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Database: PDB
Entry: 3SIL
LinkDB: 3SIL
Original site: 3SIL 
HEADER    GLYCOSIDASE                             07-JUL-98   3SIL              
TITLE     SIALIDASE FROM SALMONELLA TYPHIMURIUM                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.18;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;                         
SOURCE   3 ORGANISM_TAXID: 99287;                                               
SOURCE   4 STRAIN: LT2;                                                         
SOURCE   5 VARIANT: TA263, PROTOTROPH;                                          
SOURCE   6 GENE: NANH;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;                            
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSX62;                                    
SOURCE  11 EXPRESSION_SYSTEM_GENE: NANH                                         
KEYWDS    GLYCOSIDASE, HYDROLASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.F.GARMAN,G.M.SHELDRICK                                              
REVDAT   4   13-JUL-11 3SIL    1       VERSN                                    
REVDAT   3   24-FEB-09 3SIL    1       VERSN                                    
REVDAT   2   13-JAN-99 3SIL    2       COMPND REMARK HEADER LINK                
REVDAT   2 2                   2       SOURCE CONECT                            
REVDAT   1   11-NOV-98 3SIL    0                                                
JRNL        AUTH   E.F.GARMAN,J.WOUTERS,T.R.SCHNEIDER,E.R.VIMR,W.G.LAVER,       
JRNL        AUTH 2 G.M.SHELDRICK                                                
JRNL        TITL   AN ENZYME AT ATOMIC RESOLUTION: THE 1.05 A STRUCTURE OF      
JRNL        TITL 2 SALMONELLA TYPHIMURIUM NEURAMINIDASE (SIALIDASE)             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.J.CRENNELL,E.F.GARMAN,C.PHILIPPON,A.VASELLA,W.G.LAVER,     
REMARK   1  AUTH 2 E.R.VIMR,G.L.TAYLOR                                          
REMARK   1  TITL   THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 NEURAMINIDASE   
REMARK   1  TITL 2 AND ITS COMPLEXES WITH THREE INHIBITORS AT HIGH RESOLUTION   
REMARK   1  REF    J.MOL.BIOL.                   V. 259   264 1996              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   S.J.CRENNELL,E.F.GARMAN,W.G.LAVER,E.R.VIMR,G.L.TAYLOR        
REMARK   1  TITL   CRYSTAL STRUCTURE OF A BACTERIAL SIALIDASE (FROM SALMONELLA  
REMARK   1  TITL 2 TYPHIMURIUM LT2) SHOWS THE SAME FOLD AS AN INFLUENZA VIRUS   
REMARK   1  TITL 3 NEURAMINIDASE                                                
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  90  9852 1993              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.1                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.116                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.116                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.147                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 3.100                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 4529                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 148474                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.094                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.094                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.121                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 3.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 3544                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 117026                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2940                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 42                                            
REMARK   3   SOLVENT ATOMS      : 561                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3526.40                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 2797.80                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 47                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 33361                   
REMARK   3   NUMBER OF RESTRAINTS                     : 41703                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.014                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.030                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.020                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.035                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.127                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.142                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.034                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.031                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.114                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL. (1973) 91: 201-228    
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R     
REMARK   3  (NO CUTOFF).                                                        
REMARK   4                                                                      
REMARK   4 3SIL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.86                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.862                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 148478                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 11.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2SIL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.86                                  
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       23.55000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.75000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.86500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.75000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.55000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.86500            
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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 A   777     O    HOH A  1041     4566     2.19            
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    ASN A 107   CB  -  CG  -  OD1 ANGL. DEV. =  13.4 DEGREES          
REMARK 500    ARG A 111   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES          
REMARK 500    ARG A 111   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    LYS A 325   N   -  CA  -  CB  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    ARG A 373   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG A 373   NE  -  CZ  -  NH2 ANGL. DEV. =   5.3 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    ILE A  38       64.97     65.72                                   
REMARK 500    ASN A 122      -62.74   -129.86                                   
REMARK 500    VAL A 178      122.34     89.77                                   
REMARK 500    SER A 208     -150.18   -165.57                                   
REMARK 500    PHE A 228     -130.53     54.03                                   
REMARK 500    SER A 230      -35.34     61.42                                   
REMARK 500    ASN A 238     -124.42     47.84                                   
REMARK 500    ALA A 239       30.53    -96.86                                   
REMARK 500    ARG A 276     -157.82     61.73                                   
REMARK 500    HIS A 278      -23.77     76.28                                   
REMARK 500    ASP A 306     -165.48   -162.91                                   
REMARK 500    VAL A 351     -118.85     64.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS A 325        23.1      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 920        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH A 990        DISTANCE =  5.18 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 450   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  62   OD2                                                    
REMARK 620 2 HOH A1052   O    56.7                                              
REMARK 620 3 PO4 A 499   O3   88.1  42.5                                        
REMARK 620 4 PO4 A 499   O4  109.9  54.3  46.5                                  
REMARK 620 5 GOL A 402   O1  163.6 128.6 105.2  74.6                            
REMARK 620 6 GOL A 402   O2  111.4 146.4 159.8 118.2  54.7                      
REMARK 620 7 HOH A 790   O    97.8 148.0 128.4 150.8  81.5  56.0                
REMARK 620 8 HOH A 982   O   156.6 124.1  83.7  79.8  38.0  79.9  71.0          
REMARK 620 9 HOH A 825   O    45.2 100.8 118.5 155.0 129.9  80.4  52.8 121.9    
REMARK 620 10 HOH A 605   O    38.2  75.4  82.2 124.9 151.4 116.0  72.7 118.7   
REMARK 620  36.4                                                                
REMARK 620 11 HOH A 958   O    71.6  63.2  41.6  88.1 124.8 148.0  92.1  88.0   
REMARK 620  81.1  46.2                                                          
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620  9     10                                                            
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 450                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 406                 
DBREF  3SIL A    4   382  UNP    P29768   NANH_SALTY       3    381             
SEQADV 3SIL ASP A  329  UNP  P29768    ALA   328 ENGINEERED                     
SEQRES   1 A  379  GLU LYS SER VAL VAL PHE LYS ALA GLU GLY GLU HIS PHE          
SEQRES   2 A  379  THR ASP GLN LYS GLY ASN THR ILE VAL GLY SER GLY SER          
SEQRES   3 A  379  GLY GLY THR THR LYS TYR PHE ARG ILE PRO ALA MET CYS          
SEQRES   4 A  379  THR THR SER LYS GLY THR ILE VAL VAL PHE ALA ASP ALA          
SEQRES   5 A  379  ARG HIS ASN THR ALA SER ASP GLN SER PHE ILE ASP THR          
SEQRES   6 A  379  ALA ALA ALA ARG SER THR ASP GLY GLY LYS THR TRP ASN          
SEQRES   7 A  379  LYS LYS ILE ALA ILE TYR ASN ASP ARG VAL ASN SER LYS          
SEQRES   8 A  379  LEU SER ARG VAL MET ASP PRO THR CYS ILE VAL ALA ASN          
SEQRES   9 A  379  ILE GLN GLY ARG GLU THR ILE LEU VAL MET VAL GLY LYS          
SEQRES  10 A  379  TRP ASN ASN ASN ASP LYS THR TRP GLY ALA TYR ARG ASP          
SEQRES  11 A  379  LYS ALA PRO ASP THR ASP TRP ASP LEU VAL LEU TYR LYS          
SEQRES  12 A  379  SER THR ASP ASP GLY VAL THR PHE SER LYS VAL GLU THR          
SEQRES  13 A  379  ASN ILE HIS ASP ILE VAL THR LYS ASN GLY THR ILE SER          
SEQRES  14 A  379  ALA MET LEU GLY GLY VAL GLY SER GLY LEU GLN LEU ASN          
SEQRES  15 A  379  ASP GLY LYS LEU VAL PHE PRO VAL GLN MET VAL ARG THR          
SEQRES  16 A  379  LYS ASN ILE THR THR VAL LEU ASN THR SER PHE ILE TYR          
SEQRES  17 A  379  SER THR ASP GLY ILE THR TRP SER LEU PRO SER GLY TYR          
SEQRES  18 A  379  CYS GLU GLY PHE GLY SER GLU ASN ASN ILE ILE GLU PHE          
SEQRES  19 A  379  ASN ALA SER LEU VAL ASN ASN ILE ARG ASN SER GLY LEU          
SEQRES  20 A  379  ARG ARG SER PHE GLU THR LYS ASP PHE GLY LYS THR TRP          
SEQRES  21 A  379  THR GLU PHE PRO PRO MET ASP LYS LYS VAL ASP ASN ARG          
SEQRES  22 A  379  ASN HIS GLY VAL GLN GLY SER THR ILE THR ILE PRO SER          
SEQRES  23 A  379  GLY ASN LYS LEU VAL ALA ALA HIS SER SER ALA GLN ASN          
SEQRES  24 A  379  LYS ASN ASN ASP TYR THR ARG SER ASP ILE SER LEU TYR          
SEQRES  25 A  379  ALA HIS ASN LEU TYR SER GLY GLU VAL LYS LEU ILE ASP          
SEQRES  26 A  379  ASP PHE TYR PRO LYS VAL GLY ASN ALA SER GLY ALA GLY          
SEQRES  27 A  379  TYR SER CYS LEU SER TYR ARG LYS ASN VAL ASP LYS GLU          
SEQRES  28 A  379  THR LEU TYR VAL VAL TYR GLU ALA ASN GLY SER ILE GLU          
SEQRES  29 A  379  PHE GLN ASP LEU SER ARG HIS LEU PRO VAL ILE LYS SER          
SEQRES  30 A  379  TYR ASN                                                      
HET      K  A 450       2                                                       
HET    PO4  A 499      10                                                       
HET    GOL  A 401       6                                                       
HET    GOL  A 402       6                                                       
HET    GOL  A 403      12                                                       
HET    GOL  A 404      12                                                       
HET    GOL  A 405       6                                                       
HET    GOL  A 406       6                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2    K    K 1+                                                         
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  GOL    6(C3 H8 O3)                                                  
FORMUL  10  HOH   *561(H2 O)                                                    
HELIX    1   1 SER A   29  GLY A   31  5                                   3    
HELIX    2   2 TRP A  128  ALA A  130  5                                   3    
HELIX    3   3 ILE A  161  ASN A  168  1                                   8    
HELIX    4   4 SER A  372  LYS A  379  5                                   8    
SHEET    1   A 4 TYR A  35  ARG A  37  0                                        
SHEET    2   A 4 ILE A  49  ARG A  56 -1  N  ARG A  56   O  TYR A  35           
SHEET    3   A 4 ILE A  66  SER A  73 -1  N  SER A  73   O  ILE A  49           
SHEET    4   A 4 ASN A  81  ILE A  86 -1  N  ILE A  86   O  THR A  68           
SHEET    1   B 2 ALA A  40  THR A  43  0                                        
SHEET    2   B 2 ILE A  49  PHE A  52 -1  N  PHE A  52   O  ALA A  40           
SHEET    1   C 3 ARG A  97  MET A  99  0                                        
SHEET    2   C 3 ILE A 114  TRP A 121 -1  N  TRP A 121   O  ARG A  97           
SHEET    3   C 3 ASP A 141  SER A 147 -1  N  SER A 147   O  ILE A 114           
SHEET    1   D 2 THR A 102  ILE A 108  0                                        
SHEET    2   D 2 ARG A 111  MET A 117 -1  N  MET A 117   O  THR A 102           
SHEET    1   E 4 TRP A 218  LEU A 220  0                                        
SHEET    2   E 4 LEU A 205  SER A 212 -1  N  TYR A 211   O  SER A 219           
SHEET    3   E 4 LEU A 189  ARG A 197 -1  N  MET A 195   O  ASN A 206           
SHEET    4   E 4 ILE A 171  GLY A 176 -1  N  LEU A 175   O  GLN A 194           
SHEET    1   F 2 ASN A 232  PHE A 237  0                                        
SHEET    2   F 2 SER A 240  ILE A 245 -1  N  ASN A 244   O  ASN A 233           
SHEET    1   G 4 SER A 283  SER A 289  0                                        
SHEET    2   G 4 LYS A 292  ALA A 300 -1  N  SER A 298   O  SER A 283           
SHEET    3   G 4 ILE A 312  HIS A 317 -1  N  HIS A 317   O  ALA A 295           
SHEET    4   G 4 VAL A 324  LEU A 326 -1  N  LYS A 325   O  ALA A 316           
SHEET    1   H 4 SER A 343  ASN A 350  0                                        
SHEET    2   H 4 LYS A 353  ALA A 362 -1  N  VAL A 359   O  CYS A 344           
SHEET    3   H 4 SER A 365  ASP A 370 -1  N  GLN A 369   O  VAL A 358           
SHEET    4   H 4 LYS A   5  PHE A   9 -1  N  PHE A   9   O  ILE A 366           
SHEET    1   I 2 ILE A 312  LEU A 314  0                                        
SHEET    2   I 2 ASP A 328  TYR A 331 -1  N  TYR A 331   O  ILE A 312           
SSBOND   1 CYS A   42    CYS A  103                          1555   1555  2.06  
LINK         K  A  K A 450                 OD2AASP A  62     1555   1555  2.70  
LINK         K  A  K A 450                 O  AHOH A1052     1555   1555  2.75  
LINK         K  A  K A 450                 O3 APO4 A 499     1555   1555  3.32  
LINK         K  A  K A 450                 O4 APO4 A 499     1555   1555  2.98  
LINK         K  A  K A 450                 O1  GOL A 402     1555   1555  3.30  
LINK         K  A  K A 450                 O2  GOL A 402     1555   1555  2.66  
LINK         K  A  K A 450                 O   HOH A 790     1555   1555  3.12  
LINK         K  A  K A 450                 O   HOH A 982     1555   1555  3.64  
LINK         K  B  K A 450                 O3 BPO4 A 499     1555   1555  2.99  
LINK         K  B  K A 450                 O   HOH A 790     1555   1555  3.02  
LINK         K  B  K A 450                 O   HOH A 825     1555   1555  3.27  
LINK         K  B  K A 450                 O   HOH A 605     1555   1555  3.17  
LINK         K  B  K A 450                 O   HOH A 958     1555   1555  2.82  
CISPEP   1 ALA A  135    PRO A  136          0        -2.77                     
SITE     1 AC1  7 ASP A  62  GOL A 402  PO4 A 499  HOH A 790                    
SITE     2 AC1  7 HOH A 958  HOH A1052  HOH A1054                               
SITE     1 AC2 15 ARG A  37  ARG A 246  TYR A 307  ARG A 309                    
SITE     2 AC2 15 TYR A 342    K A 450  HOH A 532  HOH A 958                    
SITE     3 AC2 15 HOH A 982  HOH A1051  HOH A1052  HOH A1053                    
SITE     4 AC2 15 HOH A1054  HOH A1055  HOH A1056                               
SITE     1 AC3  8 GLU A  14  HIS A  15  LYS A  82  HOH A 616                    
SITE     2 AC3  8 HOH A 869  HOH A 914  HOH A 960  HOH A1002                    
SITE     1 AC4  8 VAL A 178  GLN A 194  GLU A 231  GOL A 403                    
SITE     2 AC4  8   K A 450  HOH A 664  HOH A 790  HOH A 982                    
SITE     1 AC5 11 ASP A  62  GLN A  63  ARG A  97  MET A  99                    
SITE     2 AC5 11 ASP A 100  TRP A 121  LYS A 126  THR A 127                    
SITE     3 AC5 11 TRP A 128  GOL A 402  HOH A 825                               
SITE     1 AC6  7 VAL A 105  ALA A 106  ASN A 107  GLU A 112                    
SITE     2 AC6  7 ALA A 239  ARG A 348  HOH A 964                               
SITE     1 AC7 11 LYS A 120  ASN A 122  TRP A 140  ASP A 141                    
SITE     2 AC7 11 HIS A 374  VAL A 377  HOH A 584  HOH A 769                    
SITE     3 AC7 11 HOH A1059  HOH A1060  HOH A1061                               
SITE     1 AC8  9 CYS A  42  ILE A 104  VAL A 105  GLY A 181                    
SITE     2 AC8  9 LEU A 182  GLN A 183  HOH A 684  HOH A 749                    
SITE     3 AC8  9 HOH A 822                                                     
CRYST1   47.100   81.730   91.500  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      0.021231  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012235  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010929        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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