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Database: PDB
Entry: 5JG7
LinkDB: 5JG7
Original site: 5JG7 
HEADER    METAL TRANSPORT                         19-APR-16   5JG7              
TITLE     CRYSTAL STRUCTURE OF PUTATIVE PERIPLASMIC BINDING PROTEIN FROM        
TITLE    2 SALMONELLA TYPHIMURIUM LT2                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FUR REGULATED SALMONELLA IRON TRANSPORTER;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 28-187;                                       
COMPND   5 SYNONYM: PERIPLASMIC BINDING PROTEIN;                                
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM (STRAIN LT2 / SGSC1412 / 
SOURCE   3 ATCC 700720);                                                        
SOURCE   4 ORGANISM_TAXID: 99287;                                               
SOURCE   5 STRAIN: LT2 / SGSC1412 / ATCC 700720;                                
SOURCE   6 GENE: SITA, STM2861;                                                 
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG53                                   
KEYWDS    STRUCTURAL GENOMICS, CSGID, PERIPLASMIC BINDING PROTEIN, CENTER FOR   
KEYWDS   2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, METAL TRANSPORT          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHANG,M.ZHOU,S.SHATSMAN,A.JOACHIMIAK,W.F.ANDERSON,CENTER FOR        
AUTHOR   2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)                   
REVDAT   2   20-JUL-16 5JG7    1       REMARK                                   
REVDAT   1   27-APR-16 5JG7    0                                                
JRNL        AUTH   C.CHANG,M.ZHOU,S.SHATSMAN,A.JOACHIMIAK,W.F.ANDERSON          
JRNL        TITL   CRYSTAL STRUCTURE OF PUTATIVE PERIPLASMIC BINDING PROTEIN    
JRNL        TITL 2 FROM SALMONELLA TYPHIMURIUM LT2                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2328                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 35880                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1828                            
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 30.9895 -  3.9935    0.98     2895   193  0.1809 0.2209        
REMARK   3     2  3.9935 -  3.1708    1.00     2856   145  0.1712 0.1881        
REMARK   3     3  3.1708 -  2.7703    0.99     2772   170  0.1786 0.2077        
REMARK   3     4  2.7703 -  2.5171    0.99     2788   150  0.1762 0.2064        
REMARK   3     5  2.5171 -  2.3368    1.00     2755   152  0.1585 0.2173        
REMARK   3     6  2.3368 -  2.1990    0.99     2756   149  0.1536 0.2214        
REMARK   3     7  2.1990 -  2.0889    0.98     2723   127  0.1567 0.2160        
REMARK   3     8  2.0889 -  1.9980    0.99     2739   142  0.1624 0.2093        
REMARK   3     9  1.9980 -  1.9211    0.98     2733   131  0.1733 0.2100        
REMARK   3    10  1.9211 -  1.8548    0.96     2647   138  0.1717 0.2308        
REMARK   3    11  1.8548 -  1.7968    0.89     2443   125  0.1774 0.2229        
REMARK   3    12  1.7968 -  1.7455    0.76     2102   111  0.1863 0.2448        
REMARK   3    13  1.7455 -  1.6995    0.67     1843    95  0.2083 0.2565        
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.390           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.88                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.01                          
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      :  0.006           2409                                  
REMARK   3   ANGLE     :  0.734           3268                                  
REMARK   3   CHIRALITY :  0.050            359                                  
REMARK   3   PLANARITY :  0.004            428                                  
REMARK   3   DIHEDRAL  : 15.713           1472                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5JG7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220528.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97926                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37084                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
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) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
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: HKL-3000                                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M PROLINE, 0.1 M HEPES, 10% W/V      
REMARK 280  PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K    
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       22.02850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.52450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.29100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.52450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.02850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.29100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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     ALA A    61                                                      
REMARK 465     THR A   118                                                      
REMARK 465     GLU A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     PRO A   121                                                      
REMARK 465     TYR A   122                                                      
REMARK 465     ASN A   123                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     LYS A   125                                                      
REMARK 465     PRO A   126                                                      
REMARK 465     ASN A   127                                                      
REMARK 465     PRO A   128                                                      
REMARK 465     GLU B    62                                                      
REMARK 465     ILE B    63                                                      
REMARK 465     HIS B    64                                                      
REMARK 465     GLU B    65                                                      
REMARK 465     GLY B   116                                                      
REMARK 465     ILE B   117                                                      
REMARK 465     THR B   118                                                      
REMARK 465     GLU B   119                                                      
REMARK 465     GLY B   120                                                      
REMARK 465     PRO B   121                                                      
REMARK 465     TYR B   122                                                      
REMARK 465     ASN B   123                                                      
REMARK 465     GLY B   124                                                      
REMARK 465     LYS B   125                                                      
REMARK 465     PRO B   126                                                      
REMARK 465     ASN B   127                                                      
REMARK 465     PRO B   128                                                      
REMARK 465     HIS B   129                                                      
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     GLU A  62    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  63    CG1  CG2  CD1                                       
REMARK 470     HIS A  64    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A  65    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  91    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MSE A 115    CG  SE    CE                                        
REMARK 470     HIS A 129    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR B  66    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B  74    CG   CD   CE   NZ                                   
REMARK 470     ARG B  91    CG   CD   NE   CZ   NH1  NH2                        
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   OD1  ASP A   187     O    HOH A   301              2.11            
REMARK 500   NH2  ARG A   171     O    HOH A   302              2.16            
REMARK 500   O    HOH A   343     O    HOH B   381              2.17            
REMARK 500   O    HOH A   321     O    HOH A   430              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   305     O    HOH B   359     1455     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP01840   RELATED DB: TARGETTRACK                       
DBREF  5JG7 A   28   187  UNP    Q7CPX8   Q7CPX8_SALTY    28    187             
DBREF  5JG7 B   28   187  UNP    Q7CPX8   Q7CPX8_SALTY    28    187             
SEQRES   1 A  160  GLU LYS PHE LYS VAL ILE THR THR PHE THR VAL ILE ALA          
SEQRES   2 A  160  ASP MSE ALA LYS ASN VAL ALA GLY ASP ALA ALA GLU VAL          
SEQRES   3 A  160  SER SER ILE THR LYS PRO GLY ALA GLU ILE HIS GLU TYR          
SEQRES   4 A  160  GLN PRO THR PRO GLY ASP ILE LYS ARG ALA GLN GLY ALA          
SEQRES   5 A  160  GLN LEU ILE LEU ALA ASN GLY LEU ASN LEU GLU ARG TRP          
SEQRES   6 A  160  PHE ALA ARG PHE TYR GLN HIS LEU SER GLY VAL PRO GLU          
SEQRES   7 A  160  VAL VAL VAL SER THR GLY VAL LYS PRO MSE GLY ILE THR          
SEQRES   8 A  160  GLU GLY PRO TYR ASN GLY LYS PRO ASN PRO HIS ALA TRP          
SEQRES   9 A  160  MSE SER ALA GLU ASN ALA LEU ILE TYR VAL ASP ASN ILE          
SEQRES  10 A  160  ARG ASP ALA LEU VAL LYS TYR ASP PRO ASP ASN ALA GLN          
SEQRES  11 A  160  ILE TYR LYS GLN ASN ALA GLU ARG TYR LYS ALA LYS ILE          
SEQRES  12 A  160  ARG GLN MSE ALA ASP PRO LEU ARG ALA GLU LEU GLU LYS          
SEQRES  13 A  160  ILE PRO ALA ASP                                              
SEQRES   1 B  160  GLU LYS PHE LYS VAL ILE THR THR PHE THR VAL ILE ALA          
SEQRES   2 B  160  ASP MSE ALA LYS ASN VAL ALA GLY ASP ALA ALA GLU VAL          
SEQRES   3 B  160  SER SER ILE THR LYS PRO GLY ALA GLU ILE HIS GLU TYR          
SEQRES   4 B  160  GLN PRO THR PRO GLY ASP ILE LYS ARG ALA GLN GLY ALA          
SEQRES   5 B  160  GLN LEU ILE LEU ALA ASN GLY LEU ASN LEU GLU ARG TRP          
SEQRES   6 B  160  PHE ALA ARG PHE TYR GLN HIS LEU SER GLY VAL PRO GLU          
SEQRES   7 B  160  VAL VAL VAL SER THR GLY VAL LYS PRO MSE GLY ILE THR          
SEQRES   8 B  160  GLU GLY PRO TYR ASN GLY LYS PRO ASN PRO HIS ALA TRP          
SEQRES   9 B  160  MSE SER ALA GLU ASN ALA LEU ILE TYR VAL ASP ASN ILE          
SEQRES  10 B  160  ARG ASP ALA LEU VAL LYS TYR ASP PRO ASP ASN ALA GLN          
SEQRES  11 B  160  ILE TYR LYS GLN ASN ALA GLU ARG TYR LYS ALA LYS ILE          
SEQRES  12 B  160  ARG GLN MSE ALA ASP PRO LEU ARG ALA GLU LEU GLU LYS          
SEQRES  13 B  160  ILE PRO ALA ASP                                              
MODRES 5JG7 MSE A   42  MET  MODIFIED RESIDUE                                   
MODRES 5JG7 MSE A  115  MET  MODIFIED RESIDUE                                   
MODRES 5JG7 MSE A  132  MET  MODIFIED RESIDUE                                   
MODRES 5JG7 MSE A  173  MET  MODIFIED RESIDUE                                   
MODRES 5JG7 MSE B   42  MET  MODIFIED RESIDUE                                   
MODRES 5JG7 MSE B  115  MET  MODIFIED RESIDUE                                   
MODRES 5JG7 MSE B  132  MET  MODIFIED RESIDUE                                   
MODRES 5JG7 MSE B  173  MET  MODIFIED RESIDUE                                   
HET    MSE  A  42       8                                                       
HET    MSE  A 115       5                                                       
HET    MSE  A 132       8                                                       
HET    MSE  A 173      16                                                       
HET    MSE  B  42       8                                                       
HET    MSE  B 115       8                                                       
HET    MSE  B 132       8                                                       
HET    MSE  B 173      16                                                       
HET    GOL  A 201      12                                                       
HET    GOL  A 202       6                                                       
HET    GOL  B 201      12                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   3  GOL    3(C3 H8 O3)                                                  
FORMUL   6  HOH   *234(H2 O)                                                    
HELIX    1 AA1 PHE A   36  GLY A   48  1                                  13    
HELIX    2 AA2 THR A   69  GLN A   77  1                                   9    
HELIX    3 AA3 GLY A   86  LEU A   89  5                                   4    
HELIX    4 AA4 GLU A   90  TYR A   97  1                                   8    
HELIX    5 AA5 GLN A   98  SER A  101  5                                   4    
HELIX    6 AA6 ALA A  130  ASP A  152  1                                  23    
HELIX    7 AA7 ASN A  155  ASP A  175  1                                  21    
HELIX    8 AA8 ASP A  175  LYS A  183  1                                   9    
HELIX    9 AA9 PHE B   36  GLY B   48  1                                  13    
HELIX   10 AB1 THR B   69  GLN B   77  1                                   9    
HELIX   11 AB2 GLY B   86  LEU B   89  5                                   4    
HELIX   12 AB3 GLU B   90  TYR B   97  1                                   8    
HELIX   13 AB4 GLN B   98  SER B  101  5                                   4    
HELIX   14 AB5 SER B  133  ASP B  152  1                                  20    
HELIX   15 AB6 ASN B  155  ASP B  175  1                                  21    
HELIX   16 AB7 ASP B  175  LYS B  183  1                                   9    
SHEET    1 AA1 4 ALA A  51  SER A  55  0                                        
SHEET    2 AA1 4 PHE A  30  THR A  34  1  N  PHE A  30   O  GLU A  52           
SHEET    3 AA1 4 LEU A  81  ALA A  84  1  O  LEU A  81   N  ILE A  33           
SHEET    4 AA1 4 GLU B 105  VAL B 107  1  O  VAL B 106   N  ALA A  84           
SHEET    1 AA2 4 GLU A 105  VAL A 107  0                                        
SHEET    2 AA2 4 LEU B  81  ALA B  84  1  O  ILE B  82   N  VAL A 106           
SHEET    3 AA2 4 PHE B  30  THR B  34  1  N  ILE B  33   O  LEU B  81           
SHEET    4 AA2 4 ALA B  51  SER B  55  1  O  GLU B  52   N  PHE B  30           
LINK         C   ASP A  41                 N   MSE A  42     1555   1555  1.33  
LINK         C   MSE A  42                 N   ALA A  43     1555   1555  1.34  
LINK         C   PRO A 114                 N   MSE A 115     1555   1555  1.33  
LINK         C   MSE A 115                 N   GLY A 116     1555   1555  1.33  
LINK         C  ATRP A 131                 N   MSE A 132     1555   1555  1.33  
LINK         C  BTRP A 131                 N   MSE A 132     1555   1555  1.33  
LINK         C   MSE A 132                 N   SER A 133     1555   1555  1.34  
LINK         C  AGLN A 172                 N  AMSE A 173     1555   1555  1.33  
LINK         C  BGLN A 172                 N  BMSE A 173     1555   1555  1.33  
LINK         C  AMSE A 173                 N   ALA A 174     1555   1555  1.33  
LINK         C  BMSE A 173                 N   ALA A 174     1555   1555  1.33  
LINK         C   ASP B  41                 N   MSE B  42     1555   1555  1.33  
LINK         C   MSE B  42                 N   ALA B  43     1555   1555  1.34  
LINK         C   PRO B 114                 N   MSE B 115     1555   1555  1.33  
LINK         C   TRP B 131                 N   MSE B 132     1555   1555  1.33  
LINK         C   MSE B 132                 N   SER B 133     1555   1555  1.33  
LINK         C   GLN B 172                 N  AMSE B 173     1555   1555  1.33  
LINK         C   GLN B 172                 N  BMSE B 173     1555   1555  1.33  
LINK         C  AMSE B 173                 N   ALA B 174     1555   1555  1.33  
LINK         C  BMSE B 173                 N   ALA B 174     1555   1555  1.33  
SITE     1 AC1 12 ASN A  85  GLY A  86  LEU A  87  GLU A 105                    
SITE     2 AC1 12 HOH A 303  HOH A 306  HOH A 307  HOH A 352                    
SITE     3 AC1 12 ASN B  85  GLY B  86  LEU B  87  GLU B 105                    
SITE     1 AC2  7 THR A 110  TYR A 151  HOH A 311  HOH A 324                    
SITE     2 AC2  7 HOH A 436  PRO B 104  GLU B 105                               
SITE     1 AC3  9 PRO A 104  GLU A 105  VAL B 106  VAL B 107                    
SITE     2 AC3  9 THR B 110  TYR B 151  HOH B 303  HOH B 306                    
SITE     3 AC3  9 HOH B 315                                                     
CRYST1   44.057   84.582   91.049  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      0.022698  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011823  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010983        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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