GenomeNet

Database: PDB
Entry: 1SGH
LinkDB: 1SGH
Original site: 1SGH 
HEADER    STRUCTURAL PROTEIN                      23-FEB-04   1SGH              
TITLE     MOESIN FERM DOMAIN BOUND TO EBP50 C-TERMINAL PEPTIDE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MOESIN;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: FERM DOMAIN;                                               
COMPND   5 SYNONYM: MEMBRANE-ORGANIZING EXTENSION SPIKE PROTEIN;                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: EZRIN-RADIXIN-MOESIN BINDING PHOSPHOPROTEIN 50;            
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: EBP50, NA+, /H+, EXCHANGE REGULATORY COFACTOR NHE-          
COMPND  11 RF, NHERF-1, REGULATORY COFACTOR OF NA+, /H+, EXCHANGER,             
COMPND  12 SODIUM-HYDROGEN EXCHANGER REGULATORY FACTOR 1, SOLUTE                
COMPND  13 CARRIER FAMILY 9 ISOFORM 3 REGULATORY FACTOR 1;                      
COMPND  14 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: MSN;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE16;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: THIS SEQUENCE OCURRS NATURALLY IN HUMANS              
KEYWDS    FERM-PEPTIDE COMPLEX, STRUCTURAL PROTEIN                              
EXPDTA    X-RAY DIFFRACTION                                                     
MDLTYP    CA ATOMS ONLY, CHAIN B                                                
AUTHOR    C.M.FINNERTY,D.CHAMBERS,J.INGRAFFEA,H.R.FABER,P.A.KARPLUS,            
AUTHOR   2 A.BRETSCHER                                                          
REVDAT   2   24-FEB-09 1SGH    1       VERSN                                    
REVDAT   1   29-JUN-04 1SGH    0                                                
JRNL        AUTH   C.M.FINNERTY,D.CHAMBERS,J.INGRAFFEA,H.R.FABER,               
JRNL        AUTH 2 P.A.KARPLUS,A.BRETSCHER                                      
JRNL        TITL   THE EBP50-MOESIN INTERACTION INVOLVES A BINDING              
JRNL        TITL 2 SITE REGULATED BY DIRECT MASKING ON THE FERM DOMAIN          
JRNL        REF    J.CELL.SCI.                   V. 117  1547 2004              
JRNL        REFN                   ISSN 0021-9533                               
JRNL        PMID   15020681                                                     
JRNL        DOI    10.1242/JCS.01038                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 11.07                          
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)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 6801                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.338                           
REMARK   3   FREE R VALUE                     : 0.401                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 585                             
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) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.61                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 603                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4490                       
REMARK   3   BIN FREE R VALUE                    : 0.6310                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 46                           
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            : 2444                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 104.00                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -69.00000                                            
REMARK   3    B22 (A**2) : 38.00000                                             
REMARK   3    B33 (A**2) : 31.00000                                             
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : -22.00000                                            
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) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.75                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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: AS NOTED BY FINNERTY ET AL. IN THE        
REMARK   3  PRIMARY CITATION OF THIS STRUCTURE, A MODEL FOR THE BOUND           
REMARK   3  PEPTIDE WAS NOT INCLUDED IN THE REFINEMENT DUE TO THE VERY LOW      
REMARK   3  RESOLUTION OF THE ANALYSIS. HOWEVER, AS PART OF THE STRUCTURE       
REMARK   3  INTERPRETATION, A 38-RESIDUE PEPTIDE HAD BEEN APPROXIMATELY         
REMARK   3  MODELED INTO THE DIFFERENCE ELECTRON DENSITY THAT CORRESPONDS       
REMARK   3  TO THE BOUND PEPTIDE. TO MAXIMIZE THE VALUE OF THIS COORDINATE      
REMARK   3  SET, THE CA COORDINATES OF THE APPROXIMATELY MODELED PEPTIDE        
REMARK   3  ARE INCLUDED IN THIS PDB DEPOSITION WITH AN OCCUPANCY OF ZERO.      
REMARK   4                                                                      
REMARK   4 1SGH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021688.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAY-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 123                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.943                              
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6801                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 11.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.34300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1EF1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, PEG 4000, PH 8.0, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       63.80000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.25000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       63.80000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       35.25000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 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     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     CYS B     0                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     LEU B    1                                                       
REMARK 475     ASP B    2                                                       
REMARK 475     PHE B    3                                                       
REMARK 475     ASN B    4                                                       
REMARK 475     ILE B    5                                                       
REMARK 475     SER B    6                                                       
REMARK 475     LEU B    7                                                       
REMARK 475     ALA B    8                                                       
REMARK 475     MET B    9                                                       
REMARK 475     ALA B   10                                                       
REMARK 475     LYS B   11                                                       
REMARK 475     GLU B   12                                                       
REMARK 475     ARG B   13                                                       
REMARK 475     ALA B   14                                                       
REMARK 475     HIS B   15                                                       
REMARK 475     GLN B   16                                                       
REMARK 475     LYS B   17                                                       
REMARK 475     ARG B   18                                                       
REMARK 475     SER B   19                                                       
REMARK 475     SER B   20                                                       
REMARK 475     LYS B   21                                                       
REMARK 475     ARG B   22                                                       
REMARK 475     ALA B   23                                                       
REMARK 475     PRO B   24                                                       
REMARK 475     GLN B   25                                                       
REMARK 475     MET B   26                                                       
REMARK 475     ASP B   27                                                       
REMARK 475     TRP B   28                                                       
REMARK 475     SER B   29                                                       
REMARK 475     LYS B   30                                                       
REMARK 475     LYS B   31                                                       
REMARK 475     ASN B   32                                                       
REMARK 475     GLU B   33                                                       
REMARK 475     LEU B   34                                                       
REMARK 475     PHE B   35                                                       
REMARK 475     SER B   36                                                       
REMARK 475     ASN B   37                                                       
REMARK 475     LEU B   38                                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CH2  TRP A   175     CA   LYS B    11              1.65            
REMARK 500   NE2  HIS A   161     CA   LEU B     1              1.97            
REMARK 500   CZ3  TRP A   175     CA   LYS B    11              2.01            
REMARK 500   OE1  GLU A    41     OE1  GLN A    95              2.01            
REMARK 500   O    LEU A   192     N    ILE A   194              2.10            
REMARK 500   O    VAL A     7     OE2  GLU A    17              2.14            
REMARK 500   O    THR A   235     NZ   LYS A   237              2.17            
REMARK 500   O    ASN A   247     N    LYS A   258              2.17            
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      -31.01   -132.84                                   
REMARK 500    PRO A  22       20.45    -56.82                                   
REMARK 500    THR A  24      145.30    -20.22                                   
REMARK 500    LYS A  27      -73.37    -15.28                                   
REMARK 500    GLN A  28      -81.61    -41.87                                   
REMARK 500    LEU A  29      -66.02    -26.39                                   
REMARK 500    PHE A  30      -79.82    -30.70                                   
REMARK 500    ASP A  31      -39.81    -37.15                                   
REMARK 500    VAL A  34      -19.92    -47.36                                   
REMARK 500    ILE A  37       15.61    -68.83                                   
REMARK 500    ARG A  40       38.61   -160.85                                   
REMARK 500    GLU A  41       21.56   -147.98                                   
REMARK 500    VAL A  42      -12.02    -41.36                                   
REMARK 500    TRP A  43       48.49    -71.86                                   
REMARK 500    PHE A  44      -55.99   -148.81                                   
REMARK 500    ASP A  51     -164.32    -76.75                                   
REMARK 500    GLU A  73     -163.04   -178.64                                   
REMARK 500    PRO A  75     -179.75    -69.74                                   
REMARK 500    SER A  90      -55.90    -28.22                                   
REMARK 500    ASP A  96      -10.66    -45.04                                   
REMARK 500    LEU A 111       24.56    -63.78                                   
REMARK 500    LEU A 125      -75.64    -61.03                                   
REMARK 500    GLN A 131      -38.76    -33.38                                   
REMARK 500    LYS A 143     -168.61    -74.04                                   
REMARK 500    LEU A 152      -12.48   -144.98                                   
REMARK 500    GLN A 155      -45.26    -26.47                                   
REMARK 500    GLU A 159        4.19    -62.17                                   
REMARK 500    GLU A 170      -39.90    -39.49                                   
REMARK 500    GLU A 178      -19.22    -47.08                                   
REMARK 500    ARG A 184       11.00    -47.81                                   
REMARK 500    LYS A 193      -21.03    -31.72                                   
REMARK 500    TYR A 201      145.42    -38.01                                   
REMARK 500    ASN A 210     -143.12    -94.54                                   
REMARK 500    LYS A 212       45.98    -80.78                                   
REMARK 500    SER A 214      146.12    -38.10                                   
REMARK 500    LEU A 216     -161.08   -172.14                                   
REMARK 500    ALA A 222       19.94    -44.68                                   
REMARK 500    LEU A 223      -50.19   -122.46                                   
REMARK 500    LEU A 234      -84.76    -66.81                                   
REMARK 500    TRP A 242      -17.62    -44.87                                   
REMARK 500    SER A 249      171.92    169.42                                   
REMARK 500    ASP A 252      -84.30     61.84                                   
REMARK 500    PRO A 259     -162.26    -67.44                                   
REMARK 500    ASP A 261     -112.17    149.24                                   
REMARK 500    LYS A 262      -14.79   -176.32                                   
REMARK 500    PRO A 265     -169.92    -37.93                                   
REMARK 500    ARG A 275      -31.59    -35.35                                   
REMARK 500    LEU A 281      -80.38    -67.43                                   
REMARK 500    ALA A 282      -49.48    -22.86                                   
REMARK 500    MET A 285      -82.69    -62.83                                   
REMARK 500    ASN A 287      -84.86    -41.77                                   
REMARK 500    LYS A 296       70.47   -165.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1SGH A    1   297  UNP    P26038   MOES_HUMAN       0    296             
DBREF  1SGH B    1    38  UNP    O14745   NHERF_HUMAN    321    358             
SEQADV 1SGH CYS B    0  UNP  O14745              INSERTION                      
SEQRES   1 A  297  MET PRO LYS THR ILE SER VAL ARG VAL THR THR MET ASP          
SEQRES   2 A  297  ALA GLU LEU GLU PHE ALA ILE GLN PRO ASN THR THR GLY          
SEQRES   3 A  297  LYS GLN LEU PHE ASP GLN VAL VAL LYS THR ILE GLY LEU          
SEQRES   4 A  297  ARG GLU VAL TRP PHE PHE GLY LEU GLN TYR GLN ASP THR          
SEQRES   5 A  297  LYS GLY PHE SER THR TRP LEU LYS LEU ASN LYS LYS VAL          
SEQRES   6 A  297  THR ALA GLN ASP VAL ARG LYS GLU SER PRO LEU LEU PHE          
SEQRES   7 A  297  LYS PHE ARG ALA LYS PHE TYR PRO GLU ASP VAL SER GLU          
SEQRES   8 A  297  GLU LEU ILE GLN ASP ILE THR GLN ARG LEU PHE PHE LEU          
SEQRES   9 A  297  GLN VAL LYS GLU GLY ILE LEU ASN ASP ASP ILE TYR CYS          
SEQRES  10 A  297  PRO PRO GLU THR ALA VAL LEU LEU ALA SER TYR ALA VAL          
SEQRES  11 A  297  GLN SER LYS TYR GLY ASP PHE ASN LYS GLU VAL HIS LYS          
SEQRES  12 A  297  SER GLY TYR LEU ALA GLY ASP LYS LEU LEU PRO GLN ARG          
SEQRES  13 A  297  VAL LEU GLU GLN HIS LYS LEU ASN LYS ASP GLN TRP GLU          
SEQRES  14 A  297  GLU ARG ILE GLN VAL TRP HIS GLU GLU HIS ARG GLY MET          
SEQRES  15 A  297  LEU ARG GLU ASP ALA VAL LEU GLU TYR LEU LYS ILE ALA          
SEQRES  16 A  297  GLN ASP LEU GLU MET TYR GLY VAL ASN TYR PHE SER ILE          
SEQRES  17 A  297  LYS ASN LYS LYS GLY SER GLU LEU TRP LEU GLY VAL ASP          
SEQRES  18 A  297  ALA LEU GLY LEU ASN ILE TYR GLU GLN ASN ASP ARG LEU          
SEQRES  19 A  297  THR PRO LYS ILE GLY PHE PRO TRP SER GLU ILE ARG ASN          
SEQRES  20 A  297  ILE SER PHE ASN ASP LYS LYS PHE VAL ILE LYS PRO ILE          
SEQRES  21 A  297  ASP LYS LYS ALA PRO ASP PHE VAL PHE TYR ALA PRO ARG          
SEQRES  22 A  297  LEU ARG ILE ASN LYS ARG ILE LEU ALA LEU CYS MET GLY          
SEQRES  23 A  297  ASN HIS GLU LEU TYR MET ARG ARG ARG LYS PRO                  
SEQRES   1 B   39  CYS LEU ASP PHE ASN ILE SER LEU ALA MET ALA LYS GLU          
SEQRES   2 B   39  ARG ALA HIS GLN LYS ARG SER SER LYS ARG ALA PRO GLN          
SEQRES   3 B   39  MET ASP TRP SER LYS LYS ASN GLU LEU PHE SER ASN LEU          
HELIX    1   1 THR A   25  ILE A   37  1                                  13    
HELIX    2   2 ASP A   88  LEU A   93  1                                   6    
HELIX    3   3 ILE A   97  LEU A  111  1                                  15    
HELIX    4   4 PRO A  118  SER A  132  1                                  15    
HELIX    5   5 PRO A  154  GLU A  159  1                                   6    
HELIX    6   6 ASN A  164  GLU A  178  1                                  15    
HELIX    7   7 GLU A  185  GLN A  196  1                                  12    
HELIX    8   8 ARG A  273  LYS A  296  1                                  24    
SHEET    1   A 5 GLU A  15  PHE A  18  0                                        
SHEET    2   A 5 VAL A   7  THR A  10 -1  N  VAL A   9   O  LEU A  16           
SHEET    3   A 5 LEU A  76  ALA A  82  1  O  PHE A  78   N  THR A  10           
SHEET    4   A 5 PHE A  45  GLN A  50 -1  N  GLN A  48   O  LYS A  79           
SHEET    5   A 5 SER A  56  TRP A  58 -1  O  THR A  57   N  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  O  LEU A 218   N  PHE A 206           
SHEET    3   B 4 GLY A 224  TYR A 228 -1  O  ASN A 226   N  GLY A 219           
SHEET    4   B 4 ILE A 238  PRO A 241 -1  O  ILE A 238   N  ILE A 227           
SHEET    1   C 3 ASN A 247  ASN A 251  0                                        
SHEET    2   C 3 LYS A 254  LYS A 258 -1  O  LYS A 258   N  ASN A 247           
SHEET    3   C 3 PHE A 267  TYR A 270 -1  O  PHE A 267   N  ILE A 257           
CISPEP   1 SER A   74    PRO A   75          0        -1.52                     
CRYST1  127.600   70.500   62.800  90.00 106.10  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007837  0.000000  0.002262        0.00000                         
SCALE2      0.000000  0.014184  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016574        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system