GenomeNet

Database: PDB
Entry: 1KIT
LinkDB: 1KIT
Original site: 1KIT 
HEADER    HYDROLASE                               21-JUN-96   1KIT              
TITLE     VIBRIO CHOLERAE NEURAMINIDASE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NEURAMINIDASE;                                              
COMPND   5 EC: 3.2.1.18;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 STRAIN: CLASSICAL OGAWA 395;                                         
SOURCE   5 GENE: NANH;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PCVD364;                                  
SOURCE   9 EXPRESSION_SYSTEM_GENE: NANH                                         
KEYWDS    HYDROLASE, GLYCOSIDASE, SIGNAL, REPEAT, CALCIUM                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.L.TAYLOR,S.J.CRENNELL,E.F.GARMAN,E.R.VIMR,W.G.LAVER                 
REVDAT   2   24-FEB-09 1KIT    1       VERSN                                    
REVDAT   1   05-JUN-97 1KIT    0                                                
JRNL        AUTH   S.CRENNELL,E.GARMAN,G.LAVER,E.VIMR,G.TAYLOR                  
JRNL        TITL   CRYSTAL STRUCTURE OF VIBRIO CHOLERAE NEURAMINIDASE           
JRNL        TITL 2 REVEALS DUAL LECTIN-LIKE DOMAINS IN ADDITION TO              
JRNL        TITL 3 THE CATALYTIC DOMAIN.                                        
JRNL        REF    STRUCTURE                     V.   2   535 1994              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   7922030                                                      
JRNL        DOI    10.1016/S0969-2126(00)00053-8                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
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                 
REMARK   1  TITL 3 VIBRIO CHOLERAE AND SALMONELLA TYPHIMURIUM LT2               
REMARK   1  REF    J.MOL.BIOL.                   V. 226  1287 1992              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT V. 5-C                                           
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 40555                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
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                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1700                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5859                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 699                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.014 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 1.392 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : 0.012 ; 5.000 ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KIT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
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        : 1993                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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                  : 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          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40491                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 9.150                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
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       36.15000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.45000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.15000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.45000            
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    ASP A 637   N   -  CA  -  C   ANGL. DEV. =  17.9 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    THR A  35      -91.93    -72.73                                   
REMARK 500    GLN A  43       34.24    -80.17                                   
REMARK 500    ASN A  51      131.44      2.04                                   
REMARK 500    ASN A  52      -29.73     74.08                                   
REMARK 500    VAL A  56      148.01   -170.86                                   
REMARK 500    ASN A  59       48.61   -143.36                                   
REMARK 500    SER A 104      159.11    179.51                                   
REMARK 500    ASN A 165       79.37   -108.49                                   
REMARK 500    PRO A 166     -171.68    -67.05                                   
REMARK 500    SER A 167      173.30    171.36                                   
REMARK 500    ILE A 177      -64.73    -99.30                                   
REMARK 500    ASN A 180       24.46     82.16                                   
REMARK 500    MET A 190      169.95    170.07                                   
REMARK 500    GLN A 214     -107.49    -36.43                                   
REMARK 500    ILE A 225       47.62     74.59                                   
REMARK 500    SER A 255       49.62   -102.57                                   
REMARK 500    ASP A 273     -179.89    -68.49                                   
REMARK 500    ASN A 283       73.26   -112.61                                   
REMARK 500    ASP A 292       73.34     49.20                                   
REMARK 500    ASN A 302       60.49     60.11                                   
REMARK 500    ALA A 316     -152.92   -159.59                                   
REMARK 500    PRO A 324      -12.12    -49.70                                   
REMARK 500    PRO A 327       30.33    -78.53                                   
REMARK 500    SER A 376       -4.60    -50.25                                   
REMARK 500    GLU A 433      105.98    -57.78                                   
REMARK 500    HIS A 434      -36.58    -35.58                                   
REMARK 500    LEU A 450      -75.38    -27.06                                   
REMARK 500    ASP A 459       70.84     54.66                                   
REMARK 500    ILE A 463      -73.71    -98.95                                   
REMARK 500    GLN A 499       75.42     30.14                                   
REMARK 500    ARG A 577      -58.40   -160.90                                   
REMARK 500    SER A 618     -103.35   -121.97                                   
REMARK 500    SER A 648     -154.96    -53.45                                   
REMARK 500    ASN A 669     -157.69   -137.62                                   
REMARK 500    ALA A 683     -166.32   -119.82                                   
REMARK 500    ASN A 701      151.20    178.11                                   
REMARK 500    ALA A 707      116.22    -30.21                                   
REMARK 500    ALA A 739     -116.97   -123.31                                   
REMARK 500    SER A 748      -25.62    -36.22                                   
REMARK 500    THR A 757     -113.10   -136.08                                   
REMARK 500    SER A 760       -4.18     72.11                                   
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 857        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH A 858        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A1050        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH A1233        DISTANCE =  8.64 ANGSTROMS                       
REMARK 525    HOH A1319        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A1352        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A1356        DISTANCE =  7.66 ANGSTROMS                       
REMARK 525    HOH A1359        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH A1373        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH A1405        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH A1429        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH A1450        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH A1471        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH A1511        DISTANCE =  9.08 ANGSTROMS                       
REMARK 525    HOH A1532        DISTANCE =  9.53 ANGSTROMS                       
REMARK 525    HOH A1536        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH A1539        DISTANCE =  8.64 ANGSTROMS                       
REMARK 525    HOH A1540        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH A1543        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH A1545        DISTANCE =  8.92 ANGSTROMS                       
REMARK 525    HOH A1546        DISTANCE =  7.93 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                              CA A 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 256   OD1                                                    
REMARK 620 2 ASP A 289   OD2  77.1                                              
REMARK 620 3 THR A 313   OG1 145.2 114.3                                        
REMARK 620 4 ALA A 253   O    86.0 126.0 108.7                                  
REMARK 620 5 ASP A 289   OD1  80.0  48.7  84.3 165.8                            
REMARK 620 6 THR A 313   O   136.4  88.1  78.1  70.0 119.6                      
REMARK 620 7 ASN A 256   O    76.9 130.1  71.0  93.6  85.2 138.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 683   O                                                      
REMARK 620 2 ASP A 682   OD2  77.6                                              
REMARK 620 3 ASP A 621   OD1  81.0 137.2                                        
REMARK 620 4 ASP A 621   OD2  99.3 169.1  51.2                                  
REMARK 620 5 HOH A 931   O    76.2  84.4 125.6  84.7                            
REMARK 620 6 ASP A 682   OD1  91.4  50.5  93.9 140.4 134.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.                                       
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 802                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 803                  
DBREF  1KIT A   25   781  UNP    P37060   NANH_VIBCH      25    781             
SEQRES   1 A  757  ALA LEU PHE ASP TYR ASN ALA THR GLY ASP THR GLU PHE          
SEQRES   2 A  757  ASP SER PRO ALA LYS GLN GLY TRP MET GLN ASP ASN THR          
SEQRES   3 A  757  ASN ASN GLY SER GLY VAL LEU THR ASN ALA ASP GLY MET          
SEQRES   4 A  757  PRO ALA TRP LEU VAL GLN GLY ILE GLY GLY ARG ALA GLN          
SEQRES   5 A  757  TRP THR TYR SER LEU SER THR ASN GLN HIS ALA GLN ALA          
SEQRES   6 A  757  SER SER PHE GLY TRP ARG MET THR THR GLU MET LYS VAL          
SEQRES   7 A  757  LEU SER GLY GLY MET ILE THR ASN TYR TYR ALA ASN GLY          
SEQRES   8 A  757  THR GLN ARG VAL LEU PRO ILE ILE SER LEU ASP SER SER          
SEQRES   9 A  757  GLY ASN LEU VAL VAL GLU PHE GLU GLY GLN THR GLY ARG          
SEQRES  10 A  757  THR VAL LEU ALA THR GLY THR ALA ALA THR GLU TYR HIS          
SEQRES  11 A  757  LYS PHE GLU LEU VAL PHE LEU PRO GLY SER ASN PRO SER          
SEQRES  12 A  757  ALA SER PHE TYR PHE ASP GLY LYS LEU ILE ARG ASP ASN          
SEQRES  13 A  757  ILE GLN PRO THR ALA SER LYS GLN ASN MET ILE VAL TRP          
SEQRES  14 A  757  GLY ASN GLY SER SER ASN THR ASP GLY VAL ALA ALA TYR          
SEQRES  15 A  757  ARG ASP ILE LYS PHE GLU ILE GLN GLY ASP VAL ILE PHE          
SEQRES  16 A  757  ARG GLY PRO ASP ARG ILE PRO SER ILE VAL ALA SER SER          
SEQRES  17 A  757  VAL THR PRO GLY VAL VAL THR ALA PHE ALA GLU LYS ARG          
SEQRES  18 A  757  VAL GLY GLY GLY ASP PRO GLY ALA LEU SER ASN THR ASN          
SEQRES  19 A  757  ASP ILE ILE THR ARG THR SER ARG ASP GLY GLY ILE THR          
SEQRES  20 A  757  TRP ASP THR GLU LEU ASN LEU THR GLU GLN ILE ASN VAL          
SEQRES  21 A  757  SER ASP GLU PHE ASP PHE SER ASP PRO ARG PRO ILE TYR          
SEQRES  22 A  757  ASP PRO SER SER ASN THR VAL LEU VAL SER TYR ALA ARG          
SEQRES  23 A  757  TRP PRO THR ASP ALA ALA GLN ASN GLY ASP ARG ILE LYS          
SEQRES  24 A  757  PRO TRP MET PRO ASN GLY ILE PHE TYR SER VAL TYR ASP          
SEQRES  25 A  757  VAL ALA SER GLY ASN TRP GLN ALA PRO ILE ASP VAL THR          
SEQRES  26 A  757  ASP GLN VAL LYS GLU ARG SER PHE GLN ILE ALA GLY TRP          
SEQRES  27 A  757  GLY GLY SER GLU LEU TYR ARG ARG ASN THR SER LEU ASN          
SEQRES  28 A  757  SER GLN GLN ASP TRP GLN SER ASN ALA LYS ILE ARG ILE          
SEQRES  29 A  757  VAL ASP GLY ALA ALA ASN GLN ILE GLN VAL ALA ASP GLY          
SEQRES  30 A  757  SER ARG LYS TYR VAL VAL THR LEU SER ILE ASP GLU SER          
SEQRES  31 A  757  GLY GLY LEU VAL ALA ASN LEU ASN GLY VAL SER ALA PRO          
SEQRES  32 A  757  ILE ILE LEU GLN SER GLU HIS ALA LYS VAL HIS SER PHE          
SEQRES  33 A  757  HIS ASP TYR GLU LEU GLN TYR SER ALA LEU ASN HIS THR          
SEQRES  34 A  757  THR THR LEU PHE VAL ASP GLY GLN GLN ILE THR THR TRP          
SEQRES  35 A  757  ALA GLY GLU VAL SER GLN GLU ASN ASN ILE GLN PHE GLY          
SEQRES  36 A  757  ASN ALA ASP ALA GLN ILE ASP GLY ARG LEU HIS VAL GLN          
SEQRES  37 A  757  LYS ILE VAL LEU THR GLN GLN GLY HIS ASN LEU VAL GLU          
SEQRES  38 A  757  PHE ASP ALA PHE TYR LEU ALA GLN GLN THR PRO GLU VAL          
SEQRES  39 A  757  GLU LYS ASP LEU GLU LYS LEU GLY TRP THR LYS ILE LYS          
SEQRES  40 A  757  THR GLY ASN THR MET SER LEU TYR GLY ASN ALA SER VAL          
SEQRES  41 A  757  ASN PRO GLY PRO GLY HIS GLY ILE THR LEU THR ARG GLN          
SEQRES  42 A  757  GLN ASN ILE SER GLY SER GLN ASN GLY ARG LEU ILE TYR          
SEQRES  43 A  757  PRO ALA ILE VAL LEU ASP ARG PHE PHE LEU ASN VAL MET          
SEQRES  44 A  757  SER ILE TYR SER ASP ASP GLY GLY SER ASN TRP GLN THR          
SEQRES  45 A  757  GLY SER THR LEU PRO ILE PRO PHE ARG TRP LYS SER SER          
SEQRES  46 A  757  SER ILE LEU GLU THR LEU GLU PRO SER GLU ALA ASP MET          
SEQRES  47 A  757  VAL GLU LEU GLN ASN GLY ASP LEU LEU LEU THR ALA ARG          
SEQRES  48 A  757  LEU ASP PHE ASN GLN ILE VAL ASN GLY VAL ASN TYR SER          
SEQRES  49 A  757  PRO ARG GLN GLN PHE LEU SER LYS ASP GLY GLY ILE THR          
SEQRES  50 A  757  TRP SER LEU LEU GLU ALA ASN ASN ALA ASN VAL PHE SER          
SEQRES  51 A  757  ASN ILE SER THR GLY THR VAL ASP ALA SER ILE THR ARG          
SEQRES  52 A  757  PHE GLU GLN SER ASP GLY SER HIS PHE LEU LEU PHE THR          
SEQRES  53 A  757  ASN PRO GLN GLY ASN PRO ALA GLY THR ASN GLY ARG GLN          
SEQRES  54 A  757  ASN LEU GLY LEU TRP PHE SER PHE ASP GLU GLY VAL THR          
SEQRES  55 A  757  TRP LYS GLY PRO ILE GLN LEU VAL ASN GLY ALA SER ALA          
SEQRES  56 A  757  TYR SER ASP ILE TYR GLN LEU ASP SER GLU ASN ALA ILE          
SEQRES  57 A  757  VAL ILE VAL GLU THR ASP ASN SER ASN MET ARG ILE LEU          
SEQRES  58 A  757  ARG MET PRO ILE THR LEU LEU LYS GLN LYS LEU THR LEU          
SEQRES  59 A  757  SER GLN ASN                                                  
HET     CA  A 802       1                                                       
HET     CA  A 803       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4  HOH   *699(H2 O)                                                    
HELIX    1   1 ALA A   60  GLY A   62  5                                   3    
HELIX    2   2 THR A   83  PHE A   92  1                                  10    
HELIX    3   3 ASN A  318  ASP A  320  5                                   3    
HELIX    4   4 THR A  349  VAL A  352  1                                   4    
HELIX    5   5 HIS A  434  VAL A  437  1                                   4    
HELIX    6   6 ALA A  508  ALA A  512  1                                   5    
HELIX    7   7 LEU A  522  LEU A  525  1                                   4    
HELIX    8   8 ALA A  670  VAL A  672  5                                   3    
HELIX    9   9 ASP A  758  SER A  760  5                                   3    
HELIX   10  10 ILE A  769  THR A  777  1                                   9    
SHEET    1   A 6 LEU A  26  ASN A  30  0                                        
SHEET    2   A 6 ALA A 204  ILE A 213 -1  N  PHE A 211   O  PHE A  27           
SHEET    3   A 6 TRP A  94  VAL A 102 -1  N  LYS A 101   O  ALA A 205           
SHEET    4   A 6 HIS A 154  LEU A 161 -1  N  PHE A 160   O  TRP A  94           
SHEET    5   A 6 SER A 167  PHE A 172 -1  N  TYR A 171   O  GLU A 157           
SHEET    6   A 6 ARG A 178  ILE A 181 -1  N  ILE A 181   O  ALA A 168           
SHEET    1   B 3 SER A  54  ALA A  60  0                                        
SHEET    2   B 3 MET A  63  GLY A  70 -1  N  GLN A  69   O  SER A  54           
SHEET    3   B 3 GLY A 202  TYR A 206 -1  N  TYR A 206   O  TRP A  66           
SHEET    1   C 4 ALA A  75  TYR A  79  0                                        
SHEET    2   C 4 MET A 190  ASN A 195 -1  N  ASN A 195   O  ALA A  75           
SHEET    3   C 4 TYR A 111  ASN A 114 -1  N  ALA A 113   O  MET A 190           
SHEET    4   C 4 GLN A 117  VAL A 119 -1  N  VAL A 119   O  TYR A 112           
SHEET    1   D 3 PRO A 121  LEU A 125  0                                        
SHEET    2   D 3 LEU A 131  PHE A 135 -1  N  GLU A 134   O  ILE A 122           
SHEET    3   D 3 ARG A 141  ALA A 145 -1  N  ALA A 145   O  LEU A 131           
SHEET    1   E 3 SER A 227  ALA A 230  0                                        
SHEET    2   E 3 VAL A 238  VAL A 246 -1  N  PHE A 241   O  SER A 227           
SHEET    3   E 3 THR A 257  SER A 265 -1  N  SER A 265   O  VAL A 238           
SHEET    1   F 4 PHE A 288  SER A 291  0                                        
SHEET    2   F 4 THR A 303  PRO A 312 -1  N  TRP A 311   O  ASP A 289           
SHEET    3   F 4 GLY A 329  ASP A 336 -1  N  TYR A 335   O  VAL A 304           
SHEET    4   F 4 ASN A 341  GLN A 343 -1  N  GLN A 343   O  VAL A 334           
SHEET    1   G 2 ARG A 294  ASP A 298  0                                        
SHEET    2   G 2 THR A 303  SER A 307 -1  N  SER A 307   O  ARG A 294           
SHEET    1   H 6 MET A 536  TYR A 539  0                                        
SHEET    2   H 6 PHE A 357  ALA A 360 -1  N  ALA A 360   O  MET A 536           
SHEET    3   H 6 ARG A 488  GLN A 498 -1  N  VAL A 491   O  PHE A 357           
SHEET    4   H 6 TRP A 380  ILE A 388 -1  N  ARG A 387   O  HIS A 490           
SHEET    5   H 6 HIS A 441  SER A 448 -1  N  TYR A 447   O  TRP A 380           
SHEET    6   H 6 THR A 453  VAL A 458 -1  N  PHE A 457   O  GLU A 444           
SHEET    1   I 7 THR A 528  GLY A 533  0                                        
SHEET    2   I 7 GLY A 364  ASN A 371 -1  N  ARG A 369   O  THR A 528           
SHEET    3   I 7 ASN A 474  ASN A 480 -1  N  ASN A 480   O  GLU A 366           
SHEET    4   I 7 ASN A 394  ASP A 400 -1  N  ALA A 399   O  ASN A 475           
SHEET    5   I 7 LYS A 404  ILE A 411 -1  N  LEU A 409   O  ASN A 394           
SHEET    6   I 7 LEU A 417  LEU A 421 -1  N  ASN A 420   O  THR A 408           
SHEET    7   I 7 ILE A 428  GLN A 431 -1  N  GLN A 431   O  LEU A 417           
SHEET    1   J 3 SER A 543  ASN A 545  0                                        
SHEET    2   J 3 LEU A 568  LEU A 575 -1  N  LEU A 575   O  SER A 543           
SHEET    3   J 3 LEU A 580  SER A 587 -1  N  SER A 587   O  LEU A 568           
SHEET    1   K 3 ALA A 620  GLU A 624  0                                        
SHEET    2   K 3 LEU A 630  ARG A 635 -1  N  THR A 633   O  ASP A 621           
SHEET    3   K 3 ARG A 650  SER A 655 -1  N  SER A 655   O  LEU A 630           
SHEET    1   L 3 SER A 684  GLU A 689  0                                        
SHEET    2   L 3 HIS A 695  ASN A 701 -1  N  THR A 700   O  SER A 684           
SHEET    3   L 3 GLY A 716  SER A 720 -1  N  SER A 720   O  LEU A 697           
SHEET    1   M 4 ASP A 216  PHE A 219  0                                        
SHEET    2   M 4 MET A 762  PRO A 768 -1  N  ILE A 764   O  ASP A 216           
SHEET    3   M 4 ASN A 750  GLU A 756 -1  N  VAL A 755   O  ARG A 763           
SHEET    4   M 4 SER A 741  ASP A 747 -1  N  ASP A 747   O  ASN A 750           
SHEET    1   N 2 LYS A 493  GLN A 498  0                                        
SHEET    2   N 2 HIS A 501  ASP A 507 -1  N  PHE A 506   O  ILE A 494           
SHEET    1   O 2 ARG A 605  SER A 608  0                                        
SHEET    2   O 2 ILE A 611  GLU A 613 -1  N  GLU A 613   O  ARG A 605           
LINK        CA    CA A 802                 OD1 ASN A 256     1555   1555  2.18  
LINK        CA    CA A 802                 OD2 ASP A 289     1555   1555  2.34  
LINK        CA    CA A 802                 OG1 THR A 313     1555   1555  2.25  
LINK        CA    CA A 803                 O   ALA A 683     1555   1555  2.40  
LINK        CA    CA A 802                 O   ALA A 253     1555   1555  2.40  
LINK        CA    CA A 802                 OD1 ASP A 289     1555   1555  2.82  
LINK        CA    CA A 802                 O   THR A 313     1555   1555  2.48  
LINK        CA    CA A 802                 O   ASN A 256     1555   1555  2.51  
LINK        CA    CA A 803                 OD2 ASP A 682     1555   1555  2.51  
LINK        CA    CA A 803                 OD1 ASP A 621     1555   1555  2.50  
LINK        CA    CA A 803                 OD2 ASP A 621     1555   1555  2.56  
LINK        CA    CA A 803                 O   HOH A 931     1555   1555  2.65  
LINK        CA    CA A 803                 OD1 ASP A 682     1555   1555  2.61  
CISPEP   1 GLY A  221    PRO A  222          0         4.67                     
SITE     1 ACT 12 ARG A 224  ARG A 245  ASP A 250  ASP A 292                    
SITE     2 ACT 12 TRP A 311  ASN A 318  GLU A 619  ARG A 635                    
SITE     3 ACT 12 ASP A 637  ARG A 712  TYR A 740  GLU A 756                    
SITE     1 AC1  4 ALA A 253  ASN A 256  ASP A 289  THR A 313                    
SITE     1 AC2  5 GLY A 549  ASP A 621  ASP A 682  ALA A 683                    
SITE     2 AC2  5 HOH A 931                                                     
CRYST1   72.300   78.900  164.500  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      0.013831  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012674  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006079        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system