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Database: PDB
Entry: 2D4G
LinkDB: 2D4G
Original site: 2D4G 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   19-OCT-05   2D4G              
TITLE     STRUCTURE OF YJCG PROTEIN, A PUTATIVE 2'-5' RNA LIGASE FROM BACILLUS  
TITLE    2 SUBTILIS                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOTHETICAL PROTEIN BSU11850;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HYPOTHETICAL PROTEIN YJCG;                                  
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;                                  
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET21-DEST                                
KEYWDS    BETA BARREL, ALPHA HELIX, STRUCTURAL GENOMICS, UNKNOWN FUNCTION       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.LI,Y.H.LIANG,X.D.SU                                                 
REVDAT   4   11-OCT-17 2D4G    1       REMARK                                   
REVDAT   3   27-NOV-13 2D4G    1       JRNL   VERSN                             
REVDAT   2   24-FEB-09 2D4G    1       VERSN                                    
REVDAT   1   17-OCT-06 2D4G    0                                                
JRNL        AUTH   D.LI,C.LIU,Y.H.LIANG,L.F.LI,X.D.SU                           
JRNL        TITL   CRYSTAL STRUCTURE OF B. SUBTILIS YJCG CHARACTERIZING THE     
JRNL        TITL 2 YJCG-LIKE GROUP OF 2H PHOSPHOESTERASE SUPERFAMILY.           
JRNL        REF    PROTEINS                      V.  72  1071 2008              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   18473364                                                     
JRNL        DOI    10.1002/PROT.22093                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 17981                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3196                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2726                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 244                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.91200                                              
REMARK   3    B22 (A**2) : 0.39200                                              
REMARK   3    B33 (A**2) : -1.30300                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -5.79700                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 38.14                                                
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.PARAM                                    
REMARK   3  PARAMETER FILE  3  : MSE.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2D4G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-OCT-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000024974.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BSRF                               
REMARK 200  BEAMLINE                       : 3W1A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.981, 0.97, 1.2                   
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33260                              
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     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07900                            
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE 2.03, RESOLVE 2.03                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS, 24% PEG-MME2000, PH       
REMARK 280  7.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       49.83000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.96500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.83000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       36.96500            
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: 1970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 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      HOH A 248  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     ARG A   169                                                      
REMARK 465     GLY A   170                                                      
REMARK 465     GLU A   171                                                      
REMARK 465     ARG B   169                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     GLU B   171                                                      
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   O    ILE A     5     CA   LEU A    37              1.58            
REMARK 500   O    SER B    53     O    HOH B   290              1.98            
REMARK 500   N    ASN B    57     O    HOH B   290              2.02            
REMARK 500   O    GLN B   133     NE2  GLN B   137              2.03            
REMARK 500   O    ILE A     5     CB   LEU A    37              2.11            
REMARK 500   N    ILE A     5     CG   LEU A    37              2.15            
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   OE2  GLU A   107     OG   SER B    53     4557     2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU A  37   N     LEU A  37   CA     -0.127                       
REMARK 500    LEU A  37   CB    LEU A  37   CG      0.253                       
REMARK 500    LEU A  37   CG    LEU A  37   CD1     0.226                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR A  36   N   -  CA  -  C   ANGL. DEV. =  18.0 DEGREES          
REMARK 500    THR A  36   CA  -  C   -  N   ANGL. DEV. = -20.7 DEGREES          
REMARK 500    LEU A  37   C   -  N   -  CA  ANGL. DEV. =  18.1 DEGREES          
REMARK 500    LEU A  37   CB  -  CA  -  C   ANGL. DEV. =  22.5 DEGREES          
REMARK 500    LEU A  37   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    LEU A  37   CB  -  CG  -  CD1 ANGL. DEV. =  32.1 DEGREES          
REMARK 500    LEU A  37   CB  -  CG  -  CD2 ANGL. DEV. = -11.7 DEGREES          
REMARK 500    ARG A  38   N   -  CA  -  C   ANGL. DEV. = -29.2 DEGREES          
REMARK 500    GLU A 109   N   -  CA  -  C   ANGL. DEV. =  20.0 DEGREES          
REMARK 500    GLU A 109   CA  -  C   -  N   ANGL. DEV. = -16.1 DEGREES          
REMARK 500    TYR A 110   C   -  N   -  CA  ANGL. DEV. =  18.8 DEGREES          
REMARK 500    TYR A 110   N   -  CA  -  CB  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    TYR A 110   CA  -  CB  -  CG  ANGL. DEV. = -14.8 DEGREES          
REMARK 500    LEU A 151   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    GLY B 106   N   -  CA  -  C   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    TYR B 110   N   -  CA  -  C   ANGL. DEV. =  25.8 DEGREES          
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    ILE A  31      143.52   -174.98                                   
REMARK 500    LEU A  37     -116.38    -24.20                                   
REMARK 500    GLU A  61       33.33    -90.60                                   
REMARK 500    LYS A  71      178.97    179.04                                   
REMARK 500    VAL A 103       -7.88    -59.67                                   
REMARK 500    GLN A 108     -150.14    -38.38                                   
REMARK 500    GLU A 109     -156.73    -16.51                                   
REMARK 500    TYR A 110      110.53    134.87                                   
REMARK 500    ASN A 111      117.25     19.01                                   
REMARK 500    LEU B  51      -72.89    -57.48                                   
REMARK 500    LEU B  99        0.53    -69.31                                   
REMARK 500    ALA B 105      124.38    -31.08                                   
REMARK 500    GLU B 107       65.56     26.90                                   
REMARK 500    GLN B 108     -158.94    145.15                                   
REMARK 500    GLU B 109       52.30    125.25                                   
REMARK 500    TYR B 110     -151.03   -160.23                                   
REMARK 500    ASN B 111       83.60    -11.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2D4G A    1   171  UNP    O31629   O31629_BACSU     1    171             
DBREF  2D4G B    1   171  UNP    O31629   O31629_BACSU     1    171             
SEQRES   1 A  171  MSE LYS TYR GLY ILE VAL LEU PHE PRO SER LYS LYS LEU          
SEQRES   2 A  171  GLN ASP LEU ALA ASN SER TYR ARG LYS ARG TYR ASP PRO          
SEQRES   3 A  171  SER TYR SER LEU ILE PRO PRO HIS LEU THR LEU ARG ALA          
SEQRES   4 A  171  SER PHE GLU CYS ALA GLU GLU LYS ALA ASP GLN LEU VAL          
SEQRES   5 A  171  SER HIS LEU ARG ASN ILE ALA LYS GLU SER HIS PRO LEU          
SEQRES   6 A  171  VAL LEU LYS MSE THR LYS TYR SER SER PHE ALA PRO VAL          
SEQRES   7 A  171  ASN ASN VAL ILE TYR ILE LYS ALA GLU PRO THR GLU GLU          
SEQRES   8 A  171  LEU LYS THR LEU ASN GLU LYS LEU TYR THR GLY VAL LEU          
SEQRES   9 A  171  ALA GLY GLU GLN GLU TYR ASN PHE VAL PRO HIS VAL THR          
SEQRES  10 A  171  VAL GLY GLN ASN LEU SER ASP ASP GLU HIS SER ASP VAL          
SEQRES  11 A  171  LEU GLY GLN LEU LYS MSE GLN GLU VAL SER HIS GLU GLU          
SEQRES  12 A  171  ILE VAL ASP ARG PHE HIS LEU LEU TYR GLN LEU GLU ASN          
SEQRES  13 A  171  GLY SER TRP THR VAL TYR GLU THR PHE LEU LEU GLY ARG          
SEQRES  14 A  171  GLY GLU                                                      
SEQRES   1 B  171  MSE LYS TYR GLY ILE VAL LEU PHE PRO SER LYS LYS LEU          
SEQRES   2 B  171  GLN ASP LEU ALA ASN SER TYR ARG LYS ARG TYR ASP PRO          
SEQRES   3 B  171  SER TYR SER LEU ILE PRO PRO HIS LEU THR LEU ARG ALA          
SEQRES   4 B  171  SER PHE GLU CYS ALA GLU GLU LYS ALA ASP GLN LEU VAL          
SEQRES   5 B  171  SER HIS LEU ARG ASN ILE ALA LYS GLU SER HIS PRO LEU          
SEQRES   6 B  171  VAL LEU LYS MSE THR LYS TYR SER SER PHE ALA PRO VAL          
SEQRES   7 B  171  ASN ASN VAL ILE TYR ILE LYS ALA GLU PRO THR GLU GLU          
SEQRES   8 B  171  LEU LYS THR LEU ASN GLU LYS LEU TYR THR GLY VAL LEU          
SEQRES   9 B  171  ALA GLY GLU GLN GLU TYR ASN PHE VAL PRO HIS VAL THR          
SEQRES  10 B  171  VAL GLY GLN ASN LEU SER ASP ASP GLU HIS SER ASP VAL          
SEQRES  11 B  171  LEU GLY GLN LEU LYS MSE GLN GLU VAL SER HIS GLU GLU          
SEQRES  12 B  171  ILE VAL ASP ARG PHE HIS LEU LEU TYR GLN LEU GLU ASN          
SEQRES  13 B  171  GLY SER TRP THR VAL TYR GLU THR PHE LEU LEU GLY ARG          
SEQRES  14 B  171  GLY GLU                                                      
MODRES 2D4G MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 2D4G MSE A   69  MET  SELENOMETHIONINE                                   
MODRES 2D4G MSE A  136  MET  SELENOMETHIONINE                                   
MODRES 2D4G MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 2D4G MSE B   69  MET  SELENOMETHIONINE                                   
MODRES 2D4G MSE B  136  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  69       8                                                       
HET    MSE  A 136       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  69       8                                                       
HET    MSE  B 136       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   3  HOH   *244(H2 O)                                                    
HELIX    1   1 SER A   10  ASP A   25  1                                  16    
HELIX    2   2 PRO A   26  LEU A   30  5                                   5    
HELIX    3   3 ALA A   44  GLU A   46  5                                   3    
HELIX    4   4 LYS A   47  GLU A   61  1                                  15    
HELIX    5   5 THR A   89  LEU A   99  1                                  11    
HELIX    6   6 TYR A  100  ALA A  105  5                                   6    
HELIX    7   7 SER A  123  LYS A  135  1                                  13    
HELIX    8   8 SER B   10  ASP B   25  1                                  16    
HELIX    9   9 PRO B   26  LEU B   30  5                                   5    
HELIX   10  10 ALA B   44  LYS B   47  5                                   4    
HELIX   11  11 ALA B   48  GLU B   61  1                                  14    
HELIX   12  12 THR B   89  LEU B   99  1                                  11    
HELIX   13  13 TYR B  100  ALA B  105  5                                   6    
HELIX   14  14 SER B  123  MSE B  136  1                                  14    
SHEET    1   A 4 PHE A  41  GLU A  42  0                                        
SHEET    2   A 4 LYS A   2  VAL A   6 -1  N  TYR A   3   O  PHE A  41           
SHEET    3   A 4 ARG A 147  GLN A 153 -1  O  HIS A 149   N  VAL A   6           
SHEET    4   A 4 TRP A 159  LEU A 166 -1  O  TYR A 162   N  LEU A 150           
SHEET    1   B 4 HIS A 115  GLY A 119  0                                        
SHEET    2   B 4 ILE A  82  ALA A  86 -1  N  ILE A  84   O  VAL A 116           
SHEET    3   B 4 LEU A  65  SER A  74 -1  N  LYS A  71   O  LYS A  85           
SHEET    4   B 4 HIS A 141  VAL A 145 -1  O  GLU A 143   N  LEU A  67           
SHEET    1   C 4 LEU B  35  GLU B  42  0                                        
SHEET    2   C 4 LYS B   2  LEU B   7 -1  N  TYR B   3   O  PHE B  41           
SHEET    3   C 4 ARG B 147  GLN B 153 -1  O  LEU B 151   N  GLY B   4           
SHEET    4   C 4 TRP B 159  LEU B 166 -1  O  TYR B 162   N  LEU B 150           
SHEET    1   D 4 HIS B 115  GLY B 119  0                                        
SHEET    2   D 4 ILE B  82  ALA B  86 -1  N  ILE B  82   O  GLY B 119           
SHEET    3   D 4 LEU B  65  SER B  74 -1  N  LYS B  71   O  LYS B  85           
SHEET    4   D 4 HIS B 141  VAL B 145 -1  O  GLU B 143   N  LEU B  67           
LINK         C   MSE A   1                 N   LYS A   2     1555   1555  1.33  
LINK         C   LYS A  68                 N   MSE A  69     1555   1555  1.33  
LINK         C   MSE A  69                 N   THR A  70     1555   1555  1.33  
LINK         C   LYS A 135                 N   MSE A 136     1555   1555  1.33  
LINK         C   MSE A 136                 N   GLN A 137     1555   1555  1.33  
LINK         C   MSE B   1                 N   LYS B   2     1555   1555  1.33  
LINK         C   LYS B  68                 N   MSE B  69     1555   1555  1.33  
LINK         C   MSE B  69                 N   THR B  70     1555   1555  1.33  
LINK         C   LYS B 135                 N   MSE B 136     1555   1555  1.33  
LINK         C   MSE B 136                 N   GLN B 137     1555   1555  1.33  
CISPEP   1 ALA A   76    PRO A   77          0         3.32                     
CISPEP   2 ALA B   76    PRO B   77          0         1.18                     
CRYST1   99.660   73.930   61.770  90.00 113.56  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010034  0.000000  0.004375        0.00000                         
SCALE2      0.000000  0.013526  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017661        0.00000                         
HETATM    1  N   MSE A   1      16.272  16.789  53.256  1.00 31.95           N  
HETATM    2  CA  MSE A   1      15.408  15.939  52.384  1.00 30.64           C  
HETATM    3  C   MSE A   1      13.919  16.266  52.544  1.00 27.80           C  
HETATM    4  O   MSE A   1      13.393  16.321  53.659  1.00 26.16           O  
HETATM    5  CB  MSE A   1      15.641  14.457  52.699  1.00 34.22           C  
HETATM    6  CG  MSE A   1      14.915  13.496  51.762  1.00 39.89           C  
HETATM    7 SE   MSE A   1      15.954  12.895  50.228  1.00 50.04          SE  
HETATM    8  CE  MSE A   1      16.009  10.999  50.613  1.00 44.86           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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