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PDBsum entry 2ya6

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2ya6
Jmol
Contents
Protein chains
470 a.a.
Ligands
DAN ×2
FMT ×5
Metals
_CL ×2
Waters ×585
HEADER    HYDROLASE                               18-FEB-11   2YA6
TITLE     CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4)
TITLE    2 IN COMPLEX WITH DANA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE A;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 280-754;
COMPND   5 SYNONYM: NANA;
COMPND   6 EC: 3.2.1.18;
COMPND   7 ENGINEERED: YES;
COMPND   8 OTHER_DETAILS: THE SEQUENCE NUMBERING ABOVE CORRESPONDS TO THE
COMPND   9  CLOSEST UNIPROT SEQUENCE MATCH UNP B2DJD9. THE SEQUENCE NUMBERING
COMPND  10  FOR THE ENTRY SHOULD BE 303-777
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE   3 ORGANISM_TAXID: 170187;
SOURCE   4 STRAIN: TIGR4;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS    HYDROLASE, SIALIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.GUT,G.XU,G.L.TAYLOR,M.A.WALSH
REVDAT   2   08-JUN-11 2YA6    1       JRNL
REVDAT   1   27-APR-11 2YA6    0
JRNL        AUTH   H.GUT,G.XU,G.L.TAYLOR,M.A.WALSH
JRNL        TITL   STRUCTURAL BASIS FOR STREPTOCOCCUS PNEUMONIAE NANA
JRNL        TITL 2 INHIBITION BY INFLUENZA ANTIVIRALS ZANAMIVIR AND
JRNL        TITL 3 OSELTAMIVIR CARBOXYLATE.
JRNL        REF    J.MOL.BIOL.                   V. 409   496 2011
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   21514303
JRNL        DOI    10.1016/J.JMB.2011.04.016
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.95
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.86
REMARK   3   NUMBER OF REFLECTIONS             : 61963
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 + TEST SET) : 0.19660
REMARK   3   R VALUE            (WORKING SET) : 0.19552
REMARK   3   FREE R VALUE                     : 0.23774
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.5
REMARK   3   FREE R VALUE TEST SET COUNT      : 1578
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.004
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.056
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3685
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.09
REMARK   3   BIN R VALUE           (WORKING SET) : 0.288
REMARK   3   BIN FREE R VALUE SET COUNT          : 85
REMARK   3   BIN FREE R VALUE                    : 0.374
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7456
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 57
REMARK   3   SOLVENT ATOMS            : 583
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 32.2
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.647
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00
REMARK   3    B22 (A**2) : 0.00
REMARK   3    B33 (A**2) : 0.00
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.209
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.134
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.804
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7670 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10359 ; 1.263 ; 1.953
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   942 ; 7.040 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   370 ;34.613 ;24.486
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1340 ;14.186 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;14.205 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1094 ; 0.084 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5872 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3638 ; 0.192 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5141 ; 0.302 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   744 ; 0.144 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    32 ; 0.190 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.089 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4806 ; 0.732 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7504 ; 1.242 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3312 ; 1.570 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2855 ; 2.437 ; 4.500
REMARK   3
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3   RIDING POSITIONS.
REMARK   4
REMARK   4 2YA6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-FEB-11.
REMARK 100 THE PDBE ID CODE IS EBI-47419.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : BM14
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL CUT
REMARK 200  OPTICS                         : TOROIDAL MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RAYONICS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200  DATA SCALING SOFTWARE          : HKL2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63554
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.00
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0
REMARK 200  DATA REDUNDANCY                : 3.8
REMARK 200  R MERGE                    (I) : 0.06
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 22.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.7
REMARK 200  R MERGE FOR SHELL          (I) : 0.46
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.86
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 200 MM KFORMATE,
REMARK 280  20 MM TRIS PH 7.5 .
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       82.42850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.41750
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       82.42850
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.41750
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     ALA A   285
REMARK 465     HIS A   286
REMARK 465     HIS A   287
REMARK 465     HIS A   288
REMARK 465     HIS A   289
REMARK 465     HIS A   290
REMARK 465     HIS A   291
REMARK 465     SER A   292
REMARK 465     SER A   293
REMARK 465     GLY A   294
REMARK 465     LEU A   295
REMARK 465     GLU A   296
REMARK 465     VAL A   297
REMARK 465     LEU A   298
REMARK 465     PHE A   299
REMARK 465     GLN A   300
REMARK 465     GLY A   301
REMARK 465     PRO A   302
REMARK 465     PRO A   303
REMARK 465     GLU A   304
REMARK 465     GLY A   305
REMARK 465     ALA A   306
REMARK 465     ASN A   777
REMARK 465     ALA B   285
REMARK 465     HIS B   286
REMARK 465     HIS B   287
REMARK 465     HIS B   288
REMARK 465     HIS B   289
REMARK 465     HIS B   290
REMARK 465     HIS B   291
REMARK 465     SER B   292
REMARK 465     SER B   293
REMARK 465     GLY B   294
REMARK 465     LEU B   295
REMARK 465     GLU B   296
REMARK 465     VAL B   297
REMARK 465     LEU B   298
REMARK 465     PHE B   299
REMARK 465     GLN B   300
REMARK 465     GLY B   301
REMARK 465     PRO B   302
REMARK 465     PRO B   303
REMARK 465     GLU B   304
REMARK 465     GLY B   305
REMARK 465     ALA B   306
REMARK 465     ASN B   777
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OD1  ASN B   383     O    HOH B  2029              2.14
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 333       66.40     71.02
REMARK 500    ASP A 357       47.05    -85.70
REMARK 500    TRP A 358     -176.16   -172.32
REMARK 500    ASP A 402      116.66     66.24
REMARK 500    ARG A 461     -166.05   -112.39
REMARK 500    LYS A 549      -88.27    -93.16
REMARK 500    SER A 581       -1.11   -140.10
REMARK 500    HIS A 582     -124.73     41.87
REMARK 500    THR A 631     -115.09   -118.93
REMARK 500    TYR A 680       71.20     70.82
REMARK 500    GLU A 691       78.42     35.28
REMARK 500    LYS A 705     -153.75   -109.01
REMARK 500    ASN A 708       75.16     56.67
REMARK 500    ALA A 736     -118.45   -134.95
REMARK 500    ASN B 324     -170.42    -67.39
REMARK 500    ILE B 333       71.09     61.97
REMARK 500    ASP B 357       49.31    -84.22
REMARK 500    TRP B 358     -171.69   -175.44
REMARK 500    ASP B 370       29.74   -147.25
REMARK 500    ASP B 402      117.14     70.80
REMARK 500    LYS B 412       -3.30     72.53
REMARK 500    ARG B 461     -160.88   -107.29
REMARK 500    LYS B 549      -86.99    -95.28
REMARK 500    LYS B 567      136.56    -39.77
REMARK 500    HIS B 582     -126.54     43.00
REMARK 500    THR B 631     -116.89   -123.17
REMARK 500    TYR B 680       73.56     73.74
REMARK 500    LYS B 705     -159.88   -120.13
REMARK 500    ASN B 708       72.32     65.30
REMARK 500    LEU B 725      -63.93   -105.40
REMARK 500    GLN B 731      116.53   -164.12
REMARK 500    ALA B 736     -111.83   -129.29
REMARK 500    ASN B 745      -41.95   -139.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A1777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B1777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A1778
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1779
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1778
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A1780
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B1779
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B1780
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A1781
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YA7   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4
REMARK 900  ) IN COMPLEX WITH ZANAMIVIR
REMARK 900 RELATED ID: 2YA4   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4
REMARK 900  )
REMARK 900 RELATED ID: 2YA8   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4
REMARK 900  ) IN COMPLEX WITH OSELTAMIVIR CARBOXYLATE
REMARK 900 RELATED ID: 2YA5   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4
REMARK 900  ) IN COMPLEX WITH SIALIC ACID
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 HYPOTHETICAL PROTEIN SPNET_02001817 STREPTOCOCCUS
REMARK 999 PNEUMONIAE TIGR4. APPARENT CONFLICTS ARE DUE TO CURRENT
REMARK 999 UNIPROT MAPPING. SEQUENCE REFERENCE: UNIREF100_UPI00005582E2.
DBREF  2YA6 A  303   777  UNP    B2DJD9   B2DJD9_STRPN   280    754
DBREF  2YA6 B  303   777  UNP    B2DJD9   B2DJD9_STRPN   280    754
SEQADV 2YA6 ALA A  285  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS A  286  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS A  287  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS A  288  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS A  289  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS A  290  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS A  291  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 SER A  292  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 SER A  293  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 GLY A  294  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 LEU A  295  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 GLU A  296  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 VAL A  297  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 LEU A  298  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 PHE A  299  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 GLN A  300  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 GLY A  301  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 PRO A  302  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 LYS A  440  UNP  B2DJD9    GLU   417 SEE REMARK 999
SEQADV 2YA6 ASP A  584  UNP  B2DJD9    ASN   561 SEE REMARK 999
SEQADV 2YA6 ALA B  285  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS B  286  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS B  287  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS B  288  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS B  289  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS B  290  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 HIS B  291  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 SER B  292  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 SER B  293  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 GLY B  294  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 LEU B  295  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 GLU B  296  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 VAL B  297  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 LEU B  298  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 PHE B  299  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 GLN B  300  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 GLY B  301  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 PRO B  302  UNP  B2DJD9              EXPRESSION TAG
SEQADV 2YA6 LYS B  440  UNP  B2DJD9    GLU   417 SEE REMARK 999
SEQADV 2YA6 ASP B  584  UNP  B2DJD9    ASN   561 SEE REMARK 999
SEQRES   1 A  493  ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL
SEQRES   2 A  493  LEU PHE GLN GLY PRO PRO GLU GLY ALA ALA LEU THR GLU
SEQRES   3 A  493  LYS THR ASP ILE PHE GLU SER GLY ARG ASN GLY ASN PRO
SEQRES   4 A  493  ASN LYS ASP GLY ILE LYS SER TYR ARG ILE PRO ALA LEU
SEQRES   5 A  493  LEU LYS THR ASP LYS GLY THR LEU ILE ALA GLY ALA ASP
SEQRES   6 A  493  GLU ARG ARG LEU HIS SER SER ASP TRP GLY ASP ILE GLY
SEQRES   7 A  493  MET VAL ILE ARG ARG SER GLU ASP ASN GLY LYS THR TRP
SEQRES   8 A  493  GLY ASP ARG VAL THR ILE THR ASN LEU ARG ASP ASN PRO
SEQRES   9 A  493  LYS ALA SER ASP PRO SER ILE GLY SER PRO VAL ASN ILE
SEQRES  10 A  493  ASP MET VAL LEU VAL GLN ASP PRO GLU THR LYS ARG ILE
SEQRES  11 A  493  PHE SER ILE TYR ASP MET PHE PRO GLU GLY LYS GLY ILE
SEQRES  12 A  493  PHE GLY MET SER SER GLN LYS GLU GLU ALA TYR LYS LYS
SEQRES  13 A  493  ILE ASP GLY LYS THR TYR GLN ILE LEU TYR ARG GLU GLY
SEQRES  14 A  493  GLU LYS GLY ALA TYR THR ILE ARG GLU ASN GLY THR VAL
SEQRES  15 A  493  TYR THR PRO ASP GLY LYS ALA THR ASP TYR ARG VAL VAL
SEQRES  16 A  493  VAL ASP PRO VAL LYS PRO ALA TYR SER ASP LYS GLY ASP
SEQRES  17 A  493  LEU TYR LYS GLY ASP GLN LEU LEU GLY ASN ILE TYR PHE
SEQRES  18 A  493  THR THR ASN LYS THR SER PRO PHE ARG ILE ALA LYS ASP
SEQRES  19 A  493  SER TYR LEU TRP MET SER TYR SER ASP ASP ASP GLY LYS
SEQRES  20 A  493  THR TRP SER ALA PRO GLN ASP ILE THR PRO MET VAL LYS
SEQRES  21 A  493  ALA ASP TRP MET LYS PHE LEU GLY VAL GLY PRO GLY THR
SEQRES  22 A  493  GLY ILE VAL LEU ARG ASN GLY PRO HIS LYS GLY ARG ILE
SEQRES  23 A  493  LEU ILE PRO VAL TYR THR THR ASN ASN VAL SER HIS LEU
SEQRES  24 A  493  ASP GLY SER GLN SER SER ARG VAL ILE TYR SER ASP ASP
SEQRES  25 A  493  HIS GLY LYS THR TRP HIS ALA GLY GLU ALA VAL ASN ASP
SEQRES  26 A  493  ASN ARG GLN VAL ASP GLY GLN LYS ILE HIS SER SER THR
SEQRES  27 A  493  MET ASN ASN ARG ARG ALA GLN ASN THR GLU SER THR VAL
SEQRES  28 A  493  VAL GLN LEU ASN ASN GLY ASP VAL LYS LEU PHE MET ARG
SEQRES  29 A  493  GLY LEU THR GLY ASP LEU GLN VAL ALA THR SER LYS ASP
SEQRES  30 A  493  GLY GLY VAL THR TRP GLU LYS ASP ILE LYS ARG TYR PRO
SEQRES  31 A  493  GLN VAL LYS ASP VAL TYR VAL GLN MET SER ALA ILE HIS
SEQRES  32 A  493  THR MET HIS GLU GLY LYS GLU TYR ILE ILE LEU SER ASN
SEQRES  33 A  493  ALA GLY GLY PRO LYS ARG GLU ASN GLY MET VAL HIS LEU
SEQRES  34 A  493  ALA ARG VAL GLU GLU ASN GLY GLU LEU THR TRP LEU LYS
SEQRES  35 A  493  HIS ASN PRO ILE GLN LYS GLY GLU PHE ALA TYR ASN SER
SEQRES  36 A  493  LEU GLN GLU LEU GLY ASN GLY GLU TYR GLY ILE LEU TYR
SEQRES  37 A  493  GLU HIS THR GLU LYS GLY GLN ASN ALA TYR THR LEU SER
SEQRES  38 A  493  PHE ARG LYS PHE ASN TRP GLU PHE LEU SER LYS ASN
SEQRES   1 B  493  ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL
SEQRES   2 B  493  LEU PHE GLN GLY PRO PRO GLU GLY ALA ALA LEU THR GLU
SEQRES   3 B  493  LYS THR ASP ILE PHE GLU SER GLY ARG ASN GLY ASN PRO
SEQRES   4 B  493  ASN LYS ASP GLY ILE LYS SER TYR ARG ILE PRO ALA LEU
SEQRES   5 B  493  LEU LYS THR ASP LYS GLY THR LEU ILE ALA GLY ALA ASP
SEQRES   6 B  493  GLU ARG ARG LEU HIS SER SER ASP TRP GLY ASP ILE GLY
SEQRES   7 B  493  MET VAL ILE ARG ARG SER GLU ASP ASN GLY LYS THR TRP
SEQRES   8 B  493  GLY ASP ARG VAL THR ILE THR ASN LEU ARG ASP ASN PRO
SEQRES   9 B  493  LYS ALA SER ASP PRO SER ILE GLY SER PRO VAL ASN ILE
SEQRES  10 B  493  ASP MET VAL LEU VAL GLN ASP PRO GLU THR LYS ARG ILE
SEQRES  11 B  493  PHE SER ILE TYR ASP MET PHE PRO GLU GLY LYS GLY ILE
SEQRES  12 B  493  PHE GLY MET SER SER GLN LYS GLU GLU ALA TYR LYS LYS
SEQRES  13 B  493  ILE ASP GLY LYS THR TYR GLN ILE LEU TYR ARG GLU GLY
SEQRES  14 B  493  GLU LYS GLY ALA TYR THR ILE ARG GLU ASN GLY THR VAL
SEQRES  15 B  493  TYR THR PRO ASP GLY LYS ALA THR ASP TYR ARG VAL VAL
SEQRES  16 B  493  VAL ASP PRO VAL LYS PRO ALA TYR SER ASP LYS GLY ASP
SEQRES  17 B  493  LEU TYR LYS GLY ASP GLN LEU LEU GLY ASN ILE TYR PHE
SEQRES  18 B  493  THR THR ASN LYS THR SER PRO PHE ARG ILE ALA LYS ASP
SEQRES  19 B  493  SER TYR LEU TRP MET SER TYR SER ASP ASP ASP GLY LYS
SEQRES  20 B  493  THR TRP SER ALA PRO GLN ASP ILE THR PRO MET VAL LYS
SEQRES  21 B  493  ALA ASP TRP MET LYS PHE LEU GLY VAL GLY PRO GLY THR
SEQRES  22 B  493  GLY ILE VAL LEU ARG ASN GLY PRO HIS LYS GLY ARG ILE
SEQRES  23 B  493  LEU ILE PRO VAL TYR THR THR ASN ASN VAL SER HIS LEU
SEQRES  24 B  493  ASP GLY SER GLN SER SER ARG VAL ILE TYR SER ASP ASP
SEQRES  25 B  493  HIS GLY LYS THR TRP HIS ALA GLY GLU ALA VAL ASN ASP
SEQRES  26 B  493  ASN ARG GLN VAL ASP GLY GLN LYS ILE HIS SER SER THR
SEQRES  27 B  493  MET ASN ASN ARG ARG ALA GLN ASN THR GLU SER THR VAL
SEQRES  28 B  493  VAL GLN LEU ASN ASN GLY ASP VAL LYS LEU PHE MET ARG
SEQRES  29 B  493  GLY LEU THR GLY ASP LEU GLN VAL ALA THR SER LYS ASP
SEQRES  30 B  493  GLY GLY VAL THR TRP GLU LYS ASP ILE LYS ARG TYR PRO
SEQRES  31 B  493  GLN VAL LYS ASP VAL TYR VAL GLN MET SER ALA ILE HIS
SEQRES  32 B  493  THR MET HIS GLU GLY LYS GLU TYR ILE ILE LEU SER ASN
SEQRES  33 B  493  ALA GLY GLY PRO LYS ARG GLU ASN GLY MET VAL HIS LEU
SEQRES  34 B  493  ALA ARG VAL GLU GLU ASN GLY GLU LEU THR TRP LEU LYS
SEQRES  35 B  493  HIS ASN PRO ILE GLN LYS GLY GLU PHE ALA TYR ASN SER
SEQRES  36 B  493  LEU GLN GLU LEU GLY ASN GLY GLU TYR GLY ILE LEU TYR
SEQRES  37 B  493  GLU HIS THR GLU LYS GLY GLN ASN ALA TYR THR LEU SER
SEQRES  38 B  493  PHE ARG LYS PHE ASN TRP GLU PHE LEU SER LYS ASN
HET    DAN  A1777      20
HET    DAN  B1777      20
HET    FMT  A1778       3
HET     CL  A1779       1
HET     CL  B1778       1
HET    FMT  A1780       3
HET    FMT  B1779       3
HET    FMT  B1780       3
HET    FMT  A1781       3
HETNAM      CL CHLORIDE ION
HETNAM     FMT FORMIC ACID
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL   3   CL    2(CL 1-)
FORMUL   4  FMT    5(C H2 O2)
FORMUL   5  DAN    2(C11 H17 N O8)
FORMUL   6  HOH   *583(H2 O)
HELIX    1   1 ASP A  392  GLY A  396  5                                   5
HELIX    2   2 LYS A  425  MET A  430  5                                   6
HELIX    3   3 LYS A  484  SER A  488  5                                   5
HELIX    4   4 ILE A  539  LYS A  544  1                                   6
HELIX    5   5 SER A  581  SER A  586  1                                   6
HELIX    6   6 ASN A  625  GLN A  629  5                                   5
HELIX    7   7 TRP A  771  LYS A  776  1                                   6
HELIX    8   8 ASP B  392  GLY B  396  5                                   5
HELIX    9   9 LYS B  425  GLY B  429  5                                   5
HELIX   10  10 LYS B  484  SER B  488  5                                   5
HELIX   11  11 ILE B  539  LYS B  544  1                                   6
HELIX   12  12 SER B  581  SER B  586  1                                   6
HELIX   13  13 ASN B  625  GLN B  629  5                                   5
HELIX   14  14 TRP B  771  LYS B  776  1                                   6
SHEET    1  AA 4 THR A 312  PHE A 315  0
SHEET    2  AA 4 THR A 763  ASN A 770 -1  O  LEU A 764   N  ILE A 314
SHEET    3  AA 4 GLU A 747  HIS A 754 -1  O  TYR A 748   N  PHE A 769
SHEET    4  AA 4 ASN A 738  GLY A 744 -1  O  SER A 739   N  LEU A 751
SHEET    1  AB 4 SER A 330  LYS A 338  0
SHEET    2  AB 4 LEU A 344  ARG A 351 -1  O  ILE A 345   N  LEU A 337
SHEET    3  AB 4 ILE A 361  SER A 368 -1  O  GLY A 362   N  GLU A 350
SHEET    4  AB 4 VAL A 379  THR A 382 -1  O  VAL A 379   N  ILE A 365
SHEET    1  AC 5 GLN A 537  ASP A 538  0
SHEET    2  AC 5 TYR A 520  SER A 526 -1  O  MET A 523   N  GLN A 537
SHEET    3  AC 5 ILE A 414  PHE A 421 -1  O  ILE A 414   N  SER A 526
SHEET    4  AC 5 VAL A 399  GLN A 407 -1  O  VAL A 399   N  PHE A 421
SHEET    5  AC 5 GLY A 556  THR A 557  1  O  GLY A 556   N  LEU A 405
SHEET    1  AD 2 TYR A 438  ILE A 441  0
SHEET    2  AD 2 LYS A 444  ARG A 451 -1  O  LYS A 444   N  ILE A 441
SHEET    1  AE 7 GLN A 498  ASN A 502  0
SHEET    2  AE 7 ASP A 492  LYS A 495 -1  O  LEU A 493   N  LEU A 500
SHEET    3  AE 7 ALA A 473  VAL A 478 -1  O  ARG A 477   N  TYR A 494
SHEET    4  AE 7 THR A 465  TYR A 467 -1  O  VAL A 466   N  THR A 474
SHEET    5  AE 7 TYR A 458  ILE A 460 -1  O  THR A 459   N  TYR A 467
SHEET    6  AE 7 LYS A 444  ARG A 451 -1  O  GLN A 447   N  ILE A 460
SHEET    7  AE 7 PHE A 513  ILE A 515  1  O  ARG A 514   N  TYR A 450
SHEET    1  AF 7 GLN A 498  ASN A 502  0
SHEET    2  AF 7 ASP A 492  LYS A 495 -1  O  LEU A 493   N  LEU A 500
SHEET    3  AF 7 ALA A 473  VAL A 478 -1  O  ARG A 477   N  TYR A 494
SHEET    4  AF 7 THR A 465  TYR A 467 -1  O  VAL A 466   N  THR A 474
SHEET    5  AF 7 TYR A 458  ILE A 460 -1  O  THR A 459   N  TYR A 467
SHEET    6  AF 7 LYS A 444  ARG A 451 -1  O  GLN A 447   N  ILE A 460
SHEET    7  AF 7 TYR A 438  ILE A 441 -1  O  LYS A 439   N  TYR A 446
SHEET    1  AG 2 PHE A 513  ILE A 515  0
SHEET    2  AG 2 LYS A 444  ARG A 451  1  O  TYR A 450   N  ARG A 514
SHEET    1  AH 2 MET A 548  VAL A 553  0
SHEET    2  AH 2 ILE A 570  ASN A 578 -1  O  TYR A 575   N  GLY A 552
SHEET    1  AI 2 ILE A 559  VAL A 560  0
SHEET    2  AI 2 ILE A 570  ASN A 578  1  O  LEU A 571   N  ILE A 559
SHEET    1  AJ 4 HIS A 602  ALA A 603  0
SHEET    2  AJ 4 SER A 588  SER A 594 -1  O  TYR A 593   N  HIS A 602
SHEET    3  AJ 4 ILE A 570  ASN A 578 -1  O  ILE A 570   N  SER A 594
SHEET    4  AJ 4 ILE A 559  VAL A 560  1  O  ILE A 559   N  LEU A 571
SHEET    1  AK 4 HIS A 602  ALA A 603  0
SHEET    2  AK 4 SER A 588  SER A 594 -1  O  TYR A 593   N  HIS A 602
SHEET    3  AK 4 ILE A 570  ASN A 578 -1  O  ILE A 570   N  SER A 594
SHEET    4  AK 4 MET A 548  VAL A 553 -1  N  LYS A 549   O  THR A 577
SHEET    1  AL 2 ARG A 611  VAL A 613  0
SHEET    2  AL 2 GLN A 616  ILE A 618 -1  O  GLN A 616   N  VAL A 613
SHEET    1  AM 4 SER A 633  GLN A 637  0
SHEET    2  AM 4 VAL A 643  MET A 647 -1  O  LYS A 644   N  VAL A 636
SHEET    3  AM 4 ASP A 653  SER A 659 -1  O  GLN A 655   N  MET A 647
SHEET    4  AM 4 LYS A 671  LYS A 677 -1  O  LYS A 671   N  VAL A 656
SHEET    1  AN 4 SER A 684  HIS A 690  0
SHEET    2  AN 4 LYS A 693  ALA A 701 -1  O  LYS A 693   N  HIS A 690
SHEET    3  AN 4 GLU A 707  VAL A 716 -1  O  MET A 710   N  ASN A 700
SHEET    4  AN 4 LEU A 722  GLU A 734 -1  O  THR A 723   N  ARG A 715
SHEET    1  BA 4 THR B 312  PHE B 315  0
SHEET    2  BA 4 THR B 763  ASN B 770 -1  O  LEU B 764   N  ILE B 314
SHEET    3  BA 4 GLU B 747  HIS B 754 -1  O  TYR B 748   N  PHE B 769
SHEET    4  BA 4 ASN B 738  GLU B 742 -1  O  SER B 739   N  LEU B 751
SHEET    1  BB 4 SER B 330  LYS B 338  0
SHEET    2  BB 4 LEU B 344  ARG B 351 -1  O  ILE B 345   N  LEU B 337
SHEET    3  BB 4 ILE B 361  SER B 368 -1  O  GLY B 362   N  GLU B 350
SHEET    4  BB 4 VAL B 379  THR B 382 -1  O  VAL B 379   N  ILE B 365
SHEET    1  BC 5 GLN B 537  ASP B 538  0
SHEET    2  BC 5 TYR B 520  SER B 526 -1  O  MET B 523   N  GLN B 537
SHEET    3  BC 5 ILE B 414  PHE B 421 -1  O  ILE B 414   N  SER B 526
SHEET    4  BC 5 VAL B 399  GLN B 407 -1  O  VAL B 399   N  PHE B 421
SHEET    5  BC 5 GLY B 556  THR B 557  1  O  GLY B 556   N  LEU B 405
SHEET    1  BD 2 TYR B 438  ILE B 441  0
SHEET    2  BD 2 LYS B 444  ARG B 451 -1  O  LYS B 444   N  ILE B 441
SHEET    1  BE 7 GLN B 498  ASN B 502  0
SHEET    2  BE 7 ASP B 492  LYS B 495 -1  O  LEU B 493   N  LEU B 500
SHEET    3  BE 7 ALA B 473  VAL B 478 -1  O  ARG B 477   N  TYR B 494
SHEET    4  BE 7 THR B 465  TYR B 467 -1  O  VAL B 466   N  THR B 474
SHEET    5  BE 7 ALA B 457  ILE B 460 -1  O  THR B 459   N  TYR B 467
SHEET    6  BE 7 LYS B 444  ARG B 451 -1  O  GLN B 447   N  ILE B 460
SHEET    7  BE 7 PHE B 513  ARG B 514  1  O  ARG B 514   N  TYR B 450
SHEET    1  BF 7 GLN B 498  ASN B 502  0
SHEET    2  BF 7 ASP B 492  LYS B 495 -1  O  LEU B 493   N  LEU B 500
SHEET    3  BF 7 ALA B 473  VAL B 478 -1  O  ARG B 477   N  TYR B 494
SHEET    4  BF 7 THR B 465  TYR B 467 -1  O  VAL B 466   N  THR B 474
SHEET    5  BF 7 ALA B 457  ILE B 460 -1  O  THR B 459   N  TYR B 467
SHEET    6  BF 7 LYS B 444  ARG B 451 -1  O  GLN B 447   N  ILE B 460
SHEET    7  BF 7 TYR B 438  ILE B 441 -1  O  LYS B 439   N  TYR B 446
SHEET    1  BG 2 PHE B 513  ARG B 514  0
SHEET    2  BG 2 LYS B 444  ARG B 451  1  O  TYR B 450   N  ARG B 514
SHEET    1  BH 2 LEU B 551  VAL B 553  0
SHEET    2  BH 2 ILE B 570  THR B 576 -1  O  TYR B 575   N  GLY B 552
SHEET    1  BI 2 ILE B 559  VAL B 560  0
SHEET    2  BI 2 ILE B 570  THR B 576  1  O  LEU B 571   N  ILE B 559
SHEET    1  BJ 4 HIS B 602  ALA B 603  0
SHEET    2  BJ 4 SER B 588  SER B 594 -1  O  TYR B 593   N  HIS B 602
SHEET    3  BJ 4 ILE B 570  THR B 576 -1  O  ILE B 570   N  SER B 594
SHEET    4  BJ 4 ILE B 559  VAL B 560  1  O  ILE B 559   N  LEU B 571
SHEET    1  BK 4 HIS B 602  ALA B 603  0
SHEET    2  BK 4 SER B 588  SER B 594 -1  O  TYR B 593   N  HIS B 602
SHEET    3  BK 4 ILE B 570  THR B 576 -1  O  ILE B 570   N  SER B 594
SHEET    4  BK 4 LEU B 551  VAL B 553 -1  O  GLY B 552   N  TYR B 575
SHEET    1  BL 2 ARG B 611  VAL B 613  0
SHEET    2  BL 2 GLN B 616  ILE B 618 -1  O  GLN B 616   N  VAL B 613
SHEET    1  BM 4 SER B 633  GLN B 637  0
SHEET    2  BM 4 VAL B 643  MET B 647 -1  O  LYS B 644   N  VAL B 636
SHEET    3  BM 4 ASP B 653  SER B 659 -1  O  GLN B 655   N  MET B 647
SHEET    4  BM 4 LYS B 671  LYS B 677 -1  O  LYS B 671   N  VAL B 656
SHEET    1  BN 4 SER B 684  HIS B 690  0
SHEET    2  BN 4 LYS B 693  ALA B 701 -1  O  LYS B 693   N  HIS B 690
SHEET    3  BN 4 GLU B 707  VAL B 716 -1  O  MET B 710   N  ASN B 700
SHEET    4  BN 4 LEU B 722  GLU B 734 -1  O  THR B 723   N  ARG B 715
CISPEP   1 GLU A  691    GLY A  692          0       -28.28
CISPEP   2 GLY A  703    PRO A  704          0         2.14
CISPEP   3 ALA A  761    TYR A  762          0        -6.26
CISPEP   4 GLY B  703    PRO B  704          0         3.21
CISPEP   5 ALA B  761    TYR B  762          0        -8.81
SITE     1 AC1 19 ARG A 332  ILE A 333  ARG A 351  ASP A 357
SITE     2 AC1 19 ILE A 401  ASP A 402  ASP A 419  ILE A 427
SITE     3 AC1 19 PHE A 428  TYR A 575  LEU A 583  GLN A 587
SITE     4 AC1 19 ARG A 648  ARG A 706  TYR A 737  HOH A2295
SITE     5 AC1 19 HOH A2296  HOH A2297  HOH A2298
SITE     1 AC2 16 ARG B 332  ILE B 333  ARG B 351  ASP B 357
SITE     2 AC2 16 ASP B 402  ASP B 419  ILE B 427  PHE B 428
SITE     3 AC2 16 TYR B 575  GLN B 587  ARG B 648  ARG B 706
SITE     4 AC2 16 TYR B 737  HOH B2282  HOH B2283  HOH B2284
SITE     1 AC3  4 SER A 526  ASP A 527  ASP A 528  THR A 532
SITE     1 AC4  4 ASN A 502  LYS A 509  THR A 510  SER A 511
SITE     1 AC5  5 GLY B 501  ASN B 502  LYS B 509  THR B 510
SITE     2 AC5  5 SER B 511
SITE     1 AC6  4 PRO A 541  LYS A 544  ALA A 545  HOH A2168
SITE     1 AC7  7 TYR B 525  SER B 526  ASP B 527  ASP B 528
SITE     2 AC7  7 THR B 532  SER B 534  HOH B2285
SITE     1 AC8  5 HIS B 566  ARG B 569  GLU B 717  ASN B 719
SITE     2 AC8  5 HOH B2190
SITE     1 AC9  3 GLN A 741  HOH A2286  HOH A2300
CRYST1  164.857   48.835  125.383  90.00 104.13  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      0.006066  0.000000  0.001527        0.00000
SCALE2      0.000000  0.020477  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008224        0.00000
MTRIX1   1 -0.829500 -0.476500  0.291400       48.74000    1
MTRIX2   1 -0.475900  0.329900 -0.815300       34.22000    1
MTRIX3   1  0.292300 -0.814900 -0.500400       27.38000    1
      
PROCHECK
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