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Database: PDB
Entry: 1E5W
LinkDB: 1E5W
Original site: 1E5W 
HEADER    MEMBRANE PROTEIN                        03-AUG-00   1E5W              
TITLE     STRUCTURE OF ISOLATED FERM DOMAIN AND FIRST LONG HELIX OF MOESIN      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MOESIN;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: FERM DOMAIN AND HELIX RESIDUE 1-345;                       
COMPND   5 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;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: BLR;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET;                                      
SOURCE  11 EXPRESSION_SYSTEM_GENE: MOESIN;                                      
SOURCE  12 OTHER_DETAILS: RECOMBINANT EXPRESSION IN E.COLI OF                   
SOURCE  13  NON-FUSION PROTEIN                                                  
KEYWDS    MEMBRANE PROTEIN, MOESIN, FERM, ERM                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.D.EDWARDS,N.H.KEEP                                                  
REVDAT   3   11-FEB-15 1E5W    1       TITLE  SOURCE JRNL   REMARK              
REVDAT   3 2                           VERSN  FORMUL                            
REVDAT   2   24-FEB-09 1E5W    1       VERSN                                    
REVDAT   1   27-JUN-01 1E5W    0                                                
JRNL        AUTH   S.D.EDWARDS,N.H.KEEP                                         
JRNL        TITL   THE 2.7 A CRYSTAL STRUCTURE OF THE ACTIVATED FERM            
JRNL        TITL 2 DOMAIN OF MOESIN: AN ANALYSIS OF STRUCTURAL                  
JRNL        TITL 3 CHANGES ON ACTIVATION                                        
JRNL        REF    BIOCHEMISTRY                  V.  40  7061 2001              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11401550                                                     
JRNL        DOI    10.1021/BI010419H                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.7  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1200346.62                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 19994                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.254                           
REMARK   3   FREE R VALUE                     : 0.297                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1019                            
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           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.8                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3077                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.427                        
REMARK   3   BIN FREE R VALUE                    : 0.450                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.9                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 160                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.036                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2889                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 36                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.3                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 73.5                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.35                                                
REMARK   3    B22 (A**2) : -5.35                                                
REMARK   3    B33 (A**2) : 10.71                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.45                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.48                            
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) : 0.55                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.63                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.3                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.2                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.88                            
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) : NULL  ; 1.5                  
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.0                  
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.0                  
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.5                  
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.314713                                             
REMARK   3   BSOL        : 38.5186                                              
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1E5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  04-AUG-00.                 
REMARK 100 THE PDBE ID CODE IS EBI-5226.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87, 1.3                          
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19994                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.24600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE, SHARP                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 66                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% ETHYLENE GLYCOL, 100MM HEPES PH7.5,  
REMARK 280  10-15 MG/ML PROTEIN                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       47.18000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.18000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       78.02500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.18000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.18000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       78.02500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.18000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.18000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       78.02500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.18000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.18000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       78.02500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  PROBABLY INVOLVED IN ANCHORING OF MAJOR CYTOSKELETAL                
REMARK 400  STRUCTURES TO THE PLASMA MEMBRANE.                                  
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    PRO A   2      137.36     12.05                                   
REMARK 500    THR A  36      -70.30    -51.34                                   
REMARK 500    GLU A  41       58.62    -90.51                                   
REMARK 500    ASP A  69       93.22    -24.29                                   
REMARK 500    SER A 144      131.78    -21.64                                   
REMARK 500    ALA A 148       -7.84    -47.15                                   
REMARK 500    LEU A 158     -169.91    -72.00                                   
REMARK 500    GLU A 159      -19.34     77.73                                   
REMARK 500    HIS A 161       28.26   -147.08                                   
REMARK 500    GLU A 169       -9.51    -59.47                                   
REMARK 500    ALA A 222       -4.74    -57.80                                   
REMARK 500    PHE A 240       65.51   -156.51                                   
REMARK 500    ASN A 247      128.53   -178.28                                   
REMARK 500    ASN A 251       84.84   -153.08                                   
REMARK 500    ASP A 252       79.04     46.32                                   
REMARK 500    LYS A 253        1.99     84.84                                   
REMARK 500    LYS A 262       82.00    -17.73                                   
REMARK 500    LYS A 263       71.95      8.20                                   
REMARK 500    PRO A 265     -137.67    -62.20                                   
REMARK 500    PRO A 272      -74.40    -55.51                                   
REMARK 500    THR A 299     -148.54    -72.44                                   
REMARK 500    GLN A 308        9.42    -65.80                                   
REMARK 500    GLU A 326       18.58    -67.71                                   
REMARK 500    LYS A 327      -19.27   -147.98                                   
REMARK 500    LYS A 339      -36.08    -37.14                                   
REMARK 500    GLU A 345       68.78   -105.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EF1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN             
REMARK 900  COMPLEX                                                             
DBREF  1E5W A    1     1  PDB    1E5W     1E5W             1      1             
DBREF  1E5W A    2   346  UNP    P26038   MOES_HUMAN       1    345             
SEQRES   1 A  346  MET PRO LYS THR ILE SER VAL ARG VAL THR THR MET ASP          
SEQRES   2 A  346  ALA GLU LEU GLU PHE ALA ILE GLN PRO ASN THR THR GLY          
SEQRES   3 A  346  LYS GLN LEU PHE ASP GLN VAL VAL LYS THR ILE GLY LEU          
SEQRES   4 A  346  ARG GLU VAL TRP PHE PHE GLY LEU GLN TYR GLN ASP THR          
SEQRES   5 A  346  LYS GLY PHE SER THR TRP LEU LYS LEU ASN LYS LYS VAL          
SEQRES   6 A  346  THR ALA GLN ASP VAL ARG LYS GLU SER PRO LEU LEU PHE          
SEQRES   7 A  346  LYS PHE ARG ALA LYS PHE TYR PRO GLU ASP VAL SER GLU          
SEQRES   8 A  346  GLU LEU ILE GLN ASP ILE THR GLN ARG LEU PHE PHE LEU          
SEQRES   9 A  346  GLN VAL LYS GLU GLY ILE LEU ASN ASP ASP ILE TYR CYS          
SEQRES  10 A  346  PRO PRO GLU THR ALA VAL LEU LEU ALA SER TYR ALA VAL          
SEQRES  11 A  346  GLN SER LYS TYR GLY ASP PHE ASN LYS GLU VAL HIS LYS          
SEQRES  12 A  346  SER GLY TYR LEU ALA GLY ASP LYS LEU LEU PRO GLN ARG          
SEQRES  13 A  346  VAL LEU GLU GLN HIS LYS LEU ASN LYS ASP GLN TRP GLU          
SEQRES  14 A  346  GLU ARG ILE GLN VAL TRP HIS GLU GLU HIS ARG GLY MET          
SEQRES  15 A  346  LEU ARG GLU ASP ALA VAL LEU GLU TYR LEU LYS ILE ALA          
SEQRES  16 A  346  GLN ASP LEU GLU MET TYR GLY VAL ASN TYR PHE SER ILE          
SEQRES  17 A  346  LYS ASN LYS LYS GLY SER GLU LEU TRP LEU GLY VAL ASP          
SEQRES  18 A  346  ALA LEU GLY LEU ASN ILE TYR GLU GLN ASN ASP ARG LEU          
SEQRES  19 A  346  THR PRO LYS ILE GLY PHE PRO TRP SER GLU ILE ARG ASN          
SEQRES  20 A  346  ILE SER PHE ASN ASP LYS LYS PHE VAL ILE LYS PRO ILE          
SEQRES  21 A  346  ASP LYS LYS ALA PRO ASP PHE VAL PHE TYR ALA PRO ARG          
SEQRES  22 A  346  LEU ARG ILE ASN LYS ARG ILE LEU ALA LEU CYS MET GLY          
SEQRES  23 A  346  ASN HIS GLU LEU TYR MET ARG ARG ARG LYS PRO ASP THR          
SEQRES  24 A  346  ILE GLU VAL GLN GLN MET LYS ALA GLN ALA ARG GLU GLU          
SEQRES  25 A  346  LYS HIS GLN LYS GLN MET GLU ARG ALA MET LEU GLU ASN          
SEQRES  26 A  346  GLU LYS LYS LYS ARG GLU MET ALA GLU LYS GLU LYS GLU          
SEQRES  27 A  346  LYS ILE GLU ARG GLU LYS GLU GLU                              
FORMUL   2  HOH   *36(H2 O)                                                     
HELIX    1   1 THR A   25  GLY A   38  1                                  14    
HELIX    2   2 GLU A   41  TRP A   43  5                                   3    
HELIX    3   3 VAL A   65  GLN A   68  5                                   4    
HELIX    4   4 ASP A   88  LEU A   93  1                                   6    
HELIX    5   5 GLN A   95  ASN A  112  1                                  18    
HELIX    6   6 PRO A  118  TYR A  134  1                                  17    
HELIX    7   7 ASN A  164  GLU A  178  1                                  15    
HELIX    8   8 LEU A  183  GLN A  196  1                                  14    
HELIX    9   9 ARG A  273  LYS A  296  1                                  24    
HELIX   10  10 ILE A  300  LYS A  344  1                                  45    
SHEET    1   A 5 LEU A  16  GLN A  21  0                                        
SHEET    2   A 5 THR A   4  THR A  10 -1  N  VAL A   9   O  LEU A  16           
SHEET    3   A 5 LEU A  76  ALA A  82  1  N  LEU A  76   O  ARG A   8           
SHEET    4   A 5 PHE A  45  GLN A  50 -1  N  GLN A  48   O  LYS A  79           
SHEET    5   A 5 SER A  56  TRP A  58 -1  N  THR A  57   O  TYR A  49           
SHEET    1   B 4 ASN A 204  LYS A 209  0                                        
SHEET    2   B 4 GLU A 215  ASP A 221 -1  N  VAL A 220   O  ASN A 204           
SHEET    3   B 4 GLY A 224  GLU A 229 -1  N  TYR A 228   O  TRP A 217           
SHEET    4   B 4 PRO A 236  PRO A 241 -1  N  PHE A 240   O  LEU A 225           
SHEET    1   C 3 PHE A 267  TYR A 270  0                                        
SHEET    2   C 3 LYS A 254  PRO A 259 -1  N  ILE A 257   O  PHE A 267           
SHEET    3   C 3 ILE A 245  PHE A 250 -1  N  SER A 249   O  VAL A 256           
CISPEP   1 SER A   74    PRO A   75          0         0.27                     
CRYST1   94.360   94.360  156.050  90.00  90.00  90.00 P 42 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010598  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010598  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006408        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system