HEADER    TOXIN                                   10-FEB-05   2BK1              
TITLE     THE PORE STRUCTURE OF PNEUMOLYSIN, OBTAINED BY FITTING THE ALPHA      
TITLE    2 CARBON TRACE OF PERFRINGOLYSIN O INTO A CRYO-EM MAP                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PERFRINGOLYSIN O;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 53-500;                                           
COMPND   5 SYNONYM: THETA-TOXIN, THIOL-ACTIVATED CYTOLYSIN;                     
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PERFRINGENS;                        
SOURCE   3 ORGANISM_TAXID: 1502;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYTOLYSIS, HEMOLYSIS, THIOL-ACTIVATED CYTOLYSIN, TOXIN, CRYOEM,       
KEYWDS   2 CYTOLYTIC PROTEIN                                                    
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A                                                
AUTHOR    S.J.TILLEY,E.V.ORLOVA,R.J.C.GILBERT,P.W.ANDREW,H.R.SAIBIL             
REVDAT   4   19-APR-17 2BK1    1       REMARK                                   
REVDAT   3   16-JAN-13 2BK1    1       REMARK VERSN                             
REVDAT   2   24-FEB-09 2BK1    1       VERSN                                    
REVDAT   1   04-MAY-05 2BK1    0                                                
JRNL        AUTH   S.J.TILLEY,E.V.ORLOVA,R.J.C.GILBERT,P.W.ANDREW,H.R.SAIBIL    
JRNL        TITL   STRUCTURAL BASIS OF PORE FORMATION BY THE BACTERIAL TOXIN    
JRNL        TITL 2 PNEUMOLYSIN                                                  
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 121   247 2005              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   15851031                                                     
JRNL        DOI    10.1016/J.CELL.2005.02.033                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.ROSSJOHN,S.C.FEIL,W.J.MCKINSTRY,R.K.TWETEN,M.W.PARKER      
REMARK   1  TITL   STRUCTURE OF A CHOLESTEROL-BINDING, THIOL-ACTIVATED          
REMARK   1  TITL 2 CYTOLYSIN AND A MODEL OF ITS MEMBRANE FORM                   
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  89   685 1997              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  PMID   9182756                                                      
REMARK   1  DOI    10.1016/S0092-8674(00)80251-2                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.   29.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 1PFO                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : METHOD--THE CRYSTAL STRUCTURE OF                 
REMARK   3  PERFRINOGLYSIN O (1PFO, ROSSJOHN ET AL., 1998, CELL 89, 685)WAS     
REMARK   3  PLACED INTO THE CRYO-EM DENSITY MAP (EMD-1107). THE ALPHA CARBON    
REMARK   3  TRACE OF PERFRINGOLYSIN 0 WAS MANUALLY POSITIONED INTO THE CRYO-    
REMARK   3  EM DENSITY CORRESPONDING TO THE POSITION OF ONE SUBUNIT. THE        
REMARK   3  BEST FIT WAS OBTAINED BY SEPARATING THE MONOMER INTO SIX RIGID      
REMARK   3  BODIES- DOMAIN 1(91-172, 231-272 354-373), DOMAIN 2 UPPER (53-      
REMARK   3  62, 83-90, 374-381), DOMAIN 2 LOWER (63-82, 382-390), DOMAIN 3      
REMARK   3  (177-186, 221-230, 273-283, 316-353), DOMAIN 3 HAIRPINS (187-       
REMARK   3  220, 284-315), AND DOMAIN 4 (391-500). THE COMPLETE OLIGOMER (38-   
REMARK   3  MER) WAS GENERATED AND CHECKED FOR CLOSE CONTACTS BOTH BY EYE       
REMARK   3  AND USING THE CCP4 PROGRAM CONTACT.TO IMPROVE THE FIT SECTIONS      
REMARK   3  CORRESPONDING TO 3 SUBUNITS WERE EXTRACTED FROM THE 38-MER MAP      
REMARK   3  (EMD-1107) AND A 44-MER MAP AND ALIGNED. THE WEIGHTED AVERAGE       
REMARK   3  WAS CALCULATED AND THE IMPROVED MAP USED FOR THE FINAL MANUAL       
REMARK   3  FITTING. THE TWO SECTIONS ARE CONSISTENT TO A RESOLUTION OF 28      
REMARK   3  ANGSTROMS (0.5 CORRELATION FSC) AND THE WEIGHTED AVERAGE MAP WAS    
REMARK   3  RECONSTRUCTED FROM 131 PARTICLES.                                   
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 3.500                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 29.00                          
REMARK   3   NUMBER OF PARTICLES               : 88                             
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: RESIDUES 134-142 ARE MISSING FROM THE SEQUENCE.       
REMARK   3  RESIDUES CORRESPONDING TO TO TM1 AND TM2 (187-220,284-315) WERE     
REMARK   3  MODELLED AS A POLY-ALANINE FLAT BETA HAIRPINS. THE OLIGOMER CAN     
REMARK   3  BE GENERATED BY APPLYING 38-FOLD ROTATIONAL SYMMETRY.               
REMARK   4                                                                      
REMARK   4 2BK1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-17.                  
REMARK 100 THE PDBE ID CODE IS EBI-22920.                                       
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE                      
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : PNEUMOLYSIN                       
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.05                              
REMARK 245   SAMPLE SUPPORT DETAILS         : HOLEY CARBON                      
REMARK 245   SAMPLE VITRIFICATION DETAILS   : PLUNGED INTO ETHANE               
REMARK 245   SAMPLE BUFFER                  : 8 MM NA2HP04, 1.5MM KH2PO4, 2.5   
REMARK 245                                    MM KCL, 0.25 MM NACL              
REMARK 245   PH                             : 6.95                              
REMARK 245   SAMPLE DETAILS                 : THE SAMPLE CONSISTS OF            
REMARK 245  PNEUMOLYSIN IN A MEMBRANE-INSERTED PORE STATE                       
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 100.00                         
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI F20                 
REMARK 245   DETECTOR TYPE                     : KODAK SO-163 FILM              
REMARK 245   MINIMUM DEFOCUS (NM)              : 1100.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3200.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   NOMINAL CS                        : 2.00                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 20.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 42000                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
REMARK 245   IMAGING DETAILS                   : SAMPLES WERE MAINTAINED AT     
REMARK 245  LIQUID NITROGEN TEMPERATURES IN THE ELECTRON MICROSCOPE.            
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR                   
REMARK 300 CYCLIC POINT SYMMETRY (SCHOENFLIES SYMBOL = C38).                    
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 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   BIOMT1   2  0.986361 -0.164595  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.164595  0.986361  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.945817 -0.324699  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.324699  0.945817  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.879474 -0.475947  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.475947  0.879474  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5  0.789141 -0.614213  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.614213  0.789141  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6  0.677282 -0.735724  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.735724  0.677282  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   7  0.546948 -0.837166  0.000000        0.00000            
REMARK 350   BIOMT2   7  0.837166  0.546948  0.000000        0.00000            
REMARK 350   BIOMT3   7  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   8  0.401695 -0.915773  0.000000        0.00000            
REMARK 350   BIOMT2   8  0.915773  0.401695  0.000000        0.00000            
REMARK 350   BIOMT3   8  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   9  0.245485 -0.969400  0.000000        0.00000            
REMARK 350   BIOMT2   9  0.969400  0.245485  0.000000        0.00000            
REMARK 350   BIOMT3   9  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  10  0.082579 -0.996584  0.000000        0.00000            
REMARK 350   BIOMT2  10  0.996584  0.082579  0.000000        0.00000            
REMARK 350   BIOMT3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  11 -0.082579 -0.996584  0.000000        0.00000            
REMARK 350   BIOMT2  11  0.996584 -0.082579  0.000000        0.00000            
REMARK 350   BIOMT3  11  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  12 -0.245485 -0.969400  0.000000        0.00000            
REMARK 350   BIOMT2  12  0.969400 -0.245485  0.000000        0.00000            
REMARK 350   BIOMT3  12  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  13 -0.401695 -0.915773  0.000000        0.00000            
REMARK 350   BIOMT2  13  0.915773 -0.401695  0.000000        0.00000            
REMARK 350   BIOMT3  13  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  14 -0.546948 -0.837166  0.000000        0.00000            
REMARK 350   BIOMT2  14  0.837166 -0.546948  0.000000        0.00000            
REMARK 350   BIOMT3  14  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  15 -0.677282 -0.735724  0.000000        0.00000            
REMARK 350   BIOMT2  15  0.735724 -0.677282  0.000000        0.00000            
REMARK 350   BIOMT3  15  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  16 -0.789141 -0.614213  0.000000        0.00000            
REMARK 350   BIOMT2  16  0.614213 -0.789141  0.000000        0.00000            
REMARK 350   BIOMT3  16  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  17 -0.879474 -0.475947  0.000000        0.00000            
REMARK 350   BIOMT2  17  0.475947 -0.879474  0.000000        0.00000            
REMARK 350   BIOMT3  17  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  18 -0.945817 -0.324699  0.000000        0.00000            
REMARK 350   BIOMT2  18  0.324699 -0.945817  0.000000        0.00000            
REMARK 350   BIOMT3  18  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  19 -0.986361 -0.164595  0.000000        0.00000            
REMARK 350   BIOMT2  19  0.164595 -0.986361  0.000000        0.00000            
REMARK 350   BIOMT3  19  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  20 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  20  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  20  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  21 -0.986361  0.164595  0.000000        0.00000            
REMARK 350   BIOMT2  21 -0.164595 -0.986361  0.000000        0.00000            
REMARK 350   BIOMT3  21  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  22 -0.945817  0.324699  0.000000        0.00000            
REMARK 350   BIOMT2  22 -0.324699 -0.945817  0.000000        0.00000            
REMARK 350   BIOMT3  22  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  23 -0.879474  0.475947  0.000000        0.00000            
REMARK 350   BIOMT2  23 -0.475947 -0.879474  0.000000        0.00000            
REMARK 350   BIOMT3  23  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  24 -0.789141  0.614213  0.000000        0.00000            
REMARK 350   BIOMT2  24 -0.614213 -0.789141  0.000000        0.00000            
REMARK 350   BIOMT3  24  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  25 -0.677282  0.735724  0.000000        0.00000            
REMARK 350   BIOMT2  25 -0.735724 -0.677282  0.000000        0.00000            
REMARK 350   BIOMT3  25  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  26 -0.546948  0.837166  0.000000        0.00000            
REMARK 350   BIOMT2  26 -0.837166 -0.546948  0.000000        0.00000            
REMARK 350   BIOMT3  26  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  27 -0.401695  0.915773  0.000000        0.00000            
REMARK 350   BIOMT2  27 -0.915773 -0.401695  0.000000        0.00000            
REMARK 350   BIOMT3  27  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  28 -0.245485  0.969400  0.000000        0.00000            
REMARK 350   BIOMT2  28 -0.969400 -0.245485  0.000000        0.00000            
REMARK 350   BIOMT3  28  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  29 -0.082579  0.996584  0.000000        0.00000            
REMARK 350   BIOMT2  29 -0.996584 -0.082579  0.000000        0.00000            
REMARK 350   BIOMT3  29  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  30  0.082579  0.996584  0.000000        0.00000            
REMARK 350   BIOMT2  30 -0.996584  0.082579  0.000000        0.00000            
REMARK 350   BIOMT3  30  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  31  0.245485  0.969400  0.000000        0.00000            
REMARK 350   BIOMT2  31 -0.969400  0.245485  0.000000        0.00000            
REMARK 350   BIOMT3  31  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  32  0.401695  0.915773  0.000000        0.00000            
REMARK 350   BIOMT2  32 -0.915773  0.401695  0.000000        0.00000            
REMARK 350   BIOMT3  32  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  33  0.546948  0.837166  0.000000        0.00000            
REMARK 350   BIOMT2  33 -0.837166  0.546948  0.000000        0.00000            
REMARK 350   BIOMT3  33  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  34  0.677282  0.735724  0.000000        0.00000            
REMARK 350   BIOMT2  34 -0.735724  0.677282  0.000000        0.00000            
REMARK 350   BIOMT3  34  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  35  0.789141  0.614213  0.000000        0.00000            
REMARK 350   BIOMT2  35 -0.614213  0.789141  0.000000        0.00000            
REMARK 350   BIOMT3  35  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  36  0.879474  0.475947  0.000000        0.00000            
REMARK 350   BIOMT2  36 -0.475947  0.879474  0.000000        0.00000            
REMARK 350   BIOMT3  36  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  37  0.945817  0.324699  0.000000        0.00000            
REMARK 350   BIOMT2  37 -0.324699  0.945817  0.000000        0.00000            
REMARK 350   BIOMT3  37  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  38  0.986361  0.164595  0.000000        0.00000            
REMARK 350   BIOMT2  38 -0.164595  0.986361  0.000000        0.00000            
REMARK 350   BIOMT3  38  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A   173                                                      
REMARK 465     THR A   174                                                      
REMARK 465     LEU A   175                                                      
REMARK 465     PRO A   176                                                      
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   CA   ALA A    54     CA   ASP A   111              0.96            
REMARK 500   CA   LEU A    53     CA   PHE A   114              1.52            
REMARK 500   CA   SER A    55     CA   LYS A   112              1.67            
REMARK 500   CA   PHE A   351     CA   PRO A   356              1.84            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M3I   RELATED DB: PDB                                   
REMARK 900 PERFRINGOLYSIN O, NEW CRYSTAL FORM                                   
REMARK 900 RELATED ID: 1M3J   RELATED DB: PDB                                   
REMARK 900 CRYSTAL FORM II OF PERFRINGOLYSIN O                                  
REMARK 900 RELATED ID: 1PFO   RELATED DB: PDB                                   
REMARK 900 PERFRINGOLYSIN O                                                     
REMARK 900 RELATED ID: 2BK2   RELATED DB: PDB                                   
REMARK 900 THE PORE STRUCTURE OF PNEUMOLYSIN, OBTAINED BY FITTING THE ALPHA     
REMARK 900 CARBON TRACE OF PERFRINGOLYSIN O INTO A CRYO-EM MAP                  
REMARK 900 RELATED ID: EMD-1107   RELATED DB: EMDB                              
REMARK 900 THE PORE STRUCTURE OF PNEUMOLYSIN VOLUME DATA                        
REMARK 900 RELATED ID: EMD-1108   RELATED DB: EMDB                              
REMARK 900 THE PORE STRUCTURE OF PNEUMOLYSIN VOLUME DATA                        
DBREF  2BK1 A   53   500  UNP    P19995   TACY_CLOPE      53    500             
SEQRES   1 A  448  LEU ALA SER ASN GLY ASP LYS ILE GLU SER PHE VAL PRO          
SEQRES   2 A  448  LYS GLU GLY LYS LYS THR GLY ASN LYS PHE ILE VAL VAL          
SEQRES   3 A  448  GLU ARG GLN LYS ARG SER LEU THR THR SER PRO VAL ASP          
SEQRES   4 A  448  ILE SER ILE ILE ASP SER VAL ASN ASP ARG THR TYR PRO          
SEQRES   5 A  448  GLY ALA LEU GLN LEU ALA ASP LYS ALA PHE VAL GLU ASN          
SEQRES   6 A  448  ARG PRO THR ILE LEU MET VAL LYS ARG LYS PRO ILE ASN          
SEQRES   7 A  448  ILE ASN ILE ASP LEU PRO GLY LEU LYS GLY GLU ASN SER          
SEQRES   8 A  448  ILE LYS VAL ASP ASP PRO THR TYR GLY LYS VAL SER GLY          
SEQRES   9 A  448  ALA ILE ASP GLU LEU VAL SER LYS TRP ASN GLU LYS TYR          
SEQRES  10 A  448  SER SER THR HIS THR LEU PRO ALA ARG THR GLN TYR SER          
SEQRES  11 A  448  GLU SER MET VAL TYR SER LYS SER GLN ILE SER SER ALA          
SEQRES  12 A  448  LEU ASN VAL ASN ALA LYS VAL LEU GLU ASN SER LEU GLY          
SEQRES  13 A  448  VAL ASP PHE ASN ALA VAL ALA ASN ASN GLU LYS LYS VAL          
SEQRES  14 A  448  MET ILE LEU ALA TYR LYS GLN ILE PHE TYR THR VAL SER          
SEQRES  15 A  448  ALA ASP LEU PRO LYS ASN PRO SER ASP LEU PHE ASP ASP          
SEQRES  16 A  448  SER VAL THR PHE ASN ASP LEU LYS GLN LYS GLY VAL SER          
SEQRES  17 A  448  ASN GLU ALA PRO PRO LEU MET VAL SER ASN VAL ALA TYR          
SEQRES  18 A  448  GLY ARG THR ILE TYR VAL LYS LEU GLU THR THR SER SER          
SEQRES  19 A  448  SER LYS ASP VAL GLN ALA ALA PHE LYS ALA LEU ILE LYS          
SEQRES  20 A  448  ASN THR ASP ILE LYS ASN SER GLN GLN TYR LYS ASP ILE          
SEQRES  21 A  448  TYR GLU ASN SER SER PHE THR ALA VAL VAL LEU GLY GLY          
SEQRES  22 A  448  ASP ALA GLN GLU HIS ASN LYS VAL VAL THR LYS ASP PHE          
SEQRES  23 A  448  ASP GLU ILE ARG LYS VAL ILE LYS ASP ASN ALA THR PHE          
SEQRES  24 A  448  SER THR LYS ASN PRO ALA TYR PRO ILE SER TYR THR SER          
SEQRES  25 A  448  VAL PHE LEU LYS ASP ASN SER VAL ALA ALA VAL HIS ASN          
SEQRES  26 A  448  LYS THR ASP TYR ILE GLU THR THR SER THR GLU TYR SER          
SEQRES  27 A  448  LYS GLY LYS ILE ASN LEU ASP HIS SER GLY ALA TYR VAL          
SEQRES  28 A  448  ALA GLN PHE GLU VAL ALA TRP ASP GLU VAL SER TYR ASP          
SEQRES  29 A  448  LYS GLU GLY ASN GLU VAL LEU THR HIS LYS THR TRP ASP          
SEQRES  30 A  448  GLY ASN TYR GLN ASP LYS THR ALA HIS TYR SER THR VAL          
SEQRES  31 A  448  ILE PRO LEU GLU ALA ASN ALA ARG ASN ILE ARG ILE LYS          
SEQRES  32 A  448  ALA ARG GLU CYS THR GLY LEU ALA TRP GLU TRP TRP ARG          
SEQRES  33 A  448  ASP VAL ILE SER GLU TYR ASP VAL PRO LEU THR ASN ASN          
SEQRES  34 A  448  ILE ASN VAL SER ILE TRP GLY THR THR LEU TYR PRO GLY          
SEQRES  35 A  448  SER SER ILE THR TYR ASN                                      
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  CA  LEU A  53      47.401 147.826  40.026  1.00 52.64           C  
ATOM      2  CA  ALA A  54      48.404 151.159  38.519  1.00 62.98           C  
ATOM      3  CA  SER A  55      50.504 151.605  35.388  1.00 69.35           C  
ATOM      4  CA  ASN A  56      51.928 154.873  34.081  1.00 79.20           C  
ATOM      5  CA  GLY A  57      52.447 154.742  30.325  1.00 76.74           C  
ATOM      6  CA  ASP A  58      55.112 156.697  28.443  1.00 81.15           C  
ATOM      7  CA  LYS A  59      55.758 159.911  30.347  1.00 87.90           C  
ATOM      8  CA  ILE A  60      57.586 161.882  27.710  1.00 90.56           C  
ATOM      9  CA  GLU A  61      58.912 165.332  26.601  1.00 93.40           C  
ATOM     10  CA  SER A  62      60.426 166.366  23.163  1.00 88.16           C  
ATOM     11  CA  PHE A  63      53.828 166.397  25.206  1.00 75.10           C  
ATOM     12  CA  VAL A  64      52.989 163.327  23.044  1.00 59.75           C  
ATOM     13  CA  PRO A  65      50.735 163.950  20.023  1.00 49.78           C  
ATOM     14  CA  LYS A  66      48.715 160.705  20.257  1.00 46.69           C  
ATOM     15  CA  GLU A  67      48.312 158.103  23.008  1.00 47.93           C  
ATOM     16  CA  GLY A  68      46.516 154.821  23.668  1.00 52.05           C  
ATOM     17  CA  LYS A  69      45.444 154.010  27.209  1.00 51.06           C  
ATOM     18  CA  LYS A  70      43.548 151.040  28.654  1.00 47.84           C  
ATOM     19  CA  THR A  71      41.348 151.614  31.690  1.00 43.64           C  
ATOM     20  CA  GLY A  72      39.007 148.882  32.842  1.00 50.62           C  
ATOM     21  CA  ASN A  73      37.076 147.498  29.891  1.00 52.04           C  
ATOM     22  CA  LYS A  74      37.978 150.507  27.721  1.00 44.65           C  
ATOM     23  CA  PHE A  75      40.654 151.906  25.391  1.00 39.44           C  
ATOM     24  CA  ILE A  76      41.115 155.684  25.356  1.00 35.78           C  
ATOM     25  CA  VAL A  77      42.837 157.432  22.462  1.00 37.89           C  
ATOM     26  CA  VAL A  78      43.979 160.945  23.296  1.00 37.46           C  
ATOM     27  CA  GLU A  79      45.204 163.522  20.787  1.00 44.38           C  
ATOM     28  CA  ARG A  80      47.055 166.705  21.711  1.00 47.98           C  
ATOM     29  CA  GLN A  81      47.394 170.051  19.950  1.00 52.55           C  
ATOM     30  CA  LYS A  82      49.038 173.148  21.381  1.00 43.70           C  
ATOM     31  CA  ARG A  83      47.948 166.236  26.522  1.00 38.38           C  
ATOM     32  CA  SER A  84      47.502 164.051  29.616  1.00 39.66           C  
ATOM     33  CA  LEU A  85      45.023 161.237  30.219  1.00 44.16           C  
ATOM     34  CA  THR A  86      44.101 159.657  33.581  1.00 43.90           C  
ATOM     35  CA  THR A  87      41.949 156.547  33.995  1.00 49.17           C  
ATOM     36  CA  SER A  88      40.740 154.235  36.739  1.00 46.31           C  
ATOM     37  CA  PRO A  89      38.634 151.595  35.077  1.00 43.96           C  
ATOM     38  CA  VAL A  90      37.005 149.022  37.351  1.00 38.54           C  
ATOM     39  CA  ASP A  91      35.134 143.242  38.077  1.00 38.60           C  
ATOM     40  CA  ILE A  92      38.852 142.567  37.790  1.00 36.14           C  
ATOM     41  CA  SER A  93      40.137 139.170  36.714  1.00 38.16           C  
ATOM     42  CA  ILE A  94      42.637 137.422  38.981  1.00 35.84           C  
ATOM     43  CA  ILE A  95      45.584 135.551  37.451  1.00 50.82           C  
ATOM     44  CA  ASP A  96      47.133 133.152  39.988  1.00 69.54           C  
ATOM     45  CA  SER A  97      44.042 131.830  41.789  1.00 76.11           C  
ATOM     46  CA  VAL A  98      45.933 129.950  44.535  1.00 81.34           C  
ATOM     47  CA  ASN A  99      48.834 132.356  45.039  1.00 80.15           C  
ATOM     48  CA  ASP A 100      46.858 135.519  44.588  1.00 77.45           C  
ATOM     49  CA  ARG A 101      46.428 136.640  48.141  1.00 62.40           C  
ATOM     50  CA  THR A 102      43.609 139.028  47.293  1.00 49.64           C  
ATOM     51  CA  TYR A 103      41.059 139.274  50.063  1.00 41.23           C  
ATOM     52  CA  PRO A 104      38.063 141.484  50.756  1.00 37.84           C  
ATOM     53  CA  GLY A 105      39.330 144.423  52.771  1.00 40.32           C  
ATOM     54  CA  ALA A 106      42.861 144.635  51.354  1.00 40.05           C  
ATOM     55  CA  LEU A 107      44.738 147.819  50.337  1.00 39.57           C  
ATOM     56  CA  GLN A 108      46.141 148.257  46.839  1.00 41.20           C  
ATOM     57  CA  LEU A 109      47.637 151.020  44.741  1.00 44.76           C  
ATOM     58  CA  ALA A 110      45.866 152.106  41.572  1.00 43.61           C  
ATOM     59  CA  ASP A 111      48.426 152.086  38.763  1.00 49.98           C  
ATOM     60  CA  LYS A 112      49.746 150.164  35.744  1.00 50.85           C  
ATOM     61  CA  ALA A 113      50.686 147.216  37.966  1.00 45.29           C  
ATOM     62  CA  PHE A 114      47.064 146.735  39.017  1.00 41.47           C  
ATOM     63  CA  VAL A 115      46.104 146.938  35.351  1.00 45.52           C  
ATOM     64  CA  GLU A 116      48.682 144.234  34.534  1.00 46.70           C  
ATOM     65  CA  ASN A 117      46.892 141.877  36.971  1.00 46.92           C  
ATOM     66  CA  ARG A 118      49.659 142.041  39.581  1.00 45.52           C  
ATOM     67  CA  PRO A 119      48.656 144.900  41.951  1.00 45.34           C  
ATOM     68  CA  THR A 120      50.867 146.286  44.716  1.00 46.64           C  
ATOM     69  CA  ILE A 121      49.569 145.404  48.173  1.00 53.51           C  
ATOM     70  CA  LEU A 122      50.014 147.661  51.214  1.00 54.17           C  
ATOM     71  CA  MET A 123      50.381 146.222  54.706  1.00 59.98           C  
ATOM     72  CA  VAL A 124      50.048 148.203  57.932  1.00 61.75           C  
ATOM     73  CA  LYS A 125      48.377 147.745  61.327  1.00 67.63           C  
ATOM     74  CA  ARG A 126      44.623 147.837  60.710  1.00 68.78           C  
ATOM     75  CA  LYS A 127      41.348 148.498  62.504  1.00 65.63           C  
ATOM     76  CA  PRO A 128      38.697 145.743  62.320  1.00 53.87           C  
ATOM     77  CA  ILE A 129      36.562 145.307  59.209  1.00 47.59           C  
ATOM     78  CA  ASN A 130      33.168 143.747  58.531  1.00 49.89           C  
ATOM     79  CA  ILE A 131      32.743 141.135  55.802  1.00 43.93           C  
ATOM     80  CA  ASN A 132      29.587 139.794  54.135  1.00 36.94           C  
ATOM     81  CA  ILE A 133      29.106 136.733  51.934  1.00 36.45           C  
ATOM     82  CA  ASP A 134      26.321 136.528  49.329  1.00 39.39           C  
ATOM     83  CA  LEU A 135      25.408 132.848  49.721  1.00 38.45           C  
ATOM     84  CA  PRO A 136      21.640 132.338  49.535  1.00 40.63           C  
ATOM     85  CA  GLY A 137      19.583 131.674  52.662  1.00 47.62           C  
ATOM     86  CA  LEU A 138      21.884 133.307  55.194  1.00 48.68           C  
ATOM     87  CA  LYS A 139      20.176 136.709  55.183  1.00 57.86           C  
ATOM     88  CA  GLY A 140      20.703 138.351  58.568  1.00 55.84           C  
ATOM     89  CA  GLU A 141      23.572 136.055  59.622  1.00 56.03           C  
ATOM     90  CA  ASN A 142      26.114 136.430  56.790  1.00 45.96           C  
ATOM     91  CA  SER A 143      28.329 139.018  58.471  1.00 45.53           C  
ATOM     92  CA  ILE A 144      31.368 138.823  60.712  1.00 48.80           C  
ATOM     93  CA  LYS A 145      33.816 141.340  62.145  1.00 58.56           C  
ATOM     94  CA  VAL A 146      37.495 140.657  61.465  1.00 61.85           C  
ATOM     95  CA  ASP A 147      39.629 142.331  64.114  1.00 68.16           C  
ATOM     96  CA  ASP A 148      42.991 141.807  62.425  1.00 67.91           C  
ATOM     97  CA  PRO A 149      42.392 142.045  58.647  1.00 60.33           C  
ATOM     98  CA  THR A 150      45.146 139.928  57.102  1.00 58.51           C  
ATOM     99  CA  TYR A 151      44.920 137.545  54.131  1.00 55.30           C  
ATOM    100  CA  GLY A 152      45.039 134.598  56.519  1.00 52.75           C  
ATOM    101  CA  LYS A 153      42.755 136.140  59.121  1.00 49.36           C  
ATOM    102  CA  VAL A 154      40.084 137.216  56.626  1.00 41.82           C  
ATOM    103  CA  SER A 155      40.322 133.817  54.899  1.00 44.17           C  
ATOM    104  CA  GLY A 156      39.439 132.235  58.214  1.00 47.19           C  
ATOM    105  CA  ALA A 157      36.539 134.594  58.766  1.00 44.84           C  
ATOM    106  CA  ILE A 158      35.306 133.727  55.276  1.00 40.59           C  
ATOM    107  CA  ASP A 159      35.671 130.051  56.252  1.00 44.05           C  
ATOM    108  CA  GLU A 160      33.678 130.781  59.407  1.00 45.80           C  
ATOM    109  CA  LEU A 161      30.894 132.302  57.338  1.00 38.69           C  
ATOM    110  CA  VAL A 162      30.842 129.301  54.996  1.00 41.65           C  
ATOM    111  CA  SER A 163      30.763 126.933  57.983  1.00 51.51           C  
ATOM    112  CA  LYS A 164      27.723 128.833  59.247  1.00 50.15           C  
ATOM    113  CA  TRP A 165      25.959 128.221  55.935  1.00 41.64           C  
ATOM    114  CA  ASN A 166      26.936 124.539  56.095  1.00 48.04           C  
ATOM    115  CA  GLU A 167      25.680 124.236  59.667  1.00 53.67           C  
ATOM    116  CA  LYS A 168      22.325 125.669  58.587  1.00 49.36           C  
ATOM    117  CA  TYR A 169      22.064 123.521  55.452  1.00 49.66           C  
ATOM    118  CA  SER A 170      23.785 120.334  56.688  1.00 46.14           C  
ATOM    119  CA  SER A 171      22.483 117.987  53.981  1.00 40.03           C  
ATOM    120  CA  THR A 172      23.347 120.218  50.995  1.00 39.59           C  
ATOM    121  CA  ALA A 177      31.537 125.225  46.563  1.00 32.67           C  
ATOM    122  CA  ARG A 178      28.511 126.805  44.908  1.00 29.47           C  
ATOM    123  CA  THR A 179      28.672 125.078  41.542  1.00 26.97           C  
ATOM    124  CA  GLN A 180      27.136 126.693  38.471  1.00 30.03           C  
ATOM    125  CA  TYR A 181      26.918 124.435  35.429  1.00 28.02           C  
ATOM    126  CA  SER A 182      26.875 125.633  31.822  1.00 27.61           C  
ATOM    127  CA  GLU A 183      26.754 123.424  28.743  1.00 27.16           C  
ATOM    128  CA  SER A 184      26.703 124.131  25.020  1.00 26.32           C  
ATOM    129  CA  MET A 185      27.720 122.922  21.569  1.00 29.05           C  
ATOM    130  CA  VAL A 186      30.295 124.987  19.687  1.00 31.70           C  
ATOM    131  CA  TYR A 187      27.565 118.934  18.868  1.00 99.99           C  
ATOM    132  CA  SER A 188      28.113 120.785  15.590  1.00 99.99           C  
ATOM    133  CA  LYS A 189      27.440 119.096  12.313  1.00 20.00           C  
ATOM    134  CA  SER A 190      28.148 120.968   9.074  1.00 20.00           C  
ATOM    135  CA  GLN A 191      27.613 119.275   5.708  1.00 20.00           C  
ATOM    136  CA  ILE A 192      28.257 121.168   2.470  1.00 20.00           C  
ATOM    137  CA  SER A 193      27.784 119.454  -0.896  1.00 20.00           C  
ATOM    138  CA  SER A 194      28.367 121.367  -4.136  1.00 20.00           C  
ATOM    139  CA  ALA A 195      27.959 119.634  -7.501  1.00 20.00           C  
ATOM    140  CA  LEU A 196      28.479 121.565 -10.743  1.00 20.00           C  
ATOM    141  CA  ASN A 197      28.134 119.819 -14.108  1.00 20.00           C  
ATOM    142  CA  VAL A 198      28.590 121.763 -17.350  1.00 20.00           C  
ATOM    143  CA  ASN A 199      28.309 120.000 -20.711  1.00 20.00           C  
ATOM    144  CA  ALA A 200      28.699 121.956 -23.955  1.00 20.00           C  
ATOM    145  CA  LYS A 201      28.483 120.187 -27.314  1.00 20.00           C  
ATOM    146  CA  VAL A 202      28.809 122.151 -30.561  1.00 20.00           C  
ATOM    147  CA  LEU A 203      30.963 119.894 -32.742  1.00 99.99           C  
ATOM    148  CA  GLU A 204      32.282 118.386 -33.125  1.00 99.99           C  
ATOM    149  CA  ASN A 205      33.482 120.787 -30.508  1.00 20.00           C  
ATOM    150  CA  SER A 206      33.006 118.850 -27.267  1.00 20.00           C  
ATOM    151  CA  LEU A 207      33.397 120.583 -23.902  1.00 20.00           C  
ATOM    152  CA  GLY A 208      32.857 118.660 -20.663  1.00 20.00           C  
ATOM    153  CA  VAL A 209      33.311 120.378 -17.297  1.00 20.00           C  
ATOM    154  CA  ASP A 210      32.707 118.471 -14.057  1.00 20.00           C  
ATOM    155  CA  PHE A 211      33.224 120.171 -10.691  1.00 20.00           C  
ATOM    156  CA  ASN A 212      32.558 118.285  -7.450  1.00 20.00           C  
ATOM    157  CA  ALA A 213      33.140 119.963  -4.085  1.00 20.00           C  
ATOM    158  CA  VAL A 214      32.410 118.100  -0.847  1.00 20.00           C  
ATOM    159  CA  ALA A 215      33.052 119.753   2.521  1.00 20.00           C  
ATOM    160  CA  ASN A 216      32.261 117.915   5.759  1.00 20.00           C  
ATOM    161  CA  ASN A 217      32.963 119.543   9.127  1.00 20.00           C  
ATOM    162  CA  GLU A 218      32.113 117.733  12.365  1.00 20.00           C  
ATOM    163  CA  LYS A 219      32.832 118.932  15.906  1.00 99.99           C  
ATOM    164  CA  LYS A 220      33.104 116.447  18.773  1.00 99.99           C  
ATOM    165  CA  VAL A 221      32.538 120.044  20.024  1.00 31.57           C  
ATOM    166  CA  MET A 222      30.642 120.453  23.272  1.00 30.76           C  
ATOM    167  CA  ILE A 223      31.918 122.583  26.130  1.00 28.28           C  
ATOM    168  CA  LEU A 224      30.982 122.364  29.824  1.00 24.49           C  
ATOM    169  CA  ALA A 225      31.791 124.897  32.515  1.00 22.80           C  
ATOM    170  CA  TYR A 226      31.662 124.165  36.233  1.00 22.66           C  
ATOM    171  CA  LYS A 227      31.967 127.505  38.007  1.00 25.77           C  
ATOM    172  CA  GLN A 228      32.922 126.967  41.656  1.00 27.11           C  
ATOM    173  CA  ILE A 229      32.075 129.997  43.795  1.00 29.56           C  
ATOM    174  CA  PHE A 230      33.471 129.954  47.338  1.00 32.83           C  
ATOM    175  CA  TYR A 231      29.845 133.145  46.036  1.00 31.19           C  
ATOM    176  CA  THR A 232      31.411 136.571  46.630  1.00 32.62           C  
ATOM    177  CA  VAL A 233      32.541 138.289  49.847  1.00 34.56           C  
ATOM    178  CA  SER A 234      32.436 142.052  50.343  1.00 39.45           C  
ATOM    179  CA  ALA A 235      33.932 144.415  52.907  1.00 41.06           C  
ATOM    180  CA  ASP A 236      31.943 147.286  54.419  1.00 45.72           C  
ATOM    181  CA  LEU A 237      33.247 150.571  53.069  1.00 51.46           C  
ATOM    182  CA  PRO A 238      34.710 152.865  55.806  1.00 57.09           C  
ATOM    183  CA  LYS A 239      33.380 156.431  56.047  1.00 64.04           C  
ATOM    184  CA  ASN A 240      36.895 157.689  56.536  1.00 64.78           C  
ATOM    185  CA  PRO A 241      40.258 156.367  55.267  1.00 61.87           C  
ATOM    186  CA  SER A 242      41.469 156.612  58.894  1.00 61.60           C  
ATOM    187  CA  ASP A 243      38.901 154.098  60.208  1.00 60.58           C  
ATOM    188  CA  LEU A 244      40.766 151.420  58.222  1.00 56.94           C  
ATOM    189  CA  PHE A 245      44.191 152.306  59.593  1.00 64.91           C  
ATOM    190  CA  ASP A 246      45.403 151.683  63.097  1.00 71.39           C  
ATOM    191  CA  ASP A 247      46.154 155.052  64.677  1.00 77.65           C  
ATOM    192  CA  SER A 248      49.934 154.463  64.727  1.00 74.26           C  
ATOM    193  CA  VAL A 249      50.046 154.573  60.929  1.00 72.03           C  
ATOM    194  CA  THR A 250      50.883 157.993  59.496  1.00 71.67           C  
ATOM    195  CA  PHE A 251      50.289 159.425  56.044  1.00 73.20           C  
ATOM    196  CA  ASN A 252      54.072 159.240  55.744  1.00 76.14           C  
ATOM    197  CA  ASP A 253      54.125 155.457  56.037  1.00 72.82           C  
ATOM    198  CA  LEU A 254      51.580 155.355  53.197  1.00 63.60           C  
ATOM    199  CA  LYS A 255      53.614 157.509  50.801  1.00 62.30           C  
ATOM    200  CA  GLN A 256      56.665 155.501  51.774  1.00 67.75           C  
ATOM    201  CA  LYS A 257      54.675 152.407  50.773  1.00 57.09           C  
ATOM    202  CA  GLY A 258      53.919 153.941  47.382  1.00 48.72           C  
ATOM    203  CA  VAL A 259      50.867 156.166  47.735  1.00 46.13           C  
ATOM    204  CA  SER A 260      51.035 159.181  45.444  1.00 51.08           C  
ATOM    205  CA  ASN A 261      48.987 161.088  42.854  1.00 56.48           C  
ATOM    206  CA  GLU A 262      49.526 158.431  40.188  1.00 58.44           C  
ATOM    207  CA  ALA A 263      49.267 155.630  42.744  1.00 40.61           C  
ATOM    208  CA  PRO A 264      46.013 156.463  44.631  1.00 37.98           C  
ATOM    209  CA  PRO A 265      45.075 154.211  47.594  1.00 42.57           C  
ATOM    210  CA  LEU A 266      42.338 151.574  47.245  1.00 40.43           C  
ATOM    211  CA  MET A 267      40.493 148.930  49.219  1.00 37.86           C  
ATOM    212  CA  VAL A 268      39.273 145.618  47.846  1.00 37.58           C  
ATOM    213  CA  SER A 269      35.494 145.742  48.381  1.00 38.53           C  
ATOM    214  CA  ASN A 270      34.481 142.557  46.543  1.00 37.35           C  
ATOM    215  CA  VAL A 271      36.037 139.188  45.765  1.00 29.33           C  
ATOM    216  CA  ALA A 272      34.414 136.474  43.634  1.00 27.48           C  
ATOM    217  CA  TYR A 273      36.081 134.058  44.348  1.00 30.82           C  
ATOM    218  CA  GLY A 274      36.894 130.440  43.490  1.00 31.68           C  
ATOM    219  CA  ARG A 275      37.855 128.558  40.330  1.00 32.44           C  
ATOM    220  CA  THR A 276      36.360 127.094  37.150  1.00 28.56           C  
ATOM    221  CA  ILE A 277      36.554 123.667  35.503  1.00 28.00           C  
ATOM    222  CA  TYR A 278      36.224 123.711  31.737  1.00 24.23           C  
ATOM    223  CA  VAL A 279      35.595 120.503  29.796  1.00 24.35           C  
ATOM    224  CA  LYS A 280      35.671 119.826  26.061  1.00 25.99           C  
ATOM    225  CA  LEU A 281      34.028 116.761  24.459  1.00 25.92           C  
ATOM    226  CA  GLU A 282      35.173 116.358  20.853  1.00 32.89           C  
ATOM    227  CA  THR A 283      34.515 113.895  18.032  1.00 27.18           C  
ATOM    228  CA  THR A 284      37.027 117.537  15.671  1.00 99.99           C  
ATOM    229  CA  SER A 285      35.982 116.649  12.124  1.00 99.99           C  
ATOM    230  CA  SER A 286      37.746 118.164   9.182  1.00 20.00           C  
ATOM    231  CA  SER A 287      37.210 116.470   5.815  1.00 20.00           C  
ATOM    232  CA  LYS A 288      37.855 118.362   2.576  1.00 20.00           C  
ATOM    233  CA  ASP A 289      37.384 116.652  -0.791  1.00 20.00           C  
ATOM    234  CA  VAL A 290      37.967 118.562  -4.029  1.00 20.00           C  
ATOM    235  CA  GLN A 291      37.559 116.832  -7.394  1.00 20.00           C  
ATOM    236  CA  ALA A 292      38.078 118.761 -10.636  1.00 20.00           C  
ATOM    237  CA  ALA A 293      37.731 117.016 -14.000  1.00 20.00           C  
ATOM    238  CA  PHE A 294      38.189 118.957 -17.241  1.00 20.00           C  
ATOM    239  CA  LYS A 295      37.907 117.198 -20.603  1.00 20.00           C  
ATOM    240  CA  ALA A 296      38.297 119.153 -23.847  1.00 20.00           C  
ATOM    241  CA  LEU A 297      38.083 117.383 -27.210  1.00 20.00           C  
ATOM    242  CA  ILE A 298      38.407 119.348 -30.453  1.00 20.00           C  
ATOM    243  CA  LYS A 299      40.562 117.093 -32.638  1.00 99.99           C  
ATOM    244  CA  ASN A 300      41.883 115.578 -33.017  1.00 99.99           C  
ATOM    245  CA  THR A 301      43.081 117.985 -30.400  1.00 20.00           C  
ATOM    246  CA  ASP A 302      42.604 116.045 -27.160  1.00 20.00           C  
ATOM    247  CA  ILE A 303      42.996 117.780 -23.794  1.00 20.00           C  
ATOM    248  CA  LYS A 304      42.455 115.858 -20.554  1.00 20.00           C  
ATOM    249  CA  ASN A 305      42.911 117.576 -17.189  1.00 20.00           C  
ATOM    250  CA  SER A 306      42.305 115.670 -13.950  1.00 20.00           C  
ATOM    251  CA  GLN A 307      42.823 117.369 -10.585  1.00 20.00           C  
ATOM    252  CA  GLN A 308      42.157 115.482  -7.345  1.00 20.00           C  
ATOM    253  CA  TYR A 309      42.736 117.160  -3.977  1.00 20.00           C  
ATOM    254  CA  LYS A 310      42.009 115.296  -0.739  1.00 20.00           C  
ATOM    255  CA  ASP A 311      42.649 116.950   2.628  1.00 20.00           C  
ATOM    256  CA  ILE A 312      41.859 115.113   5.867  1.00 20.00           C  
ATOM    257  CA  TYR A 313      42.563 116.741   9.233  1.00 20.00           C  
ATOM    258  CA  GLU A 314      41.743 115.281  12.655  1.00 99.99           C  
ATOM    259  CA  ASN A 315      41.431 117.543  15.694  1.00 99.99           C  
ATOM    260  CA  SER A 316      35.823 111.163  20.860  1.00 33.10           C  
ATOM    261  CA  SER A 317      38.356 112.723  23.177  1.00 31.24           C  
ATOM    262  CA  PHE A 318      37.788 114.688  26.370  1.00 27.82           C  
ATOM    263  CA  THR A 319      39.893 117.515  27.788  1.00 27.16           C  
ATOM    264  CA  ALA A 320      39.665 119.102  31.255  1.00 27.06           C  
ATOM    265  CA  VAL A 321      41.516 122.153  32.575  1.00 29.40           C  
ATOM    266  CA  VAL A 322      41.129 123.919  35.910  1.00 29.76           C  
ATOM    267  CA  LEU A 323      41.554 127.699  35.875  1.00 39.58           C  
ATOM    268  CA  GLY A 324      41.577 130.104  38.776  1.00 56.31           C  
ATOM    269  CA  GLY A 325      42.616 129.720  42.385  1.00 65.78           C  
ATOM    270  CA  ASP A 326      44.779 126.944  43.804  1.00 71.84           C  
ATOM    271  CA  ALA A 327      45.593 125.264  40.490  1.00 66.18           C  
ATOM    272  CA  GLN A 328      49.078 125.004  39.011  1.00 50.67           C  
ATOM    273  CA  GLU A 329      48.795 126.871  35.733  1.00 42.02           C  
ATOM    274  CA  HIS A 330      48.387 124.920  32.490  1.00 35.02           C  
ATOM    275  CA  ASN A 331      47.242 121.758  34.211  1.00 30.77           C  
ATOM    276  CA  LYS A 332      45.373 119.500  31.821  1.00 29.18           C  
ATOM    277  CA  VAL A 333      43.797 116.117  31.290  1.00 29.30           C  
ATOM    278  CA  VAL A 334      43.226 114.518  27.870  1.00 28.88           C  
ATOM    279  CA  THR A 335      41.472 111.118  27.797  1.00 33.78           C  
ATOM    280  CA  LYS A 336      39.152 108.701  26.046  1.00 33.58           C  
ATOM    281  CA  ASP A 337      37.802 107.505  29.394  1.00 32.44           C  
ATOM    282  CA  PHE A 338      35.321 110.074  30.745  1.00 31.22           C  
ATOM    283  CA  ASP A 339      35.732 108.693  34.263  1.00 34.90           C  
ATOM    284  CA  GLU A 340      38.975 110.658  34.449  1.00 36.43           C  
ATOM    285  CA  ILE A 341      37.039 113.821  33.639  1.00 33.09           C  
ATOM    286  CA  ARG A 342      34.473 112.966  36.296  1.00 31.98           C  
ATOM    287  CA  LYS A 343      37.342 112.834  38.785  1.00 32.22           C  
ATOM    288  CA  VAL A 344      38.620 116.348  37.939  1.00 33.39           C  
ATOM    289  CA  ILE A 345      35.076 117.761  38.304  1.00 32.22           C  
ATOM    290  CA  LYS A 346      34.588 115.924  41.627  1.00 33.61           C  
ATOM    291  CA  ASP A 347      38.009 116.837  43.073  1.00 32.80           C  
ATOM    292  CA  ASN A 348      37.766 120.550  42.356  1.00 34.20           C  
ATOM    293  CA  ALA A 349      34.428 121.388  43.960  1.00 34.20           C  
ATOM    294  CA  THR A 350      35.695 121.847  47.547  1.00 33.42           C  
ATOM    295  CA  PHE A 351      36.464 125.157  49.202  1.00 34.75           C  
ATOM    296  CA  SER A 352      39.171 125.096  51.851  1.00 36.66           C  
ATOM    297  CA  THR A 353      38.342 127.988  54.166  1.00 38.40           C  
ATOM    298  CA  LYS A 354      32.907 121.670  52.065  1.00 43.40           C  
ATOM    299  CA  ASN A 355      35.992 122.217  49.873  1.00 41.32           C  
ATOM    300  CA  PRO A 356      38.179 125.355  49.828  1.00 41.41           C  
ATOM    301  CA  ALA A 357      37.498 128.077  47.237  1.00 34.76           C  
ATOM    302  CA  TYR A 358      39.881 130.638  45.731  1.00 38.32           C  
ATOM    303  CA  PRO A 359      39.532 134.210  44.420  1.00 37.20           C  
ATOM    304  CA  ILE A 360      38.720 134.424  40.726  1.00 32.53           C  
ATOM    305  CA  SER A 361      38.146 138.183  40.401  1.00 27.27           C  
ATOM    306  CA  TYR A 362      37.489 141.271  42.523  1.00 32.15           C  
ATOM    307  CA  THR A 363      36.440 144.929  42.579  1.00 42.51           C  
ATOM    308  CA  SER A 364      38.066 147.898  44.300  1.00 40.98           C  
ATOM    309  CA  VAL A 365      37.056 151.249  45.747  1.00 43.27           C  
ATOM    310  CA  PHE A 366      39.196 154.412  45.808  1.00 44.95           C  
ATOM    311  CA  LEU A 367      39.944 155.520  49.363  1.00 46.79           C  
ATOM    312  CA  LYS A 368      39.415 159.158  48.315  1.00 50.56           C  
ATOM    313  CA  ASP A 369      35.793 159.304  47.186  1.00 51.74           C  
ATOM    314  CA  ASN A 370      35.066 155.682  48.122  1.00 42.34           C  
ATOM    315  CA  SER A 371      33.990 155.142  44.505  1.00 42.90           C  
ATOM    316  CA  VAL A 372      34.275 151.874  42.568  1.00 41.75           C  
ATOM    317  CA  ALA A 373      37.510 151.639  40.573  1.00 42.29           C  
ATOM    318  CA  ALA A 374      40.785 149.593  39.851  1.00 47.04           C  
ATOM    319  CA  VAL A 375      43.698 149.875  37.411  1.00 45.67           C  
ATOM    320  CA  HIS A 376      45.141 153.356  37.480  1.00 47.09           C  
ATOM    321  CA  ASN A 377      46.657 154.668  34.270  1.00 43.52           C  
ATOM    322  CA  LYS A 378      48.312 158.024  33.660  1.00 47.10           C  
ATOM    323  CA  THR A 379      49.937 158.932  30.348  1.00 51.00           C  
ATOM    324  CA  ASP A 380      50.908 161.969  28.345  1.00 47.41           C  
ATOM    325  CA  TYR A 381      50.804 162.041  24.568  1.00 36.63           C  
ATOM    326  CA  ILE A 382      47.324 171.661  25.530  1.00 38.61           C  
ATOM    327  CA  GLU A 383      44.003 170.887  23.930  1.00 42.83           C  
ATOM    328  CA  THR A 384      42.992 167.257  24.241  1.00 44.29           C  
ATOM    329  CA  THR A 385      40.439 165.323  22.193  1.00 44.91           C  
ATOM    330  CA  SER A 386      39.646 161.714  23.020  1.00 42.59           C  
ATOM    331  CA  THR A 387      37.755 158.694  21.749  1.00 40.46           C  
ATOM    332  CA  GLU A 388      36.541 155.802  23.859  1.00 35.79           C  
ATOM    333  CA  TYR A 389      36.490 152.185  22.690  1.00 36.96           C  
ATOM    334  CA  SER A 390      34.966 149.289  24.545  1.00 42.67           C  
ATOM    335  CA  LYS A 391      51.793 153.656  19.796  1.00 39.74           C  
ATOM    336  CA  GLY A 392      48.784 152.749  17.673  1.00 36.06           C  
ATOM    337  CA  LYS A 393      47.817 151.235  14.334  1.00 39.02           C  
ATOM    338  CA  ILE A 394      45.329 151.993  11.559  1.00 31.80           C  
ATOM    339  CA  ASN A 395      43.365 148.978  10.313  1.00 37.10           C  
ATOM    340  CA  LEU A 396      41.890 149.219   6.818  1.00 34.47           C  
ATOM    341  CA  ASP A 397      39.224 146.793   5.565  1.00 38.00           C  
ATOM    342  CA  HIS A 398      37.781 147.084   2.084  1.00 38.37           C  
ATOM    343  CA  SER A 399      34.853 144.760   1.412  1.00 39.17           C  
ATOM    344  CA  GLY A 400      33.065 147.065  -1.006  1.00 36.17           C  
ATOM    345  CA  ALA A 401      31.875 146.041  -4.455  1.00 33.72           C  
ATOM    346  CA  TYR A 402      34.121 148.603  -6.153  1.00 31.59           C  
ATOM    347  CA  VAL A 403      37.705 149.728  -6.704  1.00 31.83           C  
ATOM    348  CA  ALA A 404      38.936 152.224  -4.130  1.00 29.84           C  
ATOM    349  CA  GLN A 405      42.035 154.232  -3.334  1.00 25.58           C  
ATOM    350  CA  PHE A 406      43.262 155.498  -0.003  1.00 26.27           C  
ATOM    351  CA  GLU A 407      45.091 158.476   1.277  1.00 27.26           C  
ATOM    352  CA  VAL A 408      46.556 158.119   4.739  1.00 26.76           C  
ATOM    353  CA  ALA A 409      48.826 160.851   6.074  1.00 25.38           C  
ATOM    354  CA  TRP A 410      50.050 162.155   9.411  1.00 26.91           C  
ATOM    355  CA  ASP A 411      52.825 164.108  11.098  1.00 34.42           C  
ATOM    356  CA  GLU A 412      55.425 162.975  13.618  1.00 37.51           C  
ATOM    357  CA  VAL A 413      56.146 165.601  16.272  1.00 38.86           C  
ATOM    358  CA  SER A 414      59.429 166.425  17.996  1.00 38.79           C  
ATOM    359  CA  TYR A 415      60.785 169.501  19.781  1.00 40.52           C  
ATOM    360  CA  ASP A 416      63.862 171.526  18.930  1.00 51.58           C  
ATOM    361  CA  LYS A 417      66.338 172.745  21.572  1.00 61.35           C  
ATOM    362  CA  GLU A 418      64.017 175.746  22.023  1.00 64.27           C  
ATOM    363  CA  GLY A 419      61.166 173.430  23.005  1.00 56.27           C  
ATOM    364  CA  ASN A 420      59.432 174.311  19.741  1.00 54.47           C  
ATOM    365  CA  GLU A 421      57.416 171.794  17.748  1.00 48.01           C  
ATOM    366  CA  VAL A 422      58.739 170.236  14.566  1.00 43.15           C  
ATOM    367  CA  LEU A 423      56.394 168.286  12.329  1.00 40.65           C  
ATOM    368  CA  THR A 424      57.604 165.679   9.871  1.00 38.91           C  
ATOM    369  CA  HIS A 425      55.010 164.607   7.306  1.00 39.95           C  
ATOM    370  CA  LYS A 426      54.474 160.893   6.630  1.00 33.96           C  
ATOM    371  CA  THR A 427      52.212 158.982   4.246  1.00 34.00           C  
ATOM    372  CA  TRP A 428      51.189 155.377   3.650  1.00 32.59           C  
ATOM    373  CA  ASP A 429      53.116 153.921   0.685  1.00 36.57           C  
ATOM    374  CA  GLY A 430      49.878 152.363  -0.473  1.00 29.69           C  
ATOM    375  CA  ASN A 431      48.254 155.749  -1.121  1.00 31.75           C  
ATOM    376  CA  TYR A 432      46.533 156.334  -4.476  1.00 33.47           C  
ATOM    377  CA  GLN A 433      46.597 152.696  -5.519  1.00 33.94           C  
ATOM    378  CA  ASP A 434      43.681 150.498  -6.556  1.00 37.22           C  
ATOM    379  CA  LYS A 435      42.426 148.083  -3.901  1.00 37.91           C  
ATOM    380  CA  THR A 436      39.725 145.555  -4.788  1.00 45.89           C  
ATOM    381  CA  ALA A 437      37.220 143.110  -3.253  1.00 52.93           C  
ATOM    382  CA  HIS A 438      38.667 142.432   0.186  1.00 50.13           C  
ATOM    383  CA  TYR A 439      41.938 144.068   0.971  1.00 38.33           C  
ATOM    384  CA  SER A 440      43.295 144.221   4.512  1.00 38.27           C  
ATOM    385  CA  THR A 441      46.256 146.150   5.856  1.00 38.52           C  
ATOM    386  CA  VAL A 442      47.715 147.726   8.962  1.00 32.22           C  
ATOM    387  CA  ILE A 443      49.507 151.050   9.066  1.00 32.01           C  
ATOM    388  CA  PRO A 444      51.506 151.262  12.299  1.00 35.49           C  
ATOM    389  CA  LEU A 445      51.908 154.729  13.834  1.00 36.22           C  
ATOM    390  CA  GLU A 446      54.569 156.055  16.182  1.00 36.18           C  
ATOM    391  CA  ALA A 447      53.503 157.269  19.648  1.00 35.41           C  
ATOM    392  CA  ASN A 448      54.291 160.803  18.454  1.00 32.86           C  
ATOM    393  CA  ALA A 449      51.910 160.646  15.489  1.00 31.09           C  
ATOM    394  CA  ARG A 450      49.739 163.741  14.995  1.00 31.81           C  
ATOM    395  CA  ASN A 451      47.370 165.368  12.501  1.00 30.86           C  
ATOM    396  CA  ILE A 452      46.226 161.909  11.359  1.00 27.49           C  
ATOM    397  CA  ARG A 453      43.905 161.819   8.333  1.00 30.37           C  
ATOM    398  CA  ILE A 454      42.328 158.790   6.649  1.00 27.84           C  
ATOM    399  CA  LYS A 455      40.539 159.049   3.308  1.00 26.69           C  
ATOM    400  CA  ALA A 456      39.077 156.537   0.884  1.00 30.28           C  
ATOM    401  CA  ARG A 457      37.595 157.271  -2.533  1.00 29.83           C  
ATOM    402  CA  GLU A 458      35.602 155.036  -4.890  1.00 29.61           C  
ATOM    403  CA  CYS A 459      36.946 154.939  -8.421  1.00 38.86           C  
ATOM    404  CA  THR A 460      34.059 156.068 -10.622  1.00 39.59           C  
ATOM    405  CA  GLY A 461      35.065 159.183 -12.544  1.00 38.13           C  
ATOM    406  CA  LEU A 462      38.062 160.480 -14.453  1.00 33.90           C  
ATOM    407  CA  ALA A 463      40.726 160.660 -11.737  1.00 30.15           C  
ATOM    408  CA  TRP A 464      41.442 160.891  -7.986  1.00 32.98           C  
ATOM    409  CA  GLU A 465      40.468 164.582  -7.872  1.00 38.03           C  
ATOM    410  CA  TRP A 466      36.959 163.848  -9.162  1.00 32.97           C  
ATOM    411  CA  TRP A 467      36.257 160.603  -7.314  1.00 31.84           C  
ATOM    412  CA  ARG A 468      33.624 160.136  -4.629  1.00 31.47           C  
ATOM    413  CA  ASP A 469      34.646 160.117  -0.944  1.00 28.43           C  
ATOM    414  CA  VAL A 470      33.743 156.853   0.848  1.00 23.54           C  
ATOM    415  CA  ILE A 471      35.405 158.001   4.091  1.00 25.16           C  
ATOM    416  CA  SER A 472      37.104 161.299   4.888  1.00 24.75           C  
ATOM    417  CA  GLU A 473      38.492 161.923   8.357  1.00 25.16           C  
ATOM    418  CA  TYR A 474      40.782 164.614   9.709  1.00 26.80           C  
ATOM    419  CA  ASP A 475      42.555 164.868  13.030  1.00 34.35           C  
ATOM    420  CA  VAL A 476      41.725 161.253  13.881  1.00 35.41           C  
ATOM    421  CA  PRO A 477      42.693 160.834  17.558  1.00 40.41           C  
ATOM    422  CA  LEU A 478      45.627 158.413  17.935  1.00 40.50           C  
ATOM    423  CA  THR A 479      44.699 155.353  19.999  1.00 45.33           C  
ATOM    424  CA  ASN A 480      45.661 151.652  20.121  1.00 44.74           C  
ATOM    425  CA  ASN A 481      43.530 150.692  17.141  1.00 36.66           C  
ATOM    426  CA  ILE A 482      41.887 152.866  14.493  1.00 31.44           C  
ATOM    427  CA  ASN A 483      39.532 150.612  12.558  1.00 32.39           C  
ATOM    428  CA  VAL A 484      38.431 151.911   9.179  1.00 30.74           C  
ATOM    429  CA  SER A 485      36.099 149.771   7.090  1.00 31.12           C  
ATOM    430  CA  ILE A 486      34.514 150.446   3.706  1.00 33.70           C  
ATOM    431  CA  TRP A 487      31.829 148.404   1.967  1.00 37.46           C  
ATOM    432  CA  GLY A 488      28.699 148.836  -0.119  1.00 36.89           C  
ATOM    433  CA  THR A 489      28.067 149.418  -3.790  1.00 40.45           C  
ATOM    434  CA  THR A 490      29.350 151.893  -6.343  1.00 42.17           C  
ATOM    435  CA  LEU A 491      26.090 153.833  -6.089  1.00 42.91           C  
ATOM    436  CA  TYR A 492      25.845 153.547  -2.325  1.00 39.54           C  
ATOM    437  CA  PRO A 493      29.136 152.891  -0.565  1.00 35.87           C  
ATOM    438  CA  GLY A 494      29.256 152.671   3.232  1.00 31.47           C  
ATOM    439  CA  SER A 495      31.964 153.172   5.864  1.00 35.02           C  
ATOM    440  CA  SER A 496      32.800 153.440   9.549  1.00 36.33           C  
ATOM    441  CA  ILE A 497      35.665 154.204  11.895  1.00 34.06           C  
ATOM    442  CA  THR A 498      35.935 152.663  15.355  1.00 37.92           C  
ATOM    443  CA  TYR A 499      38.514 152.899  18.127  1.00 44.44           C  
ATOM    444  CA  ASN A 500      40.157 150.710  20.781  1.00 56.44           C  
TER     445      ASN A 500                                                      
MASTER      275    0    0    0    0    0    0    6  444    1    0   35          
END                                                                             
