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Database: PDB
Entry: 1WR1
LinkDB: 1WR1
Original site: 1WR1 
HEADER    SIGNALING PROTEIN                       08-OCT-04   1WR1              
TITLE     THE COMPLEX STRUCTURE OF DSK2P UBA WITH UBIQUITIN                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: UBIQUITIN-LIKE PROTEIN DSK2;                               
COMPND   7 CHAIN: B;                                                            
COMPND   8 FRAGMENT: C-TERMINAL UBA DOMAIN;                                     
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: UBI4 (1224-1451);                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-24A;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  13 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  14 ORGANISM_TAXID: 4932;                                                
SOURCE  15 GENE: DSK2 (982-1120);                                               
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX-KG                                   
KEYWDS    UBA DOMAIN, UBA-UBIQUITIN COMPLEX, DSK2, SIGNALING PROTEIN            
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    A.OHNO,J.G.JEE,K.FUJIWARA,T.TENNO,N.GODA,H.TOCHIO,H.HIROAKI,          
AUTHOR   2 H.KOBAYASHI,M.SHIRAKAWA                                              
REVDAT   3   09-SEP-20 1WR1    1       TITLE  REMARK SEQADV                     
REVDAT   2   24-FEB-09 1WR1    1       VERSN                                    
REVDAT   1   19-APR-05 1WR1    0                                                
JRNL        AUTH   A.OHNO,J.JEE,K.FUJIWARA,T.TENNO,N.GODA,H.TOCHIO,H.KOBAYASHI, 
JRNL        AUTH 2 H.HIROAKI,M.SHIRAKAWA                                        
JRNL        TITL   STRUCTURE OF THE UBA DOMAIN OF DSK2P IN COMPLEX WITH         
JRNL        TITL 2 UBIQUITIN MOLECULAR DETERMINANTS FOR UBIQUITIN RECOGNITION.  
JRNL        REF    STRUCTURE                     V.  13   521 2005              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   15837191                                                     
JRNL        DOI    10.1016/J.STR.2005.01.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : XWINNMR 3.5, AMBER 7                                 
REMARK   3   AUTHORS     : PEARLMAN (AMBER)                                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1WR1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-OCT-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000023898.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 6.8                                
REMARK 210  IONIC STRENGTH                 : 20MM POTASSIUM PHOSPHATE, 5MM      
REMARK 210                                   POTASSIUM CHLORIDE                 
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : U-15N, 13C UBIQUITIN + DSK2-UBA    
REMARK 210                                   COMPLEX (0.9MM); U-15N, 13C DSK2-  
REMARK 210                                   UBA + UBIQUITIN COMPLEX (1.0MM)    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 4D_13C/15N-SEPARATED_NOESY;        
REMARK 210  3D_15N-SEPARATED_NOESY; 3D_13C-SEPARATED_NOESY; 3D_13C-EDITED/      
REMARK 210  13C-FILTERED-NOESY; 3D_13C-SEPARATED_ROESY                          
REMARK 210  SPECTROMETER FIELD STRENGTH    : 800 MHZ; 900 MHZ                   
REMARK 210  SPECTROMETER MODEL             : DRX; INOVA                         
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER; VARIAN                     
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : VNMR 6.1C, NMRPIPE 2.1, SPARKY     
REMARK 210                                   3.1.0.0, CYANA 2.0.17              
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS,            
REMARK 210                                   SIMULATED ANNEALING, MOLECULAR     
REMARK 210                                   DYNAMICS, ENERGY MINIMIZATION      
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   ENERGY                             
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 16                  
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;         
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 470   MODELS 1-20                                                        
REMARK 470     RES CSSEQI  ATOMS                                                
REMARK 470     MET A   1    N                                                   
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  1 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  1 ARG B 331   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500  1 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500  3 PRO B 316   CA  -  N   -  CD  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500  3 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  4 ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500  4 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  4 PRO B 316   CA  -  N   -  CD  ANGL. DEV. =  -8.8 DEGREES          
REMARK 500  4 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  5 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  5 PRO B 316   CA  -  N   -  CD  ANGL. DEV. =  -8.9 DEGREES          
REMARK 500  5 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  6 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  6 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  6 ARG B 356   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  7 ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500  7 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500  7 PRO B 316   CA  -  N   -  CD  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500  7 ARG B 331   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  7 ARG B 356   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  8 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  9 PRO B 316   CA  -  N   -  CD  ANGL. DEV. =  -9.0 DEGREES          
REMARK 500  9 ARG B 356   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500 10 ARG B 331   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500 11 ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500 11 PRO B 316   CA  -  N   -  CD  ANGL. DEV. =  -8.9 DEGREES          
REMARK 500 12 ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500 12 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500 12 ARG A  54   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500 12 PRO B 316   CA  -  N   -  CD  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500 12 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500 13 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500 13 ARG A  54   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500 13 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500 13 ARG B 356   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500 14 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500 14 PRO B 316   CA  -  N   -  CD  ANGL. DEV. =  -8.9 DEGREES          
REMARK 500 14 ARG B 331   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500 14 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500 16 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500 16 ARG B 337   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500 16 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500 17 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500 18 ARG A  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500 18 ARG A  54   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500 18 ARG B 337   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500 18 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500 19 ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500 19 PRO B 316   CA  -  N   -  CD  ANGL. DEV. =  -8.9 DEGREES          
REMARK 500 19 ARG B 349   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      51 ANGLE DEVIATIONS.                             
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  1 GLU A  64       19.03     55.93                                   
REMARK 500  1 ARG A  74      -59.60     62.44                                   
REMARK 500  1 SER B 319     -173.65     61.17                                   
REMARK 500  2 ALA A  46       29.94     47.90                                   
REMARK 500  2 ARG A  74        5.32     56.93                                   
REMARK 500  2 ASP B 346       76.31    -66.64                                   
REMARK 500  4 GLU A  64       18.69     56.61                                   
REMARK 500  4 ARG A  74       18.98     53.34                                   
REMARK 500  4 ILE B 325        6.09    -65.85                                   
REMARK 500  5 ALA A  46       27.86     48.41                                   
REMARK 500  5 GLU A  64       22.43     49.41                                   
REMARK 500  6 ALA A  46       47.58     38.66                                   
REMARK 500  6 GLU A  64       19.05     53.35                                   
REMARK 500  6 SER B 319       88.30    -69.53                                   
REMARK 500  7 ILE B 318      -56.82     66.29                                   
REMARK 500  8 GLU A  64       20.58     49.31                                   
REMARK 500  8 ILE B 318      -86.26     44.19                                   
REMARK 500  8 ASP B 346       78.55    -69.81                                   
REMARK 500  9 ALA A  46       28.54     48.79                                   
REMARK 500  9 GLU A  64       20.37     48.51                                   
REMARK 500 10 GLU A  64       21.97     49.46                                   
REMARK 500 10 ILE B 325       71.72     54.52                                   
REMARK 500 11 GLU A  64       22.48     48.77                                   
REMARK 500 11 ARG A  74      -60.95   -132.89                                   
REMARK 500 11 ILE B 325       -2.94    -59.71                                   
REMARK 500 13 GLU A  64       20.74     49.72                                   
REMARK 500 14 GLU A  64       19.00     57.93                                   
REMARK 500 14 ARG A  74      -69.78     54.62                                   
REMARK 500 14 SER B 319       18.87     48.95                                   
REMARK 500 14 ILE B 325       25.15    -75.80                                   
REMARK 500 15 GLU A  64       18.81     54.54                                   
REMARK 500 16 PHE B 344       77.10   -102.29                                   
REMARK 500 18 ARG A  74       -0.29     45.80                                   
REMARK 500 18 ILE B 318      -82.71     52.06                                   
REMARK 500 19 ALA A  46       28.95     47.86                                   
REMARK 500 19 GLU A  64       26.00     47.08                                   
REMARK 500 20 ALA A  46       29.31     48.10                                   
REMARK 500 20 GLU A  64       19.89     50.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D3Z   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF UBIQUITIN                                      
DBREF  1WR1 A    1    76  UNP    P61864   UBIQ_YEAST       1     76             
DBREF  1WR1 B  328   373  UNP    P48510   DSK2_YEAST     328    373             
SEQADV 1WR1 PRO B  316  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 GLY B  317  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 ILE B  318  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 SER B  319  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 GLY B  320  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 GLY B  321  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 GLY B  322  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 GLY B  323  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 GLY B  324  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 ILE B  325  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 LEU B  326  UNP  P48510              CLONING ARTIFACT               
SEQADV 1WR1 ASP B  327  UNP  P48510              CLONING ARTIFACT               
SEQRES   1 A   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 A   76  THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL          
SEQRES   3 A   76  LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 A   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 A   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 A   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 B   58  PRO GLY ILE SER GLY GLY GLY GLY GLY ILE LEU ASP PRO          
SEQRES   2 B   58  GLU GLU ARG TYR GLU HIS GLN LEU ARG GLN LEU ASN ASP          
SEQRES   3 B   58  MET GLY PHE PHE ASP PHE ASP ARG ASN VAL ALA ALA LEU          
SEQRES   4 B   58  ARG ARG SER GLY GLY SER VAL GLN GLY ALA LEU ASP SER          
SEQRES   5 B   58  LEU LEU ASN GLY ASP VAL                                      
HELIX    1   1 THR A   22  GLN A   31  1                                  10    
HELIX    2   2 LEU A   56  ASN A   60  5                                   5    
HELIX    3   3 GLY B  323  LEU B  326  5                                   4    
HELIX    4   4 ASP B  327  TYR B  332  1                                   6    
HELIX    5   5 TYR B  332  GLY B  343  1                                  12    
HELIX    6   6 ASP B  346  GLY B  358  1                                  13    
HELIX    7   7 SER B  360  GLY B  371  1                                  12    
SHEET    1   A 5 THR A  12  LEU A  15  0                                        
SHEET    2   A 5 ILE A   3  LYS A   6 -1  N  VAL A   5   O  ILE A  13           
SHEET    3   A 5 SER A  65  LEU A  71  1  O  SER A  65   N  PHE A   4           
SHEET    4   A 5 GLN A  41  PHE A  45 -1  N  ARG A  42   O  VAL A  70           
SHEET    5   A 5 LYS A  48  GLN A  49 -1  O  LYS A  48   N  PHE A  45           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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