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Database: PDB
Entry: 1CKI
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Original site: 1CKI 
HEADER    PHOSPHOTRANSFERASE                      25-AUG-95   1CKI              
TITLE     RECOMBINANT CASEIN KINASE I DELTA TRUNCATION MUTANT                   
TITLE    2 CONTAINING RESIDUES 1-317                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE I DELTA;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.1.-;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: 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: 293;                                                      
SOURCE   6 ORGAN: TESTES;                                                       
SOURCE   7 GENE: T7;                                                            
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: 293;                                       
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;                                   
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PET-8C;                                   
SOURCE  13 EXPRESSION_SYSTEM_GENE: T7;                                          
SOURCE  14 OTHER_DETAILS: T7 RNA POLYMERASE                                     
KEYWDS    PROTEIN KINASE, PHOSPHOTRANSFERASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.L.LONGENECKER,P.J.ROACH,T.D.HURLEY                                  
REVDAT   2   24-FEB-09 1CKI    1       VERSN                                    
REVDAT   1   07-DEC-95 1CKI    0                                                
JRNL        AUTH   K.L.LONGENECKER,P.J.ROACH,T.D.HURLEY                         
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF MAMMALIAN CASEIN              
JRNL        TITL 2 KINASE I: MOLECULAR BASIS FOR PHOSPHATE                      
JRNL        TITL 3 RECOGNITION.                                                 
JRNL        REF    J.MOL.BIOL.                   V. 257   618 1996              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8648628                                                      
JRNL        DOI    10.1006/JMBI.1996.0189                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.XU,G.CARMEL,R.M.SWEET,J.KURET,X.CHENG                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF CASEIN KINASE-1, A                      
REMARK   1  TITL 2 PHOSPHATE-DIRECTED PROTEIN KINASE                            
REMARK   1  REF    EMBO J.                       V.  14  1015 1995              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.R.GRAVES,D.W.HAAS,C.H.HAGEDORN,A.A.DEPAOLI-ROACH,          
REMARK   1  AUTH 2 P.J.ROACH                                                    
REMARK   1  TITL   MOLECULAR CLONING, EXPRESSION, AND                           
REMARK   1  TITL 2 CHARACTERIZATION OF A 49-KILODALTON CASEIN KINASE            
REMARK   1  TITL 3 I ISOFORM FROM RAT TESTIS                                    
REMARK   1  REF    J.BIOL.CHEM.                  V. 268  6394 1993              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
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) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 78.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 25781                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
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            : 4730                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 97                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.60                          
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) : 0.25                            
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) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.72                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.17                            
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1CKI 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        : 11-MAR-95                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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 RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28665                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 76.0                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.08800                            
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: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS:    MOLECULE: RECOMBINANT CASEIN          
REMARK 280  KINASE I DELTA. CRYSTALS WERE GROWN BY THE SITTING DROP             
REMARK 280  TECHNIQUE, MIXING 3 MICROLITER OF PROTEIN SOLUTION WITH 3           
REMARK 280  MICROLITER OF RESERVOIR SOLUTION. THE PROTEIN SOLUTION              
REMARK 280  CONSISTED OF 14 MG/ML PROTEIN IN 50 MM TRIS-HCL (PH=7.5), 1 MM      
REMARK 280  EDTA, 5 MM DTT, 0.2 M NACL, 2.5 MM BETA-OCTYL GLUCOSIDE. THE        
REMARK 280  RESERVOIR SOLUTION CONTAINED 15% PEG 3400, 50 MM SODIUM             
REMARK 280  CITRATE, 50 MM DIBASIC POTASSIUM PHOSPHATE, (PH=6.8). ROOM          
REMARK 280  TEMPERATURE.                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       53.42000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       30.30000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.73500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       30.30000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.42000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.73500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   222                                                      
REMARK 465     ALA A   223                                                      
REMARK 465     ALA A   224                                                      
REMARK 465     THR A   225                                                      
REMARK 465     LYS A   226                                                      
REMARK 465     ARG A   227                                                      
REMARK 465     GLN A   228                                                      
REMARK 465     ALA A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     ASP A   307                                                      
REMARK 465     ASP A   308                                                      
REMARK 465     ALA A   309                                                      
REMARK 465     GLU A   310                                                      
REMARK 465     ARG A   311                                                      
REMARK 465     GLU A   312                                                      
REMARK 465     ARG A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     ASP A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     GLU A   317                                                      
REMARK 465     GLU A   318                                                      
REMARK 465     ARG A   319                                                      
REMARK 465     LEU A   320                                                      
REMARK 465     ARG A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     LYS B   222                                                      
REMARK 465     ALA B   223                                                      
REMARK 465     ALA B   224                                                      
REMARK 465     THR B   225                                                      
REMARK 465     LYS B   226                                                      
REMARK 465     ARG B   227                                                      
REMARK 465     GLN B   228                                                      
REMARK 465     LYS B   299                                                      
REMARK 465     PHE B   300                                                      
REMARK 465     GLY B   301                                                      
REMARK 465     ALA B   302                                                      
REMARK 465     SER B   303                                                      
REMARK 465     ARG B   304                                                      
REMARK 465     ALA B   305                                                      
REMARK 465     ALA B   306                                                      
REMARK 465     ASP B   307                                                      
REMARK 465     ASP B   308                                                      
REMARK 465     ALA B   309                                                      
REMARK 465     GLU B   310                                                      
REMARK 465     ARG B   311                                                      
REMARK 465     GLU B   312                                                      
REMARK 465     ARG B   313                                                      
REMARK 465     ARG B   314                                                      
REMARK 465     ASP B   315                                                      
REMARK 465     ARG B   316                                                      
REMARK 465     GLU B   317                                                      
REMARK 465     GLU B   318                                                      
REMARK 465     ARG B   319                                                      
REMARK 465     LEU B   320                                                      
REMARK 465     ARG B   321                                                      
REMARK 465     HIS B   322                                                      
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    ARG A  11      -11.21   -141.89                                   
REMARK 500    ALA A  34        8.52   -154.79                                   
REMARK 500    VAL A  45       -8.28    -48.46                                   
REMARK 500    LYS A  46      101.95    -58.72                                   
REMARK 500    THR A  47       27.86    -62.32                                   
REMARK 500    HIS A  49       60.78   -155.85                                   
REMARK 500    ASP A  79       29.02    -76.77                                   
REMARK 500    LEU A  88     -163.62   -116.23                                   
REMARK 500    ASP A 131       62.15   -151.21                                   
REMARK 500    LYS A 146       31.94    -98.85                                   
REMARK 500    ASP A 154       93.55     70.78                                   
REMARK 500    TYR A 291       57.07   -104.88                                   
REMARK 500    SER A 303       57.28    -95.64                                   
REMARK 500    PHE B  23       29.46   -161.48                                   
REMARK 500    LEU B  88     -150.18   -104.14                                   
REMARK 500    CYS B  99       45.08    -89.03                                   
REMARK 500    ASP B 131       55.44   -155.20                                   
REMARK 500    ASN B 136       22.40    -78.93                                   
REMARK 500    ASP B 154       95.78     66.91                                   
REMARK 500    GLU B 174     -160.29   -123.54                                   
REMARK 500    LEU B 178       97.37    -61.19                                   
REMARK 500    SER B 215     -176.05   -178.31                                   
REMARK 500    TYR B 291       47.61   -105.13                                   
REMARK 500    MET B 297       44.28   -103.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1CKI A    1   322  UNP    Q06486   KC1D_RAT         1    317             
DBREF  1CKI B    1   322  UNP    Q06486   KC1D_RAT         1    317             
SEQRES   1 A  317  MET GLU LEU ARG VAL GLY ASN ARG TYR ARG LEU GLY ARG          
SEQRES   2 A  317  LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR LEU GLY          
SEQRES   3 A  317  THR ASP ILE ALA ALA GLY GLU GLU VAL ALA ILE LYS LEU          
SEQRES   4 A  317  GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS ILE GLU          
SEQRES   5 A  317  SER LYS ILE TYR LYS MET MET GLN GLY GLY VAL GLY ILE          
SEQRES   6 A  317  PRO THR ILE ARG TRP CYS GLY ALA GLU GLY ASP TYR ASN          
SEQRES   7 A  317  VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU GLU ASP          
SEQRES   8 A  317  LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU LYS THR          
SEQRES   9 A  317  VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG ILE GLU          
SEQRES  10 A  317  TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP VAL LYS          
SEQRES  11 A  317  PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS GLY ASN          
SEQRES  12 A  317  LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS LYS TYR          
SEQRES  13 A  317  ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR ARG GLU          
SEQRES  14 A  317  ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA SER ILE          
SEQRES  15 A  317  ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP ASP          
SEQRES  16 A  317  LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE ASN LEU          
SEQRES  17 A  317  GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA THR LYS          
SEQRES  18 A  317  ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS MET SER          
SEQRES  19 A  317  THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO SER GLU          
SEQRES  20 A  317  PHE ALA THR TYR LEU ASN PHE CYS ARG SER LEU ARG PHE          
SEQRES  21 A  317  ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN LEU PHE          
SEQRES  22 A  317  ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR ASP TYR          
SEQRES  23 A  317  VAL PHE ASP TRP ASN MET LEU LYS PHE GLY ALA SER ARG          
SEQRES  24 A  317  ALA ALA ASP ASP ALA GLU ARG GLU ARG ARG ASP ARG GLU          
SEQRES  25 A  317  GLU ARG LEU ARG HIS                                          
SEQRES   1 B  317  MET GLU LEU ARG VAL GLY ASN ARG TYR ARG LEU GLY ARG          
SEQRES   2 B  317  LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR LEU GLY          
SEQRES   3 B  317  THR ASP ILE ALA ALA GLY GLU GLU VAL ALA ILE LYS LEU          
SEQRES   4 B  317  GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS ILE GLU          
SEQRES   5 B  317  SER LYS ILE TYR LYS MET MET GLN GLY GLY VAL GLY ILE          
SEQRES   6 B  317  PRO THR ILE ARG TRP CYS GLY ALA GLU GLY ASP TYR ASN          
SEQRES   7 B  317  VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU GLU ASP          
SEQRES   8 B  317  LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU LYS THR          
SEQRES   9 B  317  VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG ILE GLU          
SEQRES  10 B  317  TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP VAL LYS          
SEQRES  11 B  317  PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS GLY ASN          
SEQRES  12 B  317  LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS LYS TYR          
SEQRES  13 B  317  ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR ARG GLU          
SEQRES  14 B  317  ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA SER ILE          
SEQRES  15 B  317  ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP ASP          
SEQRES  16 B  317  LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE ASN LEU          
SEQRES  17 B  317  GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA THR LYS          
SEQRES  18 B  317  ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS MET SER          
SEQRES  19 B  317  THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO SER GLU          
SEQRES  20 B  317  PHE ALA THR TYR LEU ASN PHE CYS ARG SER LEU ARG PHE          
SEQRES  21 B  317  ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN LEU PHE          
SEQRES  22 B  317  ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR ASP TYR          
SEQRES  23 B  317  VAL PHE ASP TRP ASN MET LEU LYS PHE GLY ALA SER ARG          
SEQRES  24 B  317  ALA ALA ASP ASP ALA GLU ARG GLU ARG ARG ASP ARG GLU          
SEQRES  25 B  317  GLU ARG LEU ARG HIS                                          
FORMUL   3  HOH   *97(H2 O)                                                     
HELIX    1   1 LEU A   52  MET A   61  1                                  10    
HELIX    2   2 LEU A   92  PHE A   98  1                                   7    
HELIX    3   3 LEU A  105  LYS A  125  1                                  21    
HELIX    4   4 PRO A  134  ASN A  136  5                                   3    
HELIX    5   5 GLY A  144  LYS A  146  5                                   3    
HELIX    6   6 ILE A  187  LEU A  191  1                                   5    
HELIX    7   7 ARG A  197  LEU A  213  1                                  17    
HELIX    8   8 TYR A  230  SER A  239  1                                  10    
HELIX    9   9 ILE A  242  LEU A  245  1                                   4    
HELIX   10  10 SER A  251  SER A  262  1                                  12    
HELIX   11  11 TYR A  271  GLN A  285  1                                  15    
HELIX   12  12 ASP A  294  PHE A  300  1                                   7    
HELIX   13  13 LEU B   52  MET B   62  1                                  11    
HELIX   14  14 LEU B   92  PHE B   98  1                                   7    
HELIX   15  15 LEU B  105  LYS B  125  1                                  21    
HELIX   16  16 PRO B  134  ASN B  136  5                                   3    
HELIX   17  17 GLY B  144  ASN B  148  5                                   5    
HELIX   18  18 ILE B  187  HIS B  190  1                                   4    
HELIX   19  19 ARG B  197  LEU B  213  1                                  17    
HELIX   20  20 TYR B  230  SER B  239  1                                  10    
HELIX   21  21 ILE B  242  LEU B  245  1                                   4    
HELIX   22  22 GLU B  252  SER B  262  1                                  11    
HELIX   23  23 TYR B  271  ARG B  284  1                                  14    
HELIX   24  24 ASP B  294  ASN B  296  5                                   3    
SHEET    1   A 5 TYR A  12  LEU A  14  0                                        
SHEET    2   A 5 ASP A  25  ASP A  31 -1  N  THR A  30   O  ARG A  13           
SHEET    3   A 5 GLU A  36  CYS A  44 -1  N  LEU A  42   O  ASP A  25           
SHEET    4   A 5 TYR A  80  GLU A  86 -1  N  MET A  85   O  ALA A  39           
SHEET    5   A 5 ILE A  71  GLU A  77 -1  N  GLU A  77   O  TYR A  80           
SHEET    1   B 2 PHE A 137  MET A 139  0                                        
SHEET    2   B 2 VAL A 150  ILE A 152 -1  N  TYR A 151   O  LEU A 138           
SHEET    1   C 5 TYR B  12  LEU B  14  0                                        
SHEET    2   C 5 ASP B  25  ASP B  31 -1  N  THR B  30   O  ARG B  13           
SHEET    3   C 5 GLU B  37  CYS B  44 -1  N  LEU B  42   O  ASP B  25           
SHEET    4   C 5 TYR B  80  GLU B  86 -1  N  MET B  85   O  ALA B  39           
SHEET    5   C 5 ILE B  71  ALA B  76 -1  N  GLY B  75   O  VAL B  82           
SHEET    1   D 2 PHE B 137  MET B 139  0                                        
SHEET    2   D 2 VAL B 150  ILE B 152 -1  N  TYR B 151   O  LEU B 138           
SHEET    1   E 2 LYS A  17  SER A  20  0                                        
SHEET    2   E 2 ASP A  25  TYR A  27 -1  N  ILE A  26   O  ILE A  18           
CRYST1  106.840  115.470   60.600  90.00  90.00  90.00 P 21 21 21    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      0.009360  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008660  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016502        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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