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Database: PDB
Entry: 2Q12
LinkDB: 2Q12
Original site: 2Q12 
HEADER    PROTEIN TRANSPORT                       23-MAY-07   2Q12              
TITLE     CRYSTAL STRUCTURE OF BAR DOMAIN OF APPL1                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DCC-INTERACTING PROTEIN 13 ALPHA;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 5-265, BAR DOMAIN;                                
COMPND   5 SYNONYM: DIP13 ALPHA;                                                
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: APPL1, APPL, DIP13A, KIAA1428;                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    APPL1, BAR DOMAIN, PROTEIN TRANSPORT                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.C.ZHANG,G.ZHU                                                       
REVDAT   3   13-JUL-11 2Q12    1       VERSN                                    
REVDAT   2   24-FEB-09 2Q12    1       VERSN                                    
REVDAT   1   14-AUG-07 2Q12    0                                                
JRNL        AUTH   G.ZHU,J.CHEN,J.LIU,J.S.BRUNZELLE,B.HUANG,N.WAKEHAM,          
JRNL        AUTH 2 S.TERZYAN,X.LI,Z.RAO,G.LI,X.C.ZHANG                          
JRNL        TITL   STRUCTURE OF THE APPL1 BAR-PH DOMAIN AND CHARACTERIZATION OF 
JRNL        TITL 2 ITS INTERACTION WITH RAB5.                                   
JRNL        REF    EMBO J.                       V.  26  3484 2007              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   17581628                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7601771                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22273                          
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 + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1200                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.79                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1249                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1966                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 147                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.99000                                              
REMARK   3    B22 (A**2) : -2.54000                                             
REMARK   3    B33 (A**2) : -1.45000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.155         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.146         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.106         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.355         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2025 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2734 ; 1.505 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   254 ; 4.586 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;36.524 ;25.577       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   398 ;16.695 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;21.261 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   309 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1512 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   914 ; 0.216 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1440 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   123 ; 0.156 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   125 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    18 ; 0.122 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1277 ; 3.374 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1993 ; 4.269 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   841 ; 4.328 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   734 ; 6.155 ; 3.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2Q12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAY-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043015.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE-CRYSTAL      
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23518                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.190                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MAGNESIUM FORMATE, PH 8.0, VAPOR   
REMARK 280  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       26.49250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       64.59950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.49250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       64.59950            
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 DIMER IS GENERATED FROM MOLECULES IN          
REMARK 300 ASYMMETRIC UNIT AND OPERATION -X+1, -Y, Z                            
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: 8640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 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       52.98500            
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     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MSE A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     THR A    12                                                      
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     PRO A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     TYR A   262                                                      
REMARK 465     VAL A   263                                                      
REMARK 465     PRO A   264                                                      
REMARK 465     ASP A   265                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   404     O    HOH A   412              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2Q13   RELATED DB: PDB                                   
DBREF  2Q12 A    5   265  UNP    Q9UKG1   DP13A_HUMAN      5    265             
SEQADV 2Q12 GLY A    1  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2Q12 SER A    2  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2Q12 HIS A    3  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2Q12 MSE A    4  UNP  Q9UKG1              EXPRESSION TAG                 
SEQRES   1 A  265  GLY SER HIS MSE ASP LYS LEU PRO ILE GLU GLU THR LEU          
SEQRES   2 A  265  GLU ASP SER PRO GLN THR ARG SER LEU LEU GLY VAL PHE          
SEQRES   3 A  265  GLU GLU ASP ALA THR ALA ILE SER ASN TYR MSE ASN GLN          
SEQRES   4 A  265  LEU TYR GLN ALA MSE HIS ARG ILE TYR ASP ALA GLN ASN          
SEQRES   5 A  265  GLU LEU SER ALA ALA THR HIS LEU THR SER LYS LEU LEU          
SEQRES   6 A  265  LYS GLU TYR GLU LYS GLN ARG PHE PRO LEU GLY GLY ASP          
SEQRES   7 A  265  ASP GLU VAL MSE SER SER THR LEU GLN GLN PHE SER LYS          
SEQRES   8 A  265  VAL ILE ASP GLU LEU SER SER CYS HIS ALA VAL LEU SER          
SEQRES   9 A  265  THR GLN LEU ALA ASP ALA MSE MSE PHE PRO ILE THR GLN          
SEQRES  10 A  265  PHE LYS GLU ARG ASP LEU LYS GLU ILE LEU THR LEU LYS          
SEQRES  11 A  265  GLU VAL PHE GLN ILE ALA SER ASN ASP HIS ASP ALA ALA          
SEQRES  12 A  265  ILE ASN ARG TYR SER ARG LEU SER LYS LYS ARG GLU ASN          
SEQRES  13 A  265  ASP LYS VAL LYS TYR GLU VAL THR GLU ASP VAL TYR THR          
SEQRES  14 A  265  SER ARG LYS LYS GLN HIS GLN THR MSE MSE HIS TYR PHE          
SEQRES  15 A  265  CYS ALA LEU ASN THR LEU GLN TYR LYS LYS LYS ILE ALA          
SEQRES  16 A  265  LEU LEU GLU PRO LEU LEU GLY TYR MSE GLN ALA GLN ILE          
SEQRES  17 A  265  SER PHE PHE LYS MSE GLY SER GLU ASN LEU ASN GLU GLN          
SEQRES  18 A  265  LEU GLU GLU PHE LEU ALA ASN ILE GLY THR SER VAL GLN          
SEQRES  19 A  265  ASN VAL ARG ARG GLU MSE ASP SER ASP ILE GLU THR MSE          
SEQRES  20 A  265  GLN GLN THR ILE GLU ASP LEU GLU VAL ALA SER ASP PRO          
SEQRES  21 A  265  LEU TYR VAL PRO ASP                                          
MODRES 2Q12 MSE A   37  MET  SELENOMETHIONINE                                   
MODRES 2Q12 MSE A   44  MET  SELENOMETHIONINE                                   
MODRES 2Q12 MSE A   82  MET  SELENOMETHIONINE                                   
MODRES 2Q12 MSE A  111  MET  SELENOMETHIONINE                                   
MODRES 2Q12 MSE A  112  MET  SELENOMETHIONINE                                   
MODRES 2Q12 MSE A  178  MET  SELENOMETHIONINE                                   
MODRES 2Q12 MSE A  179  MET  SELENOMETHIONINE                                   
MODRES 2Q12 MSE A  204  MET  SELENOMETHIONINE                                   
MODRES 2Q12 MSE A  213  MET  SELENOMETHIONINE                                   
MODRES 2Q12 MSE A  240  MET  SELENOMETHIONINE                                   
MODRES 2Q12 MSE A  247  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                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    11(C5 H11 N O2 SE)                                           
FORMUL   2  HOH   *147(H2 O)                                                    
HELIX    1   1 ASP A   15  GLU A   67  1                                  53    
HELIX    2   2 TYR A   68  GLN A   71  5                                   4    
HELIX    3   3 GLU A   80  MSE A  111  1                                  32    
HELIX    4   4 MSE A  111  ARG A  121  1                                  11    
HELIX    5   5 ARG A  121  LYS A  152  1                                  32    
HELIX    6   6 ASN A  156  LEU A  218  1                                  63    
HELIX    7   7 ASN A  219  SER A  258  1                                  40    
LINK         C   TYR A  36                 N   MSE A  37     1555   1555  1.32  
LINK         C   MSE A  37                 N   ASN A  38     1555   1555  1.33  
LINK         C   ALA A  43                 N   MSE A  44     1555   1555  1.32  
LINK         C   MSE A  44                 N   HIS A  45     1555   1555  1.34  
LINK         C   VAL A  81                 N   MSE A  82     1555   1555  1.34  
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  1.35  
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  1.34  
LINK         C   MSE A 204                 N   GLN A 205     1555   1555  1.33  
LINK         C   LYS A 212                 N   MSE A 213     1555   1555  1.33  
LINK         C   MSE A 213                 N   GLY A 214     1555   1555  1.33  
LINK         C   GLU A 239                 N   MSE A 240     1555   1555  1.34  
LINK         C   MSE A 240                 N   ASP A 241     1555   1555  1.33  
LINK         C   THR A 246                 N   MSE A 247     1555   1555  1.34  
LINK         C   MSE A 247                 N   GLN A 248     1555   1555  1.32  
CRYST1   52.985  129.199   36.854  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      0.018873  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007740  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027134        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system