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Database: PDB
Entry: 3LQ9
LinkDB: 3LQ9
Original site: 3LQ9 
HEADER    SIGNALING PROTEIN                       08-FEB-10   3LQ9              
TITLE     CRYSTAL STRUCTURE OF HUMAN REDD1, A HYPOXIA-INDUCED REGULATOR OF MTOR 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA-DAMAGE-INDUCIBLE TRANSCRIPT 4 PROTEIN;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: C-TERMINAL FUNCTIONAL DOMAIN;                              
COMPND   5 SYNONYM: PROTEIN REGULATED IN DEVELOPMENT AND DNA DAMAGE RESPONSE 1, 
COMPND   6 REDD-1, HIF-1 RESPONSIVE PROTEIN RTP801;                             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DDIT4, REDD1, RTP801;                                          
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: MODIFIED PET28 WITH A HIS6-SUMO TAG       
KEYWDS    REDD1 DDIT4 MTOR, HYPOXIA, CANCER, SIGNALING PROTEIN                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.VEGA-RUBIN-DE-CELIS,Z.ABDALLAH,J.BRUGAROLAS,X.ZHANG                 
REVDAT   4   01-NOV-17 3LQ9    1       REMARK                                   
REVDAT   3   21-DEC-16 3LQ9    1       TITLE  VERSN                             
REVDAT   2   31-MAR-10 3LQ9    1       JRNL                                     
REVDAT   1   09-MAR-10 3LQ9    0                                                
JRNL        AUTH   S.VEGA-RUBIN-DE-CELIS,Z.ABDALLAH,L.KINCH,N.V.GRISHIN,        
JRNL        AUTH 2 J.BRUGAROLAS,X.ZHANG                                         
JRNL        TITL   STRUCTURAL ANALYSIS AND FUNCTIONAL IMPLICATIONS OF THE       
JRNL        TITL 2 NEGATIVE MTORC1 REGULATOR REDD1.                             
JRNL        REF    BIOCHEMISTRY                  V.  49  2491 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   20166753                                                     
JRNL        DOI    10.1021/BI902135E                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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 : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.10                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 13975                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 708                             
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 27.0980 -  3.4160    0.97     2751   160  0.1680 0.1790        
REMARK   3     2  3.4160 -  2.7120    0.97     2756   143  0.1790 0.2500        
REMARK   3     3  2.7120 -  2.3700    0.95     2678   142  0.1800 0.2310        
REMARK   3     4  2.3700 -  2.1530    0.93     2641   138  0.1770 0.2150        
REMARK   3     5  2.1530 -  2.0000    0.86     2441   125  0.1980 0.2610        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 48.59                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.80600                                             
REMARK   3    B22 (A**2) : 6.71200                                              
REMARK   3    B33 (A**2) : -2.90600                                             
REMARK   3    B12 (A**2) : 1.17700                                              
REMARK   3    B13 (A**2) : 1.63500                                              
REMARK   3    B23 (A**2) : -1.82100                                             
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           1942                                  
REMARK   3   ANGLE     :  0.770           2618                                  
REMARK   3   CHIRALITY :  0.051            319                                  
REMARK   3   PLANARITY :  0.002            332                                  
REMARK   3   DIHEDRAL  : 15.690            733                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3LQ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000057594.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-08; 01-JAN-08               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; APS                           
REMARK 200  BEAMLINE                       : 19-BM; 19-BM                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97926; 1.28288                   
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE; CUSTOM-MADE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14319                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.9000                            
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) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAF, 20-26% PEG3350, 0.05 MM       
REMARK 280  C12E9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 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     SER A    88                                                      
REMARK 465     PRO A   187                                                      
REMARK 465     SER A   223                                                      
REMARK 465     SER A   224                                                      
REMARK 465     GLU A   225                                                      
REMARK 465     GLN A   226                                                      
REMARK 465     LYS B   188                                                      
REMARK 465     ALA B   196                                                      
REMARK 465     ASN B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     SER B   223                                                      
REMARK 465     SER B   224                                                      
REMARK 465     GLU B   225                                                      
REMARK 465     GLN B   226                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 155    CG   CD   CE   NZ                                   
REMARK 470     TRP A 186    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 186    CZ3  CH2                                            
REMARK 470     LYS A 188    CG   CD   CE   NZ                                   
REMARK 470     ARG B 184    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 185    CG   CD1  CD2                                       
REMARK 470     TRP B 186    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 186    CZ3  CH2                                            
REMARK 470     PRO B 187    CG   CD                                             
REMARK 470     SER B 195    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 187   N   -  CA  -  CB  ANGL. DEV. =   7.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 109       73.83   -105.66                                   
REMARK 500    CYS A 140       -1.18     69.78                                   
REMARK 500    LEU B 109       67.41   -119.99                                   
REMARK 500    ARG B 184        0.50    -65.11                                   
REMARK 500    TRP B 186     -164.68    -65.37                                   
REMARK 500    GLN B 190      -85.82    -70.03                                   
REMARK 500    SER B 194       75.70   -109.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3LQ9 A   89   226  UNP    Q9NX09   DDT4_HUMAN      89    226             
DBREF  3LQ9 B   89   226  UNP    Q9NX09   DDT4_HUMAN      89    226             
SEQADV 3LQ9 SER A   88  UNP  Q9NX09              EXPRESSION TAG                 
SEQADV 3LQ9     A       UNP  Q9NX09    PHE   200 DELETION                       
SEQADV 3LQ9     A       UNP  Q9NX09    LEU   201 DELETION                       
SEQADV 3LQ9     A       UNP  Q9NX09    PRO   202 DELETION                       
SEQADV 3LQ9     A       UNP  Q9NX09    GLY   203 DELETION                       
SEQADV 3LQ9     A       UNP  Q9NX09    PHE   204 DELETION                       
SEQADV 3LQ9 SER B   88  UNP  Q9NX09              EXPRESSION TAG                 
SEQADV 3LQ9     B       UNP  Q9NX09    PHE   200 DELETION                       
SEQADV 3LQ9     B       UNP  Q9NX09    LEU   201 DELETION                       
SEQADV 3LQ9     B       UNP  Q9NX09    PRO   202 DELETION                       
SEQADV 3LQ9     B       UNP  Q9NX09    GLY   203 DELETION                       
SEQADV 3LQ9     B       UNP  Q9NX09    PHE   204 DELETION                       
SEQRES   1 A  134  SER ASP GLU HIS LEU CYS ALA ASN LEU MSE GLN LEU LEU          
SEQRES   2 A  134  GLN GLU SER LEU ALA GLN ALA ARG LEU GLY SER ARG ARG          
SEQRES   3 A  134  PRO ALA ARG LEU LEU MSE PRO SER GLN LEU VAL SER GLN          
SEQRES   4 A  134  VAL GLY LYS GLU LEU LEU ARG LEU ALA TYR SER GLU PRO          
SEQRES   5 A  134  CYS GLY LEU ARG GLY ALA LEU LEU ASP VAL CYS VAL GLU          
SEQRES   6 A  134  GLN GLY LYS SER CYS HIS SER VAL GLY GLN LEU ALA LEU          
SEQRES   7 A  134  ASP PRO SER LEU VAL PRO THR PHE GLN LEU THR LEU VAL          
SEQRES   8 A  134  LEU ARG LEU ASP SER ARG LEU TRP PRO LYS ILE GLN GLY          
SEQRES   9 A  134  LEU PHE SER SER ALA ASN SER PRO SER GLN SER LEU THR          
SEQRES  10 A  134  LEU SER THR GLY PHE ARG VAL ILE LYS LYS LYS LEU TYR          
SEQRES  11 A  134  SER SER GLU GLN                                              
SEQRES   1 B  134  SER ASP GLU HIS LEU CYS ALA ASN LEU MSE GLN LEU LEU          
SEQRES   2 B  134  GLN GLU SER LEU ALA GLN ALA ARG LEU GLY SER ARG ARG          
SEQRES   3 B  134  PRO ALA ARG LEU LEU MSE PRO SER GLN LEU VAL SER GLN          
SEQRES   4 B  134  VAL GLY LYS GLU LEU LEU ARG LEU ALA TYR SER GLU PRO          
SEQRES   5 B  134  CYS GLY LEU ARG GLY ALA LEU LEU ASP VAL CYS VAL GLU          
SEQRES   6 B  134  GLN GLY LYS SER CYS HIS SER VAL GLY GLN LEU ALA LEU          
SEQRES   7 B  134  ASP PRO SER LEU VAL PRO THR PHE GLN LEU THR LEU VAL          
SEQRES   8 B  134  LEU ARG LEU ASP SER ARG LEU TRP PRO LYS ILE GLN GLY          
SEQRES   9 B  134  LEU PHE SER SER ALA ASN SER PRO SER GLN SER LEU THR          
SEQRES  10 B  134  LEU SER THR GLY PHE ARG VAL ILE LYS LYS LYS LEU TYR          
SEQRES  11 B  134  SER SER GLU GLN                                              
MODRES 3LQ9 MSE A   97  MET  SELENOMETHIONINE                                   
MODRES 3LQ9 MSE A  119  MET  SELENOMETHIONINE                                   
MODRES 3LQ9 MSE B   97  MET  SELENOMETHIONINE                                   
MODRES 3LQ9 MSE B  119  MET  SELENOMETHIONINE                                   
HET    MSE  A  97       8                                                       
HET    MSE  A 119       8                                                       
HET    MSE  B  97       8                                                       
HET    MSE  B 119       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   3  HOH   *203(H2 O)                                                    
HELIX    1   1 ASP A   89  ALA A  105  1                                  17    
HELIX    2   2 PRO A  120  TYR A  136  1                                  17    
HELIX    3   3 CYS A  140  ARG A  143  5                                   4    
HELIX    4   4 SER B   88  ALA B  105  1                                  18    
HELIX    5   5 PRO B  120  TYR B  136  1                                  17    
HELIX    6   6 CYS B  140  ARG B  143  5                                   4    
SHEET    1   A 2 ALA A 107  ARG A 108  0                                        
SHEET    2   A 2 PRO A 114  ALA A 115 -1  O  ALA A 115   N  ALA A 107           
SHEET    1   B 2 LEU A 117  LEU A 118  0                                        
SHEET    1   C 4 SER A 156  ALA A 164  0                                        
SHEET    2   C 4 ALA A 145  GLN A 153 -1  N  LEU A 147   O  LEU A 163           
SHEET    3   C 4 PHE A 173  ARG A 180  1  O  LEU A 179   N  GLU A 152           
SHEET    1   D 2 ALA B 107  ARG B 108  0                                        
SHEET    2   D 2 PRO B 114  ALA B 115 -1  O  ALA B 115   N  ALA B 107           
SHEET    1   E 2 LEU B 117  LEU B 118  0                                        
SHEET    1   F 4 SER B 156  ALA B 164  0                                        
SHEET    2   F 4 ALA B 145  GLN B 153 -1  N  LEU B 147   O  LEU B 163           
SHEET    3   F 4 PHE B 173  ARG B 180  1  O  LEU B 179   N  GLU B 152           
LINK         C   LEU A  96                 N   MSE A  97     1555   1555  1.33  
LINK         C   MSE A  97                 N   GLN A  98     1555   1555  1.33  
LINK         C   LEU A 118                 N   MSE A 119     1555   1555  1.33  
LINK         C   MSE A 119                 N   PRO A 120     1555   1555  1.34  
LINK         C   LEU B  96                 N   MSE B  97     1555   1555  1.33  
LINK         C   MSE B  97                 N   GLN B  98     1555   1555  1.33  
LINK         C   LEU B 118                 N   MSE B 119     1555   1555  1.33  
LINK         C   MSE B 119                 N   PRO B 120     1555   1555  1.34  
CRYST1   33.331   36.586   47.970  77.56  89.08  86.18 P 1           2          
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      0.030002 -0.002003 -0.000053        0.00000                         
SCALE2      0.000000  0.027394 -0.006026        0.00000                         
SCALE3      0.000000  0.000000  0.021348        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system