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Database: PDB
Entry: 2ELB
LinkDB: 2ELB
Original site: 2ELB 
HEADER    PROTEIN BINDING                         27-MAR-07   2ELB              
TITLE     CRYSTAL STRUCTURE OF THE BAR-PH DOMAIN OF HUMAN APPL1                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADAPTER PROTEIN CONTAINING PH DOMAIN, PTB DOMAIN AND       
COMPND   3 LEUCINE ZIPPER MOTIF 1;                                              
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: THE BAR-PH DOMAIN;                                         
COMPND   6 SYNONYM: APPL1, DIP13 ALPHA, DCC-INTERACTING PROTEIN 13 ALPHA;       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    APPL, BAR DOMAIN, PH DOMAIN, PROTEIN BINDING                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LI,X.MAO,L.Q.DONG,F.LIU,L.TONG                                      
REVDAT   3   13-JUL-11 2ELB    1       VERSN                                    
REVDAT   2   24-FEB-09 2ELB    1       VERSN                                    
REVDAT   1   29-MAY-07 2ELB    0                                                
JRNL        AUTH   J.LI,X.MAO,L.Q.DONG,F.LIU,L.TONG                             
JRNL        TITL   CRYSTAL STRUCTURES OF THE BAR-PH AND PTB DOMAINS OF HUMAN    
JRNL        TITL 2 APPL1                                                        
JRNL        REF    STRUCTURE                     V.  15   525 2007              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   17502098                                                     
JRNL        DOI    10.1016/J.STR.2007.03.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.500                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 594181.770                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 83.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 19364                          
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) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.327                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1429                            
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.69                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1145                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2870                       
REMARK   3   BIN FREE R VALUE                    : 0.3290                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 109                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.032                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2834                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.66000                                             
REMARK   3    B22 (A**2) : -18.34000                                            
REMARK   3    B33 (A**2) : 19.00000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.39                            
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) : 0.50                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.66                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 19.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.82                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.280 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.140 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.010 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.040 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 22.63                                                
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  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ELB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-APR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB026805.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : NULL                               
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   : 22741                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.5853                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.940                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SNB                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES (PH 7.5), 22% (W/V)           
REMARK 280  POLYACRYLIC ACID 5100, 20MM MAGNESIUM CHLORIDE, VAPOR DIFFUSION,    
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       50.28400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.06300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.28400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.06300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER.                          
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 11900 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      100.56800            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      104.12600            
REMARK 350   BIOMT3   2  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     MSE A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     LEU A    75                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     ASP A    79                                                      
REMARK 465     LYS A   153                                                      
REMARK 465     ARG A   154                                                      
REMARK 465     GLU A   155                                                      
REMARK 465     ASN A   156                                                      
REMARK 465     ASP A   157                                                      
REMARK 465     LEU A   292                                                      
REMARK 465     VAL A   293                                                      
REMARK 465     SER A   294                                                      
REMARK 465     SER A   295                                                      
REMARK 465     ALA A   318                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     LEU A   321                                                      
REMARK 465     LYS A   375                                                      
REMARK 465     GLN A   376                                                      
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    GLU A  69       19.61    -69.64                                   
REMARK 500    MSE A 111      -60.02   -120.84                                   
REMARK 500    ARG A 121      -81.10    -97.51                                   
REMARK 500    PRO A 264      -77.53    -35.59                                   
REMARK 500    ARG A 279      114.07   -175.66                                   
REMARK 500    ARG A 287      134.65     45.86                                   
REMARK 500    TRP A 297     -144.02   -101.02                                   
REMARK 500    ASP A 298      116.86   -164.73                                   
REMARK 500    GLN A 300      145.37   -176.06                                   
REMARK 500    GLN A 305      100.36   -171.05                                   
REMARK 500    GLN A 312      117.43   -165.64                                   
REMARK 500    ASP A 316       -1.58   -143.76                                   
REMARK 500    ILE A 325      -52.55   -141.08                                   
REMARK 500    SER A 329       19.78   -168.84                                   
REMARK 500    ALA A 332     -177.45     39.33                                   
REMARK 500    VAL A 333      105.29   -172.88                                   
REMARK 500    ASP A 334     -153.46    -63.51                                   
REMARK 500    CYS A 335     -116.38   -155.33                                   
REMARK 500    GLU A 336     -165.27     87.89                                   
REMARK 500    ASP A 337     -145.02   -145.46                                   
REMARK 500    ARG A 338       22.60   -173.64                                   
REMARK 500    ARG A 339       -9.62    103.43                                   
REMARK 500    TYR A 340     -150.12    -81.08                                   
REMARK 500    PHE A 347       34.36   -154.18                                   
REMARK 500    LYS A 350      -44.77   -145.62                                   
REMARK 500    LYS A 351     -167.08    159.73                                   
REMARK 500    ILE A 373        6.06    -62.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ELA   RELATED DB: PDB                                   
DBREF  2ELB A    1   376  UNP    Q9UKG1   DP13A_HUMAN      1    376             
SEQADV 2ELB MSE A  -19  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB GLY A  -18  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB SER A  -17  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB SER A  -16  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB HIS A  -15  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB HIS A  -14  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB HIS A  -13  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB HIS A  -12  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB HIS A  -11  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB HIS A  -10  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB SER A   -9  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB SER A   -8  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB GLY A   -7  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB LEU A   -6  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB VAL A   -5  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB PRO A   -4  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB ARG A   -3  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB GLY A   -2  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB SER A   -1  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB HIS A    0  UNP  Q9UKG1              CLONING ARTIFACT               
SEQADV 2ELB MSE A    1  UNP  Q9UKG1    MET     1 MODIFIED RESIDUE               
SEQADV 2ELB MSE A   37  UNP  Q9UKG1    MET    37 MODIFIED RESIDUE               
SEQADV 2ELB MSE A   44  UNP  Q9UKG1    MET    44 MODIFIED RESIDUE               
SEQADV 2ELB MSE A   82  UNP  Q9UKG1    MET    82 MODIFIED RESIDUE               
SEQADV 2ELB MSE A  111  UNP  Q9UKG1    MET   111 MODIFIED RESIDUE               
SEQADV 2ELB MSE A  112  UNP  Q9UKG1    MET   112 MODIFIED RESIDUE               
SEQADV 2ELB MSE A  178  UNP  Q9UKG1    MET   178 MODIFIED RESIDUE               
SEQADV 2ELB MSE A  179  UNP  Q9UKG1    MET   179 MODIFIED RESIDUE               
SEQADV 2ELB MSE A  204  UNP  Q9UKG1    MET   204 MODIFIED RESIDUE               
SEQADV 2ELB MSE A  213  UNP  Q9UKG1    MET   213 MODIFIED RESIDUE               
SEQADV 2ELB MSE A  240  UNP  Q9UKG1    MET   240 MODIFIED RESIDUE               
SEQADV 2ELB MSE A  247  UNP  Q9UKG1    MET   247 MODIFIED RESIDUE               
SEQADV 2ELB ASP A  270  UNP  Q9UKG1    LYS   270 CONFLICT                       
SEQADV 2ELB MSE A  310  UNP  Q9UKG1    MET   310 MODIFIED RESIDUE               
SEQADV 2ELB MSE A  323  UNP  Q9UKG1    MET   323 MODIFIED RESIDUE               
SEQADV 2ELB MSE A  331  UNP  Q9UKG1    MET   331 MODIFIED RESIDUE               
SEQRES   1 A  396  MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  396  LEU VAL PRO ARG GLY SER HIS MSE PRO GLY ILE ASP LYS          
SEQRES   3 A  396  LEU PRO ILE GLU GLU THR LEU GLU ASP SER PRO GLN THR          
SEQRES   4 A  396  ARG SER LEU LEU GLY VAL PHE GLU GLU ASP ALA THR ALA          
SEQRES   5 A  396  ILE SER ASN TYR MSE ASN GLN LEU TYR GLN ALA MSE HIS          
SEQRES   6 A  396  ARG ILE TYR ASP ALA GLN ASN GLU LEU SER ALA ALA THR          
SEQRES   7 A  396  HIS LEU THR SER LYS LEU LEU LYS GLU TYR GLU LYS GLN          
SEQRES   8 A  396  ARG PHE PRO LEU GLY GLY ASP ASP GLU VAL MSE SER SER          
SEQRES   9 A  396  THR LEU GLN GLN PHE SER LYS VAL ILE ASP GLU LEU SER          
SEQRES  10 A  396  SER CYS HIS ALA VAL LEU SER THR GLN LEU ALA ASP ALA          
SEQRES  11 A  396  MSE MSE PHE PRO ILE THR GLN PHE LYS GLU ARG ASP LEU          
SEQRES  12 A  396  LYS GLU ILE LEU THR LEU LYS GLU VAL PHE GLN ILE ALA          
SEQRES  13 A  396  SER ASN ASP HIS ASP ALA ALA ILE ASN ARG TYR SER ARG          
SEQRES  14 A  396  LEU SER LYS LYS ARG GLU ASN ASP LYS VAL LYS TYR GLU          
SEQRES  15 A  396  VAL THR GLU ASP VAL TYR THR SER ARG LYS LYS GLN HIS          
SEQRES  16 A  396  GLN THR MSE MSE HIS TYR PHE CYS ALA LEU ASN THR LEU          
SEQRES  17 A  396  GLN TYR LYS LYS LYS ILE ALA LEU LEU GLU PRO LEU LEU          
SEQRES  18 A  396  GLY TYR MSE GLN ALA GLN ILE SER PHE PHE LYS MSE GLY          
SEQRES  19 A  396  SER GLU ASN LEU ASN GLU GLN LEU GLU GLU PHE LEU ALA          
SEQRES  20 A  396  ASN ILE GLY THR SER VAL GLN ASN VAL ARG ARG GLU MSE          
SEQRES  21 A  396  ASP SER ASP ILE GLU THR MSE GLN GLN THR ILE GLU ASP          
SEQRES  22 A  396  LEU GLU VAL ALA SER ASP PRO LEU TYR VAL PRO ASP PRO          
SEQRES  23 A  396  ASP PRO THR ASP PHE PRO VAL ASN ARG ASN LEU THR ARG          
SEQRES  24 A  396  LYS ALA GLY TYR LEU ASN ALA ARG ASN LYS THR GLY LEU          
SEQRES  25 A  396  VAL SER SER THR TRP ASP ARG GLN PHE TYR PHE THR GLN          
SEQRES  26 A  396  GLY GLY ASN LEU MSE SER GLN ALA ARG GLY ASP VAL ALA          
SEQRES  27 A  396  GLY GLY LEU ALA MSE ASP ILE ASP ASN CYS SER VAL MSE          
SEQRES  28 A  396  ALA VAL ASP CYS GLU ASP ARG ARG TYR CYS PHE GLN ILE          
SEQRES  29 A  396  THR SER PHE ASP GLY LYS LYS SER SER ILE LEU GLN ALA          
SEQRES  30 A  396  GLU SER LYS LYS ASP HIS GLU GLU TRP ILE CYS THR ILE          
SEQRES  31 A  396  ASN ASN ILE SER LYS GLN                                      
MODRES 2ELB MSE A   37  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A   44  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A   82  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  111  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  112  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  178  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  179  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  204  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  213  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  240  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  247  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  310  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  323  MET  SELENOMETHIONINE                                   
MODRES 2ELB MSE A  331  MET  SELENOMETHIONINE                                   
HET    MSE  A  37       8                                                       
HET    MSE  A  44       8                                                       
HET    MSE  A  82       8                                                       
HET    MSE  A 111       8                                                       
HET    MSE  A 112       8                                                       
HET    MSE  A 178       8                                                       
HET    MSE  A 179       8                                                       
HET    MSE  A 204       8                                                       
HET    MSE  A 213       8                                                       
HET    MSE  A 240       8                                                       
HET    MSE  A 247       8                                                       
HET    MSE  A 310       8                                                       
HET    MSE  A 323       8                                                       
HET    MSE  A 331       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    14(C5 H11 N O2 SE)                                           
HELIX    1   1 PRO A    8  THR A   12  5                                   5    
HELIX    2   2 SER A   16  LYS A   66  1                                  51    
HELIX    3   3 GLU A   67  GLN A   71  5                                   5    
HELIX    4   4 GLU A   80  MSE A  111  1                                  32    
HELIX    5   5 MSE A  111  LYS A  119  1                                   9    
HELIX    6   6 ARG A  121  ARG A  149  1                                  29    
HELIX    7   7 LYS A  158  LEU A  218  1                                  61    
HELIX    8   8 ASN A  219  ASP A  259  1                                  41    
HELIX    9   9 PRO A  260  TYR A  262  5                                   3    
HELIX   10  10 SER A  359  ILE A  373  1                                  15    
SHEET    1   A 6 MSE A 323  ASN A 327  0                                        
SHEET    2   A 6 ASN A 308  GLN A 312 -1  N  LEU A 309   O  ASP A 326           
SHEET    3   A 6 ARG A 299  GLN A 305 -1  N  PHE A 301   O  GLN A 312           
SHEET    4   A 6 ALA A 281  ALA A 286 -1  N  LEU A 284   O  GLN A 300           
SHEET    5   A 6 LEU A 355  GLN A 356 -1  O  GLN A 356   N  ASN A 285           
SHEET    6   A 6 GLN A 343  ILE A 344 -1  N  ILE A 344   O  LEU A 355           
LINK         C   TYR A  36                 N   MSE A  37     1555   1555  1.33  
LINK         C   MSE A  37                 N   ASN A  38     1555   1555  1.33  
LINK         C   ALA A  43                 N   MSE A  44     1555   1555  1.33  
LINK         C   MSE A  44                 N   HIS A  45     1555   1555  1.32  
LINK         C   VAL A  81                 N   MSE A  82     1555   1555  1.33  
LINK         C   MSE A  82                 N   SER A  83     1555   1555  1.33  
LINK         C   ALA A 110                 N   MSE A 111     1555   1555  1.33  
LINK         C   MSE A 111                 N   MSE A 112     1555   1555  1.33  
LINK         C   MSE A 112                 N   PHE A 113     1555   1555  1.33  
LINK         C   THR A 177                 N   MSE A 178     1555   1555  1.33  
LINK         C   MSE A 178                 N   MSE A 179     1555   1555  1.33  
LINK         C   MSE A 179                 N   HIS A 180     1555   1555  1.33  
LINK         C   TYR A 203                 N   MSE A 204     1555   1555  1.33  
LINK         C   MSE A 204                 N   GLN A 205     1555   1555  1.33  
LINK         C   LYS A 212                 N   MSE A 213     1555   1555  1.32  
LINK         C   MSE A 213                 N   GLY A 214     1555   1555  1.33  
LINK         C   GLU A 239                 N   MSE A 240     1555   1555  1.34  
LINK         C   MSE A 240                 N   ASP A 241     1555   1555  1.33  
LINK         C   THR A 246                 N   MSE A 247     1555   1555  1.33  
LINK         C   MSE A 247                 N   GLN A 248     1555   1555  1.33  
LINK         C   LEU A 309                 N   MSE A 310     1555   1555  1.33  
LINK         C   MSE A 310                 N   SER A 311     1555   1555  1.33  
LINK         C   ALA A 322                 N   MSE A 323     1555   1555  1.33  
LINK         C   MSE A 323                 N   ASP A 324     1555   1555  1.33  
LINK         C   VAL A 330                 N   MSE A 331     1555   1555  1.33  
LINK         C   MSE A 331                 N   ALA A 332     1555   1555  1.33  
CRYST1  100.568  104.126   37.074  90.00  90.00  90.00 P 21 21 2     4          
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      0.009944  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009604  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.026973        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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