GenomeNet

Database: PDB
Entry: 3R3T
LinkDB: 3R3T
Original site: 3R3T 
HEADER    RNA BINDING PROTEIN                     16-MAR-11   3R3T              
TITLE     CRYSTAL STRUCTURE OF 30S RIBOSOMAL PROTEIN S FROM BACILLUS ANTHRACIS  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 30S RIBOSOMAL PROTEIN S6;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;                          
SOURCE   4 ORGANISM_TAXID: 260799;                                              
SOURCE   5 STRAIN: STERNE;                                                      
SOURCE   6 GENE: BAS5327, BA_5723, GBAA_5723, RPSF;                             
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS     
KEYWDS   2 DISEASES, CSGID, BETA-BARREL, CYTOSOL, RNA BINDING PROTEIN           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,M.ZHOU,K.KWON,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR STRUCTURAL   
AUTHOR   2 GENOMICS OF INFECTIOUS DISEASES (CSGID)                              
REVDAT   4   24-JAN-18 3R3T    1       JRNL                                     
REVDAT   3   08-NOV-17 3R3T    1       REMARK                                   
REVDAT   2   29-OCT-14 3R3T    1       AUTHOR VERSN                             
REVDAT   1   30-MAR-11 3R3T    0                                                
JRNL        AUTH   Y.KIM,M.ZHOU,K.KWON,W.F.ANDERSON,A.JOACHIMIAK,               
JRNL        AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 3 (CSGID)                                                      
JRNL        TITL   CRYSTAL STRUCTURE OF 30S RIBOSOMAL PROTEIN S FROM BACILLUS   
JRNL        TITL 2 ANTHRACIS                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_690)                      
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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.61                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 10618                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.770                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 507                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.06                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 58.71                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.500           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.02450                                             
REMARK   3    B22 (A**2) : -3.02450                                             
REMARK   3    B33 (A**2) : 6.04900                                              
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  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      :  0.012           1582                                  
REMARK   3   ANGLE     :  1.384           2124                                  
REMARK   3   CHIRALITY :  0.083            231                                  
REMARK   3   PLANARITY :  0.005            277                                  
REMARK   3   DIHEDRAL  : 20.972            611                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4613  67.6113  10.0689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3511 T22:   0.3367                                     
REMARK   3      T33:   0.2657 T12:  -0.0137                                     
REMARK   3      T13:   0.0035 T23:  -0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7851 L22:   1.0340                                     
REMARK   3      L33:   0.7464 L12:  -0.0983                                     
REMARK   3      L13:   0.2780 L23:   0.1737                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0261 S12:   0.1065 S13:  -0.0596                       
REMARK   3      S21:  -0.1182 S22:  -0.0085 S23:  -0.0017                       
REMARK   3      S31:   0.0931 S32:  -0.0305 S33:   0.0368                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4444  67.7012  29.2108              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3815 T22:   0.3957                                     
REMARK   3      T33:   0.3376 T12:  -0.0018                                     
REMARK   3      T13:  -0.0072 T23:   0.0110                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1145 L22:   0.8378                                     
REMARK   3      L33:   0.8460 L12:   0.1219                                     
REMARK   3      L13:   0.1079 L23:  -0.1719                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0248 S12:   0.0268 S13:  -0.0383                       
REMARK   3      S21:   0.1338 S22:  -0.0437 S23:   0.0269                       
REMARK   3      S31:   0.0355 S32:   0.0321 S33:   0.0057                       
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 3R3T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000064453.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-OCT-10                          
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) : 0.97942                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10636                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 12.90                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.20                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.62100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.650                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL-3000, SHELXS, MLPHARE, SOLVE, RESOLVE             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MAGNESIUM CHLORIDE, 0.1 M HEPES,   
REMARK 280  30 % V/V POLYETHYLENE GLYCOL MONOMETHYL ETHER 550, PH 7.5, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       19.72167            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       39.44333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       39.44333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       19.72167            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 24810 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 18890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -206.0 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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      143.20596            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       39.44333            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 S    SO4 B 100  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 113  LIES ON A SPECIAL POSITION.                          
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     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     GLU A    95                                                      
REMARK 465     LYS A    96                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     GLU B    95                                                      
REMARK 465     LYS B    96                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  19      -77.57    -33.48                                   
REMARK 500    ASN A  32       -5.85    -54.92                                   
REMARK 500    ARG B  11      136.55    -38.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A  85   O                                                      
REMARK 620 2 ASN A  82   O    83.1                                              
REMARK 620 3 ALA A  79   O   103.4  80.3                                        
REMARK 620 4 LYS A  80   O   173.4 103.2  75.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B  85   O                                                      
REMARK 620 2 LYS B  80   O   170.0                                              
REMARK 620 3 ASN B  82   O    88.5  85.1                                        
REMARK 620 4 ALA B  79   O   109.4  61.2  71.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 100                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 100                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 101                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP04069   RELATED DB: TARGETDB                          
DBREF  3R3T A    1    96  UNP    Q81JI2   RS6_BACAN        1     96             
DBREF  3R3T B    1    96  UNP    Q81JI2   RS6_BACAN        1     96             
SEQADV 3R3T SER A   -2  UNP  Q81JI2              EXPRESSION TAG                 
SEQADV 3R3T ASN A   -1  UNP  Q81JI2              EXPRESSION TAG                 
SEQADV 3R3T ALA A    0  UNP  Q81JI2              EXPRESSION TAG                 
SEQADV 3R3T SER B   -2  UNP  Q81JI2              EXPRESSION TAG                 
SEQADV 3R3T ASN B   -1  UNP  Q81JI2              EXPRESSION TAG                 
SEQADV 3R3T ALA B    0  UNP  Q81JI2              EXPRESSION TAG                 
SEQRES   1 A   99  SER ASN ALA MSE ARG LYS TYR GLU ILE MSE TYR ILE ILE          
SEQRES   2 A   99  ARG PRO GLY VAL GLU GLU GLU ALA GLN LYS ALA LEU VAL          
SEQRES   3 A   99  GLU ARG PHE ALA GLY VAL LEU THR ASN ASN GLY ALA GLU          
SEQRES   4 A   99  ILE ILE ASN THR LYS GLU TRP GLY LYS ARG ARG LEU ALA          
SEQRES   5 A   99  TYR GLU ILE ASN ASP LEU ARG GLU GLY PHE TYR MSE ILE          
SEQRES   6 A   99  LEU ASN VAL ASN ALA ASN ALA GLU ALA ILE ASN GLU PHE          
SEQRES   7 A   99  ASP ARG LEU ALA LYS ILE ASN GLU ASP ILE LEU ARG HIS          
SEQRES   8 A   99  ILE VAL VAL LYS GLU GLU GLU LYS                              
SEQRES   1 B   99  SER ASN ALA MSE ARG LYS TYR GLU ILE MSE TYR ILE ILE          
SEQRES   2 B   99  ARG PRO GLY VAL GLU GLU GLU ALA GLN LYS ALA LEU VAL          
SEQRES   3 B   99  GLU ARG PHE ALA GLY VAL LEU THR ASN ASN GLY ALA GLU          
SEQRES   4 B   99  ILE ILE ASN THR LYS GLU TRP GLY LYS ARG ARG LEU ALA          
SEQRES   5 B   99  TYR GLU ILE ASN ASP LEU ARG GLU GLY PHE TYR MSE ILE          
SEQRES   6 B   99  LEU ASN VAL ASN ALA ASN ALA GLU ALA ILE ASN GLU PHE          
SEQRES   7 B   99  ASP ARG LEU ALA LYS ILE ASN GLU ASP ILE LEU ARG HIS          
SEQRES   8 B   99  ILE VAL VAL LYS GLU GLU GLU LYS                              
MODRES 3R3T MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3R3T MSE A    7  MET  SELENOMETHIONINE                                   
MODRES 3R3T MSE A   61  MET  SELENOMETHIONINE                                   
MODRES 3R3T MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 3R3T MSE B    7  MET  SELENOMETHIONINE                                   
MODRES 3R3T MSE B   61  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A   7       8                                                       
HET    MSE  A  61       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B   7       8                                                       
HET    MSE  B  61       8                                                       
HET     CA  A 101       1                                                       
HET    GOL  A 100       6                                                       
HET    SO4  B 100       5                                                       
HET     CA  B 101       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   7  HOH   *41(H2 O)                                                     
HELIX    1   1 GLU A   15  ASN A   32  1                                  18    
HELIX    2   2 ASN A   68  ASN A   82  1                                  15    
HELIX    3   3 GLU B   15  ASN B   33  1                                  19    
HELIX    4   4 ASN B   68  ASN B   82  1                                  15    
LINK         C   ALA A   0                 N   MSE A   1     1555   1555  1.34  
LINK         C   MSE A   1                 N   ARG A   2     1555   1555  1.33  
LINK         C   ILE A   6                 N   MSE A   7     1555   1555  1.32  
LINK         C   MSE A   7                 N   TYR A   8     1555   1555  1.32  
LINK         C   TYR A  60                 N   MSE A  61     1555   1555  1.32  
LINK         C   MSE A  61                 N   ILE A  62     1555   1555  1.32  
LINK         C   MSE B   1                 N   ARG B   2     1555   1555  1.32  
LINK         C   ILE B   6                 N   MSE B   7     1555   1555  1.32  
LINK         C   MSE B   7                 N   TYR B   8     1555   1555  1.33  
LINK         C   TYR B  60                 N   MSE B  61     1555   1555  1.33  
LINK         C   MSE B  61                 N   ILE B  62     1555   1555  1.33  
LINK         O   ILE A  85                CA    CA A 101     1555   1555  2.55  
LINK         O   ASN A  82                CA    CA A 101     1555   1555  2.74  
LINK         O   ILE B  85                CA    CA B 101     1555   1555  2.78  
LINK         O   ALA A  79                CA    CA A 101     1555   1555  2.83  
LINK         O   LYS B  80                CA    CA B 101     1555   1555  2.87  
LINK         O   LYS A  80                CA    CA A 101     1555   1555  2.88  
LINK         O   ASN B  82                CA    CA B 101     1555   1555  2.95  
LINK         O   ALA B  79                CA    CA B 101     1555   1555  3.01  
SITE     1 AC1  4 ALA A  79  LYS A  80  ASN A  82  ILE A  85                    
SITE     1 AC2  3 HOH A 115  HOH A 119  HOH A 122                               
SITE     1 AC3  3 TYR A  50  ILE B  52  ARG B  87                               
SITE     1 AC4  4 ALA B  79  LYS B  80  ASN B  82  ILE B  85                    
CRYST1   82.680   82.680   59.165  90.00  90.00 120.00 P 31 2 1     12          
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      0.012095  0.006983  0.000000        0.00000                         
SCALE2      0.000000  0.013966  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016902        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system