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Database: PDB
Entry: 6ATP
LinkDB: 6ATP
Original site: 6ATP 
HEADER    TRANSFERASE                             29-AUG-17   6ATP              
TITLE     CRYSTAL STRUCTURE OF APO-HGSTA1-1 EXHIBITING A NEW CONFORMATION OF C- 
TITLE    2 TERMINAL HELIX                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE A1;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GST HA SUBUNIT 1,GST CLASS-ALPHA MEMBER 1,GST-EPSILON,GSTA1-
COMPND   5 1,GTH1;                                                              
COMPND   6 EC: 2.5.1.18;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSTA1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30B(+)HGSTA1                           
KEYWDS    GLUTATHIONE S-TRANSFERASE, GLUTATHIONE TRANSFERASE, GST, HGSTA1-1,    
KEYWDS   2 APO, TRANSFERASE                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.KUMARI,X.JI                                                         
REVDAT   1   12-SEP-18 6ATP    0                                                
JRNL        AUTH   V.KUMARI,X.JI                                                
JRNL        TITL   THE DYNAMIC NATURE OF HGSTA1-1 C-TERMINAL HELIX              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   I.SINNING,G.J.KLEYWEGT,S.W.COWAN,P.REINEMER,H.W.DIRR,        
REMARK   1  AUTH 2 R.HUBER,G.L.GILLILAND,R.N.ARMSTRONG,X.JI,P.G.BOARD           
REMARK   1  TITL   STRUCTURE DETERMINATION AND REFINEMENT OF HUMAN ALPHA CLASS  
REMARK   1  TITL 2 GLUTATHIONE TRANSFERASE A1-1, AND A COMPARISON WITH THE MU   
REMARK   1  TITL 3 AND PI CLASS ENZYMES.                                        
REMARK   1  REF    J. MOL. BIOL.                 V. 232   192 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   8331657                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575)                                 
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 49359                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1007                            
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 36.5800 -  3.2483    1.00     7204   151  0.1377 0.1739        
REMARK   3     2  3.2483 -  2.5785    1.00     7148   150  0.1708 0.1905        
REMARK   3     3  2.5785 -  2.2526    1.00     7089   148  0.1712 0.1936        
REMARK   3     4  2.2526 -  2.0466    1.00     7116   143  0.1712 0.2101        
REMARK   3     5  2.0466 -  1.9000    1.00     7104   150  0.2019 0.2476        
REMARK   3     6  1.9000 -  1.7879    0.99     7002   144  0.2570 0.3225        
REMARK   3     7  1.7879 -  1.7000    0.80     5689   121  0.3128 0.3359        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.760           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3817                                  
REMARK   3   ANGLE     :  0.596           5151                                  
REMARK   3   CHIRALITY :  0.043            559                                  
REMARK   3   PLANARITY :  0.003            657                                  
REMARK   3   DIHEDRAL  : 13.304           2386                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ATP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229796.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49390                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.7200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.89000                            
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 1GUH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: ROD                                                          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000 MME, 20% (W/V), 0.05 M TRIS     
REMARK 280  HCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       49.78450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.72100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.78450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.72100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 623  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 642  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 695  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 373  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 474  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 509  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 535  LIES ON A SPECIAL POSITION.                          
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     ALA B     2                                                      
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  13      -74.81    -61.26                                   
REMARK 500    GLN A  67      112.44     80.34                                   
REMARK 500    ASP A 171      104.07   -167.29                                   
REMARK 500    ASP A 171      104.33   -167.29                                   
REMARK 500    GLU A 215      -70.07    -68.03                                   
REMARK 500    ARG A 221       42.06     73.95                                   
REMARK 500    ARG B  13      -74.15    -59.62                                   
REMARK 500    GLN B  67      114.70     77.29                                   
REMARK 500    ASP B 171      104.94   -163.88                                   
REMARK 500    ARG B 221       66.88     60.72                                   
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 A 744        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH A 745        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH A 746        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH B 649        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH B 650        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH B 651        DISTANCE =  7.08 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 303                 
DBREF  6ATP A    2   222  UNP    P08263   GSTA1_HUMAN      2    222             
DBREF  6ATP B    2   222  UNP    P08263   GSTA1_HUMAN      2    222             
SEQRES   1 A  221  ALA GLU LYS PRO LYS LEU HIS TYR PHE ASN ALA ARG GLY          
SEQRES   2 A  221  ARG MET GLU SER THR ARG TRP LEU LEU ALA ALA ALA GLY          
SEQRES   3 A  221  VAL GLU PHE GLU GLU LYS PHE ILE LYS SER ALA GLU ASP          
SEQRES   4 A  221  LEU ASP LYS LEU ARG ASN ASP GLY TYR LEU MET PHE GLN          
SEQRES   5 A  221  GLN VAL PRO MET VAL GLU ILE ASP GLY MET LYS LEU VAL          
SEQRES   6 A  221  GLN THR ARG ALA ILE LEU ASN TYR ILE ALA SER LYS TYR          
SEQRES   7 A  221  ASN LEU TYR GLY LYS ASP ILE LYS GLU ARG ALA LEU ILE          
SEQRES   8 A  221  ASP MET TYR ILE GLU GLY ILE ALA ASP LEU GLY GLU MET          
SEQRES   9 A  221  ILE LEU LEU LEU PRO VAL CYS PRO PRO GLU GLU LYS ASP          
SEQRES  10 A  221  ALA LYS LEU ALA LEU ILE LYS GLU LYS ILE LYS ASN ARG          
SEQRES  11 A  221  TYR PHE PRO ALA PHE GLU LYS VAL LEU LYS SER HIS GLY          
SEQRES  12 A  221  GLN ASP TYR LEU VAL GLY ASN LYS LEU SER ARG ALA ASP          
SEQRES  13 A  221  ILE HIS LEU VAL GLU LEU LEU TYR TYR VAL GLU GLU LEU          
SEQRES  14 A  221  ASP SER SER LEU ILE SER SER PHE PRO LEU LEU LYS ALA          
SEQRES  15 A  221  LEU LYS THR ARG ILE SER ASN LEU PRO THR VAL LYS LYS          
SEQRES  16 A  221  PHE LEU GLN PRO GLY SER PRO ARG LYS PRO PRO MET ASP          
SEQRES  17 A  221  GLU LYS SER LEU GLU GLU ALA ARG LYS ILE PHE ARG PHE          
SEQRES   1 B  221  ALA GLU LYS PRO LYS LEU HIS TYR PHE ASN ALA ARG GLY          
SEQRES   2 B  221  ARG MET GLU SER THR ARG TRP LEU LEU ALA ALA ALA GLY          
SEQRES   3 B  221  VAL GLU PHE GLU GLU LYS PHE ILE LYS SER ALA GLU ASP          
SEQRES   4 B  221  LEU ASP LYS LEU ARG ASN ASP GLY TYR LEU MET PHE GLN          
SEQRES   5 B  221  GLN VAL PRO MET VAL GLU ILE ASP GLY MET LYS LEU VAL          
SEQRES   6 B  221  GLN THR ARG ALA ILE LEU ASN TYR ILE ALA SER LYS TYR          
SEQRES   7 B  221  ASN LEU TYR GLY LYS ASP ILE LYS GLU ARG ALA LEU ILE          
SEQRES   8 B  221  ASP MET TYR ILE GLU GLY ILE ALA ASP LEU GLY GLU MET          
SEQRES   9 B  221  ILE LEU LEU LEU PRO VAL CYS PRO PRO GLU GLU LYS ASP          
SEQRES  10 B  221  ALA LYS LEU ALA LEU ILE LYS GLU LYS ILE LYS ASN ARG          
SEQRES  11 B  221  TYR PHE PRO ALA PHE GLU LYS VAL LEU LYS SER HIS GLY          
SEQRES  12 B  221  GLN ASP TYR LEU VAL GLY ASN LYS LEU SER ARG ALA ASP          
SEQRES  13 B  221  ILE HIS LEU VAL GLU LEU LEU TYR TYR VAL GLU GLU LEU          
SEQRES  14 B  221  ASP SER SER LEU ILE SER SER PHE PRO LEU LEU LYS ALA          
SEQRES  15 B  221  LEU LYS THR ARG ILE SER ASN LEU PRO THR VAL LYS LYS          
SEQRES  16 B  221  PHE LEU GLN PRO GLY SER PRO ARG LYS PRO PRO MET ASP          
SEQRES  17 B  221  GLU LYS SER LEU GLU GLU ALA ARG LYS ILE PHE ARG PHE          
HET    MPD  A 301      22                                                       
HET    MPD  A 302      22                                                       
HET    MPD  A 303      22                                                       
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
FORMUL   3  MPD    3(C6 H14 O2)                                                 
FORMUL   6  HOH   *697(H2 O)                                                    
HELIX    1 AA1 MET A   16  ALA A   26  1                                  11    
HELIX    2 AA2 SER A   37  ASP A   47  1                                  11    
HELIX    3 AA3 GLN A   67  TYR A   79  1                                  13    
HELIX    4 AA4 ASP A   85  LEU A  109  1                                  25    
HELIX    5 AA5 PRO A  110  CYS A  112  5                                   3    
HELIX    6 AA6 GLU A  116  ARG A  131  1                                  16    
HELIX    7 AA7 ARG A  131  GLY A  144  1                                  14    
HELIX    8 AA8 SER A  154  ASP A  171  1                                  18    
HELIX    9 AA9 PHE A  178  LEU A  191  1                                  14    
HELIX   10 AB1 LEU A  191  GLN A  199  1                                   9    
HELIX   11 AB2 ASP A  209  PHE A  220  1                                  12    
HELIX   12 AB3 MET B   16  ALA B   26  1                                  11    
HELIX   13 AB4 SER B   37  ASP B   47  1                                  11    
HELIX   14 AB5 GLN B   67  TYR B   79  1                                  13    
HELIX   15 AB6 ASP B   85  LEU B  109  1                                  25    
HELIX   16 AB7 PRO B  110  CYS B  112  5                                   3    
HELIX   17 AB8 PRO B  113  GLU B  115  5                                   3    
HELIX   18 AB9 GLU B  116  ARG B  131  1                                  16    
HELIX   19 AC1 ARG B  131  GLY B  144  1                                  14    
HELIX   20 AC2 SER B  154  ASP B  171  1                                  18    
HELIX   21 AC3 PHE B  178  LEU B  191  1                                  14    
HELIX   22 AC4 LEU B  191  GLN B  199  1                                   9    
HELIX   23 AC5 ASP B  209  ARG B  221  1                                  13    
SHEET    1 AA1 4 GLU A  31  ILE A  35  0                                        
SHEET    2 AA1 4 LYS A   6  PHE A  10  1  N  LEU A   7   O  LYS A  33           
SHEET    3 AA1 4 MET A  57  ILE A  60 -1  O  MET A  57   N  HIS A   8           
SHEET    4 AA1 4 MET A  63  VAL A  66 -1  O  LEU A  65   N  VAL A  58           
SHEET    1 AA2 4 GLU B  31  ILE B  35  0                                        
SHEET    2 AA2 4 LYS B   6  PHE B  10  1  N  LEU B   7   O  LYS B  33           
SHEET    3 AA2 4 MET B  57  ILE B  60 -1  O  MET B  57   N  HIS B   8           
SHEET    4 AA2 4 MET B  63  VAL B  66 -1  O  LEU B  65   N  VAL B  58           
CISPEP   1 VAL A   55    PRO A   56          0         6.29                     
CISPEP   2 VAL B   55    PRO B   56          0         3.78                     
SITE     1 AC1  5 ARG A  45  GLN A  53  HOH A 520  HOH A 542                    
SITE     2 AC1  5 HOH A 554                                                     
SITE     1 AC2  5 MET A  63  LYS A  64  LYS A 141  HOH A 443                    
SITE     2 AC2  5 MET B  94                                                     
SITE     1 AC3  4 TYR A  49  GLU A  59  HOH A 550  HOH A 576                    
CRYST1   99.569   91.442   51.621  90.00  92.38  90.00 C 1 2 1       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      0.010043  0.000000  0.000418        0.00000                         
SCALE2      0.000000  0.010936  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019389        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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