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Database: PDB
Entry: 2WL1
LinkDB: 2WL1
Original site: 2WL1 
HEADER    SIGNALING PROTEIN                       19-JUN-09   2WL1              
TITLE     PYRIN PRYSPRY DOMAIN                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PYRIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PRYSPRY, RESIDUES 586-776;                                 
COMPND   5 SYNONYM: MARENOSTRIN;                                                
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX6P                                    
KEYWDS    AMYLOIDOSIS, POLYMORPHISM, CYTOSKELETON, ACTIN-BINDING INFLAMMATORY   
KEYWDS   2 RESPONSE, METAL-BINDING, SIGNALING PROTEIN, DISEASE MUTATION,        
KEYWDS   3 PRYSPRY                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.WEINERT,P.R.MITTL,M.G.GRUETTER                                      
REVDAT   3   15-MAY-19 2WL1    1       REMARK                                   
REVDAT   2   17-NOV-09 2WL1    1       JRNL                                     
REVDAT   1   20-OCT-09 2WL1    0                                                
JRNL        AUTH   C.WEINERT,C.GRUETTER,H.ROSCHITZKI-VOSER,P.R.MITTL,           
JRNL        AUTH 2 M.G.GRUETTER                                                 
JRNL        TITL   THE CRYSTAL STRUCTURE OF HUMAN PYRIN B30.2 DOMAIN:           
JRNL        TITL 2 IMPLICATIONS FOR MUTATIONS ASSOCIATED WITH FAMILIAL          
JRNL        TITL 3 MEDITERRANEAN FEVER.                                         
JRNL        REF    J.MOL.BIOL.                   V. 394   226 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19729025                                                     
JRNL        DOI    10.1016/J.JMB.2009.08.059                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.73                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.030                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 42229                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2130                            
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 29.7375 -  3.3320    1.00     3077   161  0.1874 0.1951        
REMARK   3     2  3.3320 -  2.6453    1.00     2884   153  0.1780 0.2432        
REMARK   3     3  2.6453 -  2.3110    1.00     2808   148  0.1790 0.1747        
REMARK   3     4  2.3110 -  2.0998    1.00     2807   146  0.1771 0.2014        
REMARK   3     5  2.0998 -  1.9493    1.00     2779   147  0.1779 0.1999        
REMARK   3     6  1.9493 -  1.8344    1.00     2758   144  0.1834 0.2112        
REMARK   3     7  1.8344 -  1.7426    1.00     2788   125  0.1950 0.2261        
REMARK   3     8  1.7426 -  1.6667    1.00     2733   146  0.1954 0.2265        
REMARK   3     9  1.6667 -  1.6025    1.00     2738   148  0.2026 0.2139        
REMARK   3    10  1.6025 -  1.5473    1.00     2718   147  0.2008 0.2436        
REMARK   3    11  1.5473 -  1.4989    1.00     2726   139  0.2135 0.2196        
REMARK   3    12  1.4989 -  1.4560    0.99     2718   144  0.2204 0.2583        
REMARK   3    13  1.4560 -  1.4177    0.98     2655   147  0.2326 0.2711        
REMARK   3    14  1.4177 -  1.3831    0.95     2564   161  0.2585 0.2630        
REMARK   3    15  1.3831 -  1.3517    0.50     1346    74  0.2848 0.3093        
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              : 0.39                                          
REMARK   3   B_SOL              : 53.31                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.37                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.08370                                              
REMARK   3    B22 (A**2) : 0.08370                                              
REMARK   3    B33 (A**2) : -0.16750                                             
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      :  0.010           1631                                  
REMARK   3   ANGLE     :  1.325           2231                                  
REMARK   3   CHIRALITY :  0.087            247                                  
REMARK   3   PLANARITY :  0.006            290                                  
REMARK   3   DIHEDRAL  : 16.127            617                                  
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 2WL1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290040173.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JAN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42229                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
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     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 13.10                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.850                              
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: PDB ENTRY 2FBE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KSCN 25% PEG 2K MME 0.1M TRIS       
REMARK 280  -ACOH, PH 7.5 20C, TEMPERATURE 293K                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      121.35333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       60.67667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       91.01500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       30.33833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      151.69167            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      121.35333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       60.67667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       30.33833            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       91.01500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      151.69167            
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 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    PRO A 630      104.47    -53.45                                   
REMARK 500    LEU A 649       33.61   -142.56                                   
REMARK 500    ASN A 679       45.99     74.62                                   
REMARK 500    MET A 680      148.77    -35.80                                   
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 MET A  680     THR A  681                  145.51                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 1777                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 1778                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1779                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1780                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1781                
DBREF  2WL1 A  586   776  UNP    O15553   MEFV_HUMAN     586    776             
SEQRES   1 A  191  ASN VAL PRO GLU LEU ILE GLY ALA GLN ALA HIS ALA VAL          
SEQRES   2 A  191  ASN VAL ILE LEU ASP ALA GLU THR ALA TYR PRO ASN LEU          
SEQRES   3 A  191  ILE PHE SER ASP ASP LEU LYS SER VAL ARG LEU GLY ASN          
SEQRES   4 A  191  LYS TRP GLU ARG LEU PRO ASP GLY PRO GLN ARG PHE ASP          
SEQRES   5 A  191  SER CYS ILE ILE VAL LEU GLY SER PRO SER PHE LEU SER          
SEQRES   6 A  191  GLY ARG ARG TYR TRP GLU VAL GLU VAL GLY ASP LYS THR          
SEQRES   7 A  191  ALA TRP ILE LEU GLY ALA CYS LYS THR SER ILE SER ARG          
SEQRES   8 A  191  LYS GLY ASN MET THR LEU SER PRO GLU ASN GLY TYR TRP          
SEQRES   9 A  191  VAL VAL ILE MET MET LYS GLU ASN GLU TYR GLN ALA SER          
SEQRES  10 A  191  SER VAL PRO PRO THR ARG LEU LEU ILE LYS GLU PRO PRO          
SEQRES  11 A  191  LYS ARG VAL GLY ILE PHE VAL ASP TYR ARG VAL GLY SER          
SEQRES  12 A  191  ILE SER PHE TYR ASN VAL THR ALA ARG SER HIS ILE TYR          
SEQRES  13 A  191  THR PHE ALA SER CYS SER PHE SER GLY PRO LEU GLN PRO          
SEQRES  14 A  191  ILE PHE SER PRO GLY THR ARG ASP GLY GLY LYS ASN THR          
SEQRES  15 A  191  ALA PRO LEU THR ILE CYS PRO VAL GLY                          
HET    SCN  A1777       3                                                       
HET    SCN  A1778       3                                                       
HET    EDO  A1779       4                                                       
HET    EDO  A1780       4                                                       
HET    EDO  A1781       4                                                       
HETNAM     SCN THIOCYANATE ION                                                  
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  SCN    2(C N S 1-)                                                  
FORMUL   4  EDO    3(C2 H6 O2)                                                  
FORMUL   7  HOH   *162(H2 O)                                                    
HELIX    1   1 GLU A  589  ALA A  595  1                                   7    
HELIX    2   2 SER A  683  ASN A  686  5                                   4    
HELIX    3   3 ARG A  761  LYS A  765  5                                   5    
SHEET    1  AA 7 ILE A 601  LEU A 602  0                                        
SHEET    2  AA 7 VAL A 642  SER A 645 -1  O  SER A 645   N  ILE A 601           
SHEET    3  AA 7 LEU A 752  SER A 757 -1  O  PRO A 754   N  GLY A 644           
SHEET    4  AA 7 TRP A 665  LYS A 671 -1  O  ILE A 666   N  SER A 757           
SHEET    5  AA 7 TYR A 688  LYS A 695 -1  O  TRP A 689   N  ALA A 669           
SHEET    6  AA 7 GLU A 698  ALA A 701 -1  O  GLU A 698   N  MET A 694           
SHEET    7  AA 7 THR A 707  ARG A 708 -1  O  THR A 707   N  ALA A 701           
SHEET    1  AB 7 LEU A 611  PHE A 613  0                                        
SHEET    2  AB 7 SER A 619  LEU A 622 -1  O  ARG A 621   N  ILE A 612           
SHEET    3  AB 7 LEU A 770  CYS A 773 -1  O  LEU A 770   N  VAL A 620           
SHEET    4  AB 7 ARG A 652  GLU A 658 -1  O  GLU A 656   N  CYS A 773           
SHEET    5  AB 7 ARG A 717  ASP A 723 -1  O  VAL A 718   N  VAL A 657           
SHEET    6  AB 7 SER A 728  ASN A 733 -1  O  SER A 728   N  ASP A 723           
SHEET    7  AB 7 SER A 738  PHE A 743 -1  O  SER A 738   N  ASN A 733           
CISPEP   1 SER A  645    PRO A  646          0         6.35                     
CISPEP   2 SER A  645    PRO A  646          0         6.38                     
CISPEP   3 VAL A  704    PRO A  705          0        -1.43                     
SITE     1 AC1  4 ARG A 737  PRO A 751  HOH A2127  HOH A2159                    
SITE     1 AC2  3 ILE A 612  ARG A 708  HOH A2160                               
SITE     1 AC3  5 ALA A 595  ALA A 597  PRO A 646  SER A 647                    
SITE     2 AC3  5 HOH A2020                                                     
SITE     1 AC4  6 TRP A 665  ILE A 692  MET A 693  MET A 694                    
SITE     2 AC4  6 GLY A 759  THR A 760                                          
SITE     1 AC5  4 GLU A 589  GLY A 592  HIS A 596  ARG A 652                    
CRYST1   60.270   60.270  182.030  90.00  90.00 120.00 P 65 2 2     12          
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      0.016592  0.009579  0.000000        0.00000                         
SCALE2      0.000000  0.019159  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005494        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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