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Database: PDB
Entry: 4RM9
LinkDB: 4RM9
Original site: 4RM9 
HEADER    PEPTIDE BINDING PROTEIN                 21-OCT-14   4RM9              
TITLE     CRYSTAL STRUCTURE OF HUMAN EZRIN IN SPACE GROUP C2221                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EZRIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYTOVILLIN, VILLIN-2, P81;                                  
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 GENE: EZR, VIL2;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    FERM DOMAIN, C-ERMAD DOMAIN, MEMBRANE CYTOSKELETON LINKERS, ACTIN     
KEYWDS   2 BINDING, PEPTIDE BINDING PROTEIN                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.PHANG,S.J.HARROP,R.DAVIES,A.P.DUFF,K.E.WILK,P.M.G.CURMI           
REVDAT   2   27-SEP-17 4RM9    1       JRNL   REMARK                            
REVDAT   1   09-DEC-15 4RM9    0                                                
JRNL        AUTH   J.M.PHANG,S.J.HARROP,A.P.DUFF,A.V.SOKOLOVA,B.CROSSETT,       
JRNL        AUTH 2 J.C.WALSH,S.A.BECKHAM,C.D.NGUYEN,R.B.DAVIES,C.GLOCKNER,      
JRNL        AUTH 3 E.H.BROMLEY,K.E.WILK,P.M.CURMI                               
JRNL        TITL   STRUCTURAL CHARACTERIZATION SUGGESTS MODELS FOR MONOMERIC    
JRNL        TITL 2 AND DIMERIC FORMS OF FULL-LENGTH EZRIN.                      
JRNL        REF    BIOCHEM. J.                   V. 473  2763 2016              
JRNL        REFN                   ESSN 1470-8728                               
JRNL        PMID   27364155                                                     
JRNL        DOI    10.1042/BCJ20160541                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.3_473)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.24                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 28746                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1467                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 40.2440 -  4.3074    0.98     2877   151  0.1794 0.2231        
REMARK   3     2  4.3074 -  3.4195    0.98     2790   134  0.1765 0.2035        
REMARK   3     3  3.4195 -  2.9874    0.98     2737   154  0.2037 0.2522        
REMARK   3     4  2.9874 -  2.7143    0.98     2727   155  0.2280 0.2731        
REMARK   3     5  2.7143 -  2.5198    0.98     2732   128  0.2374 0.3028        
REMARK   3     6  2.5198 -  2.3712    0.98     2705   140  0.2419 0.3045        
REMARK   3     7  2.3712 -  2.2525    0.98     2706   146  0.2496 0.3374        
REMARK   3     8  2.2525 -  2.1545    0.98     2700   146  0.2534 0.3285        
REMARK   3     9  2.1545 -  2.0715    0.97     2630   173  0.2660 0.3271        
REMARK   3    10  2.0715 -  2.0000    0.97     2675   140  0.2636 0.3057        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 47.33                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.530           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.28540                                             
REMARK   3    B22 (A**2) : -1.35890                                             
REMARK   3    B33 (A**2) : -8.92650                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3151                                  
REMARK   3   ANGLE     :  0.735           4239                                  
REMARK   3   CHIRALITY :  0.057            447                                  
REMARK   3   PLANARITY :  0.003            550                                  
REMARK   3   DIHEDRAL  : 12.637           1235                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 1:297)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4624   3.9183  25.8414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0611 T22:   0.1483                                     
REMARK   3      T33:   0.0046 T12:  -0.0947                                     
REMARK   3      T13:   0.0345 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6924 L22:   0.6395                                     
REMARK   3      L33:   4.0637 L12:  -0.1205                                     
REMARK   3      L13:   0.0750 L23:   0.4691                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1461 S12:  -0.3749 S13:   0.0393                       
REMARK   3      S21:   0.0759 S22:  -0.0995 S23:   0.0642                       
REMARK   3      S31:   0.0430 S32:   0.3337 S33:  -0.1138                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 516:540)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -17.9806  -8.8219   5.4650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3746 T22:   0.3852                                     
REMARK   3      T33:   0.0996 T12:   0.0664                                     
REMARK   3      T13:   0.0181 T23:  -0.0249                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5301 L22:   1.8062                                     
REMARK   3      L33:   2.0555 L12:   0.1573                                     
REMARK   3      L13:  -0.5058 L23:  -0.9574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0583 S12:   0.1541 S13:   0.0961                       
REMARK   3      S21:  -0.5147 S22:   0.0558 S23:  -0.3247                       
REMARK   3      S31:   0.5449 S32:   0.5334 S33:  -0.0892                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 541:574)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -26.6013   4.5505   5.6994              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2464 T22:   0.2226                                     
REMARK   3      T33:   0.2085 T12:   0.0287                                     
REMARK   3      T13:  -0.0617 T23:  -0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6386 L22:   2.6368                                     
REMARK   3      L33:   3.2526 L12:   0.1641                                     
REMARK   3      L13:   0.8039 L23:   2.4860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1778 S12:   0.1270 S13:   0.0612                       
REMARK   3      S21:  -0.7911 S22:  -0.1157 S23:   0.2197                       
REMARK   3      S31:  -0.6023 S32:  -0.2527 S33:   0.2427                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 575:586)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9328  26.2458   7.6066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5806 T22:   0.1607                                     
REMARK   3      T33:   0.3726 T12:  -0.1299                                     
REMARK   3      T13:  -0.0088 T23:  -0.0436                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4931 L22:   0.3533                                     
REMARK   3      L33:   0.7734 L12:   0.6007                                     
REMARK   3      L13:  -0.4561 L23:  -0.4529                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0228 S12:  -0.0138 S13:   0.7809                       
REMARK   3      S21:  -0.3346 S22:   0.0730 S23:   0.3302                       
REMARK   3      S31:  -1.3801 S32:   0.0982 S33:  -0.0443                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: AUTHORS DO NOT OBSERVE RESIDUES 298-515   
REMARK   3  (THE ALPHA-HELICAL DOMAIN) IN THE CRYSTAL STRUCTURE. THEY           
REMARK   3  SUSPECT LIMITED PROTEOLYSIS DURING CRYSTALLISATION                  
REMARK   4                                                                      
REMARK   4 4RM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000087520.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.954                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28759                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.970                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -4.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 14.00                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : 0.11800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.80900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.80900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2I1J                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 19.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 5.5, 18% PEG3350,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 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       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       55.88650            
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       55.88650            
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   SMTRY1   5  1.000000  0.000000  0.000000       33.71650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.75850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.71650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.75850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       55.88650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.71650            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.75850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       55.88650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.71650            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.75850            
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: PISA                                                  
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 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      HOH A 739  LIES ON A SPECIAL POSITION.                          
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     0                                                      
REMARK 465     ASP A   298                                                      
REMARK 465     THR A   299                                                      
REMARK 465     ILE A   300                                                      
REMARK 465     GLU A   301                                                      
REMARK 465     VAL A   302                                                      
REMARK 465     GLN A   303                                                      
REMARK 465     GLN A   304                                                      
REMARK 465     MET A   305                                                      
REMARK 465     LYS A   306                                                      
REMARK 465     ALA A   307                                                      
REMARK 465     GLN A   308                                                      
REMARK 465     ALA A   309                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     GLU A   311                                                      
REMARK 465     GLU A   312                                                      
REMARK 465     LYS A   313                                                      
REMARK 465     HIS A   314                                                      
REMARK 465     GLN A   315                                                      
REMARK 465     LYS A   316                                                      
REMARK 465     GLN A   317                                                      
REMARK 465     LEU A   318                                                      
REMARK 465     GLU A   319                                                      
REMARK 465     ARG A   320                                                      
REMARK 465     GLN A   321                                                      
REMARK 465     GLN A   322                                                      
REMARK 465     LEU A   323                                                      
REMARK 465     GLU A   324                                                      
REMARK 465     THR A   325                                                      
REMARK 465     GLU A   326                                                      
REMARK 465     LYS A   327                                                      
REMARK 465     LYS A   328                                                      
REMARK 465     ARG A   329                                                      
REMARK 465     ARG A   330                                                      
REMARK 465     GLU A   331                                                      
REMARK 465     THR A   332                                                      
REMARK 465     VAL A   333                                                      
REMARK 465     GLU A   334                                                      
REMARK 465     ARG A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     LYS A   337                                                      
REMARK 465     GLU A   338                                                      
REMARK 465     GLN A   339                                                      
REMARK 465     MET A   340                                                      
REMARK 465     MET A   341                                                      
REMARK 465     ARG A   342                                                      
REMARK 465     GLU A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     GLU A   346                                                      
REMARK 465     LEU A   347                                                      
REMARK 465     MET A   348                                                      
REMARK 465     LEU A   349                                                      
REMARK 465     ARG A   350                                                      
REMARK 465     LEU A   351                                                      
REMARK 465     GLN A   352                                                      
REMARK 465     ASP A   353                                                      
REMARK 465     TYR A   354                                                      
REMARK 465     GLU A   355                                                      
REMARK 465     GLU A   356                                                      
REMARK 465     LYS A   357                                                      
REMARK 465     THR A   358                                                      
REMARK 465     LYS A   359                                                      
REMARK 465     LYS A   360                                                      
REMARK 465     ALA A   361                                                      
REMARK 465     GLU A   362                                                      
REMARK 465     ARG A   363                                                      
REMARK 465     GLU A   364                                                      
REMARK 465     LEU A   365                                                      
REMARK 465     SER A   366                                                      
REMARK 465     GLU A   367                                                      
REMARK 465     GLN A   368                                                      
REMARK 465     ILE A   369                                                      
REMARK 465     GLN A   370                                                      
REMARK 465     ARG A   371                                                      
REMARK 465     ALA A   372                                                      
REMARK 465     LEU A   373                                                      
REMARK 465     GLN A   374                                                      
REMARK 465     LEU A   375                                                      
REMARK 465     GLU A   376                                                      
REMARK 465     GLU A   377                                                      
REMARK 465     GLU A   378                                                      
REMARK 465     ARG A   379                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     ARG A   381                                                      
REMARK 465     ALA A   382                                                      
REMARK 465     GLN A   383                                                      
REMARK 465     GLU A   384                                                      
REMARK 465     GLU A   385                                                      
REMARK 465     ALA A   386                                                      
REMARK 465     GLU A   387                                                      
REMARK 465     ARG A   388                                                      
REMARK 465     LEU A   389                                                      
REMARK 465     GLU A   390                                                      
REMARK 465     ALA A   391                                                      
REMARK 465     ASP A   392                                                      
REMARK 465     ARG A   393                                                      
REMARK 465     MET A   394                                                      
REMARK 465     ALA A   395                                                      
REMARK 465     ALA A   396                                                      
REMARK 465     LEU A   397                                                      
REMARK 465     ARG A   398                                                      
REMARK 465     ALA A   399                                                      
REMARK 465     LYS A   400                                                      
REMARK 465     GLU A   401                                                      
REMARK 465     GLU A   402                                                      
REMARK 465     LEU A   403                                                      
REMARK 465     GLU A   404                                                      
REMARK 465     ARG A   405                                                      
REMARK 465     GLN A   406                                                      
REMARK 465     ALA A   407                                                      
REMARK 465     VAL A   408                                                      
REMARK 465     ASP A   409                                                      
REMARK 465     GLN A   410                                                      
REMARK 465     ILE A   411                                                      
REMARK 465     LYS A   412                                                      
REMARK 465     SER A   413                                                      
REMARK 465     GLN A   414                                                      
REMARK 465     GLU A   415                                                      
REMARK 465     GLN A   416                                                      
REMARK 465     LEU A   417                                                      
REMARK 465     ALA A   418                                                      
REMARK 465     ALA A   419                                                      
REMARK 465     GLU A   420                                                      
REMARK 465     LEU A   421                                                      
REMARK 465     ALA A   422                                                      
REMARK 465     GLU A   423                                                      
REMARK 465     TYR A   424                                                      
REMARK 465     THR A   425                                                      
REMARK 465     ALA A   426                                                      
REMARK 465     LYS A   427                                                      
REMARK 465     ILE A   428                                                      
REMARK 465     ALA A   429                                                      
REMARK 465     LEU A   430                                                      
REMARK 465     LEU A   431                                                      
REMARK 465     GLU A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     ALA A   434                                                      
REMARK 465     ARG A   435                                                      
REMARK 465     ARG A   436                                                      
REMARK 465     ARG A   437                                                      
REMARK 465     LYS A   438                                                      
REMARK 465     GLU A   439                                                      
REMARK 465     ASP A   440                                                      
REMARK 465     GLU A   441                                                      
REMARK 465     VAL A   442                                                      
REMARK 465     GLU A   443                                                      
REMARK 465     GLU A   444                                                      
REMARK 465     TRP A   445                                                      
REMARK 465     GLN A   446                                                      
REMARK 465     HIS A   447                                                      
REMARK 465     ARG A   448                                                      
REMARK 465     ALA A   449                                                      
REMARK 465     LYS A   450                                                      
REMARK 465     GLU A   451                                                      
REMARK 465     ALA A   452                                                      
REMARK 465     GLN A   453                                                      
REMARK 465     ASP A   454                                                      
REMARK 465     ASP A   455                                                      
REMARK 465     LEU A   456                                                      
REMARK 465     VAL A   457                                                      
REMARK 465     LYS A   458                                                      
REMARK 465     THR A   459                                                      
REMARK 465     LYS A   460                                                      
REMARK 465     GLU A   461                                                      
REMARK 465     GLU A   462                                                      
REMARK 465     LEU A   463                                                      
REMARK 465     HIS A   464                                                      
REMARK 465     LEU A   465                                                      
REMARK 465     VAL A   466                                                      
REMARK 465     MET A   467                                                      
REMARK 465     THR A   468                                                      
REMARK 465     ALA A   469                                                      
REMARK 465     PRO A   470                                                      
REMARK 465     PRO A   471                                                      
REMARK 465     PRO A   472                                                      
REMARK 465     PRO A   473                                                      
REMARK 465     PRO A   474                                                      
REMARK 465     PRO A   475                                                      
REMARK 465     PRO A   476                                                      
REMARK 465     VAL A   477                                                      
REMARK 465     TYR A   478                                                      
REMARK 465     GLU A   479                                                      
REMARK 465     PRO A   480                                                      
REMARK 465     VAL A   481                                                      
REMARK 465     SER A   482                                                      
REMARK 465     TYR A   483                                                      
REMARK 465     HIS A   484                                                      
REMARK 465     VAL A   485                                                      
REMARK 465     GLN A   486                                                      
REMARK 465     GLU A   487                                                      
REMARK 465     SER A   488                                                      
REMARK 465     LEU A   489                                                      
REMARK 465     GLN A   490                                                      
REMARK 465     ASP A   491                                                      
REMARK 465     GLU A   492                                                      
REMARK 465     GLY A   493                                                      
REMARK 465     ALA A   494                                                      
REMARK 465     GLU A   495                                                      
REMARK 465     PRO A   496                                                      
REMARK 465     THR A   497                                                      
REMARK 465     GLY A   498                                                      
REMARK 465     TYR A   499                                                      
REMARK 465     SER A   500                                                      
REMARK 465     ALA A   501                                                      
REMARK 465     GLU A   502                                                      
REMARK 465     LEU A   503                                                      
REMARK 465     SER A   504                                                      
REMARK 465     SER A   505                                                      
REMARK 465     GLU A   506                                                      
REMARK 465     GLY A   507                                                      
REMARK 465     ILE A   508                                                      
REMARK 465     ARG A   509                                                      
REMARK 465     ASP A   510                                                      
REMARK 465     ASP A   511                                                      
REMARK 465     ARG A   512                                                      
REMARK 465     ASN A   513                                                      
REMARK 465     GLU A   514                                                      
REMARK 465     GLU A   515                                                      
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  62       68.81   -103.62                                   
REMARK 500    LYS A  63      131.23    174.40                                   
REMARK 500    ALA A  67        0.20   -159.37                                   
REMARK 500    GLU A  69       56.30     38.20                                   
REMARK 500    LYS A 162       30.89    -91.84                                   
REMARK 500    LYS A 253       -5.81     74.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4RM8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4RMA   RELATED DB: PDB                                   
DBREF  4RM9 A    1   586  UNP    P15311   EZRI_HUMAN       1    586             
SEQADV 4RM9 GLY A    0  UNP  P15311              EXPRESSION TAG                 
SEQRES   1 A  587  GLY MET PRO LYS PRO ILE ASN VAL ARG VAL THR THR MET          
SEQRES   2 A  587  ASP ALA GLU LEU GLU PHE ALA ILE GLN PRO ASN THR THR          
SEQRES   3 A  587  GLY LYS GLN LEU PHE ASP GLN VAL VAL LYS THR ILE GLY          
SEQRES   4 A  587  LEU ARG GLU VAL TRP TYR PHE GLY LEU HIS TYR VAL ASP          
SEQRES   5 A  587  ASN LYS GLY PHE PRO THR TRP LEU LYS LEU ASP LYS LYS          
SEQRES   6 A  587  VAL SER ALA GLN GLU VAL ARG LYS GLU ASN PRO LEU GLN          
SEQRES   7 A  587  PHE LYS PHE ARG ALA LYS PHE TYR PRO GLU ASP VAL ALA          
SEQRES   8 A  587  GLU GLU LEU ILE GLN ASP ILE THR GLN LYS LEU PHE PHE          
SEQRES   9 A  587  LEU GLN VAL LYS GLU GLY ILE LEU SER ASP GLU ILE TYR          
SEQRES  10 A  587  CYS PRO PRO GLU THR ALA VAL LEU LEU GLY SER TYR ALA          
SEQRES  11 A  587  VAL GLN ALA LYS PHE GLY ASP TYR ASN LYS GLU VAL HIS          
SEQRES  12 A  587  LYS SER GLY TYR LEU SER SER GLU ARG LEU ILE PRO GLN          
SEQRES  13 A  587  ARG VAL MET ASP GLN HIS LYS LEU THR ARG ASP GLN TRP          
SEQRES  14 A  587  GLU ASP ARG ILE GLN VAL TRP HIS ALA GLU HIS ARG GLY          
SEQRES  15 A  587  MET LEU LYS ASP ASN ALA MET LEU GLU TYR LEU LYS ILE          
SEQRES  16 A  587  ALA GLN ASP LEU GLU MET TYR GLY ILE ASN TYR PHE GLU          
SEQRES  17 A  587  ILE LYS ASN LYS LYS GLY THR ASP LEU TRP LEU GLY VAL          
SEQRES  18 A  587  ASP ALA LEU GLY LEU ASN ILE TYR GLU LYS ASP ASP LYS          
SEQRES  19 A  587  LEU THR PRO LYS ILE GLY PHE PRO TRP SER GLU ILE ARG          
SEQRES  20 A  587  ASN ILE SER PHE ASN ASP LYS LYS PHE VAL ILE LYS PRO          
SEQRES  21 A  587  ILE ASP LYS LYS ALA PRO ASP PHE VAL PHE TYR ALA PRO          
SEQRES  22 A  587  ARG LEU ARG ILE ASN LYS ARG ILE LEU GLN LEU CYS MET          
SEQRES  23 A  587  GLY ASN HIS GLU LEU TYR MET ARG ARG ARG LYS PRO ASP          
SEQRES  24 A  587  THR ILE GLU VAL GLN GLN MET LYS ALA GLN ALA ARG GLU          
SEQRES  25 A  587  GLU LYS HIS GLN LYS GLN LEU GLU ARG GLN GLN LEU GLU          
SEQRES  26 A  587  THR GLU LYS LYS ARG ARG GLU THR VAL GLU ARG GLU LYS          
SEQRES  27 A  587  GLU GLN MET MET ARG GLU LYS GLU GLU LEU MET LEU ARG          
SEQRES  28 A  587  LEU GLN ASP TYR GLU GLU LYS THR LYS LYS ALA GLU ARG          
SEQRES  29 A  587  GLU LEU SER GLU GLN ILE GLN ARG ALA LEU GLN LEU GLU          
SEQRES  30 A  587  GLU GLU ARG LYS ARG ALA GLN GLU GLU ALA GLU ARG LEU          
SEQRES  31 A  587  GLU ALA ASP ARG MET ALA ALA LEU ARG ALA LYS GLU GLU          
SEQRES  32 A  587  LEU GLU ARG GLN ALA VAL ASP GLN ILE LYS SER GLN GLU          
SEQRES  33 A  587  GLN LEU ALA ALA GLU LEU ALA GLU TYR THR ALA LYS ILE          
SEQRES  34 A  587  ALA LEU LEU GLU GLU ALA ARG ARG ARG LYS GLU ASP GLU          
SEQRES  35 A  587  VAL GLU GLU TRP GLN HIS ARG ALA LYS GLU ALA GLN ASP          
SEQRES  36 A  587  ASP LEU VAL LYS THR LYS GLU GLU LEU HIS LEU VAL MET          
SEQRES  37 A  587  THR ALA PRO PRO PRO PRO PRO PRO PRO VAL TYR GLU PRO          
SEQRES  38 A  587  VAL SER TYR HIS VAL GLN GLU SER LEU GLN ASP GLU GLY          
SEQRES  39 A  587  ALA GLU PRO THR GLY TYR SER ALA GLU LEU SER SER GLU          
SEQRES  40 A  587  GLY ILE ARG ASP ASP ARG ASN GLU GLU LYS ARG ILE THR          
SEQRES  41 A  587  GLU ALA GLU LYS ASN GLU ARG VAL GLN ARG GLN LEU LEU          
SEQRES  42 A  587  THR LEU SER SER GLU LEU SER GLN ALA ARG ASP GLU ASN          
SEQRES  43 A  587  LYS ARG THR HIS ASN ASP ILE ILE HIS ASN GLU ASN MET          
SEQRES  44 A  587  ARG GLN GLY ARG ASP LYS TYR LYS THR LEU ARG GLN ILE          
SEQRES  45 A  587  ARG GLN GLY ASN THR LYS GLN ARG ILE ASP GLU PHE GLU          
SEQRES  46 A  587  ALA LEU                                                      
FORMUL   2  HOH   *147(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 ASP A   88  LEU A   93  1                                   6    
HELIX    4   4 GLN A   95  SER A  112  1                                  18    
HELIX    5   5 PRO A  118  GLY A  135  1                                  18    
HELIX    6   6 PRO A  154  GLN A  160  1                                   7    
HELIX    7   7 THR A  164  HIS A  179  1                                  16    
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 THR A  519  ASN A  524  1                                   6    
HELIX   11  11 ASN A  524  GLN A  540  1                                  17    
HELIX   12  12 ALA A  541  ARG A  542  5                                   2    
HELIX   13  13 ASP A  543  ARG A  547  5                                   5    
HELIX   14  14 THR A  548  GLN A  560  1                                  13    
HELIX   15  15 ASP A  563  ARG A  572  1                                  10    
HELIX   16  16 ASN A  575  LEU A  586  1                                  12    
SHEET    1   A 5 GLU A  15  ILE A  20  0                                        
SHEET    2   A 5 ILE A   5  THR A  10 -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  VAL A  50 -1  N  HIS A  48   O  LYS A  79           
SHEET    5   A 5 PRO A  56  TRP A  58 -1  O  THR A  57   N  TYR A  49           
SHEET    1   B 4 ASN A 204  LYS A 209  0                                        
SHEET    2   B 4 ASP A 215  VAL A 220 -1  O  LEU A 218   N  PHE A 206           
SHEET    3   B 4 GLY A 224  GLU A 229 -1  O  ASN A 226   N  GLY A 219           
SHEET    4   B 4 ILE A 238  PRO A 241 -1  O  PHE A 240   N  LEU A 225           
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 258   N  ARG A 246           
SHEET    3   C 3 PHE A 267  TYR A 270 -1  O  PHE A 267   N  ILE A 257           
CISPEP   1 ASN A   74    PRO A   75          0        -1.26                     
CRYST1   67.433  113.517  111.773  90.00  90.00  90.00 C 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      0.014830  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008809  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008947        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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