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PDBsum entry 4nc5

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Hydrolase PDB id
4nc5
Jmol
Contents
Protein chain
354 a.a.
Ligands
FSI
PO4 ×2
Waters ×103
HEADER    HYDROLASE                               24-OCT-13   4NC5
TITLE     HUMAN SIALIDASE 2 IN COMPLEX WITH 2,3-DIFLUOROSIALIC ACID (COVALENT
TITLE    2 INTERMEDIATE)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE-2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: NEU2, CYTOSOLIC SIALIDASE, N-ACETYL-ALPHA-NEURAMINIDASE 2;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: NEU2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS    HUMAN NEURAMINIDASE, SIALIDASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.BUCHINI,F.-X.GALLAT,I.R.GREIG,J.-H.KIM,S.WAKATSUKI,L.M.G.CHAVAS,
AUTHOR   2 S.G.WITHERS
REVDAT   2   02-APR-14 4NC5    1       JRNL
REVDAT   1   06-NOV-13 4NC5    0
JRNL        AUTH   S.BUCHINI,F.X.GALLAT,I.R.GREIG,J.H.KIM,S.WAKATSUKI,
JRNL        AUTH 2 L.M.CHAVAS,S.G.WITHERS
JRNL        TITL   TUNING MECHANISM-BASED INACTIVATORS OF NEURAMINIDASES:
JRNL        TITL 2 MECHANISTIC AND STRUCTURAL INSIGHTS.
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  53  3382 2014
JRNL        REFN                   ISSN 1433-7851
JRNL        PMID   24591206
JRNL        DOI    10.1002/ANIE.201309675
REMARK   2
REMARK   2 RESOLUTION.    2.51 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.7.32
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) : 2.51
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.20
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8
REMARK   3   NUMBER OF REFLECTIONS             : 11706
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) : 0.178
REMARK   3   R VALUE            (WORKING SET) : 0.174
REMARK   3   FREE R VALUE                     : 0.263
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 597
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) : 2.51
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.58
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 791
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.42
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300
REMARK   3   BIN FREE R VALUE SET COUNT          : 40
REMARK   3   BIN FREE R VALUE                    : 0.3470
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2785
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 31
REMARK   3   SOLVENT ATOMS            : 103
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.56
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.58000
REMARK   3    B22 (A**2) : 0.81000
REMARK   3    B33 (A**2) : -1.39000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.338
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.247
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.023
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2913 ; 0.012 ; 0.019
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3979 ; 1.722 ; 1.959
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   355 ; 8.069 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   139 ;37.023 ;23.165
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   433 ;18.281 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;18.874 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   431 ; 0.096 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2279 ; 0.009 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  1422 ; 2.565 ; 3.568
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1773 ; 4.120 ; 5.324
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1491 ; 3.203 ; 3.878
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4431 ; 8.201 ;30.482
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL
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 : 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: NULL
REMARK   4
REMARK   4 4NC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB083016.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : AR-NW12A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11706
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.513
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.200
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.51
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.4
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1VCU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM/POTASSIUM PHOSPHATE BUFFER, PH
REMARK 280  8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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       46.19700
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.19700
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.70400
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.95800
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.70400
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.95800
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       46.19700
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.70400
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       43.95800
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       46.19700
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.70400
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       43.95800
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 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     GLY A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     ALA A     2
REMARK 465     SER A    43
REMARK 465     LYS A    44
REMARK 465     LYS A    45
REMARK 465     ALA A    46
REMARK 465     GLU A    47
REMARK 465     HIS A    48
REMARK 465     THR A   110
REMARK 465     GLU A   111
REMARK 465     GLN A   112
REMARK 465     GLN A   113
REMARK 465     GLN A   114
REMARK 465     LEU A   115
REMARK 465     GLN A   116
REMARK 465     THR A   117
REMARK 465     GLY A   227
REMARK 465     GLU A   228
REMARK 465     SER A   284
REMARK 465     GLY A   285
REMARK 465     PRO A   286
REMARK 465     GLY A   287
REMARK 465     SER A   288
REMARK 465     PRO A   289
REMARK 465     PRO A   379
REMARK 465     GLN A   380
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LEU A 378    O
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   OD2  ASP A   144     OE2  GLU A   376     6555     2.10
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    CYS A 164   CA  -  CB  -  SG  ANGL. DEV. =   7.6 DEGREES
REMARK 500    PRO A 268   C   -  N   -  CA  ANGL. DEV. =  11.4 DEGREES
REMARK 500    PRO A 269   C   -  N   -  CD  ANGL. DEV. = -13.1 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    LEU A   4      146.49    -38.79
REMARK 500    ILE A  22       76.02     71.73
REMARK 500    GLN A  32       32.67     39.92
REMARK 500    GLU A  50     -102.15     20.15
REMARK 500    GLN A 108       26.64    -61.38
REMARK 500    TYR A 151      -37.31    -37.55
REMARK 500    CYS A 164     -165.60   -106.40
REMARK 500    ASN A 168       30.76    -99.44
REMARK 500    ALA A 213      153.24    174.21
REMARK 500    LEU A 217     -133.74   -119.16
REMARK 500    PHE A 255       69.74   -106.83
REMARK 500    PRO A 268     -178.51    -39.17
REMARK 500    PRO A 269      -82.61     22.33
REMARK 500    GLN A 270       43.05   -151.19
REMARK 500    HIS A 297      149.25   -177.37
REMARK 500    ASP A 306       71.68     72.68
REMARK 500    ALA A 317      117.42    -39.42
REMARK 500    ALA A 333     -119.37   -132.12
REMARK 500    TYR A 359       19.60     59.17
REMARK 500    TYR A 377     -162.97     55.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 PRO A  268     PRO A  269                 -123.81
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 FSI A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A75   RELATED DB: PDB
REMARK 900 TRYPANOSOMA RANGELI SIALIDASE IN COMPLEX WITH 2,3-
REMARK 900 DIFLUOROSIALIC ACID (COVALENT INTERMEDIATE)
REMARK 900 RELATED ID: 2AH2   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRYPANOSOMA CRUZI TRANS-SIALIDASE IN
REMARK 900 COMPLEX WITH 2,3-DIFLUOROSIALIC ACID (COVALENT INTERMEDIATE)
DBREF  4NC5 A    1   380  UNP    Q9Y3R4   NEUR2_HUMAN      1    380
SEQADV 4NC5 GLY A   -1  UNP  Q9Y3R4              EXPRESSION TAG
SEQADV 4NC5 SER A    0  UNP  Q9Y3R4              EXPRESSION TAG
SEQADV 4NC5 ALA A   46  UNP  Q9Y3R4    ASP    46 ENGINEERED MUTATION
SEQADV 4NC5 ASN A  168  UNP  Q9Y3R4    HIS   168 ENGINEERED MUTATION
SEQRES   1 A  382  GLY SER MET ALA SER LEU PRO VAL LEU GLN LYS GLU SER
SEQRES   2 A  382  VAL PHE GLN SER GLY ALA HIS ALA TYR ARG ILE PRO ALA
SEQRES   3 A  382  LEU LEU TYR LEU PRO GLY GLN GLN SER LEU LEU ALA PHE
SEQRES   4 A  382  ALA GLU GLN ARG ALA SER LYS LYS ALA GLU HIS ALA GLU
SEQRES   5 A  382  LEU ILE VAL LEU ARG ARG GLY ASP TYR ASP ALA PRO THR
SEQRES   6 A  382  HIS GLN VAL GLN TRP GLN ALA GLN GLU VAL VAL ALA GLN
SEQRES   7 A  382  ALA ARG LEU ASP GLY HIS ARG SER MET ASN PRO CYS PRO
SEQRES   8 A  382  LEU TYR ASP ALA GLN THR GLY THR LEU PHE LEU PHE PHE
SEQRES   9 A  382  ILE ALA ILE PRO GLY GLN VAL THR GLU GLN GLN GLN LEU
SEQRES  10 A  382  GLN THR ARG ALA ASN VAL THR ARG LEU CYS GLN VAL THR
SEQRES  11 A  382  SER THR ASP HIS GLY ARG THR TRP SER SER PRO ARG ASP
SEQRES  12 A  382  LEU THR ASP ALA ALA ILE GLY PRO ALA TYR ARG GLU TRP
SEQRES  13 A  382  SER THR PHE ALA VAL GLY PRO GLY HIS CYS LEU GLN LEU
SEQRES  14 A  382  ASN ASP ARG ALA ARG SER LEU VAL VAL PRO ALA TYR ALA
SEQRES  15 A  382  TYR ARG LYS LEU HIS PRO ILE GLN ARG PRO ILE PRO SER
SEQRES  16 A  382  ALA PHE CYS PHE LEU SER HIS ASP HIS GLY ARG THR TRP
SEQRES  17 A  382  ALA ARG GLY HIS PHE VAL ALA GLN ASP THR LEU GLU CYS
SEQRES  18 A  382  GLN VAL ALA GLU VAL GLU THR GLY GLU GLN ARG VAL VAL
SEQRES  19 A  382  THR LEU ASN ALA ARG SER HIS LEU ARG ALA ARG VAL GLN
SEQRES  20 A  382  ALA GLN SER THR ASN ASP GLY LEU ASP PHE GLN GLU SER
SEQRES  21 A  382  GLN LEU VAL LYS LYS LEU VAL GLU PRO PRO PRO GLN GLY
SEQRES  22 A  382  CYS GLN GLY SER VAL ILE SER PHE PRO SER PRO ARG SER
SEQRES  23 A  382  GLY PRO GLY SER PRO ALA GLN TRP LEU LEU TYR THR HIS
SEQRES  24 A  382  PRO THR HIS SER TRP GLN ARG ALA ASP LEU GLY ALA TYR
SEQRES  25 A  382  LEU ASN PRO ARG PRO PRO ALA PRO GLU ALA TRP SER GLU
SEQRES  26 A  382  PRO VAL LEU LEU ALA LYS GLY SER CYS ALA TYR SER ASP
SEQRES  27 A  382  LEU GLN SER MET GLY THR GLY PRO ASP GLY SER PRO LEU
SEQRES  28 A  382  PHE GLY CYS LEU TYR GLU ALA ASN ASP TYR GLU GLU ILE
SEQRES  29 A  382  VAL PHE LEU MET PHE THR LEU LYS GLN ALA PHE PRO ALA
SEQRES  30 A  382  GLU TYR LEU PRO GLN
HET    FSI  A 401      21
HET    PO4  A 402       5
HET    PO4  A 403       5
HETNAM     FSI 5-(ACETYLAMINO)-3,5-DIDEOXY-3-FLUORO-D-ERYTHRO-ALPHA-L-
HETNAM   2 FSI  MANNO-NON-2-ULOPYRANOSONIC ACID
HETNAM     PO4 PHOSPHATE ION
HETSYN     FSI 3-FLUOROSIALIC ACID
FORMUL   2  FSI    C11 H18 F N O9
FORMUL   3  PO4    2(O4 P 3-)
FORMUL   5  HOH   *103(H2 O)
HELIX    1   1 PRO A   29  GLN A   31  5                                   3
HELIX    2   2 ALA A   61  HIS A   64  5                                   4
HELIX    3   3 LEU A  142  GLY A  148  1                                   7
HELIX    4   4 PRO A  149  ARG A  152  5                                   4
HELIX    5   5 ALA A  317  TRP A  321  5                                   5
HELIX    6   6 LEU A  369  PHE A  373  1                                   5
HELIX    7   7 PRO A  374  TYR A  377  5                                   4
SHEET    1   A 7 GLN A   8  GLN A  14  0
SHEET    2   A 7 GLU A 361  THR A 368 -1  O  PHE A 364   N  GLU A  10
SHEET    3   A 7 PRO A 348  ALA A 356 -1  N  CYS A 352   O  LEU A 365
SHEET    4   A 7 VAL A 325  THR A 342 -1  N  GLY A 341   O  LEU A 349
SHEET    5   A 7 ALA A 305  ASN A 312 -1  N  ASP A 306   O  GLY A 330
SHEET    6   A 7 GLN A 291  PRO A 298 -1  N  LEU A 293   O  ASN A 312
SHEET    7   A 7 SER A 275  PRO A 280 -1  N  ILE A 277   O  LEU A 294
SHEET    1   B 4 ALA A  19  LEU A  28  0
SHEET    2   B 4 SER A  33  ARG A  41 -1  O  PHE A  37   N  ALA A  24
SHEET    3   B 4 LEU A  51  ASP A  60 -1  O  ARG A  55   N  ALA A  36
SHEET    4   B 4 GLN A  65  TRP A  68 -1  O  GLN A  65   N  ASP A  60
SHEET    1   C 4 ALA A  19  LEU A  28  0
SHEET    2   C 4 SER A  33  ARG A  41 -1  O  PHE A  37   N  ALA A  24
SHEET    3   C 4 LEU A  51  ASP A  60 -1  O  ARG A  55   N  ALA A  36
SHEET    4   C 4 GLU A  72  VAL A  73 -1  O  GLU A  72   N  LEU A  54
SHEET    1   D 4 HIS A  82  ASP A  92  0
SHEET    2   D 4 THR A  97  PRO A 106 -1  O  ILE A 105   N  ARG A  83
SHEET    3   D 4 ARG A 123  SER A 129 -1  O  ARG A 123   N  ALA A 104
SHEET    4   D 4 ARG A 140  ASP A 141 -1  O  ARG A 140   N  GLN A 126
SHEET    1   E 3 TRP A 154  VAL A 159  0
SHEET    2   E 3 LEU A 174  ARG A 182 -1  O  TYR A 181   N  THR A 156
SHEET    3   E 3 LEU A 165  GLN A 166 -1  N  LEU A 165   O  VAL A 175
SHEET    1   F 4 TRP A 154  VAL A 159  0
SHEET    2   F 4 LEU A 174  ARG A 182 -1  O  TYR A 181   N  THR A 156
SHEET    3   F 4 ILE A 191  SER A 199 -1  O  ILE A 191   N  ARG A 182
SHEET    4   F 4 ALA A 207  ARG A 208 -1  O  ALA A 207   N  LEU A 198
SHEET    1   G 4 THR A 216  VAL A 224  0
SHEET    2   G 4 VAL A 231  SER A 238 -1  O  THR A 233   N  ALA A 222
SHEET    3   G 4 ALA A 242  SER A 248 -1  O  VAL A 244   N  ALA A 236
SHEET    4   G 4 GLU A 257  VAL A 265 -1  O  GLN A 259   N  GLN A 245
SSBOND   1 CYS A   88    CYS A  164                          1555   1555  2.08
LINK         OH  TYR A 334                 C2  FSI A 401     1555   1555  2.12
CISPEP   1 GLY A  160    PRO A  161          0         1.57
CISPEP   2 PRO A  315    PRO A  316          0         0.20
SITE     1 AC1 13 ARG A  21  ILE A  22  ARG A  41  ASN A  86
SITE     2 AC1 13 TYR A 179  TYR A 181  LEU A 217  GLU A 218
SITE     3 AC1 13 ARG A 237  ARG A 304  TYR A 334  HOH A 515
SITE     4 AC1 13 HOH A 585
SITE     1 AC2  5 ALA A  17  HIS A  18  TYR A  20  PRO A 316
SITE     2 AC2  5 ALA A 317
SITE     1 AC3  4 HIS A 210  PHE A 211  HOH A 571  HOH A 582
CRYST1   87.408   87.916   92.394  90.00  90.00  90.00 C 2 2 21      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      0.011441  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011374  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010823        0.00000
      
PROCHECK
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 References