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Database: PDB
Entry: 1DIM
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HEADER    GLYCOSIDASE                             23-APR-96   1DIM              
TITLE     SIALIDASE FROM SALMONELLA TYPHIMURIUM COMPLEXED WITH EPANA INHIBITOR  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.18;                                                        
COMPND   5 ENGINEERED: 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;                                        
SOURCE  12 OTHER_DETAILS: RESIDUE MET 1 WAS EXCISED BY ESCHERICHIA COLI         
KEYWDS    GLYCOSIDASE, HYDROLASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.F.GARMAN,S.C.CRENNELL,E.R.VIMR,W.G.LAVER,G.L.TAYLOR                 
REVDAT   3   13-JUL-11 1DIM    1       VERSN                                    
REVDAT   2   24-FEB-09 1DIM    1       VERSN                                    
REVDAT   1   07-DEC-96 1DIM    0                                                
JRNL        AUTH   S.J.CRENNELL,E.F.GARMAN,C.PHILIPPON,A.VASELLA,W.G.LAVER,     
JRNL        AUTH 2 E.R.VIMR,G.L.TAYLOR                                          
JRNL        TITL   THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 NEURAMINIDASE   
JRNL        TITL 2 AND ITS COMPLEXES WITH THREE INHIBITORS AT HIGH RESOLUTION.  
JRNL        REF    J.MOL.BIOL.                   V. 259   264 1996              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8656428                                                      
JRNL        DOI    10.1006/JMBI.1996.0318                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
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   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.TAYLOR,E.VIMR,E.GARMAN,G.LAVER                             
REMARK   1  TITL   PURIFICATION, CRYSTALLIZATION AND PRELIMINARY                
REMARK   1  TITL 2 CRYSTALLOGRAPHIC STUDY OF NEURAMINIDASE FROM VIBRIO CHOLERAE 
REMARK   1  TITL 3 AND SALMONELLA TYPHIMURIUM LT2                               
REMARK   1  REF    J.MOL.BIOL.                   V. 226  1287 1992              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   K.WALLIMANN,A.VASELLA                                        
REMARK   1  TITL   PHOSPHONIC-ACID ANALOGUES OF THE N-ACETYL-2-DEOXYNEURAMINIC  
REMARK   1  TITL 2 ACIDS: SYNTHESIS AND INHIBITION OF VIBRIO CHOLERAE SIALIDASE 
REMARK   1  REF    HELV.CHIM.ACTA                V.  73  1359 1990              
REMARK   1  REFN                   ISSN 0018-019X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 42613                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2954                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 219                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.42                          
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.79                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : STNA_EPANA.PAR                                 
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : STNA_EPANA.TOP                                 
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DIM 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        : 05-DEC-92                          
REMARK 200  TEMPERATURE           (KELVIN) : 289                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12091                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.07800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE MAP               
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 2SIM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       23.70000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.85000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.15000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.85000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.70000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.15000            
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: 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 A  37   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A  37   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A  90   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A  90   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A 251   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 251   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    VAL A 280   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    VAL A 358   CB  -  CA  -  C   ANGL. DEV. = -14.7 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    ASP A 100       69.87     60.41                                   
REMARK 500    ASN A 122      -50.18   -131.46                                   
REMARK 500    VAL A 178      126.10     83.33                                   
REMARK 500    SER A 208     -151.79   -169.10                                   
REMARK 500    PHE A 228     -128.56     53.07                                   
REMARK 500    SER A 230      -36.58     52.10                                   
REMARK 500    ASN A 238     -126.21     63.56                                   
REMARK 500    ARG A 276     -158.48     59.07                                   
REMARK 500    HIS A 278      -26.39     72.74                                   
REMARK 500    ARG A 309       60.79     38.57                                   
REMARK 500    VAL A 351     -103.80     54.66                                   
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    SER A 230        23.4      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 801        DISTANCE =  6.93 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 690   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  62   OD2                                                    
REMARK 620 2 EQP A   1   O2P  89.0                                              
REMARK 620 3 EQP A   1   O6   86.2  61.5                                        
REMARK 620 4 EQP A   1   O7   79.4 121.8  61.0                                  
REMARK 620 5 HOH A 691   O    52.2 141.2 111.5  59.8                            
REMARK 620 6 HOH A 692   O   154.9  66.6  76.9 107.5 152.1                      
REMARK 620 7 HOH A 697   O   112.4 156.1 127.8  74.6  60.7  92.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 690                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EQP A 1                   
DBREF  1DIM A    2   382  UNP    P29768   NANH_SALTY       1    381             
SEQADV 1DIM ASP A  329  UNP  P29768    ALA   328 CONFLICT                       
SEQRES   1 A  381  THR VAL GLU LYS SER VAL VAL PHE LYS ALA GLU GLY GLU          
SEQRES   2 A  381  HIS PHE THR ASP GLN LYS GLY ASN THR ILE VAL GLY SER          
SEQRES   3 A  381  GLY SER GLY GLY THR THR LYS TYR PHE ARG ILE PRO ALA          
SEQRES   4 A  381  MET CYS THR THR SER LYS GLY THR ILE VAL VAL PHE ALA          
SEQRES   5 A  381  ASP ALA ARG HIS ASN THR ALA SER ASP GLN SER PHE ILE          
SEQRES   6 A  381  ASP THR ALA ALA ALA ARG SER THR ASP GLY GLY LYS THR          
SEQRES   7 A  381  TRP ASN LYS LYS ILE ALA ILE TYR ASN ASP ARG VAL ASN          
SEQRES   8 A  381  SER LYS LEU SER ARG VAL MET ASP PRO THR CYS ILE VAL          
SEQRES   9 A  381  ALA ASN ILE GLN GLY ARG GLU THR ILE LEU VAL MET VAL          
SEQRES  10 A  381  GLY LYS TRP ASN ASN ASN ASP LYS THR TRP GLY ALA TYR          
SEQRES  11 A  381  ARG ASP LYS ALA PRO ASP THR ASP TRP ASP LEU VAL LEU          
SEQRES  12 A  381  TYR LYS SER THR ASP ASP GLY VAL THR PHE SER LYS VAL          
SEQRES  13 A  381  GLU THR ASN ILE HIS ASP ILE VAL THR LYS ASN GLY THR          
SEQRES  14 A  381  ILE SER ALA MET LEU GLY GLY VAL GLY SER GLY LEU GLN          
SEQRES  15 A  381  LEU ASN ASP GLY LYS LEU VAL PHE PRO VAL GLN MET VAL          
SEQRES  16 A  381  ARG THR LYS ASN ILE THR THR VAL LEU ASN THR SER PHE          
SEQRES  17 A  381  ILE TYR SER THR ASP GLY ILE THR TRP SER LEU PRO SER          
SEQRES  18 A  381  GLY TYR CYS GLU GLY PHE GLY SER GLU ASN ASN ILE ILE          
SEQRES  19 A  381  GLU PHE ASN ALA SER LEU VAL ASN ASN ILE ARG ASN SER          
SEQRES  20 A  381  GLY LEU ARG ARG SER PHE GLU THR LYS ASP PHE GLY LYS          
SEQRES  21 A  381  THR TRP THR GLU PHE PRO PRO MET ASP LYS LYS VAL ASP          
SEQRES  22 A  381  ASN ARG ASN HIS GLY VAL GLN GLY SER THR ILE THR ILE          
SEQRES  23 A  381  PRO SER GLY ASN LYS LEU VAL ALA ALA HIS SER SER ALA          
SEQRES  24 A  381  GLN ASN LYS ASN ASN ASP TYR THR ARG SER ASP ILE SER          
SEQRES  25 A  381  LEU TYR ALA HIS ASN LEU TYR SER GLY GLU VAL LYS LEU          
SEQRES  26 A  381  ILE ASP ASP PHE TYR PRO LYS VAL GLY ASN ALA SER GLY          
SEQRES  27 A  381  ALA GLY TYR SER CYS LEU SER TYR ARG LYS ASN VAL ASP          
SEQRES  28 A  381  LYS GLU THR LEU TYR VAL VAL TYR GLU ALA ASN GLY SER          
SEQRES  29 A  381  ILE GLU PHE GLN ASP LEU SER ARG HIS LEU PRO VAL ILE          
SEQRES  30 A  381  LYS SER TYR ASN                                              
HET      K  A 690       1                                                       
HET    EQP  A   1      21                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM     EQP (4-ACETAMIDO-2,4-DIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-1-            
HETNAM   2 EQP  OCTOPYRANOSYL)PHOSPHONIC ACID                                   
FORMUL   2    K    K 1+                                                         
FORMUL   3  EQP    C10 H20 N O9 P                                               
FORMUL   4  HOH   *219(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  SER A  380  5                                   9    
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  ASP A 328 -1  N  ASP A 328   O  LEU A 314           
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           
SSBOND   1 CYS A   42    CYS A  103                          1555   1555  2.05  
LINK         K     K A 690                 OD2 ASP A  62     1555   1555  2.77  
LINK         K     K A 690                 O2P EQP A   1     1555   1555  2.91  
LINK         K     K A 690                 O6  EQP A   1     1555   1555  2.83  
LINK         K     K A 690                 O7  EQP A   1     1555   1555  2.77  
LINK         K     K A 690                 O   HOH A 691     1555   1555  3.38  
LINK         K     K A 690                 O   HOH A 692     1555   1555  3.33  
LINK         K     K A 690                 O   HOH A 697     1555   1555  2.90  
CISPEP   1 ALA A  135    PRO A  136          0        -0.20                     
SITE     1 ACT 13 ARG A  37  ARG A  56  ASP A  62  MET A  99                    
SITE     2 ACT 13 ASP A 100  TRP A 121  TRP A 128  LEU A 175                    
SITE     3 ACT 13 GLU A 231  ARG A 246  ARG A 309  TYR A 342                    
SITE     4 ACT 13 GLU A 361                                                     
SITE     1 AC1  3 EQP A   1  ASP A  62  HOH A 697                               
SITE     1 AC2 20 ARG A  37  ILE A  38  ARG A  56  ASP A  62                    
SITE     2 AC2 20 ASP A 100  THR A 127  TRP A 128  LEU A 175                    
SITE     3 AC2 20 ARG A 246  ARG A 309  TYR A 342  HOH A 664                    
SITE     4 AC2 20 HOH A 688  HOH A 689    K A 690  HOH A 692                    
SITE     5 AC2 20 HOH A 693  HOH A 694  HOH A 695  HOH A 696                    
CRYST1   47.400   82.300   91.700  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      0.021097  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012151  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010905        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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