GenomeNet

Database: PDB
Entry: 1ERK
LinkDB: 1ERK
Original site: 1ERK 
HEADER    TRANSFERASE                             06-AUG-96   1ERK              
TITLE     STRUCTURE OF SIGNAL-REGULATED KINASE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXTRACELLULAR REGULATED KINASE 2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MITOGEN ACTIVATED PROTEIN (MAP) KINASE ERK2;                
COMPND   5 EC: 2.7.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 CELL_LINE: BL21;                                                     
SOURCE   6 GENE: ERK2;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: NPT7-HIS6;                                
SOURCE  11 EXPRESSION_SYSTEM_GENE: ERK2                                         
KEYWDS    TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING             
KEYWDS   2 CELL CYCLE, PHOSPHORYLATION.                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.C.HARKINS,E.J.GOLDSMITH                                             
REVDAT   2   24-FEB-09 1ERK    1       VERSN                                    
REVDAT   1   15-MAY-97 1ERK    0                                                
JRNL        AUTH   F.ZHANG,A.STRAND,D.ROBBINS,M.H.COBB,E.J.GOLDSMITH            
JRNL        TITL   ATOMIC STRUCTURE OF THE MAP KINASE ERK2 AT 2.3 A             
JRNL        TITL 2 RESOLUTION.                                                  
JRNL        REF    NATURE                        V. 367   704 1994              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   8107865                                                      
JRNL        DOI    10.1038/367704A0                                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.J.ROBINSON,P.C.HARKINS,J.ZHANG,R.BAER,                     
REMARK   1  AUTH 2 J.W.HAYCOCK,M.H.COBB,E.J.GOLDSMITH                           
REMARK   1  TITL   MUTATION OF POSITION 52 IN ERK2 CREATES A                    
REMARK   1  TITL 2 NONPRODUCTIVE BINDING MODE FOR ADENOSINE                     
REMARK   1  TITL 3 5'-TRIPHOSPHATE                                              
REMARK   1  REF    BIOCHEMISTRY                  V.  35  5641 1996              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.ZHANG,F.ZHANG,D.EBERT,M.H.COBB,E.J.GOLDSMITH               
REMARK   1  TITL   ACTIVITY OF THE MAP KINASE ERK2 IS CONTROLLED BY A           
REMARK   1  TITL 2 FLEXIBLE SURFACE LOOP                                        
REMARK   1  REF    STRUCTURE                     V.   3   299 1995              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   E.J.GOLDSMITH,M.H.COBB                                       
REMARK   1  TITL   PROTEIN KINASES                                              
REMARK   1  REF    CURR.OPIN.STRUCT.BIOL.        V.   4   833 1994              
REMARK   1  REFN                   ISSN 0959-440X                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   F.ZHANG,D.J.ROBBINS,M.H.COBB,E.J.GOLDSMITH                   
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF             
REMARK   1  TITL 2 EXTRACELLULAR SIGNAL-REGULATED KINASE-2/MAP KINASE           
REMARK   1  TITL 3 WITH AN INCORPORATED HIS-TAG                                 
REMARK   1  REF    J.MOL.BIOL.                   V. 233   550 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.50                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 16691                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : R-FREE                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 2899                                    
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) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.89                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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  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  : PARHCDX.PRO                                    
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCDX.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ERK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUN-92                          
REMARK 200  TEMPERATURE           (KELVIN) : 296                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16691                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       35.71000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
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    ALA A   3      -33.56     76.39                                   
REMARK 500    ALA A   4        7.36    -65.51                                   
REMARK 500    PRO A   9      -72.03    -63.00                                   
REMARK 500    GLU A  10       -7.84     61.77                                   
REMARK 500    MET A  11      170.67    165.47                                   
REMARK 500    VAL A  12     -126.66     49.38                                   
REMARK 500    GLN A  15     -105.45    -66.58                                   
REMARK 500    PHE A  17       51.93   -143.75                                   
REMARK 500    VAL A  19       45.09   -109.67                                   
REMARK 500    ASN A  25      109.05     55.65                                   
REMARK 500    GLU A  31     -163.13    -59.96                                   
REMARK 500    ALA A  33      -82.82    -54.37                                   
REMARK 500    MET A  36       81.50    175.72                                   
REMARK 500    LYS A  46       19.70     49.02                                   
REMARK 500    SER A  55       79.07   -160.98                                   
REMARK 500    HIS A  59      113.38   -162.93                                   
REMARK 500    THR A 116      -47.14   -145.48                                   
REMARK 500    ASN A 142       30.20     72.76                                   
REMARK 500    ARG A 146       -7.65     77.76                                   
REMARK 500    ASP A 147       44.36   -141.01                                   
REMARK 500    ASP A 165       78.97     67.63                                   
REMARK 500    ASP A 173       74.82   -165.69                                   
REMARK 500    HIS A 178      153.04    -46.25                                   
REMARK 500    VAL A 186      -62.27    -92.22                                   
REMARK 500    ALA A 187      156.44    -41.37                                   
REMARK 500    ASN A 199       29.59   -165.39                                   
REMARK 500    TYR A 231      -69.63    -27.79                                   
REMARK 500    ASN A 255      106.54    -51.88                                   
REMARK 500    LEU A 292       54.76    -91.59                                   
REMARK 500    ASP A 316       88.49   -153.76                                   
REMARK 500    PRO A 321      157.78    -48.41                                   
REMARK 500    GLU A 332       36.11     29.85                                   
REMARK 500    LEU A 333      143.87   -174.89                                   
REMARK 500    ASP A 334       33.91    -80.83                                   
REMARK 500    TYR A 356       68.34    -67.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1ERK A    1   358  UNP    P63086   MK01_RAT         1    358             
SEQRES   1 A  364  HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA ALA ALA          
SEQRES   2 A  364  GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY          
SEQRES   3 A  364  PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA          
SEQRES   4 A  364  TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS          
SEQRES   5 A  364  VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS          
SEQRES   6 A  364  GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE          
SEQRES   7 A  364  LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN          
SEQRES   8 A  364  ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP          
SEQRES   9 A  364  VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR          
SEQRES  10 A  364  LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE          
SEQRES  11 A  364  CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR          
SEQRES  12 A  364  ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  13 A  364  SER ASN LEU LEU LEU ASN THR THR CYS ASP LEU LYS ILE          
SEQRES  14 A  364  CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS          
SEQRES  15 A  364  ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG          
SEQRES  16 A  364  TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY          
SEQRES  17 A  364  TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE          
SEQRES  18 A  364  LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY          
SEQRES  19 A  364  LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE          
SEQRES  20 A  364  LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE ILE          
SEQRES  21 A  364  ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS          
SEQRES  22 A  364  LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA          
SEQRES  23 A  364  ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR          
SEQRES  24 A  364  PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU          
SEQRES  25 A  364  ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP          
SEQRES  26 A  364  GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU          
SEQRES  27 A  364  LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE          
SEQRES  28 A  364  PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER          
HELIX    1   1 PRO A   56  GLU A   58  5                                   3    
HELIX    2   2 GLN A   60  ARG A   75  1                                  16    
HELIX    3   3 LEU A  110  THR A  116  1                                   7    
HELIX    4   4 ASN A  121  ALA A  141  1                                  21    
HELIX    5   5 PRO A  150  ASN A  152  5                                   3    
HELIX    6   6 PRO A  174  HIS A  176  5                                   3    
HELIX    7   7 ARG A  189  TYR A  191  5                                   3    
HELIX    8   8 PRO A  194  LEU A  198  1                                   5    
HELIX    9   9 LYS A  205  SER A  221  5                                  17    
HELIX   10  10 TYR A  231  LEU A  242  1                                  12    
HELIX   11  11 GLN A  247  CYS A  252  1                                   6    
HELIX   12  12 LEU A  256  SER A  264  1                                   9    
HELIX   13  13 TRP A  273  LEU A  276  1                                   4    
HELIX   14  14 SER A  282  MET A  291  1                                  10    
HELIX   15  15 VAL A  302  LEU A  306  1                                   5    
HELIX   16  16 PRO A  309  LEU A  311  5                                   3    
HELIX   17  17 PRO A  317  ASP A  319  5                                   3    
HELIX   18  18 LYS A  338  PHE A  352  1                                  15    
SHEET    1   A 4 GLY A  35  ASP A  42  0                                        
SHEET    2   A 4 VAL A  47  ILE A  54 -1  N  LYS A  53   O  MET A  36           
SHEET    3   A 4 VAL A  99  ASP A 104 -1  N  GLN A 103   O  ALA A  50           
SHEET    4   A 4 ASP A  86  ARG A  89 -1  N  ILE A  88   O  TYR A 100           
SHEET    1   B 2 LEU A 153  LEU A 155  0                                        
SHEET    2   B 2 LEU A 161  ILE A 163 -1  N  LYS A 162   O  LEU A 154           
CRYST1   49.320   71.420   61.250  90.00 109.75  90.00 P 1 21 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      0.020276  0.000000  0.007280        0.00000                         
SCALE2      0.000000  0.014002  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017347        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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