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PDBsum entry 3h71

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Top Page protein Protein-protein interface(s) links
Hydrolase PDB id
3h71
Jmol
Contents
Protein chains
474 a.a.
Waters ×1745
HEADER    HYDROLASE                               24-APR-09   3H71
TITLE     CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE D39
TITLE    2 NEURAMINIDASE A PRECURSOR (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 3H71    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) : 27.39
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 495064.760
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.4
REMARK   3   NUMBER OF REFLECTIONS             : 98994
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) : 0.172
REMARK   3   FREE R VALUE                     : 0.198
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 13133
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002
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) (%) : 89.50
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 27263
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040
REMARK   3   BIN FREE R VALUE                    : 0.2340
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.30
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 2146
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.005
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          : 0
REMARK   3   SOLVENT ATOMS            : 1745
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 11.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.02000
REMARK   3    B22 (A**2) : 0.94000
REMARK   3    B33 (A**2) : 1.08000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.73000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16
REMARK   3   ESD FROM SIGMAA              (A) : 0.10
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) : 0.19
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.12
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) : 0.81
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) : 1.200 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.620 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.870 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.510 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.35
REMARK   3   BSOL        : 44.21
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  : 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   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK   4
REMARK   4 3H71 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 RCSB052772.
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                       : X4A
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          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 98994
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     (%) : 92.7
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : 0.04100
REMARK 200  R SYM                      (I) : 0.00000
REMARK 200   FOR THE DATA SET  : 34.8688
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     (%) : 89.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.09400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 14.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHAKE&BAKE THEN SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 30% JEFFAMINE ED-
REMARK 280  2001, THE DROPS ALSO CONTAINED TRYPSIN AT 5000:1 PROTEIN/
REMARK 280  TRYPSIN RATIO, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  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       79.02000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.83500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.02000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.83500
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: 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. = -17.2 DEGREES
REMARK 500    GLY B 569   N   -  CA  -  C   ANGL. DEV. = -17.5 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       70.86     62.60
REMARK 500    ASP A 372       46.30    -74.17
REMARK 500    VAL A 421      147.12   -170.64
REMARK 500    LYS A 440       31.04    -89.79
REMARK 500    ARG A 476     -154.69   -111.97
REMARK 500    ASN A 523       45.19     36.99
REMARK 500    HIS A 597     -124.86     44.37
REMARK 500    ARG A 605     -176.34   -175.72
REMARK 500    THR A 646     -114.37   -113.11
REMARK 500    TYR A 695       67.30     73.61
REMARK 500    LYS A 720     -144.34   -107.95
REMARK 500    ASN A 723       71.03     58.06
REMARK 500    ALA A 751     -117.14   -130.67
REMARK 500    ILE B 348       71.98     61.29
REMARK 500    ASP B 372       47.05    -77.33
REMARK 500    TRP B 373     -177.76   -170.66
REMARK 500    VAL B 421      146.20   -170.70
REMARK 500    LYS B 440       32.24    -98.23
REMARK 500    ARG B 476     -158.56   -105.66
REMARK 500    ASN B 523       44.95     39.56
REMARK 500    HIS B 597     -125.54     45.33
REMARK 500    ARG B 605     -177.99   -173.52
REMARK 500    THR B 646     -114.37   -114.41
REMARK 500    ASP B 684       94.16     67.68
REMARK 500    TYR B 695       69.55     74.18
REMARK 500    LYS B 720     -159.54   -104.23
REMARK 500    ASN B 723       73.03     53.20
REMARK 500    HIS B 742       44.25   -144.43
REMARK 500    ALA B 751     -117.70   -131.41
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        45.4      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 B1437        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH A1582        DISTANCE =  6.40 ANGSTROMS
REMARK 525    HOH A1633        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH A1685        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH B1609        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A1761        DISTANCE =  5.74 ANGSTROMS
REMARK 525    HOH A1774        DISTANCE =  5.61 ANGSTROMS
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: 3H72   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE D39
REMARK 900 NEURAMINIDASE A PRECURSOR (NANA) IN COMPLEX WITH NANA
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  3H71 A  317   793  UNP    P62576   NANA_STRR6     317    793
DBREF  3H71 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 MSE 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 MSE VAL LEU
SEQRES   9 A  477  VAL GLN ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR
SEQRES  10 A  477  ASP MSE PHE PRO GLU GLY LYS GLY ILE PHE GLY MSE 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  MSE SER TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA
SEQRES  19 A  477  PRO GLN ASP ILE THR PRO MSE VAL LYS ALA ASP TRP MSE
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 MSE 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 MSE 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 MSE SER ALA ILE HIS THR MSE 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 MSE 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 MSE 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 MSE VAL LEU
SEQRES   9 B  477  VAL GLN ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR
SEQRES  10 B  477  ASP MSE PHE PRO GLU GLY LYS GLY ILE PHE GLY MSE 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  MSE SER TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA
SEQRES  19 B  477  PRO GLN ASP ILE THR PRO MSE VAL LYS ALA ASP TRP MSE
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 MSE 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 MSE 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 MSE SER ALA ILE HIS THR MSE 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 MSE 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
MODRES 3H71 MSE A  378  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  418  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  435  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  445  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  538  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  557  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  563  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  638  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  662  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  698  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  704  MET  SELENOMETHIONINE
MODRES 3H71 MSE A  725  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  378  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  418  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  435  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  445  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  538  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  557  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  563  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  638  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  662  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  698  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  704  MET  SELENOMETHIONINE
MODRES 3H71 MSE B  725  MET  SELENOMETHIONINE
HET    MSE  A 378       8
HET    MSE  A 418       8
HET    MSE  A 435       8
HET    MSE  A 445       8
HET    MSE  A 538       8
HET    MSE  A 557       8
HET    MSE  A 563       8
HET    MSE  A 638       8
HET    MSE  A 662       8
HET    MSE  A 698       8
HET    MSE  A 704       8
HET    MSE  A 725       8
HET    MSE  B 378       8
HET    MSE  B 418       8
HET    MSE  B 435       8
HET    MSE  B 445       8
HET    MSE  B 538       8
HET    MSE  B 557       8
HET    MSE  B 563       8
HET    MSE  B 638       8
HET    MSE  B 662       8
HET    MSE  B 698       8
HET    MSE  B 704       8
HET    MSE  B 725       8
HETNAM     MSE SELENOMETHIONINE
FORMUL   1  MSE    24(C5 H11 N O2 SE)
FORMUL   3  HOH   *1745(H2 O)
HELIX    1   1 ASP A  407  GLY A  411  5                                   5
HELIX    2   2 LYS A  440  MSE 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  LYS A  791  1                                   6
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 ASN B  640  ALA B  643  5                                   4
HELIX   14  14 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 767   O  SER A 780
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  GLY A 362   N  ALA A 350
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  MSE 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  MSE 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  MSE A 418
SHEET    1   D 7 TYR A 453  ILE A 456  0
SHEET    2   D 7 LYS A 459  ARG A 466 -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 TYR A 453  ILE A 456  0
SHEET    2   E 3 LYS A 459  ARG A 466 -1  O  LYS A 459   N  ILE A 456
SHEET    3   E 3 PHE A 528  ARG A 529 -1  O  ARG A 529   N  TYR A 465
SHEET    1   F 3 LEU A 566  VAL A 568  0
SHEET    2   F 3 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567
SHEET    3   F 3 ILE A 574  VAL A 575 -1  N  ILE A 574   O  LEU A 586
SHEET    1   G 4 LEU A 566  VAL A 568  0
SHEET    2   G 4 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567
SHEET    3   G 4 SER A 603  SER A 609 -1  O  ARG A 605   N  VAL A 589
SHEET    4   G 4 HIS A 617  ALA A 618 -1  O  HIS A 617   N  TYR A 608
SHEET    1   H 2 ARG A 626  VAL A 628  0
SHEET    2   H 2 GLN A 631  ILE A 633 -1  O  GLN A 631   N  VAL A 628
SHEET    1   I 4 SER A 648  GLN A 652  0
SHEET    2   I 4 VAL A 658  MSE A 662 -1  O  LYS A 659   N  VAL A 651
SHEET    3   I 4 ASP A 668  SER A 674 -1  O  ALA A 672   N  LEU A 660
SHEET    4   I 4 LYS A 686  LYS A 692 -1  O  LYS A 686   N  VAL A 671
SHEET    1   J 4 SER A 699  HIS A 705  0
SHEET    2   J 4 LYS A 708  ALA A 716 -1  O  TYR A 710   N  THR A 703
SHEET    3   J 4 GLU A 722  VAL A 731 -1  O  HIS A 727   N  LEU A 713
SHEET    4   J 4 LEU A 737  GLU A 749 -1  O  ILE A 745   N  GLY A 724
SHEET    1   K 4 THR B 327  PHE B 330  0
SHEET    2   K 4 THR B 778  ASN B 785 -1  O  PHE B 781   N  THR B 327
SHEET    3   K 4 GLU B 762  HIS B 769 -1  N  TYR B 763   O  PHE B 784
SHEET    4   K 4 ASN B 753  GLY B 759 -1  N  GLN B 756   O  GLY B 764
SHEET    1   L 4 SER B 345  LYS B 353  0
SHEET    2   L 4 LEU B 359  ARG B 366 -1  O  ASP B 364   N  ARG B 347
SHEET    3   L 4 ILE B 376  SER B 383 -1  O  GLY B 377   N  GLU B 365
SHEET    4   L 4 VAL B 394  THR B 397 -1  O  VAL B 394   N  ILE B 380
SHEET    1   M 5 GLN B 552  ASP B 553  0
SHEET    2   M 5 TYR B 535  SER B 541 -1  N  MSE B 538   O  GLN B 552
SHEET    3   M 5 ILE B 429  PHE B 436 -1  N  TYR B 433   O  TRP B 537
SHEET    4   M 5 VAL B 414  GLN B 422 -1  N  VAL B 414   O  PHE B 436
SHEET    5   M 5 GLY B 571  THR B 572  1  O  GLY B 571   N  LEU B 420
SHEET    1   N 7 TYR B 453  ILE B 456  0
SHEET    2   N 7 LYS B 459  ARG B 466 -1  O  LYS B 459   N  ILE B 456
SHEET    3   N 7 TYR B 473  ILE B 475 -1  O  TYR B 473   N  LEU B 464
SHEET    4   N 7 THR B 480  TYR B 482 -1  O  TYR B 482   N  THR B 474
SHEET    5   N 7 ALA B 488  VAL B 493 -1  O  TYR B 491   N  VAL B 481
SHEET    6   N 7 ASP B 507  LYS B 510 -1  O  TYR B 509   N  ARG B 492
SHEET    7   N 7 GLN B 513  ASN B 517 -1  O  LEU B 515   N  LEU B 508
SHEET    1   O 3 TYR B 453  ILE B 456  0
SHEET    2   O 3 LYS B 459  ARG B 466 -1  O  LYS B 459   N  ILE B 456
SHEET    3   O 3 PHE B 528  ARG B 529 -1  O  ARG B 529   N  TYR B 465
SHEET    1   P 3 LEU B 566  VAL B 568  0
SHEET    2   P 3 ILE B 585  THR B 591 -1  O  TYR B 590   N  GLY B 567
SHEET    3   P 3 ILE B 574  VAL B 575 -1  N  ILE B 574   O  LEU B 586
SHEET    1   Q 4 LEU B 566  VAL B 568  0
SHEET    2   Q 4 ILE B 585  THR B 591 -1  O  TYR B 590   N  GLY B 567
SHEET    3   Q 4 SER B 603  SER B 609 -1  O  ARG B 605   N  VAL B 589
SHEET    4   Q 4 HIS B 617  ALA B 618 -1  O  HIS B 617   N  TYR B 608
SHEET    1   R 2 ARG B 626  VAL B 628  0
SHEET    2   R 2 GLN B 631  ILE B 633 -1  O  GLN B 631   N  VAL B 628
SHEET    1   S 4 ASN B 645  GLN B 652  0
SHEET    2   S 4 VAL B 658  GLY B 664 -1  O  LYS B 659   N  VAL B 651
SHEET    3   S 4 ASP B 668  SER B 674 -1  O  ALA B 672   N  LEU B 660
SHEET    4   S 4 LYS B 686  LYS B 692 -1  O  LYS B 686   N  VAL B 671
SHEET    1   T 4 SER B 699  HIS B 705  0
SHEET    2   T 4 LYS B 708  ALA B 716 -1  O  TYR B 710   N  THR B 703
SHEET    3   T 4 GLU B 722  VAL B 731 -1  O  HIS B 727   N  LEU B 713
SHEET    4   T 4 LEU B 737  GLU B 749 -1  O  ILE B 745   N  GLY B 724
LINK         C   GLY A 377                 N   MSE A 378     1555   1555  1.33
LINK         C   MSE A 378                 N   VAL A 379     1555   1555  1.33
LINK         C   ASP A 417                 N   MSE A 418     1555   1555  1.33
LINK         C   MSE A 418                 N   VAL A 419     1555   1555  1.33
LINK         C   ASP A 434                 N   MSE A 435     1555   1555  1.33
LINK         C   MSE A 435                 N   PHE A 436     1555   1555  1.33
LINK         C   GLY A 444                 N   MSE A 445     1555   1555  1.33
LINK         C   MSE A 445                 N   SER A 446     1555   1555  1.33
LINK         C   TRP A 537                 N   MSE A 538     1555   1555  1.33
LINK         C   MSE A 538                 N   SER A 539     1555   1555  1.33
LINK         C   PRO A 556                 N   MSE A 557     1555   1555  1.33
LINK         C   MSE A 557                 N   VAL A 558     1555   1555  1.33
LINK         C   TRP A 562                 N   MSE A 563     1555   1555  1.33
LINK         C   MSE A 563                 N   LYS A 564     1555   1555  1.32
LINK         C   THR A 637                 N   MSE A 638     1555   1555  1.33
LINK         C   MSE A 638                 N   ASN A 639     1555   1555  1.33
LINK         C   PHE A 661                 N   MSE A 662     1555   1555  1.33
LINK         C   MSE A 662                 N   ARG A 663     1555   1555  1.33
LINK         C   GLN A 697                 N   MSE A 698     1555   1555  1.33
LINK         C   MSE A 698                 N   SER A 699     1555   1555  1.33
LINK         C   THR A 703                 N   MSE A 704     1555   1555  1.33
LINK         C   MSE A 704                 N   HIS A 705     1555   1555  1.33
LINK         C   GLY A 724                 N   MSE A 725     1555   1555  1.33
LINK         C   MSE A 725                 N   VAL A 726     1555   1555  1.33
LINK         C   GLY B 377                 N   MSE B 378     1555   1555  1.33
LINK         C   MSE B 378                 N   VAL B 379     1555   1555  1.33
LINK         C   ASP B 417                 N   MSE B 418     1555   1555  1.33
LINK         C   MSE B 418                 N   VAL B 419     1555   1555  1.32
LINK         C   ASP B 434                 N   MSE B 435     1555   1555  1.33
LINK         C   MSE B 435                 N   PHE B 436     1555   1555  1.33
LINK         C   GLY B 444                 N   MSE B 445     1555   1555  1.33
LINK         C   MSE B 445                 N   SER B 446     1555   1555  1.33
LINK         C   TRP B 537                 N   MSE B 538     1555   1555  1.33
LINK         C   MSE B 538                 N   SER B 539     1555   1555  1.33
LINK         C   PRO B 556                 N   MSE B 557     1555   1555  1.33
LINK         C   MSE B 557                 N   VAL B 558     1555   1555  1.33
LINK         C   TRP B 562                 N   MSE B 563     1555   1555  1.33
LINK         C   MSE B 563                 N   LYS B 564     1555   1555  1.33
LINK         C   THR B 637                 N   MSE B 638     1555   1555  1.32
LINK         C   MSE B 638                 N   ASN B 639     1555   1555  1.33
LINK         C   PHE B 661                 N   MSE B 662     1555   1555  1.33
LINK         C   MSE B 662                 N   ARG B 663     1555   1555  1.33
LINK         C   GLN B 697                 N   MSE B 698     1555   1555  1.33
LINK         C   MSE B 698                 N   SER B 699     1555   1555  1.33
LINK         C   THR B 703                 N   MSE B 704     1555   1555  1.33
LINK         C   MSE B 704                 N   HIS B 705     1555   1555  1.33
LINK         C   GLY B 724                 N   MSE B 725     1555   1555  1.33
LINK         C   MSE B 725                 N   VAL B 726     1555   1555  1.33
CISPEP   1 GLY A  718    PRO A  719          0         0.09
CISPEP   2 ALA A  776    TYR A  777          0        -1.43
CISPEP   3 GLY B  718    PRO B  719          0        -0.04
CISPEP   4 ALA B  776    TYR B  777          0        -1.39
CRYST1  158.040   47.670  137.270  90.00 116.56  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      0.006328  0.000000  0.003163        0.00000
SCALE2      0.000000  0.020978  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008144        0.00000
      
PROCHECK
Go to PROCHECK summary
 References