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Database: PDB
Entry: 2Z0O
LinkDB: 2Z0O
Original site: 2Z0O 
HEADER    SIGNALING PROTEIN                       07-MAY-07   2Z0O              
TITLE     CRYSTAL STRUCTURE OF APPL1-BAR-PH DOMAIN                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DCC-INTERACTING PROTEIN 13-ALPHA;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-385;                                            
COMPND   5 SYNONYM: APPL1, DIP13-ALPHA, ADAPTER PROTEIN CONTAINING PH           
COMPND   6 DOMAIN, PTB DOMAIN AND LEUCINE ZIPPER MOTIF 1;                       
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: CELL-FREE PROTEIN SYNTHESIS;                      
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PX061018-05                               
KEYWDS    HELIX BUNDLE, CELL CYCLE, COILED COIL, ENDOSOME, MEMBRANE,            
KEYWDS   2 NUCLEUS, PHOSPHORYLATION, SIGNALING PROTEIN, STRUCTURAL              
KEYWDS   3 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL             
KEYWDS   4 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL                            
KEYWDS   5 GENOMICS/PROTEOMICS INITIATIVE, RSGI                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.MURAYAMA,M.KATO-MURAYAMA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,            
AUTHOR   2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)               
REVDAT   2   24-FEB-09 2Z0O    1       VERSN                                    
REVDAT   1   13-MAY-08 2Z0O    0                                                
JRNL        AUTH   K.MURAYAMA,M.KATO-MURAYAMA,T.TERADA,M.SHIROUZU,              
JRNL        AUTH 2 S.YOKOYAMA                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF APPL1-BAR-PH DOMAIN                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.58 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) : 2.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1036991.960                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 13508                          
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) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.299                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1377                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
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) : 2.58                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.74                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1787                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE                    : 0.3810                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 195                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2848                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 69                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.87000                                             
REMARK   3    B22 (A**2) : 8.40000                                              
REMARK   3    B33 (A**2) : -3.52000                                             
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) : 0.32                            
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) : 0.47                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.46                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 19.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.71                            
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) : 1.340 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.260 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.140 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.200 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 42.95                                                
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  : 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                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2Z0O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-AUG-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB027372.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792, 0.964, 0.97942             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13536                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.17000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.2M AMMONIUM ACETATE,      
REMARK 280  0.1M BIS-TRIS, 0.3M NON-DETERGENT SULFO-BETAINE 195, PH 5.5,        
REMARK 280  VAPOR DIFFUSION, HANGING 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       51.72450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.50150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.72450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.50150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13160 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 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        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
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     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     ASN A   288                                                      
REMARK 465     LYS A   289                                                      
REMARK 465     THR A   290                                                      
REMARK 465     GLY A   291                                                      
REMARK 465     LEU A   292                                                      
REMARK 465     VAL A   293                                                      
REMARK 465     SER A   294                                                      
REMARK 465     SER A   295                                                      
REMARK 465     THR A   296                                                      
REMARK 465     TRP A   297                                                      
REMARK 465     PHE A   347                                                      
REMARK 465     ASP A   348                                                      
REMARK 465     GLY A   349                                                      
REMARK 465     LYS A   350                                                      
REMARK 465     LYS A   351                                                      
REMARK 465     ILE A   373                                                      
REMARK 465     SER A   374                                                      
REMARK 465     LYS A   375                                                      
REMARK 465     GLN A   376                                                      
REMARK 465     ILE A   377                                                      
REMARK 465     TYR A   378                                                      
REMARK 465     LEU A   379                                                      
REMARK 465     SER A   380                                                      
REMARK 465     GLU A   381                                                      
REMARK 465     ASN A   382                                                      
REMARK 465     PRO A   383                                                      
REMARK 465     GLU A   384                                                      
REMARK 465     GLU A   385                                                      
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    LYS A  70       47.61    -83.96                                   
REMARK 500    ARG A 121      -70.45    -93.61                                   
REMARK 500    ARG A 154      -97.87    -94.84                                   
REMARK 500    GLU A 155      111.00     54.70                                   
REMARK 500    ASN A 276       58.81   -107.34                                   
REMARK 500    GLN A 305      113.68   -167.31                                   
REMARK 500    GLN A 312      113.70   -161.94                                   
REMARK 500    ALA A 318      -38.67   -149.42                                   
REMARK 500    ASN A 327       22.11    167.69                                   
REMARK 500    GLU A 336     -143.43     42.96                                   
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 A 453        DISTANCE =  5.67 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: HSO003007272.3   RELATED DB: TARGETDB                    
DBREF  2Z0O A    1   385  UNP    Q9UKG1   DP13A_HUMAN      1    385             
SEQADV 2Z0O GLY A   -1  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2Z0O SER A    0  UNP  Q9UKG1              EXPRESSION TAG                 
SEQRES   1 A  387  GLY SER MSE PRO GLY ILE ASP LYS LEU PRO ILE GLU GLU          
SEQRES   2 A  387  THR LEU GLU ASP SER PRO GLN THR ARG SER LEU LEU GLY          
SEQRES   3 A  387  VAL PHE GLU GLU ASP ALA THR ALA ILE SER ASN TYR MSE          
SEQRES   4 A  387  ASN GLN LEU TYR GLN ALA MSE HIS ARG ILE TYR ASP ALA          
SEQRES   5 A  387  GLN ASN GLU LEU SER ALA ALA THR HIS LEU THR SER LYS          
SEQRES   6 A  387  LEU LEU LYS GLU TYR GLU LYS GLN ARG PHE PRO LEU GLY          
SEQRES   7 A  387  GLY ASP ASP GLU VAL MSE SER SER THR LEU GLN GLN PHE          
SEQRES   8 A  387  SER LYS VAL ILE ASP GLU LEU SER SER CYS HIS ALA VAL          
SEQRES   9 A  387  LEU SER THR GLN LEU ALA ASP ALA MSE MSE PHE PRO ILE          
SEQRES  10 A  387  THR GLN PHE LYS GLU ARG ASP LEU LYS GLU ILE LEU THR          
SEQRES  11 A  387  LEU LYS GLU VAL PHE GLN ILE ALA SER ASN ASP HIS ASP          
SEQRES  12 A  387  ALA ALA ILE ASN ARG TYR SER ARG LEU SER LYS LYS ARG          
SEQRES  13 A  387  GLU ASN ASP LYS VAL LYS TYR GLU VAL THR GLU ASP VAL          
SEQRES  14 A  387  TYR THR SER ARG LYS LYS GLN HIS GLN THR MSE MSE HIS          
SEQRES  15 A  387  TYR PHE CYS ALA LEU ASN THR LEU GLN TYR LYS LYS LYS          
SEQRES  16 A  387  ILE ALA LEU LEU GLU PRO LEU LEU GLY TYR MSE GLN ALA          
SEQRES  17 A  387  GLN ILE SER PHE PHE LYS MSE GLY SER GLU ASN LEU ASN          
SEQRES  18 A  387  GLU GLN LEU GLU GLU PHE LEU ALA ASN ILE GLY THR SER          
SEQRES  19 A  387  VAL GLN ASN VAL ARG ARG GLU MSE ASP SER ASP ILE GLU          
SEQRES  20 A  387  THR MSE GLN GLN THR ILE GLU ASP LEU GLU VAL ALA SER          
SEQRES  21 A  387  ASP PRO LEU TYR VAL PRO ASP PRO ASP PRO THR LYS PHE          
SEQRES  22 A  387  PRO VAL ASN ARG ASN LEU THR ARG LYS ALA GLY TYR LEU          
SEQRES  23 A  387  ASN ALA ARG ASN LYS THR GLY LEU VAL SER SER THR TRP          
SEQRES  24 A  387  ASP ARG GLN PHE TYR PHE THR GLN GLY GLY ASN LEU MSE          
SEQRES  25 A  387  SER GLN ALA ARG GLY ASP VAL ALA GLY GLY LEU ALA MSE          
SEQRES  26 A  387  ASP ILE ASP ASN CYS SER VAL MSE ALA VAL ASP CYS GLU          
SEQRES  27 A  387  ASP ARG ARG TYR CYS PHE GLN ILE THR SER PHE ASP GLY          
SEQRES  28 A  387  LYS LYS SER SER ILE LEU GLN ALA GLU SER LYS LYS ASP          
SEQRES  29 A  387  HIS GLU GLU TRP ILE CYS THR ILE ASN ASN ILE SER LYS          
SEQRES  30 A  387  GLN ILE TYR LEU SER GLU ASN PRO GLU GLU                      
MODRES 2Z0O MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A   37  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A   44  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A   82  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  111  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  112  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  178  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  179  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  204  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  213  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  240  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  247  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  310  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  323  MET  SELENOMETHIONINE                                   
MODRES 2Z0O MSE A  331  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
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    15(C5 H11 N O2 SE)                                           
FORMUL   2  HOH   *69(H2 O)                                                     
HELIX    1   1 PRO A    8  THR A   12  5                                   5    
HELIX    2   2 SER A   16  TYR A   68  1                                  53    
HELIX    3   3 ASP A   79  MSE A  111  1                                  33    
HELIX    4   4 MSE A  111  ARG A  121  1                                  11    
HELIX    5   5 ARG A  121  SER A  148  1                                  28    
HELIX    6   6 ASN A  156  GLU A  216  1                                  61    
HELIX    7   7 ASN A  219  ASP A  259  1                                  41    
HELIX    8   8 PRO A  260  TYR A  262  5                                   3    
HELIX    9   9 SER A  359  ASN A  372  1                                  14    
SHEET    1   A 7 GLY A 320  ASP A 324  0                                        
SHEET    2   A 7 ASN A 308  GLN A 312 -1  N  SER A 311   O  GLY A 320           
SHEET    3   A 7 ARG A 299  GLN A 305 -1  N  PHE A 303   O  MSE A 310           
SHEET    4   A 7 ALA A 281  ALA A 286 -1  N  GLY A 282   O  TYR A 302           
SHEET    5   A 7 LEU A 355  GLN A 356 -1  O  GLN A 356   N  ASN A 285           
SHEET    6   A 7 CYS A 341  THR A 345 -1  N  PHE A 342   O  LEU A 355           
SHEET    7   A 7 SER A 329  VAL A 333 -1  N  SER A 329   O  THR A 345           
LINK         C   MSE A   1                 N   PRO A   2     1555   1555  1.35  
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  1.33  
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  1.34  
LINK         C   MSE A 112                 N   PHE A 113     1555   1555  1.33  
LINK         C   THR A 177                 N   MSE A 178     1555   1555  1.32  
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  1.32  
LINK         C   LYS A 212                 N   MSE A 213     1555   1555  1.33  
LINK         C   MSE A 213                 N   GLY A 214     1555   1555  1.33  
LINK         C   GLU A 239                 N   MSE A 240     1555   1555  1.33  
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  103.449  111.003   36.853  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      0.009667  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009009  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027135        0.00000                         
HETATM    1  N   MSE A   1      35.445  15.720  56.428  1.00 67.47           N  
HETATM    2  CA  MSE A   1      36.522  16.535  55.795  1.00 68.30           C  
HETATM    3  C   MSE A   1      37.887  15.830  55.833  1.00 66.91           C  
HETATM    4  O   MSE A   1      38.495  15.589  54.786  1.00 68.15           O  
HETATM    5  CB  MSE A   1      36.615  17.906  56.492  1.00 70.77           C  
HETATM    6  CG  MSE A   1      37.692  18.871  55.966  1.00 73.90           C  
HETATM    7 SE   MSE A   1      37.059  20.277  54.741  1.00 83.11          SE  
HETATM    8  CE  MSE A   1      36.580  21.691  55.975  1.00 77.14           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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