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Database: PDB
Entry: 1JAD
LinkDB: 1JAD
Original site: 1JAD 
HEADER    HYDROLASE                               30-MAY-01   1JAD              
TITLE     C-TERMINAL DOMAIN OF TURKEY PLC-BETA                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOLIPASE C BETA;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: C-TERMINUS;                                                
COMPND   5 SYNONYM: PLC-BETA;                                                   
COMPND   6 EC: 3.1.4.11;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MELEAGRIS GALLOPAVO;                            
SOURCE   3 ORGANISM_COMMON: TURKEY;                                             
SOURCE   4 ORGANISM_TAXID: 9103;                                                
SOURCE   5 CELL: ERYTHROCYTE;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPROEX HTB                                
KEYWDS    ALPHA HELICAL COILED COIL, HYDROLASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.U.SINGER,G.L.WALDO,T.K.HARDEN,J.SONDEK                              
REVDAT   2   24-FEB-09 1JAD    1       VERSN                                    
REVDAT   1   28-DEC-01 1JAD    0                                                
JRNL        AUTH   A.U.SINGER,G.L.WALDO,T.K.HARDEN,J.SONDEK                     
JRNL        TITL   A UNIQUE FOLD OF PHOSPHOLIPASE C-BETA MEDIATES               
JRNL        TITL 2 DIMERIZATION AND INTERACTION WITH G ALPHA Q.                 
JRNL        REF    NAT.STRUCT.BIOL.              V.   9    32 2002              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11753430                                                     
JRNL        DOI    10.1038/NSB731                                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.3                                              
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
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)   (%) : 90.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 20931                          
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) : 0.254                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1061                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2097                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE                    : 0.3410                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 113                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.029                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4008                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 143                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.00000                                              
REMARK   3    B22 (A**2) : -9.37000                                             
REMARK   3    B33 (A**2) : 3.37000                                              
REMARK   3    B12 (A**2) : 10.00000                                             
REMARK   3    B13 (A**2) : 7.16000                                              
REMARK   3    B23 (A**2) : -4.68000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.37                            
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) : 0.40                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.43                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.25                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 14.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.73                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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 : CNS BULK SOLVENT MODEL USED                          
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 29.72                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : &_1_PARAMETER_INFILE_4                         
REMARK   3  PARAMETER FILE  5  : &_1_PARAMETER_INFILE_5                         
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JAD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013557.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL1-5                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949, 0.97940, 0.97526          
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20867                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.20000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000, BIS-TRIS, LITHIUM              
REMARK 280  SULFATE, GLYCEROL, PH 6.0, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     ALA A    -1                                                      
REMARK 465     MSE A     0                                                      
REMARK 465     ASP A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ASP A   245                                                      
REMARK 465     GLY A   246                                                      
REMARK 465     PRO A   247                                                      
REMARK 465     GLU A   248                                                      
REMARK 465     GLY B   279                                                      
REMARK 465     ALA B   280                                                      
REMARK 465     MSE B   281                                                      
REMARK 465     ASP B   282                                                      
REMARK 465     GLY B   283                                                      
REMARK 465     ASP B   526                                                      
REMARK 465     GLY B   527                                                      
REMARK 465     PRO B   528                                                      
REMARK 465     GLU B   529                                                      
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    SER A 156       43.78   -109.60                                   
REMARK 500    LYS A 158      -82.46    -37.89                                   
REMARK 500    ALA A 159      -37.42    -33.00                                   
REMARK 500    PHE A 243      -69.11    -96.80                                   
REMARK 500    GLN B 290      -91.00   -108.52                                   
REMARK 500    LEU B 291      116.70     69.59                                   
REMARK 500    PRO B 294       91.18    -60.90                                   
REMARK 500    ASP B 351        7.97    -55.69                                   
REMARK 500    SER B 352       43.22    -78.79                                   
REMARK 500    GLN B 353       22.64    -73.68                                   
REMARK 500    GLU B 370      -70.18    -56.58                                   
REMARK 500    SER B 435       37.96   -142.72                                   
REMARK 500    THR B 436      145.40    179.96                                   
REMARK 500    ASP B 438       85.70   -158.74                                   
REMARK 500    LYS B 439      -31.39    -28.03                                   
REMARK 500    PHE B 524      -78.58   -123.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B5153        DISTANCE =  5.80 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4001                
DBREF  1JAD A    1   248  UNP    Q91086   Q91086_MELGA   878   1158             
DBREF  1JAD B  282   529  UNP    Q91086   Q91086_MELGA   878   1158             
SEQADV 1JAD GLY A   -2  UNP  Q91086              CLONING ARTIFACT               
SEQADV 1JAD ALA A   -1  UNP  Q91086              CLONING ARTIFACT               
SEQADV 1JAD MSE A    0  UNP  Q91086              CLONING ARTIFACT               
SEQADV 1JAD MSE A    4  UNP  Q91086    MET   881 MODIFIED RESIDUE               
SEQADV 1JAD MSE A   24  UNP  Q91086    MET   901 MODIFIED RESIDUE               
SEQADV 1JAD     A       UNP  Q91086    LYS   946 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    LYS   947 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    ARG   948 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    SER   949 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    MET   950 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    HIS   951 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    SER   952 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    ARG   953 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    LYS   954 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    THR   955 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    GLN   956 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    LYS   957 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    LYS   958 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    ARG   959 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    SER   960 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    LEU   961 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    THR   962 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    THR   963 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    GLY   964 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    ASP   965 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    VAL   966 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    GLY   967 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    THR   968 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    CYS   969 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    MET   970 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    GLN   971 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    PRO   972 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    VAL   973 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    GLU   974 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    MET   975 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    ALA   976 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    GLU   977 DELETION                       
SEQADV 1JAD     A       UNP  Q91086    LYS   978 DELETION                       
SEQADV 1JAD MSE A   82  UNP  Q91086    MET   992 MODIFIED RESIDUE               
SEQADV 1JAD MSE A  151  UNP  Q91086    MET  1061 MODIFIED RESIDUE               
SEQADV 1JAD MSE A  152  UNP  Q91086    MET  1062 MODIFIED RESIDUE               
SEQADV 1JAD MSE A  234  UNP  Q91086    MET  1144 MODIFIED RESIDUE               
SEQADV 1JAD MSE A  239  UNP  Q91086    MET  1149 MODIFIED RESIDUE               
SEQADV 1JAD GLY B  279  UNP  Q91086              CLONING ARTIFACT               
SEQADV 1JAD ALA B  280  UNP  Q91086              CLONING ARTIFACT               
SEQADV 1JAD MSE B  281  UNP  Q91086              CLONING ARTIFACT               
SEQADV 1JAD MSE B  285  UNP  Q91086    MET   881 MODIFIED RESIDUE               
SEQADV 1JAD MSE B  305  UNP  Q91086    MET   901 MODIFIED RESIDUE               
SEQADV 1JAD     B       UNP  Q91086    LYS   946 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    LYS   947 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    ARG   948 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    SER   949 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    MET   950 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    HIS   951 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    SER   952 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    ARG   953 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    LYS   954 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    THR   955 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    GLN   956 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    LYS   957 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    LYS   958 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    ARG   959 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    SER   960 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    LEU   961 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    THR   962 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    THR   963 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    GLY   964 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    ASP   965 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    VAL   966 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    GLY   967 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    THR   968 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    CYS   969 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    MET   970 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    GLN   971 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    PRO   972 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    VAL   973 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    GLU   974 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    MET   975 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    ALA   976 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    GLU   977 DELETION                       
SEQADV 1JAD     B       UNP  Q91086    LYS   978 DELETION                       
SEQADV 1JAD MSE B  363  UNP  Q91086    MET   992 MODIFIED RESIDUE               
SEQADV 1JAD MSE B  432  UNP  Q91086    MET  1061 MODIFIED RESIDUE               
SEQADV 1JAD MSE B  433  UNP  Q91086    MET  1062 MODIFIED RESIDUE               
SEQADV 1JAD MSE B  515  UNP  Q91086    MET  1144 MODIFIED RESIDUE               
SEQADV 1JAD MSE B  520  UNP  Q91086    MET  1149 MODIFIED RESIDUE               
SEQRES   1 A  251  GLY ALA MSE ASP GLY ASN MSE LYS GLU VAL THR GLN LEU          
SEQRES   2 A  251  PRO GLU PRO GLN THR ALA SER LEU ALA GLU LEU GLN GLN          
SEQRES   3 A  251  MSE LYS LEU PHE LEU LYS LEU LEU LYS LYS GLN GLU LYS          
SEQRES   4 A  251  GLU LEU LYS GLU LEU GLU ARG LYS GLY SER LYS ARG ARG          
SEQRES   5 A  251  GLU GLU LEU LEU GLN LYS TYR SER VAL LEU PHE LEU GLU          
SEQRES   6 A  251  PRO VAL TYR PRO ARG GLY LEU ASP SER GLN VAL VAL GLU          
SEQRES   7 A  251  LEU LYS GLU ARG LEU GLU MSE GLU LEU ILE HIS LEU GLY          
SEQRES   8 A  251  GLU GLU TYR HIS ASP GLY ILE ARG ARG ARG LYS GLU GLN          
SEQRES   9 A  251  HIS ALA THR GLU GLN THR ALA LYS ILE THR GLU LEU ALA          
SEQRES  10 A  251  ARG GLU LYS GLN ILE ALA GLU LEU LYS ALA LEU LYS GLU          
SEQRES  11 A  251  SER SER GLU SER ASN ILE LYS ASP ILE LYS LYS LYS LEU          
SEQRES  12 A  251  GLU ALA LYS ARG LEU ASP ARG ILE GLN VAL MSE MSE ARG          
SEQRES  13 A  251  SER THR SER ASP LYS ALA ALA GLN GLU ARG LEU LYS LYS          
SEQRES  14 A  251  GLU ILE ASN ASN SER HIS ILE GLN GLU VAL VAL GLN THR          
SEQRES  15 A  251  ILE LYS LEU LEU THR GLU LYS THR ALA ARG TYR GLN GLN          
SEQRES  16 A  251  LYS LEU GLU GLU LYS GLN ALA GLU ASN LEU ARG ALA ILE          
SEQRES  17 A  251  GLN GLU LYS GLU GLY GLN LEU GLN GLN GLU ALA VAL ALA          
SEQRES  18 A  251  GLU TYR GLU GLU LYS LEU LYS THR LEU THR VAL GLU VAL          
SEQRES  19 A  251  GLN GLU MSE VAL LYS ASN TYR MSE LYS GLU VAL PHE PRO          
SEQRES  20 A  251  ASP GLY PRO GLU                                              
SEQRES   1 B  251  GLY ALA MSE ASP GLY ASN MSE LYS GLU VAL THR GLN LEU          
SEQRES   2 B  251  PRO GLU PRO GLN THR ALA SER LEU ALA GLU LEU GLN GLN          
SEQRES   3 B  251  MSE LYS LEU PHE LEU LYS LEU LEU LYS LYS GLN GLU LYS          
SEQRES   4 B  251  GLU LEU LYS GLU LEU GLU ARG LYS GLY SER LYS ARG ARG          
SEQRES   5 B  251  GLU GLU LEU LEU GLN LYS TYR SER VAL LEU PHE LEU GLU          
SEQRES   6 B  251  PRO VAL TYR PRO ARG GLY LEU ASP SER GLN VAL VAL GLU          
SEQRES   7 B  251  LEU LYS GLU ARG LEU GLU MSE GLU LEU ILE HIS LEU GLY          
SEQRES   8 B  251  GLU GLU TYR HIS ASP GLY ILE ARG ARG ARG LYS GLU GLN          
SEQRES   9 B  251  HIS ALA THR GLU GLN THR ALA LYS ILE THR GLU LEU ALA          
SEQRES  10 B  251  ARG GLU LYS GLN ILE ALA GLU LEU LYS ALA LEU LYS GLU          
SEQRES  11 B  251  SER SER GLU SER ASN ILE LYS ASP ILE LYS LYS LYS LEU          
SEQRES  12 B  251  GLU ALA LYS ARG LEU ASP ARG ILE GLN VAL MSE MSE ARG          
SEQRES  13 B  251  SER THR SER ASP LYS ALA ALA GLN GLU ARG LEU LYS LYS          
SEQRES  14 B  251  GLU ILE ASN ASN SER HIS ILE GLN GLU VAL VAL GLN THR          
SEQRES  15 B  251  ILE LYS LEU LEU THR GLU LYS THR ALA ARG TYR GLN GLN          
SEQRES  16 B  251  LYS LEU GLU GLU LYS GLN ALA GLU ASN LEU ARG ALA ILE          
SEQRES  17 B  251  GLN GLU LYS GLU GLY GLN LEU GLN GLN GLU ALA VAL ALA          
SEQRES  18 B  251  GLU TYR GLU GLU LYS LEU LYS THR LEU THR VAL GLU VAL          
SEQRES  19 B  251  GLN GLU MSE VAL LYS ASN TYR MSE LYS GLU VAL PHE PRO          
SEQRES  20 B  251  ASP GLY PRO GLU                                              
MODRES 1JAD MSE A    4  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE A   24  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE A   82  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE A  151  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE A  152  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE A  234  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE A  239  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE B  285  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE B  305  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE B  363  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE B  432  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE B  433  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE B  515  MET  SELENOMETHIONINE                                   
MODRES 1JAD MSE B  520  MET  SELENOMETHIONINE                                   
HET    MSE  A   4       8                                                       
HET    MSE  A  24       8                                                       
HET    MSE  A  82       8                                                       
HET    MSE  A 151       8                                                       
HET    MSE  A 152       8                                                       
HET    MSE  A 234       8                                                       
HET    MSE  A 239       8                                                       
HET    MSE  B 285       8                                                       
HET    MSE  B 305       8                                                       
HET    MSE  B 363       8                                                       
HET    MSE  B 432       8                                                       
HET    MSE  B 433       8                                                       
HET    MSE  B 515       8                                                       
HET    MSE  B 520       8                                                       
HET    SO4  A4001       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    14(C5 H11 N O2 SE)                                           
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *143(H2 O)                                                    
HELIX    1   1 SER A   17  GLN A   22  1                                   6    
HELIX    2   2 MSE A   24  GLU A   62  1                                  39    
HELIX    3   3 SER A   71  ARG A  153  1                                  83    
HELIX    4   4 ASP A  157  PHE A  243  1                                  87    
HELIX    5   5 SER B  298  GLN B  304  1                                   7    
HELIX    6   6 MSE B  305  PHE B  341  1                                  37    
HELIX    7   7 SER B  352  ARG B  434  1                                  83    
HELIX    8   8 ASP B  438  PHE B  524  1                                  87    
LINK         C   ASN A   3                 N   MSE A   4     1555   1555  1.33  
LINK         C   MSE A   4                 N   LYS A   5     1555   1555  1.33  
LINK         C   GLN A  23                 N   MSE A  24     1555   1555  1.33  
LINK         C   MSE A  24                 N   LYS A  25     1555   1555  1.33  
LINK         C   GLU A  81                 N   MSE A  82     1555   1555  1.33  
LINK         C   MSE A  82                 N   GLU A  83     1555   1555  1.33  
LINK         C   VAL A 150                 N   MSE A 151     1555   1555  1.33  
LINK         C   MSE A 151                 N   MSE A 152     1555   1555  1.33  
LINK         C   MSE A 152                 N   ARG A 153     1555   1555  1.33  
LINK         C   GLU A 233                 N   MSE A 234     1555   1555  1.33  
LINK         C   MSE A 234                 N   VAL A 235     1555   1555  1.33  
LINK         C   TYR A 238                 N   MSE A 239     1555   1555  1.33  
LINK         C   MSE A 239                 N   LYS A 240     1555   1555  1.33  
LINK         C   ASN B 284                 N   MSE B 285     1555   1555  1.33  
LINK         C   MSE B 285                 N   LYS B 286     1555   1555  1.33  
LINK         C   GLN B 304                 N   MSE B 305     1555   1555  1.33  
LINK         C   MSE B 305                 N   LYS B 306     1555   1555  1.33  
LINK         C   GLU B 362                 N   MSE B 363     1555   1555  1.33  
LINK         C   MSE B 363                 N   GLU B 364     1555   1555  1.33  
LINK         C   VAL B 431                 N   MSE B 432     1555   1555  1.33  
LINK         C   MSE B 432                 N   MSE B 433     1555   1555  1.33  
LINK         C   MSE B 433                 N   ARG B 434     1555   1555  1.33  
LINK         C   GLU B 514                 N   MSE B 515     1555   1555  1.32  
LINK         C   MSE B 515                 N   VAL B 516     1555   1555  1.33  
LINK         C   TYR B 519                 N   MSE B 520     1555   1555  1.33  
LINK         C   MSE B 520                 N   LYS B 521     1555   1555  1.33  
SITE     1 AC1  4 LYS A 186  ARG A 189  TYR A 190  ARG B 329                    
CRYST1   39.111   51.928   79.350 101.07  96.96 100.70 P 1           2          
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      0.025568  0.004833  0.004288        0.00000                         
SCALE2      0.000000  0.019598  0.004418        0.00000                         
SCALE3      0.000000  0.000000  0.013014        0.00000                         
MTRIX1   1  0.298100  0.238300  0.924300      -36.26670    1                    
MTRIX2   1  0.239700 -0.956000  0.169100       51.71610    1                    
MTRIX3   1  0.923900  0.171100 -0.342100       36.96130    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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