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Database: PDB
Entry: 1EF1
LinkDB: 1EF1
Original site: 1EF1 
HEADER    MEMBRANE PROTEIN                        04-FEB-00   1EF1              
TITLE     CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MOESIN;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: N-TERMINAL FERM DOMAIN;                                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: MOESIN;                                                    
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: C-TERMINAL TAIL DOMAIN;                                    
COMPND  10 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: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MEMBRANE, FERM DOMAIN, TAIL DOMAIN, MEMBRANE PROTEIN                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.PEARSON,D.RECZEK,A.BRETSCHER,P.A.KARPLUS                          
REVDAT   4   13-JUL-11 1EF1    1       VERSN                                    
REVDAT   3   24-FEB-09 1EF1    1       VERSN                                    
REVDAT   2   01-APR-03 1EF1    1       JRNL                                     
REVDAT   1   10-MAY-00 1EF1    0                                                
JRNL        AUTH   M.A.PEARSON,D.RECZEK,A.BRETSCHER,P.A.KARPLUS                 
JRNL        TITL   STRUCTURE OF THE ERM PROTEIN MOESIN REVEALS THE FERM DOMAIN  
JRNL        TITL 2 FOLD MASKED BY AN EXTENDED ACTIN BINDING TAIL DOMAIN.        
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 101   259 2000              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   10847681                                                     
JRNL        DOI    10.1016/S0092-8674(00)80836-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 66990                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3568                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6266                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 412                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.016                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1EF1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010513.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-98; 15-MAY-98               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : CHESS; CHESS                       
REMARK 200  BEAMLINE                       : F1; F2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918; NULL                        
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; ADSC Q4            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71584                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MADSYS                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, LITHIUM SULFATE, HEPES, PH      
REMARK 280  7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   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       56.05000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.05000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D                            
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 13880 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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      153.30000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      112.10000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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      306.60000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      112.10000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 S    SO4 A2001  LIES ON A SPECIAL POSITION.                          
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  64    CG   CD   CE   NZ                                   
REMARK 470     ASP A  69    CG   OD1  OD2                                       
REMARK 470     LYS A  72    CG   CD   CE   NZ                                   
REMARK 470     LYS A 139    CG   CD   CE   NZ                                   
REMARK 470     ARG C 495    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 497    CG   OD1  OD2                                       
REMARK 470     MET C 499    CG   SD   CE                                        
REMARK 470     GLU C 516    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 517    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  64    CG   CD   CE   NZ                                   
REMARK 470     ASP B  69    CG   OD1  OD2                                       
REMARK 470     LYS B  72    CG   CD   CE   NZ                                   
REMARK 470     LYS B 139    CG   CD   CE   NZ                                   
REMARK 470     ARG D 495    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 497    CG   OD1  OD2                                       
REMARK 470     MET D 499    CG   SD   CE                                        
REMARK 470     GLU D 516    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 517    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MSE A 200  SE     MSE A 200   CE     -0.564                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 197   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    PRO A 259   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO A 297   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASP A  13       28.05   -147.59                                   
REMARK 500    ARG A  71       97.14    -60.78                                   
REMARK 500    LYS A  72      109.33    -49.70                                   
REMARK 500    LYS A 212        1.11    -69.04                                   
REMARK 500    ASP A 252     -116.48     58.92                                   
REMARK 500    ASP A 261     -114.85    169.93                                   
REMARK 500    LYS A 262      -24.41   -179.71                                   
REMARK 500    ALA C 500     -173.05    -67.97                                   
REMARK 500    LYS C 501      135.50    171.71                                   
REMARK 500    ASP B  13       21.62   -140.34                                   
REMARK 500    ASP B  69       45.67    -75.25                                   
REMARK 500    ARG B  71       91.79    -54.56                                   
REMARK 500    LYS B  72      109.83    -45.46                                   
REMARK 500    LEU B  93       74.40   -112.71                                   
REMARK 500    SER B 243        0.67    -63.25                                   
REMARK 500    ASP B 252     -114.24     66.96                                   
REMARK 500    ASP B 261     -113.10    170.56                                   
REMARK 500    LYS B 262      -32.44   -178.34                                   
REMARK 500    ALA D 492      117.99   -167.18                                   
REMARK 500    ASP D 497       63.19   -104.64                                   
REMARK 500    ALA D 498      105.83    -34.75                                   
REMARK 500    ARG D 503       13.84     58.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3001                
DBREF  1EF1 A    4   297  UNP    P26038   MOES_HUMAN       3    296             
DBREF  1EF1 C  488   577  UNP    P26038   MOES_HUMAN     487    576             
DBREF  1EF1 B    4   297  UNP    P26038   MOES_HUMAN       3    296             
DBREF  1EF1 D  488   577  UNP    P26038   MOES_HUMAN     487    576             
SEQADV 1EF1 MSE A   12  UNP  P26038    MET    11 MODIFIED RESIDUE               
SEQADV 1EF1 MSE A  182  UNP  P26038    MET   181 MODIFIED RESIDUE               
SEQADV 1EF1 MSE A  200  UNP  P26038    MET   199 MODIFIED RESIDUE               
SEQADV 1EF1 MSE A  285  UNP  P26038    MET   184 MODIFIED RESIDUE               
SEQADV 1EF1 MSE A  292  UNP  P26038    MET   291 MODIFIED RESIDUE               
SEQADV 1EF1 MSE C  543  UNP  P26038    MET   542 MODIFIED RESIDUE               
SEQADV 1EF1 MSE C  549  UNP  P26038    MET   548 MODIFIED RESIDUE               
SEQADV 1EF1 MSE C  577  UNP  P26038    MET   576 MODIFIED RESIDUE               
SEQADV 1EF1 MSE B   12  UNP  P26038    MET    11 MODIFIED RESIDUE               
SEQADV 1EF1 MSE B  182  UNP  P26038    MET   181 MODIFIED RESIDUE               
SEQADV 1EF1 MSE B  200  UNP  P26038    MET   199 MODIFIED RESIDUE               
SEQADV 1EF1 MSE B  285  UNP  P26038    MET   184 MODIFIED RESIDUE               
SEQADV 1EF1 MSE B  292  UNP  P26038    MET   291 MODIFIED RESIDUE               
SEQADV 1EF1 MSE D  543  UNP  P26038    MET   542 MODIFIED RESIDUE               
SEQADV 1EF1 MSE D  549  UNP  P26038    MET   548 MODIFIED RESIDUE               
SEQADV 1EF1 MSE D  577  UNP  P26038    MET   576 MODIFIED RESIDUE               
SEQRES   1 A  294  THR ILE SER VAL ARG VAL THR THR MSE ASP ALA GLU LEU          
SEQRES   2 A  294  GLU PHE ALA ILE GLN PRO ASN THR THR GLY LYS GLN LEU          
SEQRES   3 A  294  PHE ASP GLN VAL VAL LYS THR ILE GLY LEU ARG GLU VAL          
SEQRES   4 A  294  TRP PHE PHE GLY LEU GLN TYR GLN ASP THR LYS GLY PHE          
SEQRES   5 A  294  SER THR TRP LEU LYS LEU ASN LYS LYS VAL THR ALA GLN          
SEQRES   6 A  294  ASP VAL ARG LYS GLU SER PRO LEU LEU PHE LYS PHE ARG          
SEQRES   7 A  294  ALA LYS PHE TYR PRO GLU ASP VAL SER GLU GLU LEU ILE          
SEQRES   8 A  294  GLN ASP ILE THR GLN ARG LEU PHE PHE LEU GLN VAL LYS          
SEQRES   9 A  294  GLU GLY ILE LEU ASN ASP ASP ILE TYR CYS PRO PRO GLU          
SEQRES  10 A  294  THR ALA VAL LEU LEU ALA SER TYR ALA VAL GLN SER LYS          
SEQRES  11 A  294  TYR GLY ASP PHE ASN LYS GLU VAL HIS LYS SER GLY TYR          
SEQRES  12 A  294  LEU ALA GLY ASP LYS LEU LEU PRO GLN ARG VAL LEU GLU          
SEQRES  13 A  294  GLN HIS LYS LEU ASN LYS ASP GLN TRP GLU GLU ARG ILE          
SEQRES  14 A  294  GLN VAL TRP HIS GLU GLU HIS ARG GLY MSE LEU ARG GLU          
SEQRES  15 A  294  ASP ALA VAL LEU GLU TYR LEU LYS ILE ALA GLN ASP LEU          
SEQRES  16 A  294  GLU MSE TYR GLY VAL ASN TYR PHE SER ILE LYS ASN LYS          
SEQRES  17 A  294  LYS GLY SER GLU LEU TRP LEU GLY VAL ASP ALA LEU GLY          
SEQRES  18 A  294  LEU ASN ILE TYR GLU GLN ASN ASP ARG LEU THR PRO LYS          
SEQRES  19 A  294  ILE GLY PHE PRO TRP SER GLU ILE ARG ASN ILE SER PHE          
SEQRES  20 A  294  ASN ASP LYS LYS PHE VAL ILE LYS PRO ILE ASP LYS LYS          
SEQRES  21 A  294  ALA PRO ASP PHE VAL PHE TYR ALA PRO ARG LEU ARG ILE          
SEQRES  22 A  294  ASN LYS ARG ILE LEU ALA LEU CYS MSE GLY ASN HIS GLU          
SEQRES  23 A  294  LEU TYR MSE ARG ARG ARG LYS PRO                              
SEQRES   1 C   90  ALA GLU ALA SER ALA ASP LEU ARG ALA ASP ALA MET ALA          
SEQRES   2 C   90  LYS ASP ARG SER GLU GLU GLU ARG THR THR GLU ALA GLU          
SEQRES   3 C   90  LYS ASN GLU ARG VAL GLN LYS HIS LEU LYS ALA LEU THR          
SEQRES   4 C   90  SER GLU LEU ALA ASN ALA ARG ASP GLU SER LYS LYS THR          
SEQRES   5 C   90  ALA ASN ASP MSE ILE HIS ALA GLU ASN MSE ARG LEU GLY          
SEQRES   6 C   90  ARG ASP LYS TYR LYS THR LEU ARG GLN ILE ARG GLN GLY          
SEQRES   7 C   90  ASN THR LYS GLN ARG ILE ASP GLU PHE GLU SER MSE              
SEQRES   1 B  294  THR ILE SER VAL ARG VAL THR THR MSE ASP ALA GLU LEU          
SEQRES   2 B  294  GLU PHE ALA ILE GLN PRO ASN THR THR GLY LYS GLN LEU          
SEQRES   3 B  294  PHE ASP GLN VAL VAL LYS THR ILE GLY LEU ARG GLU VAL          
SEQRES   4 B  294  TRP PHE PHE GLY LEU GLN TYR GLN ASP THR LYS GLY PHE          
SEQRES   5 B  294  SER THR TRP LEU LYS LEU ASN LYS LYS VAL THR ALA GLN          
SEQRES   6 B  294  ASP VAL ARG LYS GLU SER PRO LEU LEU PHE LYS PHE ARG          
SEQRES   7 B  294  ALA LYS PHE TYR PRO GLU ASP VAL SER GLU GLU LEU ILE          
SEQRES   8 B  294  GLN ASP ILE THR GLN ARG LEU PHE PHE LEU GLN VAL LYS          
SEQRES   9 B  294  GLU GLY ILE LEU ASN ASP ASP ILE TYR CYS PRO PRO GLU          
SEQRES  10 B  294  THR ALA VAL LEU LEU ALA SER TYR ALA VAL GLN SER LYS          
SEQRES  11 B  294  TYR GLY ASP PHE ASN LYS GLU VAL HIS LYS SER GLY TYR          
SEQRES  12 B  294  LEU ALA GLY ASP LYS LEU LEU PRO GLN ARG VAL LEU GLU          
SEQRES  13 B  294  GLN HIS LYS LEU ASN LYS ASP GLN TRP GLU GLU ARG ILE          
SEQRES  14 B  294  GLN VAL TRP HIS GLU GLU HIS ARG GLY MSE LEU ARG GLU          
SEQRES  15 B  294  ASP ALA VAL LEU GLU TYR LEU LYS ILE ALA GLN ASP LEU          
SEQRES  16 B  294  GLU MSE TYR GLY VAL ASN TYR PHE SER ILE LYS ASN LYS          
SEQRES  17 B  294  LYS GLY SER GLU LEU TRP LEU GLY VAL ASP ALA LEU GLY          
SEQRES  18 B  294  LEU ASN ILE TYR GLU GLN ASN ASP ARG LEU THR PRO LYS          
SEQRES  19 B  294  ILE GLY PHE PRO TRP SER GLU ILE ARG ASN ILE SER PHE          
SEQRES  20 B  294  ASN ASP LYS LYS PHE VAL ILE LYS PRO ILE ASP LYS LYS          
SEQRES  21 B  294  ALA PRO ASP PHE VAL PHE TYR ALA PRO ARG LEU ARG ILE          
SEQRES  22 B  294  ASN LYS ARG ILE LEU ALA LEU CYS MSE GLY ASN HIS GLU          
SEQRES  23 B  294  LEU TYR MSE ARG ARG ARG LYS PRO                              
SEQRES   1 D   90  ALA GLU ALA SER ALA ASP LEU ARG ALA ASP ALA MET ALA          
SEQRES   2 D   90  LYS ASP ARG SER GLU GLU GLU ARG THR THR GLU ALA GLU          
SEQRES   3 D   90  LYS ASN GLU ARG VAL GLN LYS HIS LEU LYS ALA LEU THR          
SEQRES   4 D   90  SER GLU LEU ALA ASN ALA ARG ASP GLU SER LYS LYS THR          
SEQRES   5 D   90  ALA ASN ASP MSE ILE HIS ALA GLU ASN MSE ARG LEU GLY          
SEQRES   6 D   90  ARG ASP LYS TYR LYS THR LEU ARG GLN ILE ARG GLN GLY          
SEQRES   7 D   90  ASN THR LYS GLN ARG ILE ASP GLU PHE GLU SER MSE              
MODRES 1EF1 MSE A   12  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE A  182  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE A  200  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE A  285  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE A  292  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE C  543  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE C  549  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE C  577  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE B   12  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE B  182  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE B  200  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE B  285  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE B  292  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE D  543  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE D  549  MET  SELENOMETHIONINE                                   
MODRES 1EF1 MSE D  577  MET  SELENOMETHIONINE                                   
HET    MSE  A  12       8                                                       
HET    MSE  A 182       8                                                       
HET    MSE  A 200       8                                                       
HET    MSE  A 285       8                                                       
HET    MSE  A 292       8                                                       
HET    MSE  C 543       8                                                       
HET    MSE  C 549       8                                                       
HET    MSE  C 577       9                                                       
HET    MSE  B  12       8                                                       
HET    MSE  B 182       8                                                       
HET    MSE  B 200       8                                                       
HET    MSE  B 285       8                                                       
HET    MSE  B 292       8                                                       
HET    MSE  D 543       8                                                       
HET    MSE  D 549       8                                                       
HET    MSE  D 577       9                                                       
HET    SO4  A2001       5                                                       
HET    SO4  B3001       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   7  HOH   *412(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  GLY A  135  1                                  18    
HELIX    7   7 PRO A  154  HIS A  161  1                                   8    
HELIX    8   8 ASN A  164  HIS A  179  1                                  16    
HELIX    9   9 LEU A  183  GLN A  196  1                                  14    
HELIX   10  10 ARG A  273  LYS A  296  1                                  24    
HELIX   11  11 ARG C  503  ARG C  508  5                                   6    
HELIX   12  12 THR C  510  ASN C  515  1                                   6    
HELIX   13  13 ASN C  515  ASN C  531  1                                  17    
HELIX   14  14 THR C  539  LEU C  551  1                                  13    
HELIX   15  15 ASP C  554  ARG C  563  1                                  10    
HELIX   16  16 ASN C  566  SER C  576  1                                  11    
HELIX   17  17 THR B   25  GLY B   38  1                                  14    
HELIX   18  18 GLU B   41  TRP B   43  5                                   3    
HELIX   19  19 ASP B   88  LEU B   93  1                                   6    
HELIX   20  20 GLN B   95  ASN B  112  1                                  18    
HELIX   21  21 PRO B  118  GLY B  135  1                                  18    
HELIX   22  22 PRO B  154  HIS B  161  1                                   8    
HELIX   23  23 ASN B  164  HIS B  179  1                                  16    
HELIX   24  24 LEU B  183  GLN B  196  1                                  14    
HELIX   25  25 ARG B  273  LYS B  296  1                                  24    
HELIX   26  26 ARG D  503  ARG D  508  5                                   6    
HELIX   27  27 THR D  510  ASN D  515  1                                   6    
HELIX   28  28 ASN D  515  ASN D  531  1                                  17    
HELIX   29  29 THR D  539  LEU D  551  1                                  13    
HELIX   30  30 ASP D  554  ARG D  563  1                                  10    
HELIX   31  31 ASN D  566  MSE D  577  1                                  12    
SHEET    1   A 5 ALA A  14  ILE A  20  0                                        
SHEET    2   A 5 ILE A   5  THR A  11 -1  N  ILE A   5   O  ILE A  20           
SHEET    3   A 5 LEU A  76  ALA A  82  1  O  LEU A  76   N  ARG A   8           
SHEET    4   A 5 PHE A  45  GLN A  50 -1  N  GLY A  46   O  ARG A  81           
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  LEU A 216   O  ILE A 208           
SHEET    3   B 4 GLY A 224  GLU A 229 -1  O  GLY A 224   N  ASP A 221           
SHEET    4   B 4 ILE A 238  PRO A 241 -1  O  ILE A 238   N  ILE A 227           
SHEET    1   C 3 ILE A 245  ASN A 251  0                                        
SHEET    2   C 3 LYS A 254  PRO A 259 -1  O  LYS A 254   N  ASN A 251           
SHEET    3   C 3 PHE A 267  TYR A 270 -1  O  PHE A 267   N  ILE A 257           
SHEET    1   D 5 GLU B  15  ILE B  20  0                                        
SHEET    2   D 5 ILE B   5  THR B  10 -1  N  ILE B   5   O  ILE B  20           
SHEET    3   D 5 LEU B  76  ALA B  82  1  O  LEU B  76   N  ARG B   8           
SHEET    4   D 5 PHE B  45  GLN B  50 -1  N  GLY B  46   O  ARG B  81           
SHEET    5   D 5 SER B  56  TRP B  58 -1  N  THR B  57   O  TYR B  49           
SHEET    1   E 4 ASN B 204  LYS B 209  0                                        
SHEET    2   E 4 GLU B 215  ASP B 221 -1  N  LEU B 216   O  ILE B 208           
SHEET    3   E 4 GLY B 224  GLU B 229 -1  O  GLY B 224   N  ASP B 221           
SHEET    4   E 4 ILE B 238  PRO B 241 -1  O  ILE B 238   N  ILE B 227           
SHEET    1   F 3 ILE B 245  ASN B 251  0                                        
SHEET    2   F 3 LYS B 254  PRO B 259 -1  O  LYS B 254   N  ASN B 251           
SHEET    3   F 3 PHE B 267  TYR B 270 -1  N  PHE B 267   O  ILE B 257           
LINK         C   THR A  11                 N   MSE A  12     1555   1555  1.32  
LINK         C   MSE A  12                 N   ASP A  13     1555   1555  1.33  
LINK         C   GLY A 181                 N   MSE A 182     1555   1555  1.33  
LINK         C   MSE A 182                 N   LEU A 183     1555   1555  1.33  
LINK         C   GLU A 199                 N   MSE A 200     1555   1555  1.32  
LINK         C   MSE A 200                 N   TYR A 201     1555   1555  1.32  
LINK         C   CYS A 284                 N   MSE A 285     1555   1555  1.33  
LINK         C   MSE A 285                 N   GLY A 286     1555   1555  1.33  
LINK         C   TYR A 291                 N   MSE A 292     1555   1555  1.33  
LINK         C   MSE A 292                 N   ARG A 293     1555   1555  1.33  
LINK         C   THR B  11                 N   MSE B  12     1555   1555  1.32  
LINK         C   MSE B  12                 N   ASP B  13     1555   1555  1.33  
LINK         C   GLY B 181                 N   MSE B 182     1555   1555  1.32  
LINK         C   MSE B 182                 N   LEU B 183     1555   1555  1.33  
LINK         C   GLU B 199                 N   MSE B 200     1555   1555  1.33  
LINK         C   MSE B 200                 N   TYR B 201     1555   1555  1.33  
LINK         C   CYS B 284                 N   MSE B 285     1555   1555  1.34  
LINK         C   MSE B 285                 N   GLY B 286     1555   1555  1.33  
LINK         C   TYR B 291                 N   MSE B 292     1555   1555  1.33  
LINK         C   MSE B 292                 N   ARG B 293     1555   1555  1.34  
LINK         C   ASP C 542                 N   MSE C 543     1555   1555  1.33  
LINK         C   MSE C 543                 N   ILE C 544     1555   1555  1.32  
LINK         C   ASN C 548                 N   MSE C 549     1555   1555  1.34  
LINK         C   MSE C 549                 N   ARG C 550     1555   1555  1.34  
LINK         C   SER C 576                 N   MSE C 577     1555   1555  1.33  
LINK         C   ASP D 542                 N   MSE D 543     1555   1555  1.32  
LINK         C   MSE D 543                 N   ILE D 544     1555   1555  1.33  
LINK         C   ASN D 548                 N   MSE D 549     1555   1555  1.34  
LINK         C   MSE D 549                 N   ARG D 550     1555   1555  1.33  
LINK         C   SER D 576                 N   MSE D 577     1555   1555  1.34  
CISPEP   1 SER A   74    PRO A   75          0        -0.20                     
CISPEP   2 SER B   74    PRO B   75          0        -0.72                     
SITE     1 AC1  3 GLN A  95  ASP A  96  HOH A 726                               
SITE     1 AC2  4 GLN B  95  ASP B  96  ILE B  97  HOH B1726                    
CRYST1   54.200  153.300  112.100  90.00  90.00  90.00 P 2 2 21      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      0.018450  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006523  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008921        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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