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Database: PDB
Entry: 1YDO
LinkDB: 1YDO
Original site: 1YDO 
HEADER    LYASE                                   24-DEC-04   1YDO              
TITLE     CRYSTAL STRUCTURE OF THE BACILLIS SUBTILIS HMG-COA LYASE, NORTHEAST   
TITLE    2 STRUCTURAL GENOMICS TARGET SR181.                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HMG-COA LYASE;                                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HYPOTHETICAL PROTEIN BSU18230;                              
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;              
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: YNGG;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21;                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: BL21                                      
KEYWDS    TIM-BARREL PROTEIN, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE       
KEYWDS   2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, LYASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FOROUHAR,M.HUSSAIN,W.EDSTROM,S.M.VOROBIEV,R.XIAO,M.CIANO,L.SHIH,    
AUTHOR   2 T.B.ACTON,G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST STRUCTURAL        
AUTHOR   3 GENOMICS CONSORTIUM (NESG)                                           
REVDAT   4   11-OCT-17 1YDO    1       REMARK                                   
REVDAT   3   13-JUL-11 1YDO    1       VERSN                                    
REVDAT   2   24-FEB-09 1YDO    1       VERSN                                    
REVDAT   1   05-JUL-05 1YDO    0                                                
JRNL        AUTH   F.FOROUHAR,M.HUSSAIN,R.FARID,J.BENACH,M.ABASHIDZE,           
JRNL        AUTH 2 W.C.EDSTROM,S.M.VOROBIEV,R.XIAO,T.B.ACTON,Z.FU,J.J.KIM,      
JRNL        AUTH 3 H.M.MIZIORKO,G.T.MONTELIONE,J.F.HUNT                         
JRNL        TITL   CRYSTAL STRUCTURES OF TWO BACTERIAL                          
JRNL        TITL 2 3-HYDROXY-3-METHYLGLUTARYL-COA LYASES SUGGEST A COMMON       
JRNL        TITL 3 CATALYTIC MECHANISM AMONG A FAMILY OF TIM BARREL             
JRNL        TITL 4 METALLOENZYMES CLEAVING CARBON-CARBON BONDS.                 
JRNL        REF    J.BIOL.CHEM.                  V. 281  7533 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16330546                                                     
JRNL        DOI    10.1074/JBC.M507996200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 297512.170                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 81.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 52284                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.263                           
REMARK   3   FREE R VALUE                     : 0.303                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5147                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 57.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5629                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320                       
REMARK   3   BIN FREE R VALUE                    : 0.3950                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 608                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9152                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 404                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 15.47000                                             
REMARK   3    B22 (A**2) : -22.43000                                            
REMARK   3    B33 (A**2) : 6.96000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 23.59000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.44                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.36                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.54                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.52                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.730                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL                                   
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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.29                                                 
REMARK   3   BSOL        : 27.10                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1YDO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000031410.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-04                          
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               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61067                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.940                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.29700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.660                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SNB, SOLVE, RESOLVE                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 100 MM NAI, AND 10 MM       
REMARK 280  DTT, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.33300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 2960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   299                                                      
REMARK 465     LEU A   300                                                      
REMARK 465     GLU A   301                                                      
REMARK 465     HIS A   302                                                      
REMARK 465     HIS A   303                                                      
REMARK 465     HIS A   304                                                      
REMARK 465     HIS A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 465     SER B   299                                                      
REMARK 465     LEU B   300                                                      
REMARK 465     GLU B   301                                                      
REMARK 465     HIS B   302                                                      
REMARK 465     HIS B   303                                                      
REMARK 465     HIS B   304                                                      
REMARK 465     HIS B   305                                                      
REMARK 465     HIS B   306                                                      
REMARK 465     HIS B   307                                                      
REMARK 465     SER C   299                                                      
REMARK 465     LEU C   300                                                      
REMARK 465     GLU C   301                                                      
REMARK 465     HIS C   302                                                      
REMARK 465     HIS C   303                                                      
REMARK 465     HIS C   304                                                      
REMARK 465     HIS C   305                                                      
REMARK 465     HIS C   306                                                      
REMARK 465     HIS C   307                                                      
REMARK 465     SER D   299                                                      
REMARK 465     LEU D   300                                                      
REMARK 465     GLU D   301                                                      
REMARK 465     HIS D   302                                                      
REMARK 465     HIS D   303                                                      
REMARK 465     HIS D   304                                                      
REMARK 465     HIS D   305                                                      
REMARK 465     HIS D   306                                                      
REMARK 465     HIS D   307                                                      
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    ARG A  15      -79.82   -114.57                                   
REMARK 500    PRO A  22       41.58    -72.88                                   
REMARK 500    ARG A  39       50.44   -100.25                                   
REMARK 500    THR A  48     -176.57   -170.90                                   
REMARK 500    ARG A  71       90.36     63.42                                   
REMARK 500    LYS A 111       56.73   -106.96                                   
REMARK 500    ASN A 112      -48.51   -167.38                                   
REMARK 500    ASN A 114       75.32     43.43                                   
REMARK 500    LYS A 115      138.64   -172.43                                   
REMARK 500    LYS A 152      -82.86     59.56                                   
REMARK 500    ALA A 182       55.37   -114.03                                   
REMARK 500    ARG A 198      -26.50   -153.73                                   
REMARK 500    ASP A 210       51.09    -90.07                                   
REMARK 500    LEU A 237      154.21    -46.11                                   
REMARK 500    ASN A 267       19.74     55.68                                   
REMARK 500    LYS A 297        9.49    -65.39                                   
REMARK 500    ARG B  15      -78.85   -113.80                                   
REMARK 500    PRO B  22       41.39    -75.08                                   
REMARK 500    ARG B  39       49.75    -99.40                                   
REMARK 500    ARG B  71       91.31     62.85                                   
REMARK 500    LYS B 111       56.86   -107.35                                   
REMARK 500    ASN B 112      -47.47   -167.23                                   
REMARK 500    ASN B 114       75.95     41.60                                   
REMARK 500    LYS B 115      138.46   -172.18                                   
REMARK 500    LYS B 152      -83.12     60.22                                   
REMARK 500    ALA B 182       54.55   -115.15                                   
REMARK 500    ARG B 198      -25.95   -153.22                                   
REMARK 500    ASP B 210       51.37    -93.52                                   
REMARK 500    LEU B 237      154.38    -46.90                                   
REMARK 500    ASN B 267       19.82     56.04                                   
REMARK 500    LYS B 297        7.77    -64.95                                   
REMARK 500    ARG C  15      -78.85   -114.28                                   
REMARK 500    PRO C  22       40.27    -74.27                                   
REMARK 500    ARG C  39       51.18   -100.68                                   
REMARK 500    THR C  48     -176.35   -170.65                                   
REMARK 500    ARG C  71       90.17     64.12                                   
REMARK 500    LYS C 111       58.75   -107.77                                   
REMARK 500    ASN C 112      -47.72   -168.66                                   
REMARK 500    ASN C 114       75.48     43.04                                   
REMARK 500    LYS C 115      138.59   -172.75                                   
REMARK 500    LYS C 152      -82.88     58.37                                   
REMARK 500    ALA C 182       54.94   -112.90                                   
REMARK 500    ARG C 198      -27.35   -154.14                                   
REMARK 500    ASP C 210       51.28    -91.00                                   
REMARK 500    LEU C 237      154.43    -47.92                                   
REMARK 500    ASN C 267       19.82     55.84                                   
REMARK 500    LYS C 297        9.24    -66.38                                   
REMARK 500    ARG D  15      -78.11   -114.76                                   
REMARK 500    PRO D  22       42.10    -74.49                                   
REMARK 500    ARG D  39       51.42    -99.46                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
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 IOD B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: SR181   RELATED DB: TARGETDB                             
REMARK 900 RELATED ID: 1YDN   RELATED DB: PDB                                   
DBREF  1YDO A    1   299  UNP    O34873   O34873_BACSU     1    299             
DBREF  1YDO B    1   299  UNP    O34873   O34873_BACSU     1    299             
DBREF  1YDO C    1   299  UNP    O34873   O34873_BACSU     1    299             
DBREF  1YDO D    1   299  UNP    O34873   O34873_BACSU     1    299             
SEQADV 1YDO MSE A    1  UNP  O34873    MET     1 MODIFIED RESIDUE               
SEQADV 1YDO MSE A  102  UNP  O34873    MET   102 MODIFIED RESIDUE               
SEQADV 1YDO MSE A  219  UNP  O34873    MET   219 MODIFIED RESIDUE               
SEQADV 1YDO MSE A  225  UNP  O34873    MET   225 MODIFIED RESIDUE               
SEQADV 1YDO MSE A  258  UNP  O34873    MET   258 MODIFIED RESIDUE               
SEQADV 1YDO MSE A  262  UNP  O34873    MET   262 MODIFIED RESIDUE               
SEQADV 1YDO MSE A  284  UNP  O34873    MET   284 MODIFIED RESIDUE               
SEQADV 1YDO LEU A  300  UNP  O34873              CLONING ARTIFACT               
SEQADV 1YDO GLU A  301  UNP  O34873              CLONING ARTIFACT               
SEQADV 1YDO HIS A  302  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS A  303  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS A  304  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS A  305  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS A  306  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS A  307  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO MSE B    1  UNP  O34873    MET     1 MODIFIED RESIDUE               
SEQADV 1YDO MSE B  102  UNP  O34873    MET   102 MODIFIED RESIDUE               
SEQADV 1YDO MSE B  219  UNP  O34873    MET   219 MODIFIED RESIDUE               
SEQADV 1YDO MSE B  225  UNP  O34873    MET   225 MODIFIED RESIDUE               
SEQADV 1YDO MSE B  258  UNP  O34873    MET   258 MODIFIED RESIDUE               
SEQADV 1YDO MSE B  262  UNP  O34873    MET   262 MODIFIED RESIDUE               
SEQADV 1YDO MSE B  284  UNP  O34873    MET   284 MODIFIED RESIDUE               
SEQADV 1YDO LEU B  300  UNP  O34873              CLONING ARTIFACT               
SEQADV 1YDO GLU B  301  UNP  O34873              CLONING ARTIFACT               
SEQADV 1YDO HIS B  302  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS B  303  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS B  304  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS B  305  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS B  306  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS B  307  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO MSE C    1  UNP  O34873    MET     1 MODIFIED RESIDUE               
SEQADV 1YDO MSE C  102  UNP  O34873    MET   102 MODIFIED RESIDUE               
SEQADV 1YDO MSE C  219  UNP  O34873    MET   219 MODIFIED RESIDUE               
SEQADV 1YDO MSE C  225  UNP  O34873    MET   225 MODIFIED RESIDUE               
SEQADV 1YDO MSE C  258  UNP  O34873    MET   258 MODIFIED RESIDUE               
SEQADV 1YDO MSE C  262  UNP  O34873    MET   262 MODIFIED RESIDUE               
SEQADV 1YDO MSE C  284  UNP  O34873    MET   284 MODIFIED RESIDUE               
SEQADV 1YDO LEU C  300  UNP  O34873              CLONING ARTIFACT               
SEQADV 1YDO GLU C  301  UNP  O34873              CLONING ARTIFACT               
SEQADV 1YDO HIS C  302  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS C  303  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS C  304  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS C  305  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS C  306  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS C  307  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO MSE D    1  UNP  O34873    MET     1 MODIFIED RESIDUE               
SEQADV 1YDO MSE D  102  UNP  O34873    MET   102 MODIFIED RESIDUE               
SEQADV 1YDO MSE D  219  UNP  O34873    MET   219 MODIFIED RESIDUE               
SEQADV 1YDO MSE D  225  UNP  O34873    MET   225 MODIFIED RESIDUE               
SEQADV 1YDO MSE D  258  UNP  O34873    MET   258 MODIFIED RESIDUE               
SEQADV 1YDO MSE D  262  UNP  O34873    MET   262 MODIFIED RESIDUE               
SEQADV 1YDO MSE D  284  UNP  O34873    MET   284 MODIFIED RESIDUE               
SEQADV 1YDO LEU D  300  UNP  O34873              CLONING ARTIFACT               
SEQADV 1YDO GLU D  301  UNP  O34873              CLONING ARTIFACT               
SEQADV 1YDO HIS D  302  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS D  303  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS D  304  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS D  305  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS D  306  UNP  O34873              EXPRESSION TAG                 
SEQADV 1YDO HIS D  307  UNP  O34873              EXPRESSION TAG                 
SEQRES   1 A  307  MSE PRO TYR PRO LYS LYS VAL THR ILE LYS GLU VAL GLY          
SEQRES   2 A  307  PRO ARG ASP GLY LEU GLN ASN GLU PRO VAL TRP ILE ALA          
SEQRES   3 A  307  THR GLU ASP LYS ILE THR TRP ILE ASN GLN LEU SER ARG          
SEQRES   4 A  307  THR GLY LEU SER TYR ILE GLU ILE THR SER PHE VAL HIS          
SEQRES   5 A  307  PRO LYS TRP ILE PRO ALA LEU ARG ASP ALA ILE ASP VAL          
SEQRES   6 A  307  ALA LYS GLY ILE ASP ARG GLU LYS GLY VAL THR TYR ALA          
SEQRES   7 A  307  ALA LEU VAL PRO ASN GLN ARG GLY LEU GLU ASN ALA LEU          
SEQRES   8 A  307  GLU GLY GLY ILE ASN GLU ALA CYS VAL PHE MSE SER ALA          
SEQRES   9 A  307  SER GLU THR HIS ASN ARG LYS ASN ILE ASN LYS SER THR          
SEQRES  10 A  307  SER GLU SER LEU HIS ILE LEU LYS GLN VAL ASN ASN ASP          
SEQRES  11 A  307  ALA GLN LYS ALA ASN LEU THR THR ARG ALA TYR LEU SER          
SEQRES  12 A  307  THR VAL PHE GLY CYS PRO TYR GLU LYS ASP VAL PRO ILE          
SEQRES  13 A  307  GLU GLN VAL ILE ARG LEU SER GLU ALA LEU PHE GLU PHE          
SEQRES  14 A  307  GLY ILE SER GLU LEU SER LEU GLY ASP THR ILE GLY ALA          
SEQRES  15 A  307  ALA ASN PRO ALA GLN VAL GLU THR VAL LEU GLU ALA LEU          
SEQRES  16 A  307  LEU ALA ARG PHE PRO ALA ASN GLN ILE ALA LEU HIS PHE          
SEQRES  17 A  307  HIS ASP THR ARG GLY THR ALA LEU ALA ASN MSE VAL THR          
SEQRES  18 A  307  ALA LEU GLN MSE GLY ILE THR VAL PHE ASP GLY SER ALA          
SEQRES  19 A  307  GLY GLY LEU GLY GLY CYS PRO TYR ALA PRO GLY SER SER          
SEQRES  20 A  307  GLY ASN ALA ALA THR GLU ASP ILE VAL TYR MSE LEU GLU          
SEQRES  21 A  307  GLN MSE ASP ILE LYS THR ASN VAL LYS LEU GLU LYS LEU          
SEQRES  22 A  307  LEU SER ALA ALA LYS TRP ILE GLU GLU LYS MSE GLY LYS          
SEQRES  23 A  307  PRO LEU PRO SER ARG ASN LEU GLN VAL PHE LYS SER SER          
SEQRES  24 A  307  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  307  MSE PRO TYR PRO LYS LYS VAL THR ILE LYS GLU VAL GLY          
SEQRES   2 B  307  PRO ARG ASP GLY LEU GLN ASN GLU PRO VAL TRP ILE ALA          
SEQRES   3 B  307  THR GLU ASP LYS ILE THR TRP ILE ASN GLN LEU SER ARG          
SEQRES   4 B  307  THR GLY LEU SER TYR ILE GLU ILE THR SER PHE VAL HIS          
SEQRES   5 B  307  PRO LYS TRP ILE PRO ALA LEU ARG ASP ALA ILE ASP VAL          
SEQRES   6 B  307  ALA LYS GLY ILE ASP ARG GLU LYS GLY VAL THR TYR ALA          
SEQRES   7 B  307  ALA LEU VAL PRO ASN GLN ARG GLY LEU GLU ASN ALA LEU          
SEQRES   8 B  307  GLU GLY GLY ILE ASN GLU ALA CYS VAL PHE MSE SER ALA          
SEQRES   9 B  307  SER GLU THR HIS ASN ARG LYS ASN ILE ASN LYS SER THR          
SEQRES  10 B  307  SER GLU SER LEU HIS ILE LEU LYS GLN VAL ASN ASN ASP          
SEQRES  11 B  307  ALA GLN LYS ALA ASN LEU THR THR ARG ALA TYR LEU SER          
SEQRES  12 B  307  THR VAL PHE GLY CYS PRO TYR GLU LYS ASP VAL PRO ILE          
SEQRES  13 B  307  GLU GLN VAL ILE ARG LEU SER GLU ALA LEU PHE GLU PHE          
SEQRES  14 B  307  GLY ILE SER GLU LEU SER LEU GLY ASP THR ILE GLY ALA          
SEQRES  15 B  307  ALA ASN PRO ALA GLN VAL GLU THR VAL LEU GLU ALA LEU          
SEQRES  16 B  307  LEU ALA ARG PHE PRO ALA ASN GLN ILE ALA LEU HIS PHE          
SEQRES  17 B  307  HIS ASP THR ARG GLY THR ALA LEU ALA ASN MSE VAL THR          
SEQRES  18 B  307  ALA LEU GLN MSE GLY ILE THR VAL PHE ASP GLY SER ALA          
SEQRES  19 B  307  GLY GLY LEU GLY GLY CYS PRO TYR ALA PRO GLY SER SER          
SEQRES  20 B  307  GLY ASN ALA ALA THR GLU ASP ILE VAL TYR MSE LEU GLU          
SEQRES  21 B  307  GLN MSE ASP ILE LYS THR ASN VAL LYS LEU GLU LYS LEU          
SEQRES  22 B  307  LEU SER ALA ALA LYS TRP ILE GLU GLU LYS MSE GLY LYS          
SEQRES  23 B  307  PRO LEU PRO SER ARG ASN LEU GLN VAL PHE LYS SER SER          
SEQRES  24 B  307  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  307  MSE PRO TYR PRO LYS LYS VAL THR ILE LYS GLU VAL GLY          
SEQRES   2 C  307  PRO ARG ASP GLY LEU GLN ASN GLU PRO VAL TRP ILE ALA          
SEQRES   3 C  307  THR GLU ASP LYS ILE THR TRP ILE ASN GLN LEU SER ARG          
SEQRES   4 C  307  THR GLY LEU SER TYR ILE GLU ILE THR SER PHE VAL HIS          
SEQRES   5 C  307  PRO LYS TRP ILE PRO ALA LEU ARG ASP ALA ILE ASP VAL          
SEQRES   6 C  307  ALA LYS GLY ILE ASP ARG GLU LYS GLY VAL THR TYR ALA          
SEQRES   7 C  307  ALA LEU VAL PRO ASN GLN ARG GLY LEU GLU ASN ALA LEU          
SEQRES   8 C  307  GLU GLY GLY ILE ASN GLU ALA CYS VAL PHE MSE SER ALA          
SEQRES   9 C  307  SER GLU THR HIS ASN ARG LYS ASN ILE ASN LYS SER THR          
SEQRES  10 C  307  SER GLU SER LEU HIS ILE LEU LYS GLN VAL ASN ASN ASP          
SEQRES  11 C  307  ALA GLN LYS ALA ASN LEU THR THR ARG ALA TYR LEU SER          
SEQRES  12 C  307  THR VAL PHE GLY CYS PRO TYR GLU LYS ASP VAL PRO ILE          
SEQRES  13 C  307  GLU GLN VAL ILE ARG LEU SER GLU ALA LEU PHE GLU PHE          
SEQRES  14 C  307  GLY ILE SER GLU LEU SER LEU GLY ASP THR ILE GLY ALA          
SEQRES  15 C  307  ALA ASN PRO ALA GLN VAL GLU THR VAL LEU GLU ALA LEU          
SEQRES  16 C  307  LEU ALA ARG PHE PRO ALA ASN GLN ILE ALA LEU HIS PHE          
SEQRES  17 C  307  HIS ASP THR ARG GLY THR ALA LEU ALA ASN MSE VAL THR          
SEQRES  18 C  307  ALA LEU GLN MSE GLY ILE THR VAL PHE ASP GLY SER ALA          
SEQRES  19 C  307  GLY GLY LEU GLY GLY CYS PRO TYR ALA PRO GLY SER SER          
SEQRES  20 C  307  GLY ASN ALA ALA THR GLU ASP ILE VAL TYR MSE LEU GLU          
SEQRES  21 C  307  GLN MSE ASP ILE LYS THR ASN VAL LYS LEU GLU LYS LEU          
SEQRES  22 C  307  LEU SER ALA ALA LYS TRP ILE GLU GLU LYS MSE GLY LYS          
SEQRES  23 C  307  PRO LEU PRO SER ARG ASN LEU GLN VAL PHE LYS SER SER          
SEQRES  24 C  307  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 D  307  MSE PRO TYR PRO LYS LYS VAL THR ILE LYS GLU VAL GLY          
SEQRES   2 D  307  PRO ARG ASP GLY LEU GLN ASN GLU PRO VAL TRP ILE ALA          
SEQRES   3 D  307  THR GLU ASP LYS ILE THR TRP ILE ASN GLN LEU SER ARG          
SEQRES   4 D  307  THR GLY LEU SER TYR ILE GLU ILE THR SER PHE VAL HIS          
SEQRES   5 D  307  PRO LYS TRP ILE PRO ALA LEU ARG ASP ALA ILE ASP VAL          
SEQRES   6 D  307  ALA LYS GLY ILE ASP ARG GLU LYS GLY VAL THR TYR ALA          
SEQRES   7 D  307  ALA LEU VAL PRO ASN GLN ARG GLY LEU GLU ASN ALA LEU          
SEQRES   8 D  307  GLU GLY GLY ILE ASN GLU ALA CYS VAL PHE MSE SER ALA          
SEQRES   9 D  307  SER GLU THR HIS ASN ARG LYS ASN ILE ASN LYS SER THR          
SEQRES  10 D  307  SER GLU SER LEU HIS ILE LEU LYS GLN VAL ASN ASN ASP          
SEQRES  11 D  307  ALA GLN LYS ALA ASN LEU THR THR ARG ALA TYR LEU SER          
SEQRES  12 D  307  THR VAL PHE GLY CYS PRO TYR GLU LYS ASP VAL PRO ILE          
SEQRES  13 D  307  GLU GLN VAL ILE ARG LEU SER GLU ALA LEU PHE GLU PHE          
SEQRES  14 D  307  GLY ILE SER GLU LEU SER LEU GLY ASP THR ILE GLY ALA          
SEQRES  15 D  307  ALA ASN PRO ALA GLN VAL GLU THR VAL LEU GLU ALA LEU          
SEQRES  16 D  307  LEU ALA ARG PHE PRO ALA ASN GLN ILE ALA LEU HIS PHE          
SEQRES  17 D  307  HIS ASP THR ARG GLY THR ALA LEU ALA ASN MSE VAL THR          
SEQRES  18 D  307  ALA LEU GLN MSE GLY ILE THR VAL PHE ASP GLY SER ALA          
SEQRES  19 D  307  GLY GLY LEU GLY GLY CYS PRO TYR ALA PRO GLY SER SER          
SEQRES  20 D  307  GLY ASN ALA ALA THR GLU ASP ILE VAL TYR MSE LEU GLU          
SEQRES  21 D  307  GLN MSE ASP ILE LYS THR ASN VAL LYS LEU GLU LYS LEU          
SEQRES  22 D  307  LEU SER ALA ALA LYS TRP ILE GLU GLU LYS MSE GLY LYS          
SEQRES  23 D  307  PRO LEU PRO SER ARG ASN LEU GLN VAL PHE LYS SER SER          
SEQRES  24 D  307  LEU GLU HIS HIS HIS HIS HIS HIS                              
MODRES 1YDO MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE A  102  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE A  219  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE A  225  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE A  258  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE A  262  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE A  284  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE B  102  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE B  219  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE B  225  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE B  258  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE B  262  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE B  284  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE C  102  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE C  219  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE C  225  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE C  258  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE C  262  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE C  284  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE D    1  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE D  102  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE D  219  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE D  225  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE D  258  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE D  262  MET  SELENOMETHIONINE                                   
MODRES 1YDO MSE D  284  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A 102       8                                                       
HET    MSE  A 219       8                                                       
HET    MSE  A 225       8                                                       
HET    MSE  A 258       8                                                       
HET    MSE  A 262       8                                                       
HET    MSE  A 284       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B 102       8                                                       
HET    MSE  B 219       8                                                       
HET    MSE  B 225       8                                                       
HET    MSE  B 258       8                                                       
HET    MSE  B 262       8                                                       
HET    MSE  B 284       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C 102       8                                                       
HET    MSE  C 219       8                                                       
HET    MSE  C 225       8                                                       
HET    MSE  C 258       8                                                       
HET    MSE  C 262       8                                                       
HET    MSE  C 284       8                                                       
HET    MSE  D   1       8                                                       
HET    MSE  D 102       8                                                       
HET    MSE  D 219       8                                                       
HET    MSE  D 225       8                                                       
HET    MSE  D 258       8                                                       
HET    MSE  D 262       8                                                       
HET    MSE  D 284       8                                                       
HET    IOD  A 501       1                                                       
HET    IOD  B 502       1                                                       
HET    IOD  C 503       1                                                       
HET    IOD  D 504       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     IOD IODIDE ION                                                       
FORMUL   1  MSE    28(C5 H11 N O2 SE)                                           
FORMUL   5  IOD    4(I 1-)                                                      
FORMUL   9  HOH   *404(H2 O)                                                    
HELIX    1   1 VAL A   12  GLY A   17  1                                   6    
HELIX    2   2 LEU A   18  GLU A   21  5                                   4    
HELIX    3   3 ALA A   26  ARG A   39  1                                  14    
HELIX    4   4 ILE A   56  ARG A   60  5                                   5    
HELIX    5   5 ASP A   61  ILE A   69  1                                   9    
HELIX    6   6 ASN A   83  GLY A   94  1                                  12    
HELIX    7   7 SER A  105  LYS A  111  1                                   7    
HELIX    8   8 SER A  116  ALA A  134  1                                  19    
HELIX    9   9 PRO A  155  GLY A  170  1                                  16    
HELIX   10  10 ASN A  184  ALA A  197  1                                  14    
HELIX   11  11 PRO A  200  ASN A  202  5                                   3    
HELIX   12  12 HIS A  209  GLY A  213  5                                   5    
HELIX   13  13 THR A  214  GLY A  226  1                                  13    
HELIX   14  14 SER A  233  LEU A  237  5                                   5    
HELIX   15  15 ALA A  251  MSE A  262  1                                  12    
HELIX   16  16 LYS A  269  GLY A  285  1                                  17    
HELIX   17  17 SER A  290  LYS A  297  1                                   8    
HELIX   18  18 VAL B   12  GLY B   17  1                                   6    
HELIX   19  19 LEU B   18  GLU B   21  5                                   4    
HELIX   20  20 ALA B   26  ARG B   39  1                                  14    
HELIX   21  21 ILE B   56  ARG B   60  5                                   5    
HELIX   22  22 ASP B   61  ILE B   69  1                                   9    
HELIX   23  23 ASN B   83  GLY B   94  1                                  12    
HELIX   24  24 SER B  105  LYS B  111  1                                   7    
HELIX   25  25 SER B  116  ALA B  134  1                                  19    
HELIX   26  26 PRO B  155  GLY B  170  1                                  16    
HELIX   27  27 ASN B  184  ALA B  197  1                                  14    
HELIX   28  28 PRO B  200  ASN B  202  5                                   3    
HELIX   29  29 HIS B  209  GLY B  213  5                                   5    
HELIX   30  30 THR B  214  GLY B  226  1                                  13    
HELIX   31  31 SER B  233  LEU B  237  5                                   5    
HELIX   32  32 ALA B  251  MSE B  262  1                                  12    
HELIX   33  33 LYS B  269  GLY B  285  1                                  17    
HELIX   34  34 SER B  290  LYS B  297  1                                   8    
HELIX   35  35 VAL C   12  GLY C   17  1                                   6    
HELIX   36  36 LEU C   18  GLU C   21  5                                   4    
HELIX   37  37 ALA C   26  ARG C   39  1                                  14    
HELIX   38  38 ILE C   56  ARG C   60  5                                   5    
HELIX   39  39 ASP C   61  ILE C   69  1                                   9    
HELIX   40  40 ASN C   83  GLY C   94  1                                  12    
HELIX   41  41 SER C  105  LYS C  111  1                                   7    
HELIX   42  42 SER C  116  ALA C  134  1                                  19    
HELIX   43  43 PRO C  155  GLY C  170  1                                  16    
HELIX   44  44 ASN C  184  ALA C  197  1                                  14    
HELIX   45  45 PRO C  200  ASN C  202  5                                   3    
HELIX   46  46 HIS C  209  GLY C  213  5                                   5    
HELIX   47  47 THR C  214  GLY C  226  1                                  13    
HELIX   48  48 SER C  233  LEU C  237  5                                   5    
HELIX   49  49 ALA C  251  MSE C  262  1                                  12    
HELIX   50  50 LYS C  269  GLY C  285  1                                  17    
HELIX   51  51 SER C  290  LYS C  297  1                                   8    
HELIX   52  52 VAL D   12  GLY D   17  1                                   6    
HELIX   53  53 LEU D   18  GLU D   21  5                                   4    
HELIX   54  54 ALA D   26  ARG D   39  1                                  14    
HELIX   55  55 ILE D   56  ARG D   60  5                                   5    
HELIX   56  56 ASP D   61  ILE D   69  1                                   9    
HELIX   57  57 ASN D   83  GLY D   94  1                                  12    
HELIX   58  58 SER D  105  LYS D  111  1                                   7    
HELIX   59  59 SER D  116  ALA D  134  1                                  19    
HELIX   60  60 PRO D  155  GLY D  170  1                                  16    
HELIX   61  61 ASN D  184  ALA D  197  1                                  14    
HELIX   62  62 PRO D  200  ASN D  202  5                                   3    
HELIX   63  63 HIS D  209  GLY D  213  5                                   5    
HELIX   64  64 THR D  214  GLY D  226  1                                  13    
HELIX   65  65 SER D  233  LEU D  237  5                                   5    
HELIX   66  66 ALA D  251  MSE D  262  1                                  12    
HELIX   67  67 LYS D  269  GLY D  285  1                                  17    
HELIX   68  68 SER D  290  LYS D  297  1                                   8    
SHEET    1   A 9 THR A   8  GLU A  11  0                                        
SHEET    2   A 9 TYR A  44  SER A  49  1  O  GLU A  46   N  GLU A  11           
SHEET    3   A 9 THR A  76  LEU A  80  1  O  THR A  76   N  ILE A  45           
SHEET    4   A 9 GLU A  97  SER A 103  1  O  CYS A  99   N  ALA A  79           
SHEET    5   A 9 THR A 137  SER A 143  1  O  SER A 143   N  MSE A 102           
SHEET    6   A 9 LEU A 174  GLY A 177  1  O  SER A 175   N  ALA A 140           
SHEET    7   A 9 ILE A 204  HIS A 207  1  O  HIS A 207   N  LEU A 176           
SHEET    8   A 9 VAL A 229  GLY A 232  1  O  ASP A 231   N  LEU A 206           
SHEET    9   A 9 THR A   8  GLU A  11  1  N  LYS A  10   O  GLY A 232           
SHEET    1   B 2 GLY A 239  CYS A 240  0                                        
SHEET    2   B 2 ALA A 243  SER A 247 -1  O  SER A 246   N  CYS A 240           
SHEET    1   C 9 THR B   8  GLU B  11  0                                        
SHEET    2   C 9 TYR B  44  SER B  49  1  O  GLU B  46   N  GLU B  11           
SHEET    3   C 9 THR B  76  LEU B  80  1  O  THR B  76   N  ILE B  45           
SHEET    4   C 9 GLU B  97  SER B 103  1  O  CYS B  99   N  ALA B  79           
SHEET    5   C 9 THR B 137  SER B 143  1  O  SER B 143   N  MSE B 102           
SHEET    6   C 9 LEU B 174  GLY B 177  1  O  SER B 175   N  ALA B 140           
SHEET    7   C 9 ILE B 204  HIS B 207  1  O  HIS B 207   N  LEU B 176           
SHEET    8   C 9 VAL B 229  GLY B 232  1  O  ASP B 231   N  LEU B 206           
SHEET    9   C 9 THR B   8  GLU B  11  1  N  LYS B  10   O  GLY B 232           
SHEET    1   D 2 GLY B 239  CYS B 240  0                                        
SHEET    2   D 2 ALA B 243  SER B 247 -1  O  SER B 246   N  CYS B 240           
SHEET    1   E 9 THR C   8  GLU C  11  0                                        
SHEET    2   E 9 TYR C  44  SER C  49  1  O  GLU C  46   N  GLU C  11           
SHEET    3   E 9 THR C  76  LEU C  80  1  O  THR C  76   N  ILE C  45           
SHEET    4   E 9 GLU C  97  SER C 103  1  O  CYS C  99   N  ALA C  79           
SHEET    5   E 9 THR C 137  SER C 143  1  O  SER C 143   N  MSE C 102           
SHEET    6   E 9 LEU C 174  GLY C 177  1  O  SER C 175   N  ALA C 140           
SHEET    7   E 9 ILE C 204  HIS C 207  1  O  HIS C 207   N  LEU C 176           
SHEET    8   E 9 VAL C 229  GLY C 232  1  O  ASP C 231   N  LEU C 206           
SHEET    9   E 9 THR C   8  GLU C  11  1  N  LYS C  10   O  GLY C 232           
SHEET    1   F 2 GLY C 239  CYS C 240  0                                        
SHEET    2   F 2 ALA C 243  SER C 247 -1  O  SER C 246   N  CYS C 240           
SHEET    1   G 9 THR D   8  GLU D  11  0                                        
SHEET    2   G 9 TYR D  44  SER D  49  1  O  GLU D  46   N  GLU D  11           
SHEET    3   G 9 THR D  76  LEU D  80  1  O  THR D  76   N  ILE D  45           
SHEET    4   G 9 GLU D  97  SER D 103  1  O  CYS D  99   N  ALA D  79           
SHEET    5   G 9 THR D 137  SER D 143  1  O  SER D 143   N  MSE D 102           
SHEET    6   G 9 LEU D 174  GLY D 177  1  O  SER D 175   N  ALA D 140           
SHEET    7   G 9 ILE D 204  HIS D 207  1  O  HIS D 207   N  LEU D 176           
SHEET    8   G 9 VAL D 229  GLY D 232  1  O  ASP D 231   N  LEU D 206           
SHEET    9   G 9 THR D   8  GLU D  11  1  N  LYS D  10   O  GLY D 232           
SHEET    1   H 2 GLY D 239  CYS D 240  0                                        
SHEET    2   H 2 ALA D 243  SER D 247 -1  O  SER D 246   N  CYS D 240           
LINK         C   MSE A   1                 N   PRO A   2     1555   1555  1.34  
LINK         C   PHE A 101                 N   MSE A 102     1555   1555  1.33  
LINK         C   MSE A 102                 N   SER A 103     1555   1555  1.32  
LINK         C   ASN A 218                 N   MSE A 219     1555   1555  1.32  
LINK         C   MSE A 219                 N   VAL A 220     1555   1555  1.33  
LINK         C   GLN A 224                 N   MSE A 225     1555   1555  1.33  
LINK         C   MSE A 225                 N   GLY A 226     1555   1555  1.34  
LINK         C   TYR A 257                 N   MSE A 258     1555   1555  1.32  
LINK         C   MSE A 258                 N   LEU A 259     1555   1555  1.32  
LINK         C   GLN A 261                 N   MSE A 262     1555   1555  1.33  
LINK         C   MSE A 262                 N   ASP A 263     1555   1555  1.33  
LINK         C   LYS A 283                 N   MSE A 284     1555   1555  1.33  
LINK         C   MSE A 284                 N   GLY A 285     1555   1555  1.33  
LINK         C   MSE B   1                 N   PRO B   2     1555   1555  1.35  
LINK         C   PHE B 101                 N   MSE B 102     1555   1555  1.33  
LINK         C   MSE B 102                 N   SER B 103     1555   1555  1.32  
LINK         C   ASN B 218                 N   MSE B 219     1555   1555  1.32  
LINK         C   MSE B 219                 N   VAL B 220     1555   1555  1.33  
LINK         C   GLN B 224                 N   MSE B 225     1555   1555  1.33  
LINK         C   MSE B 225                 N   GLY B 226     1555   1555  1.33  
LINK         C   TYR B 257                 N   MSE B 258     1555   1555  1.32  
LINK         C   MSE B 258                 N   LEU B 259     1555   1555  1.32  
LINK         C   GLN B 261                 N   MSE B 262     1555   1555  1.32  
LINK         C   MSE B 262                 N   ASP B 263     1555   1555  1.33  
LINK         C   LYS B 283                 N   MSE B 284     1555   1555  1.33  
LINK         C   MSE B 284                 N   GLY B 285     1555   1555  1.33  
LINK         C   MSE C   1                 N   PRO C   2     1555   1555  1.34  
LINK         C   PHE C 101                 N   MSE C 102     1555   1555  1.32  
LINK         C   MSE C 102                 N   SER C 103     1555   1555  1.32  
LINK         C   ASN C 218                 N   MSE C 219     1555   1555  1.32  
LINK         C   MSE C 219                 N   VAL C 220     1555   1555  1.33  
LINK         C   GLN C 224                 N   MSE C 225     1555   1555  1.33  
LINK         C   MSE C 225                 N   GLY C 226     1555   1555  1.33  
LINK         C   TYR C 257                 N   MSE C 258     1555   1555  1.32  
LINK         C   MSE C 258                 N   LEU C 259     1555   1555  1.32  
LINK         C   GLN C 261                 N   MSE C 262     1555   1555  1.33  
LINK         C   MSE C 262                 N   ASP C 263     1555   1555  1.33  
LINK         C   LYS C 283                 N   MSE C 284     1555   1555  1.33  
LINK         C   MSE C 284                 N   GLY C 285     1555   1555  1.33  
LINK         C   MSE D   1                 N   PRO D   2     1555   1555  1.35  
LINK         C   PHE D 101                 N   MSE D 102     1555   1555  1.33  
LINK         C   MSE D 102                 N   SER D 103     1555   1555  1.32  
LINK         C   ASN D 218                 N   MSE D 219     1555   1555  1.32  
LINK         C   MSE D 219                 N   VAL D 220     1555   1555  1.33  
LINK         C   GLN D 224                 N   MSE D 225     1555   1555  1.33  
LINK         C   MSE D 225                 N   GLY D 226     1555   1555  1.33  
LINK         C   TYR D 257                 N   MSE D 258     1555   1555  1.32  
LINK         C   MSE D 258                 N   LEU D 259     1555   1555  1.33  
LINK         C   GLN D 261                 N   MSE D 262     1555   1555  1.33  
LINK         C   MSE D 262                 N   ASP D 263     1555   1555  1.33  
LINK         C   LYS D 283                 N   MSE D 284     1555   1555  1.33  
LINK         C   MSE D 284                 N   GLY D 285     1555   1555  1.33  
SITE     1 AC1  2 VAL B  51  HIS B  52                                          
SITE     1 AC2  2 VAL C  51  HIS C  52                                          
SITE     1 AC3  1 HIS D  52                                                     
CRYST1   62.693  104.666   97.445  90.00 107.43  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015951  0.000000  0.005008        0.00000                         
SCALE2      0.000000  0.009554  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010756        0.00000                         
HETATM    1  N   MSE A   1      43.499  22.044  49.627  1.00 75.29           N  
HETATM    2  CA  MSE A   1      44.126  23.363  49.306  1.00 74.08           C  
HETATM    3  C   MSE A   1      43.129  24.402  48.796  1.00 70.08           C  
HETATM    4  O   MSE A   1      42.934  25.439  49.423  1.00 70.67           O  
HETATM    5  CB  MSE A   1      45.226  23.193  48.264  1.00 78.96           C  
HETATM    6  CG  MSE A   1      45.842  24.515  47.857  1.00 85.14           C  
HETATM    7 SE   MSE A   1      46.852  25.291  49.310  1.00 95.89          SE  
HETATM    8  CE  MSE A   1      45.507  26.436  50.129  1.00 92.86           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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