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Database: PDB
Entry: 4FPK
LinkDB: 4FPK
Original site: 4FPK 
HEADER    HYDROLASE/INHIBITOR                     22-JUN-12   4FPK              
TITLE     CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM STREPTOCOCCUS PNEUMONIAE 
TITLE    2 IN COMPLEX WITH 2-[(3-METHYLBENZYL)AMMONIO]ETHANESULFONATE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE B;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NEURAMINIDASE B;                                            
COMPND   5 EC: 3.2.1.18;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 1313;                                                
SOURCE   4 STRAIN: TIGR4;                                                       
SOURCE   5 GENE: NANB, SP_1687;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET23B                                    
KEYWDS    HYDROLASE, INTRAMOLECULAR TRANS-SIALIDASE, GLYCOSIDASE, DRUG DESIGN,  
KEYWDS   2 NEURAMINIDASE, HYDROLASE-INHIBITOR COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.BREAR                                                               
REVDAT   2   14-NOV-12 4FPK    1       JRNL                                     
REVDAT   1   31-OCT-12 4FPK    0                                                
JRNL        AUTH   P.BREAR,J.TELFORD,G.L.TAYLOR,N.J.WESTWOOD                    
JRNL        TITL   SYNTHESIS AND STRUCTURAL CHARACTERISATION OF SELECTIVE       
JRNL        TITL 2 NON-CARBOHYDRATE-BASED INHIBITORS OF BACTERIAL SIALIDASES.   
JRNL        REF    CHEMBIOCHEM                   V.  13  2374 2012              
JRNL        REFN                   ISSN 1439-4227                               
JRNL        PMID   23070966                                                     
JRNL        DOI    10.1002/CBIC.201200433                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 25339                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1269                            
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 14.8700 -  4.9378    0.96     3112   157  0.1817 0.2390        
REMARK   3     2  4.9378 -  3.9433    0.86     2712   129  0.1581 0.2109        
REMARK   3     3  3.9433 -  3.4520    0.95     2931   157  0.1831 0.2333        
REMARK   3     4  3.4520 -  3.1396    0.53     1629    78  0.1909 0.2746        
REMARK   3     5  3.1396 -  2.9164    0.60     1815   107  0.1946 0.2682        
REMARK   3     6  2.9164 -  2.7456    0.94     2854   158  0.1779 0.2891        
REMARK   3     7  2.7456 -  2.6088    0.99     3013   169  0.1630 0.2750        
REMARK   3     8  2.6088 -  2.4958    0.99     3008   155  0.1653 0.2611        
REMARK   3     9  2.4958 -  2.4000    0.99     2996   159  0.1821 0.2903        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.39                                          
REMARK   3   B_SOL              : 50.31                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.340           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.34890                                             
REMARK   3    B22 (A**2) : -3.04960                                             
REMARK   3    B33 (A**2) : 5.39840                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           5316                                  
REMARK   3   ANGLE     :  1.087           7188                                  
REMARK   3   CHIRALITY :  0.073            782                                  
REMARK   3   PLANARITY :  0.004            927                                  
REMARK   3   DIHEDRAL  : 14.110           1952                                  
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 4FPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073194.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25385                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.8                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 8000, 0.1M IMIDAZOLE, PH 8.0,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
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       38.11550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.14950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.27550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.14950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.11550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.27550            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     TYR A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     MET A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     VAL A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     THR A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     ILE A    27                                                      
REMARK 465     HIS A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     GLU A    31                                                      
REMARK 465     LEU A    32                                                      
REMARK 465     ASN A    33                                                      
REMARK 465     TYR A    34                                                      
REMARK 465     GLY A    35                                                      
REMARK 465     GLN A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     LYS A   697                                                      
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    ASN A  51       61.25   -113.85                                   
REMARK 500    ILE A 232      -64.96    -90.81                                   
REMARK 500    ILE A 246       64.27     61.65                                   
REMARK 500    SER A 273     -175.19    175.80                                   
REMARK 500    ASP A 327       89.26     67.98                                   
REMARK 500    ASN A 356       96.28    -52.88                                   
REMARK 500    LYS A 357       48.75    -90.46                                   
REMARK 500    ALA A 358        2.82   -160.92                                   
REMARK 500    ASN A 376      109.93    -37.83                                   
REMARK 500    ASN A 397       18.17     59.28                                   
REMARK 500    SER A 615      139.05   -171.77                                   
REMARK 500    ASP A 633        4.40   -157.06                                   
REMARK 500    ALA A 652     -122.68   -121.77                                   
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 IJ1 A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 702                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VW0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2VW1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2VW2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FOQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FOV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FOW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FOY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FP2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FP3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FPC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FPE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FPF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FPG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FPH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FPJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FPL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FPO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FPY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FQ4   RELATED DB: PDB                                   
DBREF  4FPK A    1   697  UNP    Q54727   NANB_STRPN       1    697             
SEQRES   1 A  697  MET ASN LYS ARG GLY LEU TYR SER LYS LEU GLY ILE SER          
SEQRES   2 A  697  VAL VAL GLY ILE SER LEU LEU MET GLY VAL PRO THR LEU          
SEQRES   3 A  697  ILE HIS ALA ASN GLU LEU ASN TYR GLY GLN LEU SER ILE          
SEQRES   4 A  697  SER PRO ILE PHE GLN GLY GLY SER TYR GLN LEU ASN ASN          
SEQRES   5 A  697  LYS SER ILE ASP ILE SER SER LEU LEU LEU ASP LYS LEU          
SEQRES   6 A  697  SER GLY GLU SER GLN THR VAL VAL MET LYS PHE LYS ALA          
SEQRES   7 A  697  ASP LYS PRO ASN SER LEU GLN ALA LEU PHE GLY LEU SER          
SEQRES   8 A  697  ASN SER LYS ALA GLY PHE LYS ASN ASN TYR PHE SER ILE          
SEQRES   9 A  697  PHE MET ARG ASP SER GLY GLU ILE GLY VAL GLU ILE ARG          
SEQRES  10 A  697  ASP ALA GLN LYS GLY ILE ASN TYR LEU PHE SER ARG PRO          
SEQRES  11 A  697  ALA SER LEU TRP GLY LYS HIS LYS GLY GLN ALA VAL GLU          
SEQRES  12 A  697  ASN THR LEU VAL PHE VAL SER ASP SER LYS ASP LYS THR          
SEQRES  13 A  697  TYR THR MET TYR VAL ASN GLY ILE GLU VAL PHE SER GLU          
SEQRES  14 A  697  THR VAL ASP THR PHE LEU PRO ILE SER ASN ILE ASN GLY          
SEQRES  15 A  697  ILE ASP LYS ALA THR LEU GLY ALA VAL ASN ARG GLU GLY          
SEQRES  16 A  697  LYS GLU HIS TYR LEU ALA LYS GLY SER ILE ASP GLU ILE          
SEQRES  17 A  697  SER LEU PHE ASN LYS ALA ILE SER ASP GLN GLU VAL SER          
SEQRES  18 A  697  THR ILE PRO LEU SER ASN PRO PHE GLN LEU ILE PHE GLN          
SEQRES  19 A  697  SER GLY ASP SER THR GLN ALA ASN TYR PHE ARG ILE PRO          
SEQRES  20 A  697  THR LEU TYR THR LEU SER SER GLY ARG VAL LEU SER SER          
SEQRES  21 A  697  ILE ASP ALA ARG TYR GLY GLY THR HIS ASP SER LYS SER          
SEQRES  22 A  697  LYS ILE ASN ILE ALA THR SER TYR SER ASP ASP ASN GLY          
SEQRES  23 A  697  LYS THR TRP SER GLU PRO ILE PHE ALA MET LYS PHE ASN          
SEQRES  24 A  697  ASP TYR GLU GLU GLN LEU VAL TYR TRP PRO ARG ASP ASN          
SEQRES  25 A  697  LYS LEU LYS ASN SER GLN ILE SER GLY SER ALA SER PHE          
SEQRES  26 A  697  ILE ASP SER SER ILE VAL GLU ASP LYS LYS SER GLY LYS          
SEQRES  27 A  697  THR ILE LEU LEU ALA ASP VAL MET PRO ALA GLY ILE GLY          
SEQRES  28 A  697  ASN ASN ASN ALA ASN LYS ALA ASP SER GLY PHE LYS GLU          
SEQRES  29 A  697  ILE ASN GLY HIS TYR TYR LEU LYS LEU LYS LYS ASN GLY          
SEQRES  30 A  697  ASP ASN ASP PHE ARG TYR THR VAL ARG GLU ASN GLY VAL          
SEQRES  31 A  697  VAL TYR ASN GLU THR THR ASN LYS PRO THR ASN TYR THR          
SEQRES  32 A  697  ILE ASN ASP LYS TYR GLU VAL LEU GLU GLY GLY LYS SER          
SEQRES  33 A  697  LEU THR VAL GLU GLN TYR SER VAL ASP PHE ASP SER GLY          
SEQRES  34 A  697  SER LEU ARG GLU ARG HIS ASN GLY LYS GLN VAL PRO MET          
SEQRES  35 A  697  ASN VAL PHE TYR LYS ASP SER LEU PHE LYS VAL THR PRO          
SEQRES  36 A  697  THR ASN TYR ILE ALA MET THR THR SER GLN ASN ARG GLY          
SEQRES  37 A  697  GLU SER TRP GLU GLN PHE LYS LEU LEU PRO PRO PHE LEU          
SEQRES  38 A  697  GLY GLU LYS HIS ASN GLY THR TYR LEU CYS PRO GLY GLN          
SEQRES  39 A  697  GLY LEU ALA LEU LYS SER SER ASN ARG LEU ILE PHE ALA          
SEQRES  40 A  697  THR TYR THR SER GLY GLU LEU THR TYR LEU ILE SER ASP          
SEQRES  41 A  697  ASP SER GLY GLN THR TRP LYS LYS SER SER ALA SER ILE          
SEQRES  42 A  697  PRO PHE LYS ASN ALA THR ALA GLU ALA GLN MET VAL GLU          
SEQRES  43 A  697  LEU ARG ASP GLY VAL ILE ARG THR PHE PHE ARG THR THR          
SEQRES  44 A  697  THR GLY LYS ILE ALA TYR MET THR SER ARG ASP SER GLY          
SEQRES  45 A  697  GLU THR TRP SER LYS VAL SER TYR ILE ASP GLY ILE GLN          
SEQRES  46 A  697  GLN THR SER TYR GLY THR GLN VAL SER ALA ILE LYS TYR          
SEQRES  47 A  697  SER GLN LEU ILE ASP GLY LYS GLU ALA VAL ILE LEU SER          
SEQRES  48 A  697  THR PRO ASN SER ARG SER GLY ARG LYS GLY GLY GLN LEU          
SEQRES  49 A  697  VAL VAL GLY LEU VAL ASN LYS GLU ASP ASP SER ILE ASP          
SEQRES  50 A  697  TRP LYS TYR HIS TYR ASP ILE ASP LEU PRO SER TYR GLY          
SEQRES  51 A  697  TYR ALA TYR SER ALA ILE THR GLU LEU PRO ASN HIS HIS          
SEQRES  52 A  697  ILE GLY VAL LEU PHE GLU LYS TYR ASP SER TRP SER ARG          
SEQRES  53 A  697  ASN GLU LEU HIS LEU SER ASN VAL VAL GLN TYR ILE ASP          
SEQRES  54 A  697  LEU GLU ILE ASN ASP LEU THR LYS                              
HET    IJ1  A 701      15                                                       
HET    DMS  A 702       4                                                       
HETNAM     IJ1 2-[(3-METHYLBENZYL)AMINO]ETHANESULFONIC ACID                     
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   2  IJ1    C10 H15 N O3 S                                               
FORMUL   3  DMS    C2 H6 O S                                                    
FORMUL   4  HOH   *451(H2 O)                                                    
HELIX    1   1 ILE A   57  LEU A   62  1                                   6    
HELIX    2   2 ASP A   63  LEU A   65  5                                   3    
HELIX    3   3 SER A  216  THR A  222  1                                   7    
HELIX    4   4 GLU A  691  THR A  696  1                                   6    
SHEET    1   A 6 PHE A  43  ASN A  51  0                                        
SHEET    2   A 6 LYS A 202  PHE A 211 -1  O  ILE A 205   N  TYR A  48           
SHEET    3   A 6 GLN A  70  LYS A  77 -1  N  VAL A  73   O  SER A 209           
SHEET    4   A 6 ASN A 144  ASP A 151 -1  O  ASN A 144   N  PHE A  76           
SHEET    5   A 6 THR A 156  VAL A 161 -1  O  THR A 158   N  VAL A 149           
SHEET    6   A 6 ILE A 164  THR A 170 -1  O  GLU A 169   N  TYR A 157           
SHEET    1   B 6 ILE A  55  ASP A  56  0                                        
SHEET    2   B 6 LYS A 185  LEU A 188 -1  O  LEU A 188   N  ILE A  55           
SHEET    3   B 6 LEU A  84  SER A  91 -1  N  GLY A  89   O  THR A 187           
SHEET    4   B 6 TYR A 101  ARG A 107 -1  O  PHE A 102   N  LEU A  90           
SHEET    5   B 6 ILE A 112  ASP A 118 -1  O  ARG A 117   N  TYR A 101           
SHEET    6   B 6 ILE A 123  ARG A 129 -1  O  ILE A 123   N  ASP A 118           
SHEET    1   C 2 LYS A 136  HIS A 137  0                                        
SHEET    2   C 2 GLN A 140  ALA A 141 -1  O  GLN A 140   N  HIS A 137           
SHEET    1   D 2 VAL A 191  ARG A 193  0                                        
SHEET    2   D 2 LYS A 196  HIS A 198 -1  O  HIS A 198   N  VAL A 191           
SHEET    1   E 3 TYR A 243  ARG A 245  0                                        
SHEET    2   E 3 VAL A 257  ARG A 264 -1  O  ASP A 262   N  ARG A 245           
SHEET    3   E 3 TYR A 250  THR A 251 -1  N  TYR A 250   O  LEU A 258           
SHEET    1   F 4 TYR A 243  ARG A 245  0                                        
SHEET    2   F 4 VAL A 257  ARG A 264 -1  O  ASP A 262   N  ARG A 245           
SHEET    3   F 4 ILE A 275  SER A 282 -1  O  ASN A 276   N  ALA A 263           
SHEET    4   F 4 ILE A 293  MET A 296 -1  O  ILE A 293   N  THR A 279           
SHEET    1   G 5 LYS A 475  LEU A 476  0                                        
SHEET    2   G 5 TYR A 458  SER A 464 -1  N  MET A 461   O  LYS A 475           
SHEET    3   G 5 THR A 339  MET A 346 -1  N  LEU A 341   O  THR A 462           
SHEET    4   G 5 SER A 324  GLU A 332 -1  N  VAL A 331   O  ILE A 340           
SHEET    5   G 5 GLY A 493  GLN A 494  1  O  GLY A 493   N  ILE A 330           
SHEET    1   H 7 PHE A 362  GLU A 364  0                                        
SHEET    2   H 7 TYR A 369  LYS A 375 -1  O  TYR A 370   N  LYS A 363           
SHEET    3   H 7 TYR A 383  VAL A 385 -1  O  TYR A 383   N  LEU A 373           
SHEET    4   H 7 VAL A 390  ASN A 393 -1  O  TYR A 392   N  THR A 384           
SHEET    5   H 7 PRO A 399  ILE A 404 -1  O  THR A 400   N  VAL A 391           
SHEET    6   H 7 VAL A 410  GLU A 412 -1  O  LEU A 411   N  THR A 403           
SHEET    7   H 7 LYS A 415  SER A 416 -1  O  LYS A 415   N  GLU A 412           
SHEET    1   I 3 PHE A 362  GLU A 364  0                                        
SHEET    2   I 3 TYR A 369  LYS A 375 -1  O  TYR A 370   N  LYS A 363           
SHEET    3   I 3 PHE A 451  LYS A 452 -1  O  LYS A 452   N  LYS A 374           
SHEET    1   J 2 THR A 418  ASP A 425  0                                        
SHEET    2   J 2 ARG A 432  PRO A 441 -1  O  LYS A 438   N  GLN A 421           
SHEET    1   K 3 TYR A 489  LEU A 490  0                                        
SHEET    2   K 3 LEU A 504  THR A 510 -1  O  TYR A 509   N  TYR A 489           
SHEET    3   K 3 LEU A 496  ALA A 497 -1  N  LEU A 496   O  ILE A 505           
SHEET    1   L 4 TYR A 489  LEU A 490  0                                        
SHEET    2   L 4 LEU A 504  THR A 510 -1  O  TYR A 509   N  TYR A 489           
SHEET    3   L 4 GLU A 513  SER A 519 -1  O  LEU A 517   N  PHE A 506           
SHEET    4   L 4 LYS A 527  SER A 532 -1  O  LYS A 527   N  ILE A 518           
SHEET    1   M 4 ALA A 542  ARG A 548  0                                        
SHEET    2   M 4 VAL A 551  PHE A 556 -1  O  ARG A 553   N  VAL A 545           
SHEET    3   M 4 ALA A 564  SER A 568 -1  O  SER A 568   N  ILE A 552           
SHEET    4   M 4 SER A 579  TYR A 580 -1  O  SER A 579   N  TYR A 565           
SHEET    1   N 4 SER A 594  ILE A 602  0                                        
SHEET    2   N 4 LYS A 605  PRO A 613 -1  O  ILE A 609   N  ILE A 596           
SHEET    3   N 4 GLY A 622  VAL A 629 -1  O  GLY A 627   N  VAL A 608           
SHEET    4   N 4 ILE A 636  ASP A 643 -1  O  TYR A 642   N  LEU A 624           
SHEET    1   O 3 SER A 654  GLU A 658  0                                        
SHEET    2   O 3 ILE A 664  GLU A 669 -1  O  GLY A 665   N  THR A 657           
SHEET    3   O 3 VAL A 685  LEU A 690 -1  O  LEU A 690   N  ILE A 664           
CISPEP   1 SER A  271    LYS A  272          0        13.59                     
SITE     1 AC1 12 ARG A 245  ASP A 270  SER A 271  ASP A 327                    
SITE     2 AC1 12 ASP A 344  ASN A 352  TYR A 489  ARG A 557                    
SITE     3 AC1 12 ARG A 619  TYR A 653  HOH A1101  HOH A1202                    
SITE     1 AC2  4 TYR A 250  THR A 251  GLN A 494  THR A 657                    
CRYST1   76.231   82.551  116.299  90.00  90.00  90.00 P 21 21 21    4          
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      0.013118  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012114  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008599        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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