GenomeNet

Database: PDB
Entry: 4L6B
LinkDB: 4L6B
Original site: 4L6B 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           12-JUN-13   4L6B              
TITLE     ENDOTHIAPEPSIN IN COMPLEX WITH THIOPHEN-BASED INHIBITOR SAP128        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOTHIAPEPSIN;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 90-419;                                       
COMPND   5 SYNONYM: ASPARTATE PROTEASE;                                         
COMPND   6 EC: 3.4.23.22                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA;                       
SOURCE   3 ORGANISM_COMMON: CHESNUT BLIGHT FUNGUS;                              
SOURCE   4 ORGANISM_TAXID: 5116                                                 
KEYWDS    ASPARTATE PROTEASE, INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR  
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.PARK,A.HEINE,G.KLEBE                                                
REVDAT   1   18-JUN-14 4L6B    0                                                
JRNL        AUTH   M.KUHNERT,A.PARK,A.HEINE,G.KLEBE,W.E.DIEDERICH               
JRNL        TITL   ENDOTHIAPEPSIN IN COMPLEX WITH THIOPHEN BASED INHIBITORS     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.37 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.37                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 68853                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3450                            
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 29.5897 -  3.9967    1.00     2698   135  0.1721 0.2072        
REMARK   3     2  3.9967 -  3.1735    1.00     2646   138  0.1860 0.1983        
REMARK   3     3  3.1735 -  2.7727    1.00     2646   138  0.1912 0.2023        
REMARK   3     4  2.7727 -  2.5193    1.00     2580   162  0.1812 0.2067        
REMARK   3     5  2.5193 -  2.3388    1.00     2642   146  0.1738 0.2056        
REMARK   3     6  2.3388 -  2.2010    1.00     2611   147  0.1657 0.1716        
REMARK   3     7  2.2010 -  2.0908    1.00     2649   123  0.1564 0.1703        
REMARK   3     8  2.0908 -  1.9998    1.00     2622   148  0.1515 0.2063        
REMARK   3     9  1.9998 -  1.9228    1.00     2592   140  0.1451 0.1521        
REMARK   3    10  1.9228 -  1.8565    1.00     2630   140  0.1443 0.1794        
REMARK   3    11  1.8565 -  1.7985    1.00     2633   129  0.1522 0.1995        
REMARK   3    12  1.7985 -  1.7471    1.00     2581   144  0.1553 0.2005        
REMARK   3    13  1.7471 -  1.7011    1.00     2635   130  0.1493 0.2052        
REMARK   3    14  1.7011 -  1.6596    1.00     2578   162  0.1511 0.1958        
REMARK   3    15  1.6596 -  1.6218    1.00     2611   132  0.1504 0.1908        
REMARK   3    16  1.6218 -  1.5873    1.00     2627   135  0.1475 0.1898        
REMARK   3    17  1.5873 -  1.5556    1.00     2610   132  0.1524 0.2522        
REMARK   3    18  1.5556 -  1.5262    1.00     2619   142  0.1484 0.2146        
REMARK   3    19  1.5262 -  1.4990    1.00     2605   129  0.1503 0.1853        
REMARK   3    20  1.4990 -  1.4736    1.00     2581   136  0.1489 0.1761        
REMARK   3    21  1.4736 -  1.4498    1.00     2680   130  0.1549 0.2012        
REMARK   3    22  1.4498 -  1.4275    1.00     2574   160  0.1623 0.2091        
REMARK   3    23  1.4275 -  1.4065    1.00     2613   143  0.1662 0.2045        
REMARK   3    24  1.4065 -  1.3867    1.00     2615   109  0.1667 0.2406        
REMARK   3    25  1.3867 -  1.3700    0.96     2525   120  0.1849 0.2098        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.110            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.970           
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      :  0.007           2519                                  
REMARK   3   ANGLE     :  1.235           3462                                  
REMARK   3   CHIRALITY :  0.080            408                                  
REMARK   3   PLANARITY :  0.006            441                                  
REMARK   3   DIHEDRAL  : 12.369            833                                  
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 4L6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080235.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : SI-111 DOUBLE CRYSTAL              
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68886                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.370                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NH4AC, 0.1M ACETATE-BUFFER, 26%     
REMARK 280  PEG4000, , PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.75250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  68    CG   CD   CE   NZ                                   
REMARK 470     LYS A 149    CG   CD   CE   NZ                                   
REMARK 470     LYS A 191    CG   CD   CE   NZ                                   
REMARK 470     LYS A 243    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   120     O    HOH A   806              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 129     -167.69    -79.20                                   
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 758        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH A 766        DISTANCE =  5.01 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1VS A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3T7X   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LAP   RELATED DB: PDB                                   
DBREF  4L6B A    1   330  UNP    P11838   CARP_CRYPA      90    419             
SEQRES   1 A  330  SER THR GLY SER ALA THR THR THR PRO ILE ASP SER LEU          
SEQRES   2 A  330  ASP ASP ALA TYR ILE THR PRO VAL GLN ILE GLY THR PRO          
SEQRES   3 A  330  ALA GLN THR LEU ASN LEU ASP PHE ASP THR GLY SER SER          
SEQRES   4 A  330  ASP LEU TRP VAL PHE SER SER GLU THR THR ALA SER GLU          
SEQRES   5 A  330  VAL ASP GLY GLN THR ILE TYR THR PRO SER LYS SER THR          
SEQRES   6 A  330  THR ALA LYS LEU LEU SER GLY ALA THR TRP SER ILE SER          
SEQRES   7 A  330  TYR GLY ASP GLY SER SER SER SER GLY ASP VAL TYR THR          
SEQRES   8 A  330  ASP THR VAL SER VAL GLY GLY LEU THR VAL THR GLY GLN          
SEQRES   9 A  330  ALA VAL GLU SER ALA LYS LYS VAL SER SER SER PHE THR          
SEQRES  10 A  330  GLU ASP SER THR ILE ASP GLY LEU LEU GLY LEU ALA PHE          
SEQRES  11 A  330  SER THR LEU ASN THR VAL SER PRO THR GLN GLN LYS THR          
SEQRES  12 A  330  PHE PHE ASP ASN ALA LYS ALA SER LEU ASP SER PRO VAL          
SEQRES  13 A  330  PHE THR ALA ASP LEU GLY TYR HIS ALA PRO GLY THR TYR          
SEQRES  14 A  330  ASN PHE GLY PHE ILE ASP THR THR ALA TYR THR GLY SER          
SEQRES  15 A  330  ILE THR TYR THR ALA VAL SER THR LYS GLN GLY PHE TRP          
SEQRES  16 A  330  GLU TRP THR SER THR GLY TYR ALA VAL GLY SER GLY THR          
SEQRES  17 A  330  PHE LYS SER THR SER ILE ASP GLY ILE ALA ASP THR GLY          
SEQRES  18 A  330  THR THR LEU LEU TYR LEU PRO ALA THR VAL VAL SER ALA          
SEQRES  19 A  330  TYR TRP ALA GLN VAL SER GLY ALA LYS SER SER SER SER          
SEQRES  20 A  330  VAL GLY GLY TYR VAL PHE PRO CYS SER ALA THR LEU PRO          
SEQRES  21 A  330  SER PHE THR PHE GLY VAL GLY SER ALA ARG ILE VAL ILE          
SEQRES  22 A  330  PRO GLY ASP TYR ILE ASP PHE GLY PRO ILE SER THR GLY          
SEQRES  23 A  330  SER SER SER CYS PHE GLY GLY ILE GLN SER SER ALA GLY          
SEQRES  24 A  330  ILE GLY ILE ASN ILE PHE GLY ASP VAL ALA LEU LYS ALA          
SEQRES  25 A  330  ALA PHE VAL VAL PHE ASN GLY ALA THR THR PRO THR LEU          
SEQRES  26 A  330  GLY PHE ALA SER LYS                                          
HET    DMS  A 401       4                                                       
HET    DMS  A 402       4                                                       
HET    1VS  A 403      32                                                       
HET    GOL  A 404       6                                                       
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     1VS N-ETHYL-2-({N-[2-(1H-INDOL-3-YL)ETHYL]GLYCYL}AMINO)-4-           
HETNAM   2 1VS  PHENYLTHIOPHENE-3-CARBOXAMIDE                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  DMS    2(C2 H6 O S)                                                 
FORMUL   4  1VS    C25 H26 N4 O2 S                                              
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *324(H2 O)                                                    
HELIX    1   1 THR A   49  VAL A   53  5                                   5    
HELIX    2   2 THR A   60  SER A   64  5                                   5    
HELIX    3   3 SER A  113  ASP A  119  1                                   7    
HELIX    4   4 PHE A  130  ASN A  134  5                                   5    
HELIX    5   5 THR A  143  LYS A  149  1                                   7    
HELIX    6   6 ALA A  150  LEU A  152  5                                   3    
HELIX    7   7 PRO A  228  ALA A  237  1                                  10    
HELIX    8   8 PRO A  274  TYR A  277  5                                   4    
HELIX    9   9 GLY A  306  LYS A  311  1                                   6    
SHEET    1   A 9 LYS A  68  SER A  78  0                                        
SHEET    2   A 9 SER A  84  VAL A  96 -1  O  SER A  85   N  ILE A  77           
SHEET    3   A 9 TYR A  17  ILE A  23 -1  N  GLN A  22   O  SER A  95           
SHEET    4   A 9 GLY A   3  PRO A   9 -1  N  THR A   8   O  ILE A  18           
SHEET    5   A 9 GLY A 167  PHE A 171 -1  O  PHE A 171   N  GLY A   3           
SHEET    6   A 9 VAL A 156  ASP A 160 -1  N  THR A 158   O  ASN A 170           
SHEET    7   A 9 PHE A 314  ASN A 318 -1  O  PHE A 317   N  PHE A 157           
SHEET    8   A 9 THR A 324  ALA A 328 -1  O  GLY A 326   N  VAL A 316           
SHEET    9   A 9 THR A 184  ALA A 187 -1  N  THR A 184   O  PHE A 327           
SHEET    1   B13 LYS A  68  SER A  78  0                                        
SHEET    2   B13 SER A  84  VAL A  96 -1  O  SER A  85   N  ILE A  77           
SHEET    3   B13 LEU A  99  VAL A 112 -1  O  VAL A 106   N  TYR A  90           
SHEET    4   B13 TRP A  42  VAL A  43  1  N  VAL A  43   O  ALA A 109           
SHEET    5   B13 GLY A 124  GLY A 127 -1  O  LEU A 125   N  TRP A  42           
SHEET    6   B13 GLN A  28  ASP A  35  1  N  ASP A  35   O  LEU A 126           
SHEET    7   B13 TYR A  17  ILE A  23 -1  N  VAL A  21   O  LEU A  30           
SHEET    8   B13 GLY A   3  PRO A   9 -1  N  THR A   8   O  ILE A  18           
SHEET    9   B13 GLY A 167  PHE A 171 -1  O  PHE A 171   N  GLY A   3           
SHEET   10   B13 VAL A 156  ASP A 160 -1  N  THR A 158   O  ASN A 170           
SHEET   11   B13 PHE A 314  ASN A 318 -1  O  PHE A 317   N  PHE A 157           
SHEET   12   B13 THR A 324  ALA A 328 -1  O  GLY A 326   N  VAL A 316           
SHEET   13   B13 THR A 184  ALA A 187 -1  N  THR A 184   O  PHE A 327           
SHEET    1   C 7 ALA A 269  ILE A 273  0                                        
SHEET    2   C 7 PHE A 262  VAL A 266 -1  N  PHE A 262   O  ILE A 273           
SHEET    3   C 7 GLU A 196  VAL A 204 -1  N  ALA A 203   O  THR A 263           
SHEET    4   C 7 LYS A 210  ALA A 218 -1  O  LYS A 210   N  TYR A 202           
SHEET    5   C 7 ASN A 303  PHE A 305  1  O  PHE A 305   N  ILE A 217           
SHEET    6   C 7 LEU A 225  LEU A 227 -1  N  TYR A 226   O  ILE A 304           
SHEET    7   C 7 ILE A 294  SER A 296  1  O  GLN A 295   N  LEU A 225           
SHEET    1   D 4 LYS A 243  SER A 245  0                                        
SHEET    2   D 4 GLY A 250  PRO A 254 -1  O  GLY A 250   N  SER A 245           
SHEET    3   D 4 SER A 289  GLY A 292 -1  O  CYS A 290   N  PHE A 253           
SHEET    4   D 4 ASP A 279  PRO A 282 -1  N  GLY A 281   O  PHE A 291           
SSBOND   1 CYS A  255    CYS A  290                          1555   1555  2.04  
CISPEP   1 THR A   25    PRO A   26          0        -6.15                     
CISPEP   2 SER A  137    PRO A  138          0         5.97                     
SITE     1 AC1  6 ASP A  81  GLY A 221  THR A 222  THR A 223                    
SITE     2 AC1  6 1VS A 403  HOH A 512                                          
SITE     1 AC2  6 GLY A  37  ILE A  77  SER A  78  PHE A 194                    
SITE     2 AC2  6 HOH A 535  HOH A 745                                          
SITE     1 AC3 15 ASP A  33  ASP A  35  GLY A  37  TYR A  79                    
SITE     2 AC3 15 GLY A  80  ASP A  81  SER A  83  PHE A 116                    
SITE     3 AC3 15 ASP A 119  ILE A 217  ASP A 219  GLY A 221                    
SITE     4 AC3 15 THR A 222  DMS A 401  HOH A 546                               
SITE     1 AC4  7 VAL A 272  TYR A 277  ALA A 312  SER A 329                    
SITE     2 AC4  7 LYS A 330  HOH A 536  HOH A 688                               
CRYST1   45.420   73.505   52.996  90.00 109.83  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022017  0.000000  0.007940        0.00000                         
SCALE2      0.000000  0.013605  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020059        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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