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Database: PDB
Entry: 3L9B
LinkDB: 3L9B
Original site: 3L9B 
HEADER    MEMBRANE PROTEIN                        04-JAN-10   3L9B              
TITLE     CRYSTAL STRUCTURE OF RAT OTOFERLIN C2A                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OTOFERLIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: C2A DOMAIN;                                                
COMPND   5 SYNONYM: FER-1-LIKE PROTEIN 2;                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: FER1L2, OTOF;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    OTOFERLIN, C2-DOMAIN, BETA-SHEETS, CELL MEMBRANE, SYNAPTIC VESICLE,   
KEYWDS   2 HEARING, MEMBRANE, SYNAPSE, TRANSMEMBRANE, MEMBRANE PROTEIN          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HELFMANN,P.NEUMANN                                                  
REVDAT   2   17-SEP-14 3L9B    1       JRNL   VERSN                             
REVDAT   1   19-JAN-11 3L9B    0                                                
JRNL        AUTH   S.HELFMANN,P.NEUMANN,K.TITTMANN,T.MOSER,R.FICNER,E.REISINGER 
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE C2A DOMAIN OF OTOFERLIN REVEALS 
JRNL        TITL 2 AN UNCONVENTIONAL TOP LOOP REGION.                           
JRNL        REF    J.MOL.BIOL.                   V. 406   479 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   21216247                                                     
JRNL        DOI    10.1016/J.JMB.2010.12.031                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 10990                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 551                             
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 24.9390 -  3.0940    0.97     2650   140  0.1590 0.1960        
REMARK   3     2  3.0940 -  2.4570    0.99     2615   138  0.1830 0.2520        
REMARK   3     3  2.4570 -  2.1460    0.99     2576   135  0.2030 0.2540        
REMARK   3     4  2.1460 -  1.9500    0.99     2598   138  0.2360 0.3000        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 39.36                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.18                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.87                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.22700                                             
REMARK   3    B22 (A**2) : -1.22700                                             
REMARK   3    B33 (A**2) : 2.45400                                              
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      :  0.006           1059                                  
REMARK   3   ANGLE     :  0.981           1434                                  
REMARK   3   CHIRALITY :  0.073            167                                  
REMARK   3   PLANARITY :  0.003            186                                  
REMARK   3   DIHEDRAL  : 17.992            392                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4466  -3.1639  -1.4974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1643 T22:   0.1096                                     
REMARK   3      T33:   0.1526 T12:  -0.0174                                     
REMARK   3      T13:  -0.0434 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0604 L22:   1.5969                                     
REMARK   3      L33:   1.6557 L12:   0.8731                                     
REMARK   3      L13:  -0.4101 L23:   0.0373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0395 S12:   0.0495 S13:   0.1597                       
REMARK   3      S21:  -0.1033 S22:  -0.0182 S23:   0.1978                       
REMARK   3      S31:  -0.2324 S32:   0.0137 S33:   0.0604                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINEMENT IN PHENIX.REFINE USING         
REMARK   3  AUTOMATIC PROCEDURE TO DETERMINE THE WEIGHTS BETWEEN X-RAY TARGET   
REMARK   3  AND STEREOCHEMISTRY/ADP RESTRAINTS, MASK OPTIMISATION               
REMARK   4                                                                      
REMARK   4 3L9B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JAN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB056995.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10992                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.010                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.93                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.57700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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 1DSY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MGCL2, PH 8.5, VAPOR           
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       50.15000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       50.15000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       15.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       50.15000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        7.50000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       50.15000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       22.50000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       50.15000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.15000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       15.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       50.15000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       22.50000            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       50.15000            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000        7.50000            
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 MG    MG A 125  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 242  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 248  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     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
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    LYS A   8      -82.53    -91.52                                   
REMARK 500    GLU A  39     -108.70    -83.09                                   
REMARK 500    SER A  54      -76.33   -122.77                                   
REMARK 500    ASN A  92      -22.78     72.21                                   
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 MG A 125                  
DBREF  3L9B A    1   124  UNP    Q9ERC5   OTOF_RAT         1    124             
SEQADV 3L9B MET A  -19  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B GLY A  -18  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B SER A  -17  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B SER A  -16  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B HIS A  -15  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B HIS A  -14  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B HIS A  -13  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B HIS A  -12  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B HIS A  -11  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B HIS A  -10  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B SER A   -9  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B SER A   -8  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B GLY A   -7  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B LEU A   -6  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B VAL A   -5  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B PRO A   -4  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B ARG A   -3  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B GLY A   -2  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B SER A   -1  UNP  Q9ERC5              EXPRESSION TAG                 
SEQADV 3L9B HIS A    0  UNP  Q9ERC5              EXPRESSION TAG                 
SEQRES   1 A  144  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  144  LEU VAL PRO ARG GLY SER HIS MET ALA LEU ILE VAL HIS          
SEQRES   3 A  144  LEU LYS THR VAL SER GLU LEU ARG GLY ARG ALA ASP ARG          
SEQRES   4 A  144  ILE ALA LYS VAL THR PHE ARG GLY GLN SER PHE TYR SER          
SEQRES   5 A  144  ARG VAL LEU GLU ASN CYS GLU ASP VAL ALA ASP PHE ASP          
SEQRES   6 A  144  GLU THR PHE ARG TRP PRO VAL ALA SER SER ILE ASP ARG          
SEQRES   7 A  144  ASN GLU VAL LEU GLU ILE GLN ILE PHE ASN TYR SER LYS          
SEQRES   8 A  144  VAL PHE SER ASN LYS LEU ILE GLY THR PHE ARG MET VAL          
SEQRES   9 A  144  LEU GLN LYS VAL VAL GLU GLU ASN ARG VAL GLU VAL SER          
SEQRES  10 A  144  ASP THR LEU ILE ASP ASP ASN ASN ALA ILE ILE LYS THR          
SEQRES  11 A  144  SER LEU SER MET GLU VAL ARG TYR GLN ALA ALA ASP GLY          
SEQRES  12 A  144  THR                                                          
HET     MG  A 125       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  HOH   *143(H2 O)                                                    
HELIX    1   1 LEU A   85  ASN A   92  1                                   8    
SHEET    1   A 4 ALA A  42  VAL A  52  0                                        
SHEET    2   A 4 MET A   1  SER A  11 -1  N  VAL A  10   O  ALA A  42           
SHEET    3   A 4 ILE A 107  ALA A 120 -1  O  ARG A 117   N  ILE A   4           
SHEET    4   A 4 ARG A  93  ILE A 101 -1  N  VAL A  96   O  MET A 114           
SHEET    1   B 3 GLN A  28  TYR A  31  0                                        
SHEET    2   B 3 ALA A  17  PHE A  25 -1  N  VAL A  23   O  PHE A  30           
SHEET    3   B 3 LEU A  35  CYS A  38 -1  O  LEU A  35   N  ARG A  19           
SHEET    1   C 4 GLN A  28  TYR A  31  0                                        
SHEET    2   C 4 ALA A  17  PHE A  25 -1  N  VAL A  23   O  PHE A  30           
SHEET    3   C 4 VAL A  61  TYR A  69 -1  O  PHE A  67   N  ILE A  20           
SHEET    4   C 4 LYS A  76  VAL A  84 -1  O  ILE A  78   N  ILE A  66           
SITE     1 AC1  3 GLU A  46  THR A  47  HOH A 152                               
CRYST1  100.300  100.300   30.000  90.00  90.00  90.00 I 41          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      0.009970  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009970  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.033333        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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