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Database: PDB
Entry: 1XSV
LinkDB: 1XSV
Original site: 1XSV 
HEADER    UNKNOWN FUNCTION                        20-OCT-04   1XSV              
TITLE     X-RAY CRYSTAL STRUCTURE OF CONSERVED HYPOTHETICAL UPF0122             
TITLE    2 PROTEIN SAV1236 FROM STAPHYLOCOCCUS AUREUS SUBSP. AUREUS             
TITLE    3 MU50                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOTHETICAL UPF0122 PROTEIN SAV1236;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;            
SOURCE   3 ORGANISM_TAXID: 46170;                                               
SOURCE   4 STRAIN: SUBSP. AUREUS;                                               
SOURCE   5 ATCC: 700699;                                                        
SOURCE   6 GENE: SAV1236;                                                       
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPW2                                      
KEYWDS    HELIX-TURN-HELIX, PUTATIVE DNA-BINDING PROTEIN, SIGNAL                
KEYWDS   2 RECOGNITION PARTICLE, UPF0122, UNKNOWN FUNCTION                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.WALKER,X.XU,C.VIRAG,M.-L.MCDONALD,S.HOUSTON,K.BUZADZIJA,          
AUTHOR   2 M.VEDADI,A.DHARAMSI,K.M.FIEBIG,A.SAVCHENKO                           
REVDAT   2   24-FEB-09 1XSV    1       VERSN                                    
REVDAT   1   26-OCT-04 1XSV    0                                                
JRNL        AUTH   J.R.WALKER,X.XU,C.VIRAG,M.-L.MCDONALD,S.HOUSTON,             
JRNL        AUTH 2 K.BUZADZIJA,M.VEDADI,A.DHARAMSI,K.M.FIEBIG,                  
JRNL        AUTH 3 A.SAVCHENKO                                                  
JRNL        TITL   1.7 ANGSTROM CRYSTAL STRUCTURE OF CONSERVED                  
JRNL        TITL 2 HYPOTHETICAL UPF0122 PROTEIN SAV1236 FROM                    
JRNL        TITL 3 STAPHYLOCOCCUS AUREUS                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1237412.100                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24963                          
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) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1241                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3893                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1830                       
REMARK   3   BIN FREE R VALUE                    : 0.2310                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 180                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1858                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 272                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.40000                                             
REMARK   3    B22 (A**2) : -4.47000                                             
REMARK   3    B33 (A**2) : 4.87000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.03                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.21                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.11                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.81                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.420 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.070 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.810 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.320 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.41                                                 
REMARK   3   BSOL        : 52.59                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XSV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030728.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-AUG-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97936                            
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24963                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.680                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
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) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23000                            
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: SAD                          
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   (%): 46.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, 2.0M AMMONIUM       
REMARK 280  SULFATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       18.54800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.98900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.89200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       43.98900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.54800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.89200            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER, CONSISTING OF CHAINS     
REMARK 300 A AND B.                                                             
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: 2140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     ASN B     4                                                      
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   OD2  ASP B    68     O    HOH B   158              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  92       35.97   -141.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1XSV A    1   110  UNP    P67248   Y1236_STAAM      1    110             
DBREF  1XSV B    1   110  UNP    P67248   Y1236_STAAM      1    110             
SEQADV 1XSV GLY A   -2  UNP  P67248              CLONING ARTIFACT               
SEQADV 1XSV SER A   -1  UNP  P67248              CLONING ARTIFACT               
SEQADV 1XSV HIS A    0  UNP  P67248              CLONING ARTIFACT               
SEQADV 1XSV MSE A   12  UNP  P67248    MET    12 MODIFIED RESIDUE               
SEQADV 1XSV MSE A   89  UNP  P67248    MET    89 MODIFIED RESIDUE               
SEQADV 1XSV GLY B   -2  UNP  P67248              CLONING ARTIFACT               
SEQADV 1XSV SER B   -1  UNP  P67248              CLONING ARTIFACT               
SEQADV 1XSV HIS B    0  UNP  P67248              CLONING ARTIFACT               
SEQADV 1XSV MSE B   12  UNP  P67248    MET    12 MODIFIED RESIDUE               
SEQADV 1XSV MSE B   89  UNP  P67248    MET    89 MODIFIED RESIDUE               
SEQRES   1 A  113  GLY SER HIS MET GLY GLN ASN ASP LEU VAL LYS THR LEU          
SEQRES   2 A  113  ARG MSE ASN TYR LEU PHE ASP PHE TYR GLN SER LEU LEU          
SEQRES   3 A  113  THR ASN LYS GLN ARG ASN TYR LEU GLU LEU PHE TYR LEU          
SEQRES   4 A  113  GLU ASP TYR SER LEU SER GLU ILE ALA ASP THR PHE ASN          
SEQRES   5 A  113  VAL SER ARG GLN ALA VAL TYR ASP ASN ILE ARG ARG THR          
SEQRES   6 A  113  GLY ASP LEU VAL GLU ASP TYR GLU LYS LYS LEU GLU LEU          
SEQRES   7 A  113  TYR GLN LYS PHE GLU GLN ARG ARG GLU ILE TYR ASP GLU          
SEQRES   8 A  113  MSE LYS GLN HIS LEU SER ASN PRO GLU GLN ILE GLN ARG          
SEQRES   9 A  113  TYR ILE GLN GLN LEU GLU ASP LEU GLU                          
SEQRES   1 B  113  GLY SER HIS MET GLY GLN ASN ASP LEU VAL LYS THR LEU          
SEQRES   2 B  113  ARG MSE ASN TYR LEU PHE ASP PHE TYR GLN SER LEU LEU          
SEQRES   3 B  113  THR ASN LYS GLN ARG ASN TYR LEU GLU LEU PHE TYR LEU          
SEQRES   4 B  113  GLU ASP TYR SER LEU SER GLU ILE ALA ASP THR PHE ASN          
SEQRES   5 B  113  VAL SER ARG GLN ALA VAL TYR ASP ASN ILE ARG ARG THR          
SEQRES   6 B  113  GLY ASP LEU VAL GLU ASP TYR GLU LYS LYS LEU GLU LEU          
SEQRES   7 B  113  TYR GLN LYS PHE GLU GLN ARG ARG GLU ILE TYR ASP GLU          
SEQRES   8 B  113  MSE LYS GLN HIS LEU SER ASN PRO GLU GLN ILE GLN ARG          
SEQRES   9 B  113  TYR ILE GLN GLN LEU GLU ASP LEU GLU                          
MODRES 1XSV MSE A   12  MET  SELENOMETHIONINE                                   
MODRES 1XSV MSE A   89  MET  SELENOMETHIONINE                                   
MODRES 1XSV MSE B   12  MET  SELENOMETHIONINE                                   
MODRES 1XSV MSE B   89  MET  SELENOMETHIONINE                                   
HET    MSE  A  12       8                                                       
HET    MSE  A  89       8                                                       
HET    MSE  B  12       8                                                       
HET    MSE  B  89       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   3  HOH   *272(H2 O)                                                    
HELIX    1   1 ASP A    5  GLN A   20  1                                  16    
HELIX    2   2 SER A   21  LEU A   23  5                                   3    
HELIX    3   3 THR A   24  LEU A   36  1                                  13    
HELIX    4   4 SER A   40  PHE A   48  1                                   9    
HELIX    5   5 SER A   51  GLU A   74  1                                  24    
HELIX    6   6 GLU A   74  LYS A   90  1                                  17    
HELIX    7   7 ASN A   95  GLU A  110  1                                  16    
HELIX    8   8 THR B    9  GLN B   20  1                                  12    
HELIX    9   9 SER B   21  LEU B   23  5                                   3    
HELIX   10  10 THR B   24  TYR B   35  1                                  12    
HELIX   11  11 SER B   40  ASN B   49  1                                  10    
HELIX   12  12 SER B   51  GLU B   74  1                                  24    
HELIX   13  13 GLU B   74  LYS B   90  1                                  17    
HELIX   14  14 ASN B   95  LEU B  109  1                                  15    
LINK         C   ARG A  11                 N   MSE A  12     1555   1555  1.33  
LINK         C   MSE A  12                 N   ASN A  13     1555   1555  1.33  
LINK         C   GLU A  88                 N   MSE A  89     1555   1555  1.33  
LINK         C   MSE A  89                 N   LYS A  90     1555   1555  1.33  
LINK         C   ARG B  11                 N   MSE B  12     1555   1555  1.33  
LINK         C   MSE B  12                 N   ASN B  13     1555   1555  1.34  
LINK         C   GLU B  88                 N   MSE B  89     1555   1555  1.33  
LINK         C   MSE B  89                 N   LYS B  90     1555   1555  1.33  
CRYST1   37.096   67.784   87.978  90.00  90.00  90.00 P 21 21 21    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      0.026957  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014753  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011366        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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