 D  143  GLY PHE ALA ILE THR LYS ILE ALA LEU LYS SER GLU VAL          
SEQRES   9 D  143  ALA VAL PRO GLY ILE ASP ALA SER THR PHE ASP GLY ILE          
SEQRES  10 D  143  ILE GLN LYS ALA LYS ALA GLY CYS PRO VAL SER GLN VAL          
SEQRES  11 D  143  LEU LYS ALA GLU ILE THR LEU ASP TYR GLN LEU LYS SER          
MODRES 1QWI MSE A   62  MET  SELENOMETHIONINE                                   
MODRES 1QWI MSE A   67  MET  SELENOMETHIONINE                                   
MODRES 1QWI MSE B   62  MET  SELENOMETHIONINE                                   
MODRES 1QWI MSE B   67  MET  SELENOMETHIONINE                                   
MODRES 1QWI MSE C   62  MET  SELENOMETHIONINE                                   
MODRES 1QWI MSE C   67  MET  SELENOMETHIONINE                                   
MODRES 1QWI MSE D   62  MET  SELENOMETHIONINE                                   
MODRES 1QWI MSE D   67  MET  SELENOMETHIONINE                                   
HET    MSE  A  62       8                                                       
HET    MSE  A  67       8                                                       
HET    MSE  B  62       8                                                       
HET    MSE  B  67       8                                                       
HET    MSE  C  62       8                                                       
HET    MSE  C  67       8                                                       
HET    MSE  D  62       8                                                       
HET    MSE  D  67       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   5  HOH   *504(H2 O)                                                    
HELIX    1   1 GLY A   35  GLU A   41  1                                   7    
HELIX    2   2 ASN A   47  ALA A   71  1                                  25    
HELIX    3   3 ASP A  110  CYS A  125  1                                  16    
HELIX    4   4 CYS A  125  LEU A  131  1                                   7    
HELIX    5   5 GLY B   35  GLU B   41  1                                   7    
HELIX    6   6 ASN B   47  ALA B   71  1                                  25    
HELIX    7   7 ASP B  110  CYS B  125  1                                  16    
HELIX    8   8 CYS B  125  LEU B  131  1                                   7    
HELIX    9   9 GLY C   35  GLU C   41  1                                   7    
HELIX   10  10 ASN C   47  ALA C   71  1                                  25    
HELIX   11  11 ASP C  110  CYS C  125  1                                  16    
HELIX   12  12 CYS C  125  LEU C  131  1                                   7    
HELIX   13  13 GLY D   35  GLU D   41  1                                   7    
HELIX   14  14 ASN D   47  ALA D   71  1                                  25    
HELIX   15  15 ASP D  110  CYS D  125  1                                  16    
HELIX   16  16 CYS D  125  LEU D  131  1                                   7    
SHEET    1   A 6 GLN A  32  TYR A  34  0                                        
SHEET    2   A 6 LYS A  19  THR A  24 -1  N  VAL A  22   O  GLN A  32           
SHEET    3   A 6 ILE A   3  GLU A  12 -1  N  GLN A   8   O  SER A  23           
SHEET    4   A 6 SER B  77  VAL B  89 -1  O  VAL B  84   N  LYS A   5           
SHEET    5   A 6 GLY B  92  ALA B 105 -1  O  LYS B  97   N  SER B  85           
SHEET    6   A 6 GLU B 134  LYS B 142  1  O  THR B 136   N  LEU B 100           
SHEET    1   B 6 GLU A 134  LYS A 142  0                                        
SHEET    2   B 6 GLY A  92  ALA A 105  1  N  VAL A 104   O  LYS A 142           
SHEET    3   B 6 SER A  77  VAL A  89 -1  N  VAL A  89   O  GLY A  92           
SHEET    4   B 6 ILE B   3  GLU B  12 -1  O  GLY B   7   N  ALA A  82           
SHEET    5   B 6 LYS B  19  THR B  24 -1  O  SER B  23   N  GLN B   8           
SHEET    6   B 6 GLN B  32  TYR B  34 -1  O  GLN B  32   N  VAL B  22           
SHEET    1   C 6 GLN C  32  TYR C  34  0                                        
SHEET    2   C 6 LYS C  19  THR C  24 -1  N  VAL C  22   O  GLN C  32           
SHEET    3   C 6 ILE C   3  GLU C  12 -1  N  GLN C   8   O  SER C  23           
SHEET    4   C 6 SER D  77  VAL D  89 -1  O  VAL D  84   N  LYS C   5           
SHEET    5   C 6 GLY D  92  ALA D 105 -1  O  LYS D  97   N  SER D  85           
SHEET    6   C 6 GLU D 134  LYS D 142  1  O  THR D 136   N  LEU D 100           
SHEET    1   D 6 GLU C 134  LYS C 142  0                                        
SHEET    2   D 6 GLY C  92  ALA C 105  1  N  ILE C  98   O  GLU C 134           
SHEET    3   D 6 SER C  77  VAL C  89 -1  N  SER C  85   O  LYS C  97           
SHEET    4   D 6 ILE D   3  GLU D  12 -1  O  LYS D   5   N  VAL C  84           
SHEET    5   D 6 LYS D  19  THR D  24 -1  O  SER D  23   N  GLN D   8           
SHEET    6   D 6 GLN D  32  TYR D  34 -1  O  GLN D  32   N  VAL D  22           
LINK         C   SER A  61                 N   MSE A  62     1555   1555  1.33  
LINK         C   MSE A  62                 N   ALA A  63     1555   1555  1.33  
LINK         C   LEU A  66                 N   MSE A  67     1555   1555  1.33  
LINK         C   MSE A  67                 N   LEU A  68     1555   1555  1.33  
LINK         C   SER B  61                 N   MSE B  62     1555   1555  1.33  
LINK         C   MSE B  62                 N   ALA B  63     1555   1555  1.33  
LINK         C   LEU B  66                 N   MSE B  67     1555   1555  1.33  
LINK         C   MSE B  67                 N   LEU B  68     1555   1555  1.33  
LINK         C   SER C  61                 N   MSE C  62     1555   1555  1.33  
LINK         C   MSE C  62                 N   ALA C  63     1555   1555  1.33  
LINK         C   LEU C  66                 N   MSE C  67     1555   1555  1.33  
LINK         C   MSE C  67                 N   LEU C  68     1555   1555  1.33  
LINK         C   SER D  61                 N   MSE D  62     1555   1555  1.33  
LINK         C   MSE D  62                 N   ALA D  63     1555   1555  1.33  
LINK         C   LEU D  66                 N   MSE D  67     1555   1555  1.33  
LINK         C   MSE D  67                 N   LEU D  68     1555   1555  1.33  
CRYST1   65.747   64.229   67.585  90.00  92.62  90.00 P 1 21 1      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      0.015210  0.000000  0.000696        0.00000                         
SCALE2      0.000000  0.015569  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014812        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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