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PDBsum entry 2f25

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2f25
Jmol
Contents
Protein chain
373 a.a.
Ligands
DAN ×2
EPE ×4
Waters ×460
HEADER    HYDROLASE                               15-NOV-05   2F25
TITLE     CRYSTAL STRUCTURE OF THE HUMAN SIALIDASE NEU2 E111Q MUTANT
TITLE    2 IN COMPLEX WITH DANA INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE 2;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: NEU2, CYTOSOLIC SIALIDASE, N-ACETYL-ALPHA-
COMPND   5 NEURAMINIDASE 2;
COMPND   6 EC: 3.2.1.18;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS    SIALIDASE, NEURAMINIDASE, GANGLIOSIDE, DRUG DESIGN,
KEYWDS   2 HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.M.G.CHAVAS,R.KATO,P.FUSI,C.TRINGALI,B.VENERANDO,
AUTHOR   2 G.TETTAMANTI,E.MONTI,S.WAKATSUKI
REVDAT   2   24-FEB-09 2F25    1       VERSN
REVDAT   1   21-NOV-06 2F25    0
JRNL        AUTH   L.M.G.CHAVAS,R.KATO,P.FUSI,C.TRINGALI,B.VENERANDO,
JRNL        AUTH 2 G.TETTAMANTI,E.MONTI,S.WAKATSUKI
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN SIALIDASE NEU2
JRNL        TITL 2 E111Q MUTANT IN COMPLEX WITH DANA INHIBITOR
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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) : 1.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.06
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.6
REMARK   3   NUMBER OF REFLECTIONS             : 60460
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) : 0.192
REMARK   3   FREE R VALUE                     : 0.222
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 3201
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5850
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 100
REMARK   3   SOLVENT ATOMS            : 460
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.31
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.11200
REMARK   3    B22 (A**2) : -4.06000
REMARK   3    B33 (A**2) : 1.94800
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.99100
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 1.405
REMARK   3   BOND ANGLES            (DEGREES) : 0.01
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 67.63
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  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : DANA_HEPES_REP.PARAM
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2F25 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-NOV-05.
REMARK 100 THE RCSB ID CODE IS RCSB035358.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-18B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63661
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.060
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.7
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.07600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.34300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.400
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 1SNT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-METHYL-2,4-PENTANEDIOL, GUANIDINE
REMARK 280  HYDROCHLORIDE, 2-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID, PH
REMARK 280  7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
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       78.68500
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.82000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       78.68500
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       36.82000
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 300 REMARK: THE BIOLOGICAL UNIT IS A MONOMER. THERE ARE 2 BIOLOGICAL
REMARK 300 UNITS IN THE ASYMMETRIC UNIT (CHAIN A AND CHAIN B)
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH B1196  LIES ON A SPECIAL POSITION.
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     SER A   284
REMARK 465     GLY A   285
REMARK 465     PRO A   286
REMARK 465     GLY A   287
REMARK 465     LEU A   378
REMARK 465     PRO A   379
REMARK 465     GLN A   380
REMARK 465     GLY B    -1
REMARK 465     SER B     0
REMARK 465     THR B   226
REMARK 465     GLY B   227
REMARK 465     GLU B   228
REMARK 465     SER B   284
REMARK 465     GLY B   285
REMARK 465     PRO B   286
REMARK 465     GLY B   287
REMARK 465     LEU B   378
REMARK 465     PRO B   379
REMARK 465     GLN B   380
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  22       72.74     61.03
REMARK 500    GLU A  50      -73.90   -135.45
REMARK 500    ALA A 213       52.25    -60.60
REMARK 500    ASP A 215       93.19    -68.23
REMARK 500    LEU A 217     -137.13   -114.62
REMARK 500    ASP A 306       73.95     55.99
REMARK 500    ALA A 333     -114.36   -131.26
REMARK 500    ILE B  22       72.57     64.23
REMARK 500    GLU B  50      -75.49   -136.62
REMARK 500    THR B 156      169.46    178.75
REMARK 500    CYS B 164     -163.69   -102.21
REMARK 500    LEU B 217     -136.03   -113.17
REMARK 500    ASP B 306       74.94     60.09
REMARK 500    ARG B 314       55.15   -140.81
REMARK 500    ALA B 317      105.30    -46.47
REMARK 500    ALA B 333     -118.29   -134.30
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 A 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B 1002
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1003
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 1004
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1005
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 1006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SNT   RELATED DB: PDB
REMARK 900 HUMAN NEU2 APO-FORM
REMARK 900 RELATED ID: 1SO7   RELATED DB: PDB
REMARK 900 HUMAN NEU2 SUGAR-INDUCED FORM
REMARK 900 RELATED ID: 1VCU   RELATED DB: PDB
REMARK 900 HUMAN NEU2-DANA COMPLEX
REMARK 900 RELATED ID: 2F0Z   RELATED DB: PDB
REMARK 900 RELATED ID: 2F10   RELATED DB: PDB
REMARK 900 RELATED ID: 2F11   RELATED DB: PDB
REMARK 900 RELATED ID: 2F12   RELATED DB: PDB
REMARK 900 RELATED ID: 2F13   RELATED DB: PDB
REMARK 900 RELATED ID: 2F24   RELATED DB: PDB
REMARK 900 RELATED ID: 2F26   RELATED DB: PDB
REMARK 900 RELATED ID: 2F27   RELATED DB: PDB
REMARK 900 RELATED ID: 2F28   RELATED DB: PDB
REMARK 900 RELATED ID: 2F29   RELATED DB: PDB
DBREF  2F25 A    1   380  UNP    Q9Y3R4   NEUR2_HUMAN      1    380
DBREF  2F25 B    1   380  UNP    Q9Y3R4   NEUR2_HUMAN      1    380
SEQADV 2F25 GLY A   -1  UNP  Q9Y3R4              CLONING ARTIFACT
SEQADV 2F25 SER A    0  UNP  Q9Y3R4              CLONING ARTIFACT
SEQADV 2F25 GLN A  111  UNP  Q9Y3R4    GLU   111 ENGINEERED
SEQADV 2F25 GLY B   -1  UNP  Q9Y3R4              CLONING ARTIFACT
SEQADV 2F25 SER B    0  UNP  Q9Y3R4              CLONING ARTIFACT
SEQADV 2F25 GLN B  111  UNP  Q9Y3R4    GLU   111 ENGINEERED
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 ASP 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 GLN 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
SEQRES   1 B  382  GLY SER MET ALA SER LEU PRO VAL LEU GLN LYS GLU SER
SEQRES   2 B  382  VAL PHE GLN SER GLY ALA HIS ALA TYR ARG ILE PRO ALA
SEQRES   3 B  382  LEU LEU TYR LEU PRO GLY GLN GLN SER LEU LEU ALA PHE
SEQRES   4 B  382  ALA GLU GLN ARG ALA SER LYS LYS ASP GLU HIS ALA GLU
SEQRES   5 B  382  LEU ILE VAL LEU ARG ARG GLY ASP TYR ASP ALA PRO THR
SEQRES   6 B  382  HIS GLN VAL GLN TRP GLN ALA GLN GLU VAL VAL ALA GLN
SEQRES   7 B  382  ALA ARG LEU ASP GLY HIS ARG SER MET ASN PRO CYS PRO
SEQRES   8 B  382  LEU TYR ASP ALA GLN THR GLY THR LEU PHE LEU PHE PHE
SEQRES   9 B  382  ILE ALA ILE PRO GLY GLN VAL THR GLN GLN GLN GLN LEU
SEQRES  10 B  382  GLN THR ARG ALA ASN VAL THR ARG LEU CYS GLN VAL THR
SEQRES  11 B  382  SER THR ASP HIS GLY ARG THR TRP SER SER PRO ARG ASP
SEQRES  12 B  382  LEU THR ASP ALA ALA ILE GLY PRO ALA TYR ARG GLU TRP
SEQRES  13 B  382  SER THR PHE ALA VAL GLY PRO GLY HIS CYS LEU GLN LEU
SEQRES  14 B  382  ASN ASP ARG ALA ARG SER LEU VAL VAL PRO ALA TYR ALA
SEQRES  15 B  382  TYR ARG LYS LEU HIS PRO ILE GLN ARG PRO ILE PRO SER
SEQRES  16 B  382  ALA PHE CYS PHE LEU SER HIS ASP HIS GLY ARG THR TRP
SEQRES  17 B  382  ALA ARG GLY HIS PHE VAL ALA GLN ASP THR LEU GLU CYS
SEQRES  18 B  382  GLN VAL ALA GLU VAL GLU THR GLY GLU GLN ARG VAL VAL
SEQRES  19 B  382  THR LEU ASN ALA ARG SER HIS LEU ARG ALA ARG VAL GLN
SEQRES  20 B  382  ALA GLN SER THR ASN ASP GLY LEU ASP PHE GLN GLU SER
SEQRES  21 B  382  GLN LEU VAL LYS LYS LEU VAL GLU PRO PRO PRO GLN GLY
SEQRES  22 B  382  CYS GLN GLY SER VAL ILE SER PHE PRO SER PRO ARG SER
SEQRES  23 B  382  GLY PRO GLY SER PRO ALA GLN TRP LEU LEU TYR THR HIS
SEQRES  24 B  382  PRO THR HIS SER TRP GLN ARG ALA ASP LEU GLY ALA TYR
SEQRES  25 B  382  LEU ASN PRO ARG PRO PRO ALA PRO GLU ALA TRP SER GLU
SEQRES  26 B  382  PRO VAL LEU LEU ALA LYS GLY SER CYS ALA TYR SER ASP
SEQRES  27 B  382  LEU GLN SER MET GLY THR GLY PRO ASP GLY SER PRO LEU
SEQRES  28 B  382  PHE GLY CYS LEU TYR GLU ALA ASN ASP TYR GLU GLU ILE
SEQRES  29 B  382  VAL PHE LEU MET PHE THR LEU LYS GLN ALA PHE PRO ALA
SEQRES  30 B  382  GLU TYR LEU PRO GLN
HET    DAN  A1001      20
HET    DAN  B1002      20
HET    EPE  A1003      15
HET    EPE  B1004      15
HET    EPE  A1005      15
HET    EPE  B1006      15
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN     EPE HEPES
FORMUL   3  DAN    2(C11 H17 N O8)
FORMUL   5  EPE    4(C8 H18 N2 O4 S)
FORMUL   9  HOH   *460(H2 O)
HELIX    1   1 LYS A   45  GLU A   47  5                                   3
HELIX    2   2 THR A  110  ARG A  118  1                                   9
HELIX    3   3 LEU A  142  ILE A  147  1                                   6
HELIX    4   4 GLY A  148  ARG A  152  5                                   5
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
HELIX    8   8 LYS B   45  GLU B   47  5                                   3
HELIX    9   9 THR B  110  ARG B  118  1                                   9
HELIX   10  10 LEU B  142  ILE B  147  1                                   6
HELIX   11  11 GLY B  148  ARG B  152  5                                   5
HELIX   12  12 ALA B  317  TRP B  321  5                                   5
HELIX   13  13 LEU B  369  PHE B  373  1                                   5
HELIX   14  14 PRO B  374  TYR B  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  PHE A 350   O  PHE A 367
SHEET    4   A 7 VAL A 325  THR A 342 -1  N  MET A 340   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  TYR A 295   O  TYR A 310
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  SER A  33   N  LEU A  28
SHEET    3   B 4 ALA A  49  ASP A  60 -1  O  LEU A  51   N  GLN A  40
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  SER A  33   N  LEU A  28
SHEET    3   C 4 ALA A  49  ASP A  60 -1  O  LEU A  51   N  GLN A  40
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  PHE A  99   N  LEU A  90
SHEET    3   D 4 ARG A 123  SER A 129 -1  O  CYS A 125   N  PHE A 102
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  PHE A 197   N  VAL A 176
SHEET    4   F 4 ALA A 207  ARG A 208 -1  O  ALA A 207   N  LEU A 198
SHEET    1   G 4 CYS A 219  GLU A 225  0
SHEET    2   G 4 ARG A 230  ALA A 236 -1  O  VAL A 231   N  VAL A 224
SHEET    3   G 4 ALA A 242  SER A 248 -1  O  VAL A 244   N  ALA A 236
SHEET    4   G 4 GLN A 256  VAL A 265 -1  O  GLN A 256   N  GLN A 247
SHEET    1   H 7 GLN B   8  GLN B  14  0
SHEET    2   H 7 GLU B 361  THR B 368 -1  O  PHE B 364   N  GLU B  10
SHEET    3   H 7 PRO B 348  ALA B 356 -1  N  CYS B 352   O  LEU B 365
SHEET    4   H 7 VAL B 325  THR B 342 -1  N  MET B 340   O  LEU B 349
SHEET    5   H 7 ALA B 305  ASN B 312 -1  N  ASP B 306   O  GLY B 330
SHEET    6   H 7 GLN B 291  PRO B 298 -1  N  TYR B 295   O  TYR B 310
SHEET    7   H 7 SER B 275  PRO B 280 -1  N  PHE B 279   O  TRP B 292
SHEET    1   I 4 ALA B  19  LEU B  28  0
SHEET    2   I 4 SER B  33  ARG B  41 -1  O  ARG B  41   N  ALA B  19
SHEET    3   I 4 ALA B  49  ASP B  60 -1  O  GLY B  57   N  LEU B  34
SHEET    4   I 4 GLN B  65  TRP B  68 -1  O  GLN B  65   N  ASP B  60
SHEET    1   J 4 ALA B  19  LEU B  28  0
SHEET    2   J 4 SER B  33  ARG B  41 -1  O  ARG B  41   N  ALA B  19
SHEET    3   J 4 ALA B  49  ASP B  60 -1  O  GLY B  57   N  LEU B  34
SHEET    4   J 4 GLU B  72  VAL B  73 -1  O  GLU B  72   N  LEU B  54
SHEET    1   K 4 HIS B  82  TYR B  91  0
SHEET    2   K 4 LEU B  98  PRO B 106 -1  O  PHE B  99   N  LEU B  90
SHEET    3   K 4 ARG B 123  SER B 129 -1  O  CYS B 125   N  PHE B 102
SHEET    4   K 4 ARG B 140  ASP B 141 -1  O  ARG B 140   N  GLN B 126
SHEET    1   L 3 TRP B 154  VAL B 159  0
SHEET    2   L 3 LEU B 174  ARG B 182 -1  O  TYR B 181   N  SER B 155
SHEET    3   L 3 LEU B 165  GLN B 166 -1  N  LEU B 165   O  VAL B 175
SHEET    1   M 4 TRP B 154  VAL B 159  0
SHEET    2   M 4 LEU B 174  ARG B 182 -1  O  TYR B 181   N  SER B 155
SHEET    3   M 4 ILE B 191  SER B 199 -1  O  PHE B 195   N  ALA B 178
SHEET    4   M 4 ALA B 207  ARG B 208 -1  O  ALA B 207   N  LEU B 198
SHEET    1   N 4 CYS B 219  VAL B 224  0
SHEET    2   N 4 VAL B 231  ALA B 236 -1  O  VAL B 231   N  VAL B 224
SHEET    3   N 4 ALA B 242  SER B 248 -1  O  VAL B 244   N  ALA B 236
SHEET    4   N 4 GLU B 257  VAL B 265 -1  O  VAL B 261   N  ARG B 243
CISPEP   1 GLY A  160    PRO A  161          0         0.28
CISPEP   2 PRO A  268    PRO A  269          0        -0.07
CISPEP   3 PRO A  315    PRO A  316          0         0.17
CISPEP   4 GLY B  160    PRO B  161          0         0.39
CISPEP   5 PRO B  268    PRO B  269          0        -0.04
CISPEP   6 PRO B  315    PRO B  316          0        -0.04
SITE     1 AC1 15 ARG A  21  ASP A  46  GLN A 111  TYR A 179
SITE     2 AC1 15 TYR A 181  GLU A 218  ARG A 237  ARG A 304
SITE     3 AC1 15 TYR A 334  EPE A1005  HOH A1019  HOH A1031
SITE     4 AC1 15 HOH A1033  HOH A1132  HOH A1193
SITE     1 AC2 17 ARG B  21  ARG B  41  ASP B  46  MET B  85
SITE     2 AC2 17 GLN B 111  TYR B 179  TYR B 181  GLU B 218
SITE     3 AC2 17 ARG B 237  GLN B 270  ARG B 304  TYR B 334
SITE     4 AC2 17 HOH B1047  HOH B1056  HOH B1061  HOH B1107
SITE     5 AC2 17 HOH B1115
SITE     1 AC3 15 SER A  11  VAL A  12  PHE A  13  GLN A  14
SITE     2 AC3 15 GLY A  16  ALA A  17  HIS A  18  TYR A  20
SITE     3 AC3 15 ARG A  55  HOH A1006  HOH A1016  HOH A1126
SITE     4 AC3 15 HOH A1166  VAL B   6  LEU B   7
SITE     1 AC4 12 VAL A   6  LEU A   7  HOH A1034  SER B  11
SITE     2 AC4 12 VAL B  12  PHE B  13  GLN B  14  GLY B  16
SITE     3 AC4 12 ALA B  17  HIS B  18  TYR B  20  HOH B1007
SITE     1 AC5 13 ARG A  21  ARG A  41  LYS A  44  ASP A  46
SITE     2 AC5 13 ARG A 237  PRO A 269  GLN A 270  ARG A 304
SITE     3 AC5 13 TYR A 359  DAN A1001  HOH A1033  HOH A1046
SITE     4 AC5 13 HOH A1077
SITE     1 AC6 10 ARG B  21  ARG B  41  LYS B  44  ASP B  46
SITE     2 AC6 10 PRO B 269  GLN B 270  TYR B 359  HOH B1047
SITE     3 AC6 10 HOH B1063  HOH B1096
CRYST1  157.370   73.640   78.950  90.00  90.31  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      0.006354  0.000000  0.000034        0.00000
SCALE2      0.000000  0.013580  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012666        0.00000
      
PROCHECK
Go to PROCHECK summary
 References