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PDBsum entry 1b9t

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Hydrolase PDB id
1b9t
Jmol
Contents
Protein chain
390 a.a. *
Ligands
NAG
RAI
Metals
_CA ×2
Waters ×112
* Residue conservation analysis
HEADER    HYDROLASE                               15-FEB-99   1B9T
TITLE     NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE MAKE
TITLE    2 SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND WATER MOLECULES IN
TITLE    3 THE ACTIVE SITE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (NEURAMINIDASE);
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: SIALIDASE;
COMPND   5 EC: 3.2.1.18
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA B VIRUS (B/LEE/40);
SOURCE   3 ORGANISM_TAXID: 107412;
SOURCE   4 STRAIN: B/LEE/40
KEYWDS    INFLUENZA, NEURAMINIDASE, SIALIDASE, INHIBITOR, B/LEE/40, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.B.FINLEY,V.R.ATIGADDA,F.DUARTE,J.J.ZHAO,W.J.BROUILLETTE,G.M.AIR,
AUTHOR   2 M.LUO
REVDAT   5   13-JUL-11 1B9T    1       VERSN
REVDAT   4   24-FEB-09 1B9T    1       VERSN
REVDAT   3   01-MAY-00 1B9T    1       DBREF
REVDAT   2   23-DEC-99 1B9T    1       JRNL   HEADER COMPND
REVDAT   1   27-FEB-99 1B9T    0
JRNL        AUTH   J.B.FINLEY,V.R.ATIGADDA,F.DUARTE,J.J.ZHAO,W.J.BROUILLETTE,
JRNL        AUTH 2 G.M.AIR,M.LUO
JRNL        TITL   NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE
JRNL        TITL 2 MAKE SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND
JRNL        TITL 3 WATER MOLECULES IN THE ACTIVE SITE.
JRNL        REF    J.MOL.BIOL.                   V. 293  1107 1999
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   10547289
JRNL        DOI    10.1006/JMBI.1999.3180
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.85
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 67.9
REMARK   3   NUMBER OF REFLECTIONS             : 17565
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) : 0.195
REMARK   3   FREE R VALUE                     : 0.271
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 3040
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 39
REMARK   3   SOLVENT ATOMS            : 112
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.38
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  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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1B9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-99.
REMARK 100 THE RCSB ID CODE IS RCSB000490.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : AUG-98
REMARK 200  TEMPERATURE           (KELVIN) : 297
REMARK 200  PH                             : 6.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI FILTER
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200  DATA SCALING SOFTWARE          : SAINT
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17565
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.9
REMARK 200  DATA REDUNDANCY                : 2.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.09000
REMARK 200   FOR THE DATA SET  : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.45000
REMARK 200   FOR SHELL         : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: 1IVB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
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   -Y+1/2,X+1/2,Z
REMARK 290       4555   Y+1/2,-X+1/2,Z
REMARK 290       5555   -X+1/2,Y+1/2,-Z
REMARK 290       6555   X+1/2,-Y+1/2,-Z
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       62.25000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       62.25000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       62.25000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       62.25000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       62.25000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       62.25000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       62.25000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       62.25000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 19470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 KCAL/MOL
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   BIOMT1   2 -1.000000  0.000000  0.000000      124.50000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000       62.25000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000      -62.25000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000       62.25000
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000       62.25000
REMARK 350   BIOMT3   4  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 CA    CA A 501  LIES ON A SPECIAL POSITION.
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   O    HOH A   605     O    HOH A   610              2.09
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    SER A  90       14.37   -152.70
REMARK 500    ALA A  95      -66.51   -102.17
REMARK 500    TYR A 142       56.23   -119.73
REMARK 500    ARG A 186      -51.44   -120.77
REMARK 500    ASP A 199       50.80   -151.51
REMARK 500    ASN A 220       86.19   -155.97
REMARK 500    ILE A 221       77.26     57.40
REMARK 500    THR A 224     -168.14   -129.70
REMARK 500    GLU A 226       27.43     82.57
REMARK 500    GLU A 276       62.51     28.40
REMARK 500    SER A 283     -171.01   -179.67
REMARK 500    GLU A 313      130.89    178.79
REMARK 500    ARG A 315      133.10   -172.03
REMARK 500    CYS A 337       -8.47    -56.53
REMARK 500    LEU A 345      122.06    -35.35
REMARK 500    PHE A 352      130.46   -171.02
REMARK 500    SER A 359       14.08   -141.74
REMARK 500    ASP A 384     -175.31     56.54
REMARK 500    TRP A 408     -122.75   -103.33
REMARK 500    MET A 464      -23.69    -33.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     NAG A  467
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 500  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 297   O
REMARK 620 2 HOH A 502   O    91.5
REMARK 620 3 HOH A 503   O    76.0  86.4
REMARK 620 4 ASP A 293   O    93.9 172.2  89.4
REMARK 620 5 ASP A 324   OD2  92.1  83.5 164.2 101.9
REMARK 620 6 GLY A 346   O   151.9  76.5  78.0  96.2 111.3
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RAI A 468
DBREF  1B9T A   77   466  UNP    P03474   NRAM_INBLE      77    466
SEQRES   1 A  390  GLU PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY
SEQRES   2 A  390  SER THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG
SEQRES   3 A  390  PHE GLY GLU ILE LYS GLY ASN SER ALA PRO LEU ILE ILE
SEQRES   4 A  390  ARG GLU PRO PHE VAL ALA CYS GLY PRO LYS GLU CYS ARG
SEQRES   5 A  390  HIS PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY
SEQRES   6 A  390  TYR TYR ASN GLY THR ARG LYS ASP ARG ASN LYS LEU ARG
SEQRES   7 A  390  HIS LEU VAL SER VAL LYS LEU GLY LYS ILE PRO THR VAL
SEQRES   8 A  390  GLU ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER
SEQRES   9 A  390  ALA CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL
SEQRES  10 A  390  ASP GLY PRO ASP ASN ASP ALA LEU VAL LYS ILE LYS TYR
SEQRES  11 A  390  GLY GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA HIS
SEQRES  12 A  390  ASN ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE
SEQRES  13 A  390  GLY GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA
SEQRES  14 A  390  SER GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU
SEQRES  15 A  390  GLY ARG ILE ILE LYS GLU ILE LEU PRO THR GLY ARG VAL
SEQRES  16 A  390  GLU HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN
SEQRES  17 A  390  LYS THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR
SEQRES  18 A  390  ALA LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP
SEQRES  19 A  390  THR ALA GLU ILE ARG LEU MET CYS THR LYS THR TYR LEU
SEQRES  20 A  390  ASP THR PRO ARG PRO ASP ASP GLY SER ILE ALA GLY PRO
SEQRES  21 A  390  CYS GLU SER ASN GLY ASP LYS TRP LEU GLY GLY ILE LYS
SEQRES  22 A  390  GLY GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY
SEQRES  23 A  390  ARG TRP TYR SER ARG THR MET SER LYS THR ASN ARG MET
SEQRES  24 A  390  GLY MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP
SEQRES  25 A  390  THR ASP SER ASP ALA LEU THR LEU SER GLY VAL MET VAL
SEQRES  26 A  390  SER ILE GLU GLU PRO GLY TRP TYR SER PHE GLY PHE GLU
SEQRES  27 A  390  ILE LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE
SEQRES  28 A  390  GLU MET VAL HIS ASP GLY GLY LYS ASP THR TRP HIS SER
SEQRES  29 A  390  ALA ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN
SEQRES  30 A  390  LEU LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU
HET    NAG  A 467      14
HET     CA  A 500       1
HET     CA  A 501       1
HET    RAI  A 468      23
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      CA CALCIUM ION
HETNAM     RAI 1-(4-CARBOXY-2-GUANIDINOPENTYL)-5,5'-DI(HYDROXYMETHYL)
HETNAM   2 RAI  PYRROLIDIN-2-ONE
FORMUL   2  NAG    C8 H15 N O6
FORMUL   3   CA    2(CA 2+)
FORMUL   5  RAI    C14 H18 N4 O5
FORMUL   6  HOH   *112(H2 O)
HELIX    1   1 PRO A  100  ARG A  102  5                                   3
HELIX    2   2 ASP A  197  ASP A  199  5                                   3
SHEET    1   A 4 PHE A 119  CYS A 122  0
SHEET    2   A 4 CYS A 127  THR A 133 -1  N  PHE A 130   O  PHE A 119
SHEET    3   A 4 HIS A 155  LYS A 160 -1  N  VAL A 159   O  HIS A 129
SHEET    4   A 4 ILE A 171  ALA A 175 -1  N  MET A 174   O  LEU A 156
SHEET    1   B 4 SER A 178  HIS A 183  0
SHEET    2   B 4 TRP A 188  ASP A 194 -1  N  VAL A 193   O  SER A 178
SHEET    3   B 4 LEU A 201  TYR A 206 -1  N  LYS A 205   O  TYR A 190
SHEET    4   B 4 ALA A 209  HIS A 215 -1  N  TYR A 214   O  VAL A 202
SHEET    1   C 4 ASN A 230  ILE A 232  0
SHEET    2   C 4 ASP A 235  GLY A 243 -1  N  TYR A 237   O  ASN A 230
SHEET    3   C 4 SER A 249  ARG A 257 -1  N  ILE A 256   O  CYS A 236
SHEET    4   C 4 ARG A 260  ILE A 265 -1  N  ILE A 265   O  PHE A 253
SHEET    1   D 4 THR A 278  PHE A 281  0
SHEET    2   D 4 THR A 286  ALA A 290 -1  N  ALA A 290   O  THR A 278
SHEET    3   D 4 PRO A 301  ASN A 306 -1  N  LEU A 305   O  ILE A 287
SHEET    4   D 4 ILE A 314  LEU A 316 -1  N  ARG A 315   O  PHE A 302
SHEET    1   E 4 PHE A 352  ARG A 356  0
SHEET    2   E 4 ILE A 361  ARG A 367 -1  N  TRP A 364   O  VAL A 353
SHEET    3   E 4 MET A 377  TYR A 383 -1  N  ARG A 382   O  ARG A 363
SHEET    4   E 4 GLY A 398  VAL A 401 -1  N  VAL A 401   O  MET A 377
SHEET    1   F 4 SER A 410  LYS A 416  0
SHEET    2   F 4 ASP A 421  HIS A 431 -1  N  GLY A 426   O  PHE A 411
SHEET    3   F 4 SER A 440  LEU A 448 -1  N  TYR A 446   O  ILE A 425
SHEET    4   F 4 PHE A  92  ILE A  98 -1  N  ILE A  98   O  THR A 443
SSBOND   1 CYS A   87    CYS A  420                          1555   1555  2.03
SSBOND   2 CYS A  122    CYS A  127                          1555   1555  2.03
SSBOND   3 CYS A  182    CYS A  229                          1555   1555  2.04
SSBOND   4 CYS A  231    CYS A  236                          1555   1555  2.03
SSBOND   5 CYS A  277    CYS A  291                          1555   1555  2.02
SSBOND   6 CYS A  279    CYS A  289                          1555   1555  2.03
SSBOND   7 CYS A  318    CYS A  337                          1555   1555  2.02
SSBOND   8 CYS A  424    CYS A  447                          1555   1555  2.02
LINK        CA    CA A 500                 O   THR A 297     1555   1555  2.65
LINK        CA    CA A 500                 O   HOH A 502     1555   1555  2.23
LINK        CA    CA A 500                 O   HOH A 503     1555   1555  2.42
LINK        CA    CA A 500                 O   ASP A 293     1555   1555  2.15
LINK        CA    CA A 500                 OD2 ASP A 324     1555   1555  2.27
LINK        CA    CA A 500                 O   GLY A 346     1555   1555  2.38
LINK        CA    CA A 501                 OE1 GLU A 168     1555   1555  2.70
LINK        CA    CA A 501                 OE1 GLU A 168     1555   2655  2.70
LINK        CA    CA A 501                 OE1 GLU A 168     1555   4555  2.70
LINK        CA    CA A 501                 OE1 GLU A 168     1555   3545  2.70
CISPEP   1 GLN A  138    PRO A  139          0        -0.34
CISPEP   2 THR A  325    PRO A  326          0         0.12
SITE     1 AC1  5 TYR A  82  PRO A  83  ARG A  84  ASN A 284
SITE     2 AC1  5 ARG A 356
SITE     1 AC2  6 ASP A 293  THR A 297  ASP A 324  GLY A 346
SITE     2 AC2  6 HOH A 502  HOH A 503
SITE     1 AC3  1 GLU A 168
SITE     1 AC4 12 ARG A 116  GLU A 117  ASP A 149  ARG A 150
SITE     2 AC4 12 THR A 224  GLU A 226  ALA A 245  GLU A 275
SITE     3 AC4 12 GLU A 276  ARG A 292  ARG A 374  TYR A 409
CRYST1  124.500  124.500   71.412  90.00  90.00  90.00 P 4 21 2      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      0.008032  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008032  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014003        0.00000
      
PROCHECK
Go to PROCHECK summary
 References