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PDBsum entry 3h72

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3h72
Jmol
Contents
Protein chains
474 a.a.
Ligands
SIA ×2
Waters ×1446
HEADER    HYDROLASE                               24-APR-09   3H72
TITLE     CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE D39
TITLE    2 NEURAMINIDASE A PRECURSOR (NANA) IN COMPLEX WITH NANA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE A;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: UNP RESIDUES 317-793;
COMPND   5 SYNONYM: NEURAMINIDASE A;
COMPND   6 EC: 3.2.1.18;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE   3 ORGANISM_TAXID: 171101;
SOURCE   4 STRAIN: R6;
SOURCE   5 GENE: NANA, SPR1536;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28A
KEYWDS    SIX-BLADED BETA-PROPELLER, CELL WALL, GLYCOSIDASE,
KEYWDS   2 HYDROLASE, PEPTIDOGLYCAN-ANCHOR, SECRETED
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.-S.HSIAO,L.TONG
REVDAT   1   12-MAY-09 3H72    0
JRNL        AUTH   Y.-S.HSIAO,D.PARKER,A.J.RATNER,A.PRINCE,L.TONG
JRNL        TITL   CRYSTAL STRUCTURES OF RESPIRATORY PATHOGEN
JRNL        TITL 2 NEURAMINIDASES
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 380   467 2009
JRNL        REFN                   ISSN 0006-291X
JRNL        PMID   19284989
JRNL        DOI    10.1016/J.BBRC.2009.01.108
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.2
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.34
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 662438.230
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.2
REMARK   3   NUMBER OF REFLECTIONS             : 86772
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.175
REMARK   3   FREE R VALUE                     : 0.209
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 6556
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10793
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080
REMARK   3   BIN FREE R VALUE                    : 0.2480
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.60
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 889
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7518
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 42
REMARK   3   SOLVENT ATOMS            : 1446
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 12.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.45000
REMARK   3    B22 (A**2) : 0.50000
REMARK   3    B33 (A**2) : 1.96000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.82000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17
REMARK   3   ESD FROM SIGMAA              (A) : 0.09
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.20
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.15
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.90
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.160 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.760 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.910 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.820 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.40
REMARK   3   BSOL        : 68.67
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : SIB.PAR
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : ION.TOP
REMARK   3  TOPOLOGY FILE  5   : SIB.TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK   4
REMARK   4 3H72 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052773.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-08
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X4C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9798
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86773
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.5
REMARK 200  DATA REDUNDANCY                : 2.800
REMARK 200  R MERGE                    (I) : 0.06000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.0437
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.14200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 6.862
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: COMO
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 30% JEFFAMINE ED-
REMARK 280  2001, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       79.31500
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.68500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.31500
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.68500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     LEU A   317
REMARK 465     PRO A   318
REMARK 465     GLU A   319
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 B  1031     O    HOH B  1031     2655     1.42
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    GLY A 569   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES
REMARK 500    GLY B 569   N   -  CA  -  C   ANGL. DEV. = -17.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ILE A 348       74.19     58.89
REMARK 500    ASP A 372       46.88    -78.04
REMARK 500    TRP A 373     -173.55   -171.92
REMARK 500    ASP A 417      113.02     68.64
REMARK 500    GLU A 438      128.02    -38.55
REMARK 500    ARG A 476     -157.73   -109.19
REMARK 500    ASN A 523       43.84     38.32
REMARK 500    LYS A 564      -82.14    -95.05
REMARK 500    HIS A 597     -125.07     41.30
REMARK 500    ARG A 605     -178.76   -173.85
REMARK 500    THR A 646     -114.65   -114.40
REMARK 500    TYR A 695       68.00     74.72
REMARK 500    LYS A 720     -146.25   -106.95
REMARK 500    ASN A 723       75.37     56.19
REMARK 500    ALA A 751     -116.28   -133.71
REMARK 500    ILE B 348       73.01     58.01
REMARK 500    ASP B 372       47.42    -78.86
REMARK 500    TRP B 373     -175.40   -172.49
REMARK 500    ASP B 417      116.44     64.44
REMARK 500    LYS B 440       30.86    -99.24
REMARK 500    ARG B 476     -156.58   -107.79
REMARK 500    LYS B 564      -81.58    -93.52
REMARK 500    HIS B 597     -122.00     39.70
REMARK 500    ARG B 605     -176.87   -174.88
REMARK 500    ASP B 629       41.10     37.43
REMARK 500    ASN B 639       76.20   -153.00
REMARK 500    THR B 646     -113.24   -115.56
REMARK 500    ASP B 684       96.92     65.64
REMARK 500    TYR B 695       70.10     71.54
REMARK 500    LYS B 720     -156.75   -107.05
REMARK 500    ASN B 723       72.56     53.60
REMARK 500    HIS B 742       44.88   -143.24
REMARK 500    ALA B 751     -117.91   -131.98
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 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: (11X,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     PRO A 413        45.9      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 B 966        DISTANCE =  5.57 ANGSTROMS
REMARK 525    HOH B1125        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH B1174        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH B1224        DISTANCE =  5.78 ANGSTROMS
REMARK 525    HOH B1250        DISTANCE =  6.53 ANGSTROMS
REMARK 525    HOH B1311        DISTANCE =  6.84 ANGSTROMS
REMARK 525    HOH B1343        DISTANCE =  5.32 ANGSTROMS
REMARK 525    HOH B1444        DISTANCE =  6.91 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA A 900
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA B 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3H6J   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A PUTATIVE NEURAMINIDASE FROM
REMARK 900 PSEUDOMONAS AERUGINOSA
REMARK 900 RELATED ID: 3H71   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE D39
REMARK 900 NEURAMINIDASE A PRECURSOR (NANA), FREE ENZYME
REMARK 900 RELATED ID: 3H73   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE D39
REMARK 900 NEURAMINIDASE A PRECURSOR (NANA) IN COMPLEX WITH DANA
DBREF  3H72 A  317   793  UNP    P62576   NANA_STRR6     317    793
DBREF  3H72 B  317   793  UNP    P62576   NANA_STRR6     317    793
SEQRES   1 A  477  LEU PRO GLU GLY ALA ALA LEU THR GLU LYS THR ASP ILE
SEQRES   2 A  477  PHE GLU SER GLY ARG ASN GLY LYS PRO ASN LYS ASP GLY
SEQRES   3 A  477  ILE LYS SER TYR ARG ILE PRO ALA LEU LEU LYS THR ASP
SEQRES   4 A  477  LYS GLY THR LEU ILE ALA GLY ALA ASP GLU ARG ARG LEU
SEQRES   5 A  477  HIS SER SER ASP TRP GLY ASP ILE GLY MET VAL ILE ARG
SEQRES   6 A  477  ARG SER GLU ASP ASN GLY LYS THR TRP GLY ASP ARG VAL
SEQRES   7 A  477  THR ILE THR ASN LEU ARG ASP ASN PRO LYS ALA SER ASP
SEQRES   8 A  477  PRO SER ILE GLY SER PRO VAL ASN ILE ASP MET VAL LEU
SEQRES   9 A  477  VAL GLN ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR
SEQRES  10 A  477  ASP MET PHE PRO GLU GLY LYS GLY ILE PHE GLY MET SER
SEQRES  11 A  477  SER GLN LYS GLU GLU ALA TYR LYS LYS ILE ASP GLY LYS
SEQRES  12 A  477  THR TYR GLN ILE LEU TYR ARG GLU GLY GLU LYS GLY ALA
SEQRES  13 A  477  TYR THR ILE ARG GLU ASN GLY THR VAL TYR THR PRO ASP
SEQRES  14 A  477  GLY LYS ALA THR ASP TYR ARG VAL VAL VAL ASP PRO VAL
SEQRES  15 A  477  LYS PRO ALA TYR SER ASP LYS GLY ASP LEU TYR LYS GLY
SEQRES  16 A  477  ASN GLN LEU LEU GLY ASN ILE TYR PHE THR THR ASN LYS
SEQRES  17 A  477  THR SER PRO PHE ARG ILE ALA LYS ASP SER TYR LEU TRP
SEQRES  18 A  477  MET SER TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA
SEQRES  19 A  477  PRO GLN ASP ILE THR PRO MET VAL LYS ALA ASP TRP MET
SEQRES  20 A  477  LYS PHE LEU GLY VAL GLY PRO GLY THR GLY ILE VAL LEU
SEQRES  21 A  477  ARG ASN GLY PRO HIS LYS GLY ARG ILE LEU ILE PRO VAL
SEQRES  22 A  477  TYR THR THR ASN ASN VAL SER HIS LEU ASN GLY SER GLN
SEQRES  23 A  477  SER SER ARG ILE ILE TYR SER ASP ASP HIS GLY LYS THR
SEQRES  24 A  477  TRP HIS ALA GLY GLU ALA VAL ASN ASP ASN ARG GLN VAL
SEQRES  25 A  477  ASP GLY GLN LYS ILE HIS SER SER THR MET ASN ASN ARG
SEQRES  26 A  477  ARG ALA GLN ASN THR GLU SER THR VAL VAL GLN LEU ASN
SEQRES  27 A  477  ASN GLY ASP VAL LYS LEU PHE MET ARG GLY LEU THR GLY
SEQRES  28 A  477  ASP LEU GLN VAL ALA THR SER LYS ASP GLY GLY VAL THR
SEQRES  29 A  477  TRP GLU LYS ASP ILE LYS ARG TYR PRO GLN VAL LYS ASP
SEQRES  30 A  477  VAL TYR VAL GLN MET SER ALA ILE HIS THR MET HIS GLU
SEQRES  31 A  477  GLY LYS GLU TYR ILE ILE LEU SER ASN ALA GLY GLY PRO
SEQRES  32 A  477  LYS ARG GLU ASN GLY MET VAL HIS LEU ALA ARG VAL GLU
SEQRES  33 A  477  GLU ASN GLY GLU LEU THR TRP LEU LYS HIS ASN PRO ILE
SEQRES  34 A  477  GLN LYS GLY GLU PHE ALA TYR ASN SER LEU GLN GLU LEU
SEQRES  35 A  477  GLY ASN GLY GLU TYR GLY ILE LEU TYR GLU HIS THR GLU
SEQRES  36 A  477  LYS GLY GLN ASN ALA TYR THR LEU SER PHE ARG LYS PHE
SEQRES  37 A  477  ASN TRP ASP PHE LEU SER LYS ASP LEU
SEQRES   1 B  477  LEU PRO GLU GLY ALA ALA LEU THR GLU LYS THR ASP ILE
SEQRES   2 B  477  PHE GLU SER GLY ARG ASN GLY LYS PRO ASN LYS ASP GLY
SEQRES   3 B  477  ILE LYS SER TYR ARG ILE PRO ALA LEU LEU LYS THR ASP
SEQRES   4 B  477  LYS GLY THR LEU ILE ALA GLY ALA ASP GLU ARG ARG LEU
SEQRES   5 B  477  HIS SER SER ASP TRP GLY ASP ILE GLY MET VAL ILE ARG
SEQRES   6 B  477  ARG SER GLU ASP ASN GLY LYS THR TRP GLY ASP ARG VAL
SEQRES   7 B  477  THR ILE THR ASN LEU ARG ASP ASN PRO LYS ALA SER ASP
SEQRES   8 B  477  PRO SER ILE GLY SER PRO VAL ASN ILE ASP MET VAL LEU
SEQRES   9 B  477  VAL GLN ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR
SEQRES  10 B  477  ASP MET PHE PRO GLU GLY LYS GLY ILE PHE GLY MET SER
SEQRES  11 B  477  SER GLN LYS GLU GLU ALA TYR LYS LYS ILE ASP GLY LYS
SEQRES  12 B  477  THR TYR GLN ILE LEU TYR ARG GLU GLY GLU LYS GLY ALA
SEQRES  13 B  477  TYR THR ILE ARG GLU ASN GLY THR VAL TYR THR PRO ASP
SEQRES  14 B  477  GLY LYS ALA THR ASP TYR ARG VAL VAL VAL ASP PRO VAL
SEQRES  15 B  477  LYS PRO ALA TYR SER ASP LYS GLY ASP LEU TYR LYS GLY
SEQRES  16 B  477  ASN GLN LEU LEU GLY ASN ILE TYR PHE THR THR ASN LYS
SEQRES  17 B  477  THR SER PRO PHE ARG ILE ALA LYS ASP SER TYR LEU TRP
SEQRES  18 B  477  MET SER TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA
SEQRES  19 B  477  PRO GLN ASP ILE THR PRO MET VAL LYS ALA ASP TRP MET
SEQRES  20 B  477  LYS PHE LEU GLY VAL GLY PRO GLY THR GLY ILE VAL LEU
SEQRES  21 B  477  ARG ASN GLY PRO HIS LYS GLY ARG ILE LEU ILE PRO VAL
SEQRES  22 B  477  TYR THR THR ASN ASN VAL SER HIS LEU ASN GLY SER GLN
SEQRES  23 B  477  SER SER ARG ILE ILE TYR SER ASP ASP HIS GLY LYS THR
SEQRES  24 B  477  TRP HIS ALA GLY GLU ALA VAL ASN ASP ASN ARG GLN VAL
SEQRES  25 B  477  ASP GLY GLN LYS ILE HIS SER SER THR MET ASN ASN ARG
SEQRES  26 B  477  ARG ALA GLN ASN THR GLU SER THR VAL VAL GLN LEU ASN
SEQRES  27 B  477  ASN GLY ASP VAL LYS LEU PHE MET ARG GLY LEU THR GLY
SEQRES  28 B  477  ASP LEU GLN VAL ALA THR SER LYS ASP GLY GLY VAL THR
SEQRES  29 B  477  TRP GLU LYS ASP ILE LYS ARG TYR PRO GLN VAL LYS ASP
SEQRES  30 B  477  VAL TYR VAL GLN MET SER ALA ILE HIS THR MET HIS GLU
SEQRES  31 B  477  GLY LYS GLU TYR ILE ILE LEU SER ASN ALA GLY GLY PRO
SEQRES  32 B  477  LYS ARG GLU ASN GLY MET VAL HIS LEU ALA ARG VAL GLU
SEQRES  33 B  477  GLU ASN GLY GLU LEU THR TRP LEU LYS HIS ASN PRO ILE
SEQRES  34 B  477  GLN LYS GLY GLU PHE ALA TYR ASN SER LEU GLN GLU LEU
SEQRES  35 B  477  GLY ASN GLY GLU TYR GLY ILE LEU TYR GLU HIS THR GLU
SEQRES  36 B  477  LYS GLY GLN ASN ALA TYR THR LEU SER PHE ARG LYS PHE
SEQRES  37 B  477  ASN TRP ASP PHE LEU SER LYS ASP LEU
HET    SIA  A 900      21
HET    SIA  B 901      21
HETNAM     SIA O-SIALIC ACID
FORMUL   3  SIA    2(C11 H19 N O9)
FORMUL   5  HOH   *1446(H2 O)
HELIX    1   1 ASP A  407  GLY A  411  5                                   5
HELIX    2   2 LYS A  440  MET A  445  5                                   6
HELIX    3   3 LYS A  499  SER A  503  5                                   5
HELIX    4   4 ILE A  554  LYS A  559  1                                   6
HELIX    5   5 SER A  596  SER A  601  1                                   6
HELIX    6   6 ASN A  640  GLN A  644  5                                   5
HELIX    7   7 TRP A  786  SER A  790  1                                   5
HELIX    8   8 ASP B  407  GLY B  411  5                                   5
HELIX    9   9 LYS B  440  GLY B  444  5                                   5
HELIX   10  10 LYS B  499  SER B  503  5                                   5
HELIX   11  11 ILE B  554  LYS B  559  1                                   6
HELIX   12  12 SER B  596  SER B  601  1                                   6
HELIX   13  13 TRP B  786  LYS B  791  1                                   6
SHEET    1   A 4 THR A 327  PHE A 330  0
SHEET    2   A 4 THR A 778  ASN A 785 -1  O  PHE A 781   N  THR A 327
SHEET    3   A 4 GLU A 762  HIS A 769 -1  N  TYR A 763   O  PHE A 784
SHEET    4   A 4 ASN A 753  GLY A 759 -1  N  GLN A 756   O  GLY A 764
SHEET    1   B 4 SER A 345  LYS A 353  0
SHEET    2   B 4 LEU A 359  ARG A 366 -1  O  ASP A 364   N  ARG A 347
SHEET    3   B 4 ILE A 376  SER A 383 -1  O  GLY A 377   N  GLU A 365
SHEET    4   B 4 VAL A 394  THR A 397 -1  O  ILE A 396   N  MET A 378
SHEET    1   C 5 GLN A 552  ASP A 553  0
SHEET    2   C 5 TYR A 535  SER A 541 -1  N  MET A 538   O  GLN A 552
SHEET    3   C 5 ILE A 429  PHE A 436 -1  N  TYR A 433   O  TRP A 537
SHEET    4   C 5 VAL A 414  GLN A 422 -1  N  VAL A 421   O  PHE A 430
SHEET    5   C 5 GLY A 571  THR A 572  1  O  GLY A 571   N  MET A 418
SHEET    1   D 7 TYR A 453  ILE A 456  0
SHEET    2   D 7 LYS A 459  LEU A 464 -1  O  LYS A 459   N  ILE A 456
SHEET    3   D 7 TYR A 473  ILE A 475 -1  O  TYR A 473   N  LEU A 464
SHEET    4   D 7 THR A 480  TYR A 482 -1  O  TYR A 482   N  THR A 474
SHEET    5   D 7 ALA A 488  VAL A 493 -1  O  TYR A 491   N  VAL A 481
SHEET    6   D 7 ASP A 507  LYS A 510 -1  O  TYR A 509   N  ARG A 492
SHEET    7   D 7 GLN A 513  ASN A 517 -1  O  LEU A 515   N  LEU A 508
SHEET    1   E 3 LEU A 566  VAL A 568  0
SHEET    2   E 3 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567
SHEET    3   E 3 ILE A 574  VAL A 575 -1  N  ILE A 574   O  LEU A 586
SHEET    1   F 4 LEU A 566  VAL A 568  0
SHEET    2   F 4 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567
SHEET    3   F 4 SER A 603  SER A 609 -1  O  ARG A 605   N  VAL A 589
SHEET    4   F 4 HIS A 617  ALA A 618 -1  O  HIS A 617   N  TYR A 608
SHEET    1   G 2 ARG A 626  GLN A 627  0
SHEET    2   G 2 LYS A 632  ILE A 633 -1  O  ILE A 633   N  ARG A 626
SHEET    1   H 4 SER A 648  GLN A 652  0
SHEET    2   H 4 VAL A 658  MET A 662 -1  O  LYS A 659   N  VAL A 651
SHEET    3   H 4 ASP A 668  SER A 674 -1  O  SER A 674   N  VAL A 658
SHEET    4   H 4 LYS A 686  LYS A 692 -1  O  LYS A 686   N  VAL A 671
SHEET    1   I 4 SER A 699  HIS A 705  0
SHEET    2   I 4 LYS A 708  ALA A 716 -1  O  TYR A 710   N  THR A 703
SHEET    3   I 4 GLU A 722  VAL A 731 -1  O  HIS A 727   N  LEU A 713
SHEET    4   I 4 LEU A 737  GLU A 749 -1  O  LEU A 740   N  LEU A 728
SHEET    1   J 4 THR B 327  PHE B 330  0
SHEET    2   J 4 THR B 778  ASN B 785 -1  O  PHE B 781   N  THR B 327
SHEET    3   J 4 GLU B 762  HIS B 769 -1  N  TYR B 767   O  SER B 780
SHEET    4   J 4 ASN B 753  GLY B 759 -1  N  GLN B 756   O  GLY B 764
SHEET    1   K 4 SER B 345  LYS B 353  0
SHEET    2   K 4 LEU B 359  ARG B 366 -1  O  ASP B 364   N  ARG B 347
SHEET    3   K 4 ILE B 376  SER B 383 -1  O  GLY B 377   N  GLU B 365
SHEET    4   K 4 VAL B 394  THR B 397 -1  O  VAL B 394   N  ILE B 380
SHEET    1   L 5 GLN B 552  ASP B 553  0
SHEET    2   L 5 TYR B 535  SER B 541 -1  N  MET B 538   O  GLN B 552
SHEET    3   L 5 ILE B 429  PHE B 436 -1  N  TYR B 433   O  TRP B 537
SHEET    4   L 5 VAL B 414  GLN B 422 -1  N  VAL B 421   O  PHE B 430
SHEET    5   L 5 GLY B 571  THR B 572  1  O  GLY B 571   N  LEU B 420
SHEET    1   M 7 TYR B 453  ILE B 456  0
SHEET    2   M 7 LYS B 459  ARG B 466 -1  O  LYS B 459   N  ILE B 456
SHEET    3   M 7 TYR B 473  ILE B 475 -1  O  TYR B 473   N  LEU B 464
SHEET    4   M 7 THR B 480  TYR B 482 -1  O  TYR B 482   N  THR B 474
SHEET    5   M 7 ALA B 488  VAL B 493 -1  O  TYR B 491   N  VAL B 481
SHEET    6   M 7 ASP B 507  LYS B 510 -1  O  TYR B 509   N  ARG B 492
SHEET    7   M 7 GLN B 513  ASN B 517 -1  O  LEU B 515   N  LEU B 508
SHEET    1   N 3 TYR B 453  ILE B 456  0
SHEET    2   N 3 LYS B 459  ARG B 466 -1  O  LYS B 459   N  ILE B 456
SHEET    3   N 3 PHE B 528  ARG B 529 -1  O  ARG B 529   N  TYR B 465
SHEET    1   O 3 LEU B 566  VAL B 568  0
SHEET    2   O 3 ILE B 585  THR B 591 -1  O  TYR B 590   N  GLY B 567
SHEET    3   O 3 ILE B 574  VAL B 575 -1  N  ILE B 574   O  LEU B 586
SHEET    1   P 4 LEU B 566  VAL B 568  0
SHEET    2   P 4 ILE B 585  THR B 591 -1  O  TYR B 590   N  GLY B 567
SHEET    3   P 4 SER B 603  SER B 609 -1  O  ARG B 605   N  VAL B 589
SHEET    4   P 4 HIS B 617  ALA B 618 -1  O  HIS B 617   N  TYR B 608
SHEET    1   Q 2 ARG B 626  VAL B 628  0
SHEET    2   Q 2 GLN B 631  ILE B 633 -1  O  GLN B 631   N  VAL B 628
SHEET    1   R 4 SER B 648  GLN B 652  0
SHEET    2   R 4 VAL B 658  MET B 662 -1  O  LYS B 659   N  VAL B 651
SHEET    3   R 4 ASP B 668  SER B 674 -1  O  SER B 674   N  VAL B 658
SHEET    4   R 4 LYS B 686  LYS B 692 -1  O  LYS B 686   N  VAL B 671
SHEET    1   S 4 SER B 699  HIS B 705  0
SHEET    2   S 4 LYS B 708  ALA B 716 -1  O  SER B 714   N  SER B 699
SHEET    3   S 4 GLU B 722  VAL B 731 -1  O  HIS B 727   N  LEU B 713
SHEET    4   S 4 LEU B 737  GLU B 749 -1  O  LEU B 740   N  LEU B 728
CISPEP   1 GLY A  718    PRO A  719          0         0.18
CISPEP   2 ALA A  776    TYR A  777          0        -1.26
CISPEP   3 GLY B  718    PRO B  719          0         0.30
CISPEP   4 ALA B  776    TYR B  777          0        -1.59
SITE     1 AC1 20 HOH A  22  HOH A  36  HOH A 168  ARG A 347
SITE     2 AC1 20 ILE A 348  ARG A 366  ASP A 372  ILE A 416
SITE     3 AC1 20 ASP A 417  ASP A 434  ILE A 442  PHE A 443
SITE     4 AC1 20 TYR A 590  GLN A 602  ARG A 663  TYR A 695
SITE     5 AC1 20 ARG A 721  TYR A 752  HOH A 956  HOH A1080
SITE     1 AC2 19 HOH B  13  HOH B 121  HOH B 138  ARG B 347
SITE     2 AC2 19 ILE B 348  ARG B 366  ASP B 372  ASP B 417
SITE     3 AC2 19 ASP B 434  ILE B 442  PHE B 443  TYR B 590
SITE     4 AC2 19 GLN B 602  GLU B 647  ARG B 663  ARG B 721
SITE     5 AC2 19 TYR B 752  HOH B 886  HOH B 932
CRYST1  158.630   47.370  137.060  90.00 116.41  90.00 C 1 2 1       8
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      0.006304  0.000000  0.003131        0.00000
SCALE2      0.000000  0.021110  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008146        0.00000
      
PROCHECK
Go to PROCHECK summary
 References