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Database: PDB
Entry: 3OEF
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Original site: 3OEF 
HEADER    TRANSFERASE                             12-AUG-10   3OEF              
TITLE     CRYSTAL STRUCTURE OF Y323F INACTIVE MUTANT OF P38ALPHA MAP KINASE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;                       
COMPND   3 CHAIN: X;                                                            
COMPND   4 SYNONYM: MAP KINASE 14, MAPK 14, MITOGEN-ACTIVATED PROTEIN KINASE P38
COMPND   5 ALPHA, MAP KINASE P38 ALPHA, CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY  
COMPND   6 DRUG-BINDING PROTEIN, CSAID-BINDING PROTEIN, CSBP, MAX-INTERACTING   
COMPND   7 PROTEIN 2, MAP KINASE MXI2, SAPK2A;                                  
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAPK14, CSBP, CSBP1, CSBP2, CSPB1, MXI2;                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MAP KINASE, INACTIVE MUTANT, TCR MEDIATED ACTIVATION, KINASE FOLD,    
KEYWDS   2 KINASE, SUBSTRATES, PHOSPHOTASES, UPSTREAM ACTIVATORS, Y323F,        
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.LIVNAH,N.TZARUM                                                     
REVDAT   2   03-JUL-13 3OEF    1       JRNL   VERSN                             
REVDAT   1   12-JAN-11 3OEF    0                                                
JRNL        AUTH   N.TZARUM,R.DISKIN,D.ENGELBERG,O.LIVNAH                       
JRNL        TITL   ACTIVE MUTANTS OF THE TCR-MEDIATED P38ALPHA ALTERNATIVE      
JRNL        TITL 2 ACTIVATION SITE SHOW CHANGES IN THE PHOSPHORYLATION LIP AND  
JRNL        TITL 3 DEF SITE FORMATION.                                          
JRNL        REF    J.MOL.BIOL.                   V. 405  1154 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   21146537                                                     
JRNL        DOI    10.1016/J.JMB.2010.11.023                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_392)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.53                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 44655                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2284                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 34.5430 -  3.4461    1.00     4460   235  0.1626 0.1934        
REMARK   3     2  3.4461 -  2.7356    1.00     4271   258  0.1805 0.2163        
REMARK   3     3  2.7356 -  2.3899    1.00     4248   235  0.1880 0.2211        
REMARK   3     4  2.3899 -  2.1714    1.00     4232   237  0.1761 0.2283        
REMARK   3     5  2.1714 -  2.0158    1.00     4195   227  0.1870 0.2347        
REMARK   3     6  2.0158 -  1.8970    1.00     4250   200  0.1840 0.2238        
REMARK   3     7  1.8970 -  1.8020    1.00     4195   222  0.1895 0.2349        
REMARK   3     8  1.8020 -  1.7235    1.00     4182   217  0.2101 0.2576        
REMARK   3     9  1.7235 -  1.6572    1.00     4184   243  0.2360 0.2820        
REMARK   3    10  1.6572 -  1.6000    0.99     4154   210  0.2917 0.3059        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 41.70                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.99                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.96680                                              
REMARK   3    B22 (A**2) : -0.44740                                             
REMARK   3    B33 (A**2) : -0.51940                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           2818                                  
REMARK   3   ANGLE     :  1.368           3821                                  
REMARK   3   CHIRALITY :  0.089            434                                  
REMARK   3   PLANARITY :  0.007            482                                  
REMARK   3   DIHEDRAL  : 18.379           1081                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3703   4.8861 -18.1057              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1239 T22:   0.0972                                     
REMARK   3      T33:   0.1180 T12:  -0.0106                                     
REMARK   3      T13:   0.0032 T23:  -0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6991 L22:   0.3416                                     
REMARK   3      L33:   0.5570 L12:  -0.2761                                     
REMARK   3      L13:  -0.2812 L23:   0.2056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0012 S12:   0.0309 S13:  -0.0796                       
REMARK   3      S21:   0.0217 S22:  -0.0309 S23:   0.0372                       
REMARK   3      S31:   0.0456 S32:  -0.0444 S33:   0.0341                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3OEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061011.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-SEP-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.25                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93                               
REMARK 200  MONOCHROMATOR                  : BEAMLINE OPTICS                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44779                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% (W/V) PEG 3350, 0.1M HEPES PH        
REMARK 280  7.25, 0.2M KF, AND 25MM B-OG, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 277K                                                    
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       32.36700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.20450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.53500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.20450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.36700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.53500            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
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     MET X     1                                                      
REMARK 465     SER X     2                                                      
REMARK 465     GLN X     3                                                      
REMARK 465     GLU X     4                                                      
REMARK 465     HIS X   174                                                      
REMARK 465     THR X   175                                                      
REMARK 465     ASP X   176                                                      
REMARK 465     ASP X   177                                                      
REMARK 465     GLU X   178                                                      
REMARK 465     MET X   179                                                      
REMARK 465     THR X   180                                                      
REMARK 465     GLY X   181                                                      
REMARK 465     TYR X   182                                                      
REMARK 465     VAL X   183                                                      
REMARK 465     ALA X   184                                                      
REMARK 465     GLN X   264                                                      
REMARK 465     MET X   265                                                      
REMARK 465     PRO X   266                                                      
REMARK 465     LEU X   353                                                      
REMARK 465     ASP X   354                                                      
REMARK 465     GLN X   355                                                      
REMARK 465     GLU X   356                                                      
REMARK 465     GLU X   357                                                      
REMARK 465     MET X   358                                                      
REMARK 465     GLU X   359                                                      
REMARK 465     SER X   360                                                      
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    ASN X 100      -19.97   -142.09                                   
REMARK 500    ARG X 149      -14.32     78.26                                   
REMARK 500    ASP X 150       41.47   -140.99                                   
REMARK 500    ASP X 168     -159.47   -157.07                                   
REMARK 500    ASN X 196       46.50     35.82                                   
REMARK 500    MET X 198     -168.98     64.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN X  115     ILE X  116                 -146.65                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH X 641        DISTANCE =  5.02 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG X 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG X 1100                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3OD6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3ODY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3ODZ   RELATED DB: PDB                                   
DBREF  3OEF X    1   360  UNP    Q16539   MK14_HUMAN       1    360             
SEQADV 3OEF PHE X  323  UNP  Q16539    TYR   323 ENGINEERED MUTATION            
SEQRES   1 X  360  MET SER GLN GLU ARG PRO THR PHE TYR ARG GLN GLU LEU          
SEQRES   2 X  360  ASN LYS THR ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN          
SEQRES   3 X  360  LEU SER PRO VAL GLY SER GLY ALA TYR GLY SER VAL CYS          
SEQRES   4 X  360  ALA ALA PHE ASP THR LYS THR GLY LEU ARG VAL ALA VAL          
SEQRES   5 X  360  LYS LYS LEU SER ARG PRO PHE GLN SER ILE ILE HIS ALA          
SEQRES   6 X  360  LYS ARG THR TYR ARG GLU LEU ARG LEU LEU LYS HIS MET          
SEQRES   7 X  360  LYS HIS GLU ASN VAL ILE GLY LEU LEU ASP VAL PHE THR          
SEQRES   8 X  360  PRO ALA ARG SER LEU GLU GLU PHE ASN ASP VAL TYR LEU          
SEQRES   9 X  360  VAL THR HIS LEU MET GLY ALA ASP LEU ASN ASN ILE VAL          
SEQRES  10 X  360  LYS CYS GLN LYS LEU THR ASP ASP HIS VAL GLN PHE LEU          
SEQRES  11 X  360  ILE TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER          
SEQRES  12 X  360  ALA ASP ILE ILE HIS ARG ASP LEU LYS PRO SER ASN LEU          
SEQRES  13 X  360  ALA VAL ASN GLU ASP CYS GLU LEU LYS ILE LEU ASP PHE          
SEQRES  14 X  360  GLY LEU ALA ARG HIS THR ASP ASP GLU MET THR GLY TYR          
SEQRES  15 X  360  VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU          
SEQRES  16 X  360  ASN TRP MET HIS TYR ASN GLN THR VAL ASP ILE TRP SER          
SEQRES  17 X  360  VAL GLY CYS ILE MET ALA GLU LEU LEU THR GLY ARG THR          
SEQRES  18 X  360  LEU PHE PRO GLY THR ASP HIS ILE ASP GLN LEU LYS LEU          
SEQRES  19 X  360  ILE LEU ARG LEU VAL GLY THR PRO GLY ALA GLU LEU LEU          
SEQRES  20 X  360  LYS LYS ILE SER SER GLU SER ALA ARG ASN TYR ILE GLN          
SEQRES  21 X  360  SER LEU THR GLN MET PRO LYS MET ASN PHE ALA ASN VAL          
SEQRES  22 X  360  PHE ILE GLY ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU          
SEQRES  23 X  360  LYS MET LEU VAL LEU ASP SER ASP LYS ARG ILE THR ALA          
SEQRES  24 X  360  ALA GLN ALA LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS          
SEQRES  25 X  360  ASP PRO ASP ASP GLU PRO VAL ALA ASP PRO PHE ASP GLN          
SEQRES  26 X  360  SER PHE GLU SER ARG ASP LEU LEU ILE ASP GLU TRP LYS          
SEQRES  27 X  360  SER LEU THR TYR ASP GLU VAL ILE SER PHE VAL PRO PRO          
SEQRES  28 X  360  PRO LEU ASP GLN GLU GLU MET GLU SER                          
HET    BOG  X1000      20                                                       
HET    BOG  X1100      20                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
FORMUL   2  BOG    2(C14 H28 O6)                                                
FORMUL   4  HOH   *329(H2 O)                                                    
HELIX    1   1 SER X   61  MET X   78  1                                  18    
HELIX    2   2 SER X   95  PHE X   99  5                                   5    
HELIX    3   3 THR X  123  ALA X  144  1                                  22    
HELIX    4   4 LYS X  152  SER X  154  5                                   3    
HELIX    5   5 ALA X  190  LEU X  195  1                                   6    
HELIX    6   6 THR X  203  GLY X  219  1                                  17    
HELIX    7   7 ASP X  227  GLY X  240  1                                  14    
HELIX    8   8 GLY X  243  LYS X  248  1                                   6    
HELIX    9   9 SER X  252  LEU X  262  1                                  11    
HELIX   10  10 ASN X  269  PHE X  274  1                                   6    
HELIX   11  11 ASN X  278  LEU X  289  1                                  12    
HELIX   12  12 ASP X  292  ARG X  296  5                                   5    
HELIX   13  13 THR X  298  ALA X  304  1                                   7    
HELIX   14  14 HIS X  305  ALA X  309  5                                   5    
HELIX   15  15 ASP X  313  GLU X  317  5                                   5    
HELIX   16  16 GLN X  325  ARG X  330  5                                   6    
HELIX   17  17 LEU X  333  SER X  347  1                                  15    
SHEET    1   A 2 PHE X   8  LEU X  13  0                                        
SHEET    2   A 2 THR X  16  PRO X  21 -1  O  TRP X  18   N  GLN X  11           
SHEET    1   B 5 TYR X  24  SER X  32  0                                        
SHEET    2   B 5 GLY X  36  ASP X  43 -1  O  ALA X  40   N  SER X  28           
SHEET    3   B 5 ARG X  49  LEU X  55 -1  O  VAL X  52   N  CYS X  39           
SHEET    4   B 5 TYR X 103  HIS X 107 -1  O  LEU X 104   N  LYS X  53           
SHEET    5   B 5 ASP X  88  PHE X  90 -1  N  ASP X  88   O  VAL X 105           
SHEET    1   C 3 ALA X 111  ASP X 112  0                                        
SHEET    2   C 3 LEU X 156  VAL X 158 -1  O  VAL X 158   N  ALA X 111           
SHEET    3   C 3 LEU X 164  ILE X 166 -1  O  LYS X 165   N  ALA X 157           
SITE     1 AC1 15 GLU X 192  TRP X 197  HIS X 199  ASN X 201                    
SITE     2 AC1 15 LEU X 246  LYS X 249  LEU X 291  ASP X 292                    
SITE     3 AC1 15 SER X 293  ASP X 294  HOH X 377  HOH X 438                    
SITE     4 AC1 15 HOH X 483  HOH X 557  HOH X 596                               
SITE     1 AC2 10 LEU X 195  ASN X 196  TRP X 197  LYS X 249                    
SITE     2 AC2 10 SER X 251  ILE X 259  LEU X 262  GLU X 336                    
SITE     3 AC2 10 HOH X 530  HOH X 663                                          
CRYST1   64.734   69.070   74.409  90.00  90.00  90.00 P 21 21 21    4          
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      0.015448  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014478  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013439        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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