GenomeNet

Database: PDB
Entry: 4BHU
LinkDB: 4BHU
Original site: 4BHU 
HEADER    STRUCTURAL PROTEIN                      08-APR-13   4BHU              
TITLE     CRYSTAL STRUCTURE OF BSLA - A BACTERIAL HYDROPHOBIN                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCHARACTERIZED PROTEIN YUAB;                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, J;                                    
COMPND   4 FRAGMENT: RESIDUES 48-172;                                           
COMPND   5 SYNONYM: ORF-1, BACTERIAL HYDROPHOBIN;                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: UNCHARACTERIZED PROTEIN YUAB;                              
COMPND  10 CHAIN: I;                                                            
COMPND  11 FRAGMENT: RESIDUES 48-172;                                           
COMPND  12 SYNONYM: ORF-1, BACTERIAL HYDROPHOBIN;                               
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;              
SOURCE   3 ORGANISM_TAXID: 535026;                                              
SOURCE   4 STRAIN: NCIB 3610;                                                   
SOURCE   5 ATCC: 6051;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 37762;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PGEX6P-1;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;              
SOURCE  13 ORGANISM_TAXID: 535026;                                              
SOURCE  14 STRAIN: NCIB 3610;                                                   
SOURCE  15 ATCC: 6051;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;                               
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 37762;                                      
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: B834(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: PGEX6P-1                                   
KEYWDS    STRUCTURAL PROTEIN, BIOFILM                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.V.RAO,L.HOBLEY,A.OSTROWSKI,K.M.BROMLEY,M.PORTER,A.R.PRESCOTT,       
AUTHOR   2 J.R.SWEDLOW,C.E.MACPHEE,D.M.F.VAN AALTEN,N.R.STANLEY-WALL            
REVDAT   2   28-AUG-13 4BHU    1       JRNL                                     
REVDAT   1   14-AUG-13 4BHU    0                                                
JRNL        AUTH   L.HOBLEY,A.OSTROWSKI,F.V.RAO,K.M.BROMLEY,M.PORTER,           
JRNL        AUTH 2 A.R.PRESCOTT,C.E.MACPHEE,D.M.F.VAN AALTEN,N.R.STANLEY-WALL   
JRNL        TITL   BSLA IS A SELF-ASSEMBLING BACTERIAL HYDROPHOBIN THAT COATS   
JRNL        TITL 2 THE BACILLUS SUBTILIS BIOFILM.                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 13600 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   23904481                                                     
JRNL        DOI    10.1073/PNAS.1306390110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.91 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 77.195                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.98                          
REMARK   3   NUMBER OF REFLECTIONS             : 135905                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1665                          
REMARK   3   R VALUE            (WORKING SET) : 0.1648                          
REMARK   3   FREE R VALUE                     : 0.1988                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 6834                            
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 77.2583 -  5.9340    1.00     4644   235  0.2469 0.2479        
REMARK   3     2  5.9340 -  4.7101    1.00     4445   232  0.1666 0.1924        
REMARK   3     3  4.7101 -  4.1148    1.00     4380   238  0.1410 0.1695        
REMARK   3     4  4.1148 -  3.7386    1.00     4369   233  0.1473 0.1691        
REMARK   3     5  3.7386 -  3.4706    1.00     4350   221  0.1494 0.1622        
REMARK   3     6  3.4706 -  3.2660    1.00     4326   246  0.1588 0.1857        
REMARK   3     7  3.2660 -  3.1024    1.00     4302   222  0.1687 0.2022        
REMARK   3     8  3.1024 -  2.9674    1.00     4305   250  0.1761 0.2204        
REMARK   3     9  2.9674 -  2.8531    1.00     4351   213  0.1690 0.2178        
REMARK   3    10  2.8531 -  2.7547    1.00     4273   222  0.1587 0.2114        
REMARK   3    11  2.7547 -  2.6685    1.00     4265   236  0.1581 0.2006        
REMARK   3    12  2.6685 -  2.5923    1.00     4311   218  0.1562 0.1930        
REMARK   3    13  2.5923 -  2.5240    1.00     4243   252  0.1514 0.1920        
REMARK   3    14  2.5240 -  2.4624    1.00     4278   241  0.1549 0.2027        
REMARK   3    15  2.4624 -  2.4064    1.00     4255   240  0.1542 0.1968        
REMARK   3    16  2.4064 -  2.3552    1.00     4322   217  0.1482 0.1825        
REMARK   3    17  2.3552 -  2.3081    1.00     4262   229  0.1552 0.2096        
REMARK   3    18  2.3081 -  2.2646    1.00     4280   217  0.1556 0.1999        
REMARK   3    19  2.2646 -  2.2241    1.00     4271   224  0.1504 0.2001        
REMARK   3    20  2.2241 -  2.1864    1.00     4264   199  0.1556 0.2037        
REMARK   3    21  2.1864 -  2.1511    1.00     4268   229  0.1548 0.2153        
REMARK   3    22  2.1511 -  2.1180    1.00     4223   235  0.1560 0.2063        
REMARK   3    23  2.1180 -  2.0869    1.00     4296   218  0.1584 0.2091        
REMARK   3    24  2.0869 -  2.0575    1.00     4242   230  0.1623 0.2134        
REMARK   3    25  2.0575 -  2.0297    1.00     4302   221  0.1630 0.2357        
REMARK   3    26  2.0297 -  2.0033    1.00     4217   216  0.1690 0.2109        
REMARK   3    27  2.0033 -  1.9783    1.00     4247   234  0.1755 0.2299        
REMARK   3    28  1.9783 -  1.9544    1.00     4263   234  0.1805 0.2393        
REMARK   3    29  1.9544 -  1.9317    1.00     4222   220  0.1912 0.2267        
REMARK   3    30  1.9317 -  1.9100    1.00     4295   212  0.1903 0.2350        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.16             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.52            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.68                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.7                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           9922                                  
REMARK   3   ANGLE     :  1.362          13457                                  
REMARK   3   CHIRALITY :  0.080           1595                                  
REMARK   3   PLANARITY :  0.006           1694                                  
REMARK   3   DIHEDRAL  : 13.826           3606                                  
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 4BHU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-APR-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-56388.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-12                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : KIRKPATRICK BAEZ BIMORPH           
REMARK 200                                   MIRROR PAIR                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 135912                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.91                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 77.19                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.3                               
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.04                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.5                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.27                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX AUTOSOLVE                                      
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M LI2SO4, 0.1 M HEPES, PH            
REMARK 280  7.5                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       34.85000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      129.90500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.99000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      129.90500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.85000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.99000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19290 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 52310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -240.6 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, F, G, B, C, D, E, I, J          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   171                                                      
REMARK 465     THR A   172                                                      
REMARK 465     THR B   172                                                      
REMARK 465     THR D   172                                                      
REMARK 465     SER G   171                                                      
REMARK 465     THR G   172                                                      
REMARK 465     SER H   171                                                      
REMARK 465     THR H   172                                                      
REMARK 465     GLY I    43                                                      
REMARK 465     PRO I    44                                                      
REMARK 465     LEU I    45                                                      
REMARK 465     GLY I    46                                                      
REMARK 465     ILE I   155                                                      
REMARK 465     GLY I   156                                                      
REMARK 465     ASN I   157                                                      
REMARK 465     MLY I   158                                                      
REMARK 465     PHE I   159                                                      
REMARK 465     SER I   171                                                      
REMARK 465     THR I   172                                                      
REMARK 465     GLY J    43                                                      
REMARK 465     PRO J    44                                                      
REMARK 465     LEU J    45                                                      
REMARK 465     GLY J    46                                                      
REMARK 465     LEU J   153                                                      
REMARK 465     SER J   154                                                      
REMARK 465     ILE J   155                                                      
REMARK 465     GLY J   156                                                      
REMARK 465     ASN J   157                                                      
REMARK 465     MLY J   158                                                      
REMARK 465     SER J   171                                                      
REMARK 465     THR J   172                                                      
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   NZ   LYS A   132     O    HOH A  2094              2.20            
REMARK 500   N    GLY C    43     O    HOH C  2001              1.97            
REMARK 500   OE1  GLU C    83     NH1  ARG C   116              2.13            
REMARK 500   O    MLY D   158     O    HOH D  2122              1.92            
REMARK 500   OG   SER D   171     O    HOH D  2144              2.18            
REMARK 500   OE1  GLU F   149     O    HOH F  2130              2.17            
REMARK 500   ND2  ASN G   157     O    HOH G  2009              2.13            
REMARK 500   N    GLY H    43     O    HOH E  2132              2.13            
REMARK 500  HH11  ARG H   116     O    HOH H  2099              1.59            
REMARK 500   O    THR I    60     OG   SER I    63              2.13            
REMARK 500   O    PRO I    73     O    HOH I  2010              2.11            
REMARK 500   NH1  ARG J   104     O    HOH F  2108              2.16            
REMARK 500  HH11  ARG J   104     O    HOH F  2108              1.48            
REMARK 500   O    HOH A  2056     O    HOH A  2094              2.18            
REMARK 500   O    HOH A  2120     O    HOH A  2127              2.08            
REMARK 500   O    HOH A  2123     O    HOH A  2124              1.96            
REMARK 500   O    HOH B  2025     O    HOH B  2035              2.13            
REMARK 500   O    HOH C  2001     O    HOH C  2003              2.14            
REMARK 500   O    HOH C  2029     O    HOH H  2101              2.19            
REMARK 500   O    HOH C  2061     O    HOH C  2149              2.09            
REMARK 500   O    HOH C  2077     O    HOH C  2139              2.18            
REMARK 500   O    HOH C  2109     O    HOH C  2168              2.02            
REMARK 500   O    HOH D  2034     O    HOH D  2035              2.18            
REMARK 500   O    HOH D  2060     O    HOH D  2061              2.07            
REMARK 500   O    HOH D  2077     O    HOH E  2100              2.04            
REMARK 500   O    HOH E  2066     O    HOH E  2115              2.08            
REMARK 500   O    HOH F  2010     O    HOH F  2032              1.89            
REMARK 500   O    HOH F  2012     O    HOH F  2033              2.03            
REMARK 500   O    HOH F  2083     O    HOH F  2084              2.14            
REMARK 500   O    HOH F  2085     O    HOH F  2100              2.02            
REMARK 500   O    HOH F  2090     O    HOH F  2091              2.16            
REMARK 500   O    HOH G  2070     O    HOH G  2117              2.14            
REMARK 500   O    HOH H  2001     O    HOH H  2002              2.06            
REMARK 500   O    HOH H  2002     O    HOH H  2003              2.01            
REMARK 500   O    HOH H  2038     O    HOH H  2040              2.13            
REMARK 500   O    HOH H  2043     O    HOH H  2115              2.15            
REMARK 500   O    HOH H  2071     O    HOH H  2072              2.12            
REMARK 500   O    HOH H  2073     O    HOH H  2117              1.99            
REMARK 500   O    HOH I  2014     O    HOH I  2032              2.15            
REMARK 500   O    HOH J  2004     O    HOH J  2014              2.11            
REMARK 500   O    HOH J  2081     O    HOH J  2082              1.99            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH E  2037     O    HOH F  2155     1655     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG H  72   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG H  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG H 147   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU E  79       15.03   -141.64                                   
REMARK 500    PRO G 139     -167.14    -79.36                                   
REMARK 500    PRO H 139     -166.90    -78.07                                   
REMARK 500    TRP I  62        1.30     80.48                                   
REMARK 500    SER I  65     -168.83   -161.49                                   
REMARK 500    ALA I 140      151.58    -47.87                                   
REMARK 500    LEU I 153       58.53    -95.76                                   
REMARK 500    ASN J  74      -11.62     65.72                                   
REMARK 500    PRO J 139     -167.50    -77.16                                   
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 GOL A1171                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1172                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E1173                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F1173                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL I1171                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1173                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL H1171                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1172                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F1174                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL J1171                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1173                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL E1174                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL F1175                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL I1172                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1174                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL E1175                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST 5 AMINO ACIDS (GPLGS) ARE FROM THE EXPRESSION              
REMARK 999 VECTOR. L98 HAS BEEN MUTATED TO M                                    
DBREF  4BHU A   48   172  UNP    P71014   YUAB_BACSU      48    172             
DBREF  4BHU B   48   172  UNP    P71014   YUAB_BACSU      48    172             
DBREF  4BHU C   48   172  UNP    P71014   YUAB_BACSU      48    172             
DBREF  4BHU D   48   172  UNP    P71014   YUAB_BACSU      48    172             
DBREF  4BHU E   48   172  UNP    P71014   YUAB_BACSU      48    172             
DBREF  4BHU F   48   172  UNP    P71014   YUAB_BACSU      48    172             
DBREF  4BHU G   48   172  UNP    P71014   YUAB_BACSU      48    172             
DBREF  4BHU H   48   172  UNP    P71014   YUAB_BACSU      48    172             
DBREF  4BHU I   48   172  UNP    P71014   YUAB_BACSU      48    172             
DBREF  4BHU J   48   172  UNP    P71014   YUAB_BACSU      48    172             
SEQADV 4BHU GLY A   43  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU PRO A   44  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU LEU A   45  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU GLY A   46  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU SER A   47  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU MSE A   98  UNP  P71014    LEU    98 ENGINEERED MUTATION            
SEQADV 4BHU GLY B   43  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU PRO B   44  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU LEU B   45  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU GLY B   46  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU SER B   47  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU MSE B   98  UNP  P71014    LEU    98 ENGINEERED MUTATION            
SEQADV 4BHU GLY C   43  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU PRO C   44  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU LEU C   45  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU GLY C   46  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU SER C   47  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU MSE C   98  UNP  P71014    LEU    98 ENGINEERED MUTATION            
SEQADV 4BHU GLY D   43  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU PRO D   44  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU LEU D   45  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU GLY D   46  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU SER D   47  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU MSE D   98  UNP  P71014    LEU    98 ENGINEERED MUTATION            
SEQADV 4BHU GLY E   43  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU PRO E   44  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU LEU E   45  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU GLY E   46  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU SER E   47  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU MSE E   98  UNP  P71014    LEU    98 ENGINEERED MUTATION            
SEQADV 4BHU GLY F   43  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU PRO F   44  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU LEU F   45  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU GLY F   46  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU SER F   47  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU MSE F   98  UNP  P71014    LEU    98 ENGINEERED MUTATION            
SEQADV 4BHU GLY G   43  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU PRO G   44  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU LEU G   45  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU GLY G   46  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU SER G   47  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU MSE G   98  UNP  P71014    LEU    98 ENGINEERED MUTATION            
SEQADV 4BHU GLY H   43  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU PRO H   44  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU LEU H   45  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU GLY H   46  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU SER H   47  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU MSE H   98  UNP  P71014    LEU    98 ENGINEERED MUTATION            
SEQADV 4BHU GLY I   43  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU PRO I   44  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU LEU I   45  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU GLY I   46  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU SER I   47  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU ASP I   74  UNP  P71014    ASN    74 CONFLICT                       
SEQADV 4BHU MSE I   98  UNP  P71014    LEU    98 ENGINEERED MUTATION            
SEQADV 4BHU GLY J   43  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU PRO J   44  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU LEU J   45  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU GLY J   46  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU SER J   47  UNP  P71014              EXPRESSION TAG                 
SEQADV 4BHU MSE J   98  UNP  P71014    LEU    98 ENGINEERED MUTATION            
SEQRES   1 A  130  GLY PRO LEU GLY SER ALA SER LEU PHE ALA THR ILE THR          
SEQRES   2 A  130  GLY ALA SER MLY THR GLU TRP SER PHE SER ASP ILE GLU          
SEQRES   3 A  130  LEU THR TYR ARG PRO ASN THR LEU LEU SER LEU GLY VAL          
SEQRES   4 A  130  MSE GLU PHE THR LEU PRO SER GLY PHE THR ALA ASN THR          
SEQRES   5 A  130  LYS ASP THR MSE ASN GLY ASN ALA LEU ARG THR THR GLN          
SEQRES   6 A  130  ILE LEU ASN ASN GLY LYS THR VAL ARG VAL PRO LEU ALA          
SEQRES   7 A  130  LEU ASP LEU LEU GLY ALA GLY GLU PHE MLY LEU LYS LEU          
SEQRES   8 A  130  ASN ASN LYS THR LEU PRO ALA ALA GLY THR TYR THR PHE          
SEQRES   9 A  130  ARG ALA GLU ASN LYS SER LEU SER ILE GLY ASN MLY PHE          
SEQRES  10 A  130  TYR ALA GLU ALA SER ILE ASP VAL ALA LYS ARG SER THR          
SEQRES   1 B  130  GLY PRO LEU GLY SER ALA SER LEU PHE ALA THR ILE THR          
SEQRES   2 B  130  GLY ALA SER MLY THR GLU TRP SER PHE SER ASP ILE GLU          
SEQRES   3 B  130  LEU THR TYR ARG PRO ASN THR LEU LEU SER LEU GLY VAL          
SEQRES   4 B  130  MSE GLU PHE THR LEU PRO SER GLY PHE THR ALA ASN THR          
SEQRES   5 B  130  LYS ASP THR MSE ASN GLY ASN ALA LEU ARG THR THR GLN          
SEQRES   6 B  130  ILE LEU ASN ASN GLY LYS THR VAL ARG VAL PRO LEU ALA          
SEQRES   7 B  130  LEU ASP LEU LEU GLY ALA GLY GLU PHE MLY LEU LYS LEU          
SEQRES   8 B  130  ASN ASN LYS THR LEU PRO ALA ALA GLY THR TYR THR PHE          
SEQRES   9 B  130  ARG ALA GLU ASN LYS SER LEU SER ILE GLY ASN MLY PHE          
SEQRES  10 B  130  TYR ALA GLU ALA SER ILE ASP VAL ALA LYS ARG SER THR          
SEQRES   1 C  130  GLY PRO LEU GLY SER ALA SER LEU PHE ALA THR ILE THR          
SEQRES   2 C  130  GLY ALA SER MLY THR GLU TRP SER PHE SER ASP ILE GLU          
SEQRES   3 C  130  LEU THR TYR ARG PRO ASN THR LEU LEU SER LEU GLY VAL          
SEQRES   4 C  130  MSE GLU PHE THR LEU PRO SER GLY PHE THR ALA ASN THR          
SEQRES   5 C  130  LYS ASP THR MSE ASN GLY ASN ALA LEU ARG THR THR GLN          
SEQRES   6 C  130  ILE LEU ASN ASN GLY LYS THR VAL ARG VAL PRO LEU ALA          
SEQRES   7 C  130  LEU ASP LEU LEU GLY ALA GLY GLU PHE MLY LEU LYS LEU          
SEQRES   8 C  130  ASN ASN LYS THR LEU PRO ALA ALA GLY THR TYR THR PHE          
SEQRES   9 C  130  ARG ALA GLU ASN LYS SER LEU SER ILE GLY ASN MLY PHE          
SEQRES  10 C  130  TYR ALA GLU ALA SER ILE ASP VAL ALA LYS ARG SER THR          
SEQRES   1 D  130  GLY PRO LEU GLY SER ALA SER LEU PHE ALA THR ILE THR          
SEQRES   2 D  130  GLY ALA SER MLY THR GLU TRP SER PHE SER ASP ILE GLU          
SEQRES   3 D  130  LEU THR TYR ARG PRO ASN THR LEU LEU SER LEU GLY VAL          
SEQRES   4 D  130  MSE GLU PHE THR LEU PRO SER GLY PHE THR ALA ASN THR          
SEQRES   5 D  130  LYS ASP THR MSE ASN GLY ASN ALA LEU ARG THR THR GLN          
SEQRES   6 D  130  ILE LEU ASN ASN GLY LYS THR VAL ARG VAL PRO LEU ALA          
SEQRES   7 D  130  LEU ASP LEU LEU GLY ALA GLY GLU PHE MLY LEU LYS LEU          
SEQRES   8 D  130  ASN ASN LYS THR LEU PRO ALA ALA GLY THR TYR THR PHE          
SEQRES   9 D  130  ARG ALA GLU ASN LYS SER LEU SER ILE GLY ASN MLY PHE          
SEQRES  10 D  130  TYR ALA GLU ALA SER ILE ASP VAL ALA LYS ARG SER THR          
SEQRES   1 E  130  GLY PRO LEU GLY SER ALA SER LEU PHE ALA THR ILE THR          
SEQRES   2 E  130  GLY ALA SER MLY THR GLU TRP SER PHE SER ASP ILE GLU          
SEQRES   3 E  130  LEU THR TYR ARG PRO ASN THR LEU LEU SER LEU GLY VAL          
SEQRES   4 E  130  MSE GLU PHE THR LEU PRO SER GLY PHE THR ALA ASN THR          
SEQRES   5 E  130  LYS ASP THR MSE ASN GLY ASN ALA LEU ARG THR THR GLN          
SEQRES   6 E  130  ILE LEU ASN ASN GLY LYS THR VAL ARG VAL PRO LEU ALA          
SEQRES   7 E  130  LEU ASP LEU LEU GLY ALA GLY GLU PHE MLY LEU LYS LEU          
SEQRES   8 E  130  ASN ASN LYS THR LEU PRO ALA ALA GLY THR TYR THR PHE          
SEQRES   9 E  130  ARG ALA GLU ASN LYS SER LEU SER ILE GLY ASN MLY PHE          
SEQRES  10 E  130  TYR ALA GLU ALA SER ILE ASP VAL ALA LYS ARG SER THR          
SEQRES   1 F  130  GLY PRO LEU GLY SER ALA SER LEU PHE ALA THR ILE THR          
SEQRES   2 F  130  GLY ALA SER MLY THR GLU TRP SER PHE SER ASP ILE GLU          
SEQRES   3 F  130  LEU THR TYR ARG PRO ASN THR LEU LEU SER LEU GLY VAL          
SEQRES   4 F  130  MSE GLU PHE THR LEU PRO SER GLY PHE THR ALA ASN THR          
SEQRES   5 F  130  LYS ASP THR MSE ASN GLY ASN ALA LEU ARG THR THR GLN          
SEQRES   6 F  130  ILE LEU ASN ASN GLY LYS THR VAL ARG VAL PRO LEU ALA          
SEQRES   7 F  130  LEU ASP LEU LEU GLY ALA GLY GLU PHE MLY LEU LYS LEU          
SEQRES   8 F  130  ASN ASN LYS THR LEU PRO ALA ALA GLY THR TYR THR PHE          
SEQRES   9 F  130  ARG ALA GLU ASN LYS SER LEU SER ILE GLY ASN MLY PHE          
SEQRES  10 F  130  TYR ALA GLU ALA SER ILE ASP VAL ALA LYS ARG SER THR          
SEQRES   1 G  130  GLY PRO LEU GLY SER ALA SER LEU PHE ALA THR ILE THR          
SEQRES   2 G  130  GLY ALA SER MLY THR GLU TRP SER PHE SER ASP ILE GLU          
SEQRES   3 G  130  LEU THR TYR ARG PRO ASN THR LEU LEU SER LEU GLY VAL          
SEQRES   4 G  130  MSE GLU PHE THR LEU PRO SER GLY PHE THR ALA ASN THR          
SEQRES   5 G  130  LYS ASP THR MSE ASN GLY ASN ALA LEU ARG THR THR GLN          
SEQRES   6 G  130  ILE LEU ASN ASN GLY LYS THR VAL ARG VAL PRO LEU ALA          
SEQRES   7 G  130  LEU ASP LEU LEU GLY ALA GLY GLU PHE MLY LEU LYS LEU          
SEQRES   8 G  130  ASN ASN LYS THR LEU PRO ALA ALA GLY THR TYR THR PHE          
SEQRES   9 G  130  ARG ALA GLU ASN LYS SER LEU SER ILE GLY ASN MLY PHE          
SEQRES  10 G  130  TYR ALA GLU ALA SER ILE ASP VAL ALA LYS ARG SER THR          
SEQRES   1 H  130  GLY PRO LEU GLY SER ALA SER LEU PHE ALA THR ILE THR          
SEQRES   2 H  130  GLY ALA SER MLY THR GLU TRP SER PHE SER ASP ILE GLU          
SEQRES   3 H  130  LEU THR TYR ARG PRO ASN THR LEU LEU SER LEU GLY VAL          
SEQRES   4 H  130  MSE GLU PHE THR LEU PRO SER GLY PHE THR ALA ASN THR          
SEQRES   5 H  130  LYS ASP THR MSE ASN GLY ASN ALA LEU ARG THR THR GLN          
SEQRES   6 H  130  ILE LEU ASN ASN GLY LYS THR VAL ARG VAL PRO LEU ALA          
SEQRES   7 H  130  LEU ASP LEU LEU GLY ALA GLY GLU PHE MLY LEU LYS LEU          
SEQRES   8 H  130  ASN ASN LYS THR LEU PRO ALA ALA GLY THR TYR THR PHE          
SEQRES   9 H  130  ARG ALA GLU ASN LYS SER LEU SER ILE GLY ASN MLY PHE          
SEQRES  10 H  130  TYR ALA GLU ALA SER ILE ASP VAL ALA LYS ARG SER THR          
SEQRES   1 I  130  GLY PRO LEU GLY SER ALA SER LEU PHE ALA THR ILE THR          
SEQRES   2 I  130  GLY ALA SER MLY THR GLU TRP SER PHE SER ASP ILE GLU          
SEQRES   3 I  130  LEU THR TYR ARG PRO ASP THR LEU LEU SER LEU GLY VAL          
SEQRES   4 I  130  MSE GLU PHE THR LEU PRO SER GLY PHE THR ALA ASN THR          
SEQRES   5 I  130  LYS ASP THR MSE ASN GLY ASN ALA LEU ARG THR THR GLN          
SEQRES   6 I  130  ILE LEU ASN ASN GLY LYS THR VAL ARG VAL PRO LEU ALA          
SEQRES   7 I  130  LEU ASP LEU LEU GLY ALA GLY GLU PHE MLY LEU LYS LEU          
SEQRES   8 I  130  ASN ASN LYS THR LEU PRO ALA ALA GLY THR TYR THR PHE          
SEQRES   9 I  130  ARG ALA GLU ASN LYS SER LEU SER ILE GLY ASN MLY PHE          
SEQRES  10 I  130  TYR ALA GLU ALA SER ILE ASP VAL ALA LYS ARG SER THR          
SEQRES   1 J  130  GLY PRO LEU GLY SER ALA SER LEU PHE ALA THR ILE THR          
SEQRES   2 J  130  GLY ALA SER MLY THR GLU TRP SER PHE SER ASP ILE GLU          
SEQRES   3 J  130  LEU THR TYR ARG PRO ASN THR LEU LEU SER LEU GLY VAL          
SEQRES   4 J  130  MSE GLU PHE THR LEU PRO SER GLY PHE THR ALA ASN THR          
SEQRES   5 J  130  LYS ASP THR MSE ASN GLY ASN ALA LEU ARG THR THR GLN          
SEQRES   6 J  130  ILE LEU ASN ASN GLY LYS THR VAL ARG VAL PRO LEU ALA          
SEQRES   7 J  130  LEU ASP LEU LEU GLY ALA GLY GLU PHE MLY LEU LYS LEU          
SEQRES   8 J  130  ASN ASN LYS THR LEU PRO ALA ALA GLY THR TYR THR PHE          
SEQRES   9 J  130  ARG ALA GLU ASN LYS SER LEU SER ILE GLY ASN MLY PHE          
SEQRES  10 J  130  TYR ALA GLU ALA SER ILE ASP VAL ALA LYS ARG SER THR          
MODRES 4BHU MLY A   59  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MSE A   82  MET  SELENOMETHIONINE                                   
MODRES 4BHU MSE A   98  MET  SELENOMETHIONINE                                   
MODRES 4BHU MLY A  130  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY A  158  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY B   59  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MSE B   82  MET  SELENOMETHIONINE                                   
MODRES 4BHU MSE B   98  MET  SELENOMETHIONINE                                   
MODRES 4BHU MLY B  130  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY B  158  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY C   59  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MSE C   82  MET  SELENOMETHIONINE                                   
MODRES 4BHU MSE C   98  MET  SELENOMETHIONINE                                   
MODRES 4BHU MLY C  130  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY C  158  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY D   59  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MSE D   82  MET  SELENOMETHIONINE                                   
MODRES 4BHU MSE D   98  MET  SELENOMETHIONINE                                   
MODRES 4BHU MLY D  130  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY D  158  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY E   59  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MSE E   82  MET  SELENOMETHIONINE                                   
MODRES 4BHU MSE E   98  MET  SELENOMETHIONINE                                   
MODRES 4BHU MLY E  130  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY E  158  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY F   59  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MSE F   82  MET  SELENOMETHIONINE                                   
MODRES 4BHU MSE F   98  MET  SELENOMETHIONINE                                   
MODRES 4BHU MLY F  130  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY F  158  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY G   59  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MSE G   82  MET  SELENOMETHIONINE                                   
MODRES 4BHU MSE G   98  MET  SELENOMETHIONINE                                   
MODRES 4BHU MLY G  130  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY G  158  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY H   59  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MSE H   82  MET  SELENOMETHIONINE                                   
MODRES 4BHU MSE H   98  MET  SELENOMETHIONINE                                   
MODRES 4BHU MLY H  130  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY H  158  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY I   59  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MSE I   82  MET  SELENOMETHIONINE                                   
MODRES 4BHU MSE I   98  MET  SELENOMETHIONINE                                   
MODRES 4BHU MLY I  130  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MLY J   59  LYS  N-DIMETHYL-LYSINE                                  
MODRES 4BHU MSE J   82  MET  SELENOMETHIONINE                                   
MODRES 4BHU MSE J   98  MET  SELENOMETHIONINE                                   
MODRES 4BHU MLY J  130  LYS  N-DIMETHYL-LYSINE                                  
HET    MLY  A  59      26                                                       
HET    MSE  A  82      17                                                       
HET    MSE  A  98      17                                                       
HET    MLY  A 130      27                                                       
HET    MLY  A 158      26                                                       
HET    MLY  B  59      27                                                       
HET    MSE  B  82      17                                                       
HET    MSE  B  98      17                                                       
HET    MLY  B 130      27                                                       
HET    MLY  B 158      26                                                       
HET    MLY  C  59      27                                                       
HET    MSE  C  82      17                                                       
HET    MSE  C  98      17                                                       
HET    MLY  C 130      27                                                       
HET    MLY  C 158      27                                                       
HET    MLY  D  59      26                                                       
HET    MSE  D  82      17                                                       
HET    MSE  D  98      17                                                       
HET    MLY  D 130      27                                                       
HET    MLY  D 158      27                                                       
HET    MLY  E  59      27                                                       
HET    MSE  E  82      17                                                       
HET    MSE  E  98      17                                                       
HET    MLY  E 130      27                                                       
HET    MLY  E 158      26                                                       
HET    MLY  F  59      26                                                       
HET    MSE  F  82      17                                                       
HET    MSE  F  98      17                                                       
HET    MLY  F 130      27                                                       
HET    MLY  F 158      26                                                       
HET    MLY  G  59      27                                                       
HET    MSE  G  82      17                                                       
HET    MSE  G  98      17                                                       
HET    MLY  G 130      27                                                       
HET    MLY  G 158      27                                                       
HET    MLY  H  59      27                                                       
HET    MSE  H  82      17                                                       
HET    MSE  H  98      17                                                       
HET    MLY  H 130      27                                                       
HET    MLY  H 158      27                                                       
HET    MLY  I  59      26                                                       
HET    MSE  I  82      17                                                       
HET    MSE  I  98      17                                                       
HET    MLY  I 130      27                                                       
HET    MLY  J  59      27                                                       
HET    MSE  J  82      17                                                       
HET    MSE  J  98      17                                                       
HET    MLY  J 130      27                                                       
HET    GOL  A1171      14                                                       
HET     CL  A1172       1                                                       
HET    GOL  B1172      14                                                       
HET     CL  B1173       1                                                       
HET     CL  C1173       1                                                       
HET     CL  C1174       1                                                       
HET    GOL  E1173      14                                                       
HET     CL  E1174       1                                                       
HET     CL  E1175       1                                                       
HET    GOL  F1173      14                                                       
HET    GOL  F1174      14                                                       
HET     CL  F1175       1                                                       
HET     CL  H1171       1                                                       
HET     CL  I1171       1                                                       
HET     CL  I1172       1                                                       
HET    GOL  J1171      14                                                       
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL  11  MSE    20(C5 H11 N O2 SE)                                           
FORMUL  12  MLY    28(C8 H18 N2 O2)                                             
FORMUL  13  GOL    6(C3 H8 O3)                                                  
FORMUL  14   CL    10(CL 1-)                                                    
FORMUL  15  HOH   *1411(H2 O)                                                   
HELIX    1   1 ARG A  104  THR A  106  5                                   3    
HELIX    2   2 ARG B  104  THR B  106  5                                   3    
HELIX    3   3 ARG C  104  THR C  106  5                                   3    
HELIX    4   4 ARG D  104  THR D  106  5                                   3    
HELIX    5   5 ARG E  104  THR E  106  5                                   3    
HELIX    6   6 ARG F  104  THR F  106  5                                   3    
HELIX    7   7 ARG G  104  THR G  106  5                                   3    
HELIX    8   8 ARG H  104  THR H  106  5                                   3    
HELIX    9   9 ARG I  104  THR I  106  5                                   3    
HELIX   10  10 ARG J  104  THR J  106  5                                   3    
SHEET    1  AA 5 SER A  49  ILE A  54  0                                        
SHEET    2  AA 5 PHE A  64  ARG A  72 -1  O  GLU A  68   N  THR A  53           
SHEET    3  AA 5 PHE A 129  THR A 137 -1  O  PHE A 129   N  TYR A  71           
SHEET    4  AA 5 THR A  97  MSE A  98 -1  O  THR A  97   N  LYS A 132           
SHEET    5  AA 5 ASN A 101  ALA A 102 -1  O  ASN A 101   N  MSE A  98           
SHEET    1  AB 5 ILE A 108  LEU A 109  0                                        
SHEET    2  AB 5 THR A 114  LEU A 123 -1  O  THR A 114   N  LEU A 109           
SHEET    3  AB 5 LEU A  77  THR A  85 -1  O  SER A  78   N  ASP A 122           
SHEET    4  AB 5 GLY A 142  ASN A 150 -1  O  ARG A 147   N  THR A  85           
SHEET    5  AB 5 TYR A 160  VAL A 167 -1  O  ALA A 161   N  ALA A 148           
SHEET    1  AC 4 ILE A 108  LEU A 109  0                                        
SHEET    2  AC 4 THR A 114  LEU A 123 -1  O  THR A 114   N  LEU A 109           
SHEET    3  AC 4 LEU A  77  THR A  85 -1  O  SER A  78   N  ASP A 122           
SHEET    4  AC 4 SER A 154  ILE A 155 -1  N  ILE A 155   O  LEU A  77           
SHEET    1  BA 5 SER B  49  ILE B  54  0                                        
SHEET    2  BA 5 PHE B  64  ARG B  72 -1  O  GLU B  68   N  THR B  53           
SHEET    3  BA 5 PHE B 129  THR B 137 -1  O  PHE B 129   N  TYR B  71           
SHEET    4  BA 5 THR B  97  MSE B  98 -1  O  THR B  97   N  LYS B 132           
SHEET    5  BA 5 ASN B 101  ALA B 102 -1  O  ASN B 101   N  MSE B  98           
SHEET    1  BB 5 ILE B 108  LEU B 109  0                                        
SHEET    2  BB 5 THR B 114  LEU B 123 -1  O  THR B 114   N  LEU B 109           
SHEET    3  BB 5 LEU B  77  THR B  85 -1  O  SER B  78   N  ASP B 122           
SHEET    4  BB 5 GLY B 142  ASN B 150 -1  O  ARG B 147   N  THR B  85           
SHEET    5  BB 5 TYR B 160  VAL B 167 -1  O  ALA B 161   N  ALA B 148           
SHEET    1  BC 4 ILE B 108  LEU B 109  0                                        
SHEET    2  BC 4 THR B 114  LEU B 123 -1  O  THR B 114   N  LEU B 109           
SHEET    3  BC 4 LEU B  77  THR B  85 -1  O  SER B  78   N  ASP B 122           
SHEET    4  BC 4 SER B 154  ILE B 155 -1  N  ILE B 155   O  LEU B  77           
SHEET    1  CA 5 SER C  49  ILE C  54  0                                        
SHEET    2  CA 5 PHE C  64  ARG C  72 -1  O  GLU C  68   N  THR C  53           
SHEET    3  CA 5 PHE C 129  THR C 137 -1  O  PHE C 129   N  TYR C  71           
SHEET    4  CA 5 THR C  97  MSE C  98 -1  O  THR C  97   N  LYS C 132           
SHEET    5  CA 5 ASN C 101  ALA C 102 -1  O  ASN C 101   N  MSE C  98           
SHEET    1  CB 5 ILE C 108  LEU C 109  0                                        
SHEET    2  CB 5 THR C 114  LEU C 123 -1  O  THR C 114   N  LEU C 109           
SHEET    3  CB 5 LEU C  77  THR C  85 -1  O  SER C  78   N  ASP C 122           
SHEET    4  CB 5 GLY C 142  ILE C 155 -1  O  ARG C 147   N  THR C  85           
SHEET    5  CB 5 ALA C 161  VAL C 167 -1  O  ALA C 161   N  ALA C 148           
SHEET    1  DA 5 SER D  49  ILE D  54  0                                        
SHEET    2  DA 5 PHE D  64  ARG D  72 -1  O  GLU D  68   N  THR D  53           
SHEET    3  DA 5 PHE D 129  THR D 137 -1  O  PHE D 129   N  TYR D  71           
SHEET    4  DA 5 THR D  97  MSE D  98 -1  O  THR D  97   N  LYS D 132           
SHEET    5  DA 5 ASN D 101  ALA D 102 -1  O  ASN D 101   N  MSE D  98           
SHEET    1  DB 5 ILE D 108  LEU D 109  0                                        
SHEET    2  DB 5 THR D 114  LEU D 123 -1  O  THR D 114   N  LEU D 109           
SHEET    3  DB 5 LEU D  77  THR D  85 -1  O  SER D  78   N  ASP D 122           
SHEET    4  DB 5 GLY D 142  ILE D 155 -1  O  ARG D 147   N  THR D  85           
SHEET    5  DB 5 ALA D 161  VAL D 167 -1  O  ALA D 161   N  ALA D 148           
SHEET    1  EA 5 SER E  49  ILE E  54  0                                        
SHEET    2  EA 5 PHE E  64  ARG E  72 -1  O  GLU E  68   N  THR E  53           
SHEET    3  EA 5 PHE E 129  THR E 137 -1  O  PHE E 129   N  TYR E  71           
SHEET    4  EA 5 THR E  97  MSE E  98 -1  O  THR E  97   N  LYS E 132           
SHEET    5  EA 5 ASN E 101  ALA E 102 -1  O  ASN E 101   N  MSE E  98           
SHEET    1  EB 5 ILE E 108  LEU E 109  0                                        
SHEET    2  EB 5 THR E 114  LEU E 123 -1  O  THR E 114   N  LEU E 109           
SHEET    3  EB 5 LEU E  77  THR E  85 -1  O  SER E  78   N  ASP E 122           
SHEET    4  EB 5 GLY E 142  ASN E 150 -1  O  ARG E 147   N  THR E  85           
SHEET    5  EB 5 TYR E 160  VAL E 167 -1  O  ALA E 161   N  ALA E 148           
SHEET    1  EC 4 ILE E 108  LEU E 109  0                                        
SHEET    2  EC 4 THR E 114  LEU E 123 -1  O  THR E 114   N  LEU E 109           
SHEET    3  EC 4 LEU E  77  THR E  85 -1  O  SER E  78   N  ASP E 122           
SHEET    4  EC 4 SER E 154  ILE E 155 -1  N  ILE E 155   O  LEU E  77           
SHEET    1  FA 5 SER F  49  ILE F  54  0                                        
SHEET    2  FA 5 PHE F  64  ARG F  72 -1  O  GLU F  68   N  THR F  53           
SHEET    3  FA 5 PHE F 129  THR F 137 -1  O  PHE F 129   N  TYR F  71           
SHEET    4  FA 5 THR F  97  MSE F  98 -1  O  THR F  97   N  LYS F 132           
SHEET    5  FA 5 ASN F 101  ALA F 102 -1  O  ASN F 101   N  MSE F  98           
SHEET    1  FB 5 ILE F 108  LEU F 109  0                                        
SHEET    2  FB 5 THR F 114  LEU F 123 -1  O  THR F 114   N  LEU F 109           
SHEET    3  FB 5 LEU F  77  THR F  85 -1  O  SER F  78   N  ASP F 122           
SHEET    4  FB 5 GLY F 142  ASN F 150 -1  O  ARG F 147   N  THR F  85           
SHEET    5  FB 5 TYR F 160  VAL F 167 -1  O  ALA F 161   N  ALA F 148           
SHEET    1  FC 4 ILE F 108  LEU F 109  0                                        
SHEET    2  FC 4 THR F 114  LEU F 123 -1  O  THR F 114   N  LEU F 109           
SHEET    3  FC 4 LEU F  77  THR F  85 -1  O  SER F  78   N  ASP F 122           
SHEET    4  FC 4 SER F 154  ILE F 155 -1  N  ILE F 155   O  LEU F  77           
SHEET    1  GA 5 SER G  49  ILE G  54  0                                        
SHEET    2  GA 5 PHE G  64  ARG G  72 -1  O  GLU G  68   N  THR G  53           
SHEET    3  GA 5 PHE G 129  THR G 137 -1  O  PHE G 129   N  TYR G  71           
SHEET    4  GA 5 THR G  97  MSE G  98 -1  O  THR G  97   N  LYS G 132           
SHEET    5  GA 5 ASN G 101  ALA G 102 -1  O  ASN G 101   N  MSE G  98           
SHEET    1  GB 5 ILE G 108  LEU G 109  0                                        
SHEET    2  GB 5 THR G 114  LEU G 123 -1  O  THR G 114   N  LEU G 109           
SHEET    3  GB 5 LEU G  77  THR G  85 -1  O  SER G  78   N  ASP G 122           
SHEET    4  GB 5 GLY G 142  ILE G 155 -1  O  ARG G 147   N  THR G  85           
SHEET    5  GB 5 ALA G 161  VAL G 167 -1  O  ALA G 161   N  ALA G 148           
SHEET    1  HA 5 SER H  49  ILE H  54  0                                        
SHEET    2  HA 5 PHE H  64  ARG H  72 -1  O  GLU H  68   N  THR H  53           
SHEET    3  HA 5 PHE H 129  THR H 137 -1  O  PHE H 129   N  TYR H  71           
SHEET    4  HA 5 THR H  97  MSE H  98 -1  O  THR H  97   N  LYS H 132           
SHEET    5  HA 5 ASN H 101  ALA H 102 -1  O  ASN H 101   N  MSE H  98           
SHEET    1  HB 5 ILE H 108  LEU H 109  0                                        
SHEET    2  HB 5 THR H 114  LEU H 123 -1  O  THR H 114   N  LEU H 109           
SHEET    3  HB 5 LEU H  77  THR H  85 -1  O  SER H  78   N  ASP H 122           
SHEET    4  HB 5 GLY H 142  ILE H 155 -1  O  ARG H 147   N  THR H  85           
SHEET    5  HB 5 ALA H 161  VAL H 167 -1  O  ALA H 161   N  ALA H 148           
SHEET    1  IA 5 SER I  49  ILE I  54  0                                        
SHEET    2  IA 5 PHE I  64  ARG I  72 -1  O  GLU I  68   N  THR I  53           
SHEET    3  IA 5 PHE I 129  THR I 137 -1  O  PHE I 129   N  TYR I  71           
SHEET    4  IA 5 THR I  97  MSE I  98 -1  O  THR I  97   N  LYS I 132           
SHEET    5  IA 5 ASN I 101  ALA I 102 -1  O  ASN I 101   N  MSE I  98           
SHEET    1  IB 5 ILE I 108  LEU I 109  0                                        
SHEET    2  IB 5 THR I 114  PRO I 118 -1  O  THR I 114   N  LEU I 109           
SHEET    3  IB 5 VAL I  81  THR I  85 -1  O  MSE I  82   N  VAL I 117           
SHEET    4  IB 5 GLY I 142  LYS I 151 -1  O  ARG I 147   N  THR I  85           
SHEET    5  IB 5 ALA I 161  VAL I 167 -1  O  ALA I 161   N  ALA I 148           
SHEET    1  JA 5 SER J  49  ILE J  54  0                                        
SHEET    2  JA 5 PHE J  64  ARG J  72 -1  O  GLU J  68   N  THR J  53           
SHEET    3  JA 5 PHE J 129  THR J 137 -1  O  PHE J 129   N  TYR J  71           
SHEET    4  JA 5 THR J  97  MSE J  98 -1  O  THR J  97   N  LYS J 132           
SHEET    5  JA 5 ASN J 101  ALA J 102 -1  O  ASN J 101   N  MSE J  98           
SHEET    1  JB 5 ILE J 108  LEU J 109  0                                        
SHEET    2  JB 5 THR J 114  PRO J 118 -1  O  THR J 114   N  LEU J 109           
SHEET    3  JB 5 VAL J  81  THR J  85 -1  O  MSE J  82   N  VAL J 117           
SHEET    4  JB 5 GLY J 142  LYS J 151 -1  O  ARG J 147   N  THR J  85           
SHEET    5  JB 5 ALA J 161  VAL J 167 -1  O  ALA J 161   N  ALA J 148           
LINK         N   MLY A  59                 C   SER A  58     1555   1555  1.33  
LINK         C   MLY A  59                 N   THR A  60     1555   1555  1.33  
LINK         N   MSE A  82                 C   VAL A  81     1555   1555  1.32  
LINK         C   MSE A  82                 N   GLU A  83     1555   1555  1.33  
LINK         N   MSE A  98                 C   THR A  97     1555   1555  1.33  
LINK         C   MSE A  98                 N   ASN A  99     1555   1555  1.33  
LINK         N   MLY A 130                 C   PHE A 129     1555   1555  1.32  
LINK         C   MLY A 130                 N   LEU A 131     1555   1555  1.32  
LINK         N   MLY A 158                 C   ASN A 157     1555   1555  1.32  
LINK         C   MLY A 158                 N   PHE A 159     1555   1555  1.33  
LINK         N   MLY B  59                 C   SER B  58     1555   1555  1.33  
LINK         C   MLY B  59                 N   THR B  60     1555   1555  1.33  
LINK         N   MSE B  82                 C   VAL B  81     1555   1555  1.33  
LINK         C   MSE B  82                 N   GLU B  83     1555   1555  1.33  
LINK         N   MSE B  98                 C   THR B  97     1555   1555  1.33  
LINK         C   MSE B  98                 N   ASN B  99     1555   1555  1.32  
LINK         N   MLY B 130                 C   PHE B 129     1555   1555  1.33  
LINK         C   MLY B 130                 N   LEU B 131     1555   1555  1.32  
LINK         N   MLY B 158                 C   ASN B 157     1555   1555  1.33  
LINK         C   MLY B 158                 N   PHE B 159     1555   1555  1.33  
LINK         N   MLY C  59                 C   SER C  58     1555   1555  1.33  
LINK         C   MLY C  59                 N   THR C  60     1555   1555  1.33  
LINK         N   MSE C  82                 C   VAL C  81     1555   1555  1.34  
LINK         C   MSE C  82                 N   GLU C  83     1555   1555  1.32  
LINK         N   MSE C  98                 C   THR C  97     1555   1555  1.33  
LINK         C   MSE C  98                 N   ASN C  99     1555   1555  1.34  
LINK         N   MLY C 130                 C   PHE C 129     1555   1555  1.33  
LINK         C   MLY C 130                 N   LEU C 131     1555   1555  1.32  
LINK         N   MLY C 158                 C   ASN C 157     1555   1555  1.32  
LINK         C   MLY C 158                 N   PHE C 159     1555   1555  1.33  
LINK         N   MLY D  59                 C   SER D  58     1555   1555  1.33  
LINK         C   MLY D  59                 N   THR D  60     1555   1555  1.33  
LINK         C   MSE D  82                 N   GLU D  83     1555   1555  1.33  
LINK         N   MSE D  82                 C   VAL D  81     1555   1555  1.32  
LINK         C   MSE D  98                 N   ASN D  99     1555   1555  1.32  
LINK         N   MSE D  98                 C   THR D  97     1555   1555  1.32  
LINK         C   MLY D 130                 N   LEU D 131     1555   1555  1.33  
LINK         N   MLY D 130                 C   PHE D 129     1555   1555  1.34  
LINK         C   MLY D 158                 N   PHE D 159     1555   1555  1.32  
LINK         N   MLY D 158                 C   ASN D 157     1555   1555  1.33  
LINK         C   MLY E  59                 N   THR E  60     1555   1555  1.33  
LINK         N   MLY E  59                 C   SER E  58     1555   1555  1.33  
LINK         N   MSE E  82                 C   VAL E  81     1555   1555  1.33  
LINK         C   MSE E  82                 N   GLU E  83     1555   1555  1.33  
LINK         C   MSE E  98                 N   ASN E  99     1555   1555  1.33  
LINK         N   MSE E  98                 C   THR E  97     1555   1555  1.34  
LINK         C   MLY E 130                 N   LEU E 131     1555   1555  1.32  
LINK         N   MLY E 130                 C   PHE E 129     1555   1555  1.33  
LINK         N   MLY E 158                 C   ASN E 157     1555   1555  1.32  
LINK         C   MLY E 158                 N   PHE E 159     1555   1555  1.32  
LINK         C   MLY F  59                 N   THR F  60     1555   1555  1.33  
LINK         N   MLY F  59                 C   SER F  58     1555   1555  1.33  
LINK         N   MSE F  82                 C   VAL F  81     1555   1555  1.33  
LINK         C   MSE F  82                 N   GLU F  83     1555   1555  1.32  
LINK         N   MSE F  98                 C   THR F  97     1555   1555  1.32  
LINK         C   MSE F  98                 N   ASN F  99     1555   1555  1.32  
LINK         C   MLY F 130                 N   LEU F 131     1555   1555  1.33  
LINK         N   MLY F 130                 C   PHE F 129     1555   1555  1.32  
LINK         C   MLY F 158                 N   PHE F 159     1555   1555  1.32  
LINK         N   MLY F 158                 C   ASN F 157     1555   1555  1.33  
LINK         C   MLY G  59                 N   THR G  60     1555   1555  1.33  
LINK         N   MLY G  59                 C   SER G  58     1555   1555  1.33  
LINK         N   MSE G  82                 C   VAL G  81     1555   1555  1.34  
LINK         C   MSE G  82                 N   GLU G  83     1555   1555  1.32  
LINK         N   MSE G  98                 C   THR G  97     1555   1555  1.34  
LINK         C   MSE G  98                 N   ASN G  99     1555   1555  1.33  
LINK         C   MLY G 130                 N   LEU G 131     1555   1555  1.33  
LINK         N   MLY G 130                 C   PHE G 129     1555   1555  1.32  
LINK         C   MLY G 158                 N   PHE G 159     1555   1555  1.32  
LINK         N   MLY G 158                 C   ASN G 157     1555   1555  1.33  
LINK         C   MLY H  59                 N   THR H  60     1555   1555  1.33  
LINK         N   MLY H  59                 C   SER H  58     1555   1555  1.33  
LINK         N   MSE H  82                 C   VAL H  81     1555   1555  1.32  
LINK         C   MSE H  82                 N   GLU H  83     1555   1555  1.33  
LINK         N   MSE H  98                 C   THR H  97     1555   1555  1.33  
LINK         C   MSE H  98                 N   ASN H  99     1555   1555  1.33  
LINK         C   MLY H 130                 N   LEU H 131     1555   1555  1.32  
LINK         N   MLY H 130                 C   PHE H 129     1555   1555  1.33  
LINK         C   MLY H 158                 N   PHE H 159     1555   1555  1.33  
LINK         N   MLY H 158                 C   ASN H 157     1555   1555  1.33  
LINK         C   MLY I  59                 N   THR I  60     1555   1555  1.33  
LINK         N   MLY I  59                 C   SER I  58     1555   1555  1.33  
LINK         N   MSE I  82                 C   VAL I  81     1555   1555  1.32  
LINK         C   MSE I  82                 N   GLU I  83     1555   1555  1.33  
LINK         N   MSE I  98                 C   THR I  97     1555   1555  1.33  
LINK         C   MSE I  98                 N   ASN I  99     1555   1555  1.33  
LINK         C   MLY I 130                 N   LEU I 131     1555   1555  1.33  
LINK         N   MLY I 130                 C   PHE I 129     1555   1555  1.32  
LINK         C   MLY J  59                 N   THR J  60     1555   1555  1.33  
LINK         N   MLY J  59                 C   SER J  58     1555   1555  1.33  
LINK         N   MSE J  82                 C   VAL J  81     1555   1555  1.32  
LINK         C   MSE J  82                 N   GLU J  83     1555   1555  1.33  
LINK         N   MSE J  98                 C   THR J  97     1555   1555  1.33  
LINK         C   MSE J  98                 N   ASN J  99     1555   1555  1.32  
LINK         C   MLY J 130                 N   LEU J 131     1555   1555  1.33  
LINK         N   MLY J 130                 C   PHE J 129     1555   1555  1.33  
SITE     1 AC1 10 ASN A 150  LYS A 151  SER A 152  LEU A 153                    
SITE     2 AC1 10 SER A 154  HOH A2140  HOH A2162  LEU G 119                    
SITE     3 AC1 10 ALA G 120  LEU G 121                                          
SITE     1 AC2 10 ASN B 150  LYS B 151  SER B 152  LEU B 153                    
SITE     2 AC2 10 SER B 154  HOH B2134  HOH B2161  LEU D 119                    
SITE     3 AC2 10 ALA D 120  LEU D 121                                          
SITE     1 AC3 10 LEU C 119  ALA C 120  LEU C 121  HOH C2140                    
SITE     2 AC3 10 ASN E 150  LYS E 151  SER E 152  LEU E 153                    
SITE     3 AC3 10 SER E 154  PHE E 159                                          
SITE     1 AC4  9 ASN F 150  LYS F 151  SER F 152  LEU F 153                    
SITE     2 AC4  9 SER F 154  HOH F2134  HOH F2164  LEU H 119                    
SITE     3 AC4  9 ALA H 120                                                     
SITE     1 AC5  1 THR I 106                                                     
SITE     1 AC6  2 LYS C  95  ASN C 135                                          
SITE     1 AC7  1 THR H 105                                                     
SITE     1 AC8  6 GLY A  43  PRO A  44  LEU A  45  LEU A  76                    
SITE     2 AC8  6 GLY A 156  HOH A2003                                          
SITE     1 AC9  4 LEU F 121  GLY F 127  GLU F 128  SER G 154                    
SITE     1 BC1  3 ARG G 116  HOH G2101  SER J 152                               
SITE     1 BC2  6 GLY B  43  PRO B  44  LEU B  45  LEU B  76                    
SITE     2 BC2  6 ILE B 155  HOH B2002                                          
SITE     1 BC3  5 GLY E  43  PRO E  44  LEU E  45  LEU E  76                    
SITE     2 BC3  5 HOH E2002                                                     
SITE     1 BC4  6 GLY F  43  PRO F  44  LEU F  45  LEU F  76                    
SITE     2 BC4  6 GLY F 156  HOH F2001                                          
SITE     1 BC5  1 HOH D2047                                                     
SITE     1 BC6  3 ARG C  72  HOH C2146  ARG H  72                               
SITE     1 BC7  3 THR E  97  LYS E 132  ASN E 134                               
CRYST1   69.700   95.980  259.810  90.00  90.00  90.00 P 21 21 21   40          
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      0.014347  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010419  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003849        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system