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PDBsum entry 1vcj

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Hydrolase PDB id
1vcj
Jmol
Contents
Protein chain
389 a.a. *
Ligands
IBA
Waters ×106
* Residue conservation analysis
HEADER    HYDROLASE                               09-MAR-04   1VCJ
TITLE     INFLUENZA B VIRUS NEURAMINIDASE COMPLEXED WITH 1-(4-CARBOXY-2-(3-
TITLE    2 PENTYLAMINO)PHENYL)-5-AMINOMETHYL-5-HYDROXYMETHYL-PYRROLIDIN-2-ONE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN RESIDUES 78-466;
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    NEURAMINIDASE, BENZOIC ACID INHIBITORS, SMALL MOLECULE INHIBITOR,
KEYWDS   2 PROTEIN-INHIBITOR COMPLEX, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.S.LOMMER,S.M.ALI,S.N.BAJPAI,W.J.BROUILLETTE,G.M.AIR,M.LUO
REVDAT   5   05-OCT-11 1VCJ    1       LINK
REVDAT   4   13-JUL-11 1VCJ    1       VERSN
REVDAT   3   24-FEB-09 1VCJ    1       VERSN
REVDAT   2   21-JUN-05 1VCJ    1       JRNL
REVDAT   1   23-MAR-04 1VCJ    0
SPRSDE     23-MAR-04 1VCJ      1UJA
JRNL        AUTH   B.S.LOMMER,S.M.ALI,S.N.BAJPAI,W.J.BROUILLETTE,G.M.AIR,M.LUO
JRNL        TITL   A BENZOIC ACID INHIBITOR INDUCES A NOVEL CONFORMATIONAL
JRNL        TITL 2 CHANGE IN THE ACTIVE SITE OF INFLUENZA B VIRUS
JRNL        TITL 3 NEURAMINIDASE.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  60  1017 2004
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   15159560
JRNL        DOI    10.1107/S0907444904006225
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
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) : 6.00
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)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 18434
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHUOT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.214
REMARK   3   FREE R VALUE                     : 0.255
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1843
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) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.49
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.20
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940
REMARK   3   BIN FREE R VALUE                    : 0.3230
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            : 3031
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 25
REMARK   3   SOLVENT ATOMS            : 106
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) : 0.29
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) : 0.35
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 1.69
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 1VCJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAR-04.
REMARK 100 THE RCSB ID CODE IS RCSB006463.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-99
REMARK 200  TEMPERATURE           (KELVIN) : 295.0
REMARK 200  PH                             : 6.80
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
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE MONOCHROMATOR, 0.3 MM
REMARK 200                                   PINHOLE COLLIMATOR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS HI-STAR
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SADIE
REMARK 200  DATA SCALING SOFTWARE          : SAINT
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18434
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.9
REMARK 200  DATA REDUNDANCY                : 2.400
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08400
REMARK 200   FOR THE DATA SET  : 7.7000
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     (%) : 63.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.20700
REMARK 200   FOR SHELL         : 2.600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM CHLORIDE, SODIUM
REMARK 280  NITRATE, CALCIUM CHLORIDE, SODIUM AZIDE, PH 6.80, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K
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       62.18000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       62.18000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       62.18000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       62.18000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       62.18000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       62.18000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       62.18000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       62.18000
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: 17840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 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      124.36000
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       62.18000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000      -62.18000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000       62.18000
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000       62.18000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
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   812     O    HOH A   936              1.80
REMARK 500   O    HOH A   649     O    HOH A   969              2.07
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    ARG A 260   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG A 260   NE  -  CZ  -  NH2 ANGL. DEV. =   5.3 DEGREES
REMARK 500    LYS A 435   N   -  CA  -  CB  ANGL. DEV. = -14.9 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    SER A  90       10.74   -141.08
REMARK 500    ALA A  95      -63.37    -98.78
REMARK 500    ASP A 199       40.59   -153.68
REMARK 500    ALA A 200      170.43    -58.68
REMARK 500    ILE A 221       84.64     44.51
REMARK 500    THR A 224     -156.79   -130.31
REMARK 500    SER A 283     -164.27   -168.82
REMARK 500    CYS A 291     -169.31   -120.54
REMARK 500    LEU A 345      115.30    -37.77
REMARK 500    ASP A 384     -170.06     59.01
REMARK 500    TRP A 408     -124.76   -100.37
REMARK 500    ASP A 436       37.24    -96.65
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 IBA A 1
DBREF  1VCJ A   78   466  UNP    P03474   NRAM_INBLE      78    466
SEQADV 1VCJ ARG A  382  UNP  P03474    LYS   382 CONFLICT
SEQRES   1 A  389  PRO GLU TRP THR TYR PRO ARG LEU SER CYS GLN GLY SER
SEQRES   2 A  389  THR PHE GLN LYS ALA LEU LEU ILE SER PRO HIS ARG PHE
SEQRES   3 A  389  GLY GLU ILE LYS GLY ASN SER ALA PRO LEU ILE ILE ARG
SEQRES   4 A  389  GLU PRO PHE VAL ALA CYS GLY PRO LYS GLU CYS ARG HIS
SEQRES   5 A  389  PHE ALA LEU THR HIS TYR ALA ALA GLN PRO GLY GLY TYR
SEQRES   6 A  389  TYR ASN GLY THR ARG LYS ASP ARG ASN LYS LEU ARG HIS
SEQRES   7 A  389  LEU VAL SER VAL LYS LEU GLY LYS ILE PRO THR VAL GLU
SEQRES   8 A  389  ASN SER ILE PHE HIS MET ALA ALA TRP SER GLY SER ALA
SEQRES   9 A  389  CYS HIS ASP GLY ARG GLU TRP THR TYR ILE GLY VAL ASP
SEQRES  10 A  389  GLY PRO ASP ASN ASP ALA LEU VAL LYS ILE LYS TYR GLY
SEQRES  11 A  389  GLU ALA TYR THR ASP THR TYR HIS SER TYR ALA HIS ASN
SEQRES  12 A  389  ILE LEU ARG THR GLN GLU SER ALA CYS ASN CYS ILE GLY
SEQRES  13 A  389  GLY ASP CYS TYR LEU MET ILE THR ASP GLY SER ALA SER
SEQRES  14 A  389  GLY ILE SER LYS CYS ARG PHE LEU LYS ILE ARG GLU GLY
SEQRES  15 A  389  ARG ILE ILE LYS GLU ILE LEU PRO THR GLY ARG VAL GLU
SEQRES  16 A  389  HIS THR GLU GLU CYS THR CYS GLY PHE ALA SER ASN LYS
SEQRES  17 A  389  THR ILE GLU CYS ALA CYS ARG ASP ASN SER TYR THR ALA
SEQRES  18 A  389  LYS ARG PRO PHE VAL LYS LEU ASN VAL GLU THR ASP THR
SEQRES  19 A  389  ALA GLU ILE ARG LEU MET CYS THR LYS THR TYR LEU ASP
SEQRES  20 A  389  THR PRO ARG PRO ASP ASP GLY SER ILE ALA GLY PRO CYS
SEQRES  21 A  389  GLU SER ASN GLY ASP LYS TRP LEU GLY GLY ILE LYS GLY
SEQRES  22 A  389  GLY PHE VAL HIS GLN ARG MET ALA SER LYS ILE GLY ARG
SEQRES  23 A  389  TRP TYR SER ARG THR MET SER LYS THR ASN ARG MET GLY
SEQRES  24 A  389  MET GLU LEU TYR VAL ARG TYR ASP GLY ASP PRO TRP THR
SEQRES  25 A  389  ASP SER ASP ALA LEU THR LEU SER GLY VAL MET VAL SER
SEQRES  26 A  389  ILE GLU GLU PRO GLY TRP TYR SER PHE GLY PHE GLU ILE
SEQRES  27 A  389  LYS ASP LYS LYS CYS ASP VAL PRO CYS ILE GLY ILE GLU
SEQRES  28 A  389  MET VAL HIS ASP GLY GLY LYS ASP THR TRP HIS SER ALA
SEQRES  29 A  389  ALA THR ALA ILE TYR CYS LEU MET GLY SER GLY GLN LEU
SEQRES  30 A  389  LEU TRP ASP THR VAL THR GLY VAL ASP MET ALA LEU
HET    IBA  A   1      25
HETNAM     IBA 4-[(2R)-2-(AMINOMETHYL)-2-(HYDROXYMETHYL)-5-
HETNAM   2 IBA  OXOPYRROLIDIN-1-YL]-3-[(1-ETHYLPROPYL)AMINO]BENZOIC
HETNAM   3 IBA  ACID
HETSYN     IBA 1-(4-CARBOXY-2-(3-PENTYLAMINO)PHENYL)-5-AMINOMETHYL-5-
HETSYN   2 IBA  HYDROXYMETHYL-PYRROLIDIN-2-ONE
FORMUL   2  IBA    C18 H27 N3 O4
FORMUL   3  HOH   *106(H2 O)
HELIX    1   1 SER A   99  GLY A  104  5                                   6
HELIX    2   2 PRO A  196  ASP A  199  5                                   4
SHEET    1   A 4 PHE A  92  ILE A  98  0
SHEET    2   A 4 SER A 440  LEU A 448 -1  O  ILE A 445   N  ALA A  95
SHEET    3   A 4 ASP A 421  HIS A 431 -1  N  HIS A 431   O  SER A 440
SHEET    4   A 4 SER A 410  LYS A 416 -1  N  ILE A 415   O  VAL A 422
SHEET    1   B 4 LEU A 113  CYS A 122  0
SHEET    2   B 4 CYS A 127  ALA A 137 -1  O  ALA A 136   N  ILE A 114
SHEET    3   B 4 HIS A 155  LYS A 160 -1  O  VAL A 157   N  ALA A 131
SHEET    4   B 4 ILE A 171  ALA A 175 -1  O  HIS A 173   N  LEU A 156
SHEET    1   C 4 SER A 178  HIS A 183  0
SHEET    2   C 4 TRP A 188  ASP A 194 -1  O  ILE A 191   N  SER A 180
SHEET    3   C 4 LEU A 201  TYR A 206 -1  O  LYS A 205   N  TYR A 190
SHEET    4   C 4 ALA A 209  HIS A 215 -1  O  ASP A 212   N  ILE A 204
SHEET    1   D 3 ARG A 223  THR A 224  0
SHEET    2   D 3 ASP A 235  GLY A 243 -1  O  THR A 241   N  ARG A 223
SHEET    3   D 3 ASN A 230  ILE A 232 -1  N  ILE A 232   O  ASP A 235
SHEET    1   E 4 ARG A 223  THR A 224  0
SHEET    2   E 4 ASP A 235  GLY A 243 -1  O  THR A 241   N  ARG A 223
SHEET    3   E 4 SER A 249  ARG A 257 -1  O  ILE A 256   N  CYS A 236
SHEET    4   E 4 ARG A 260  ILE A 265 -1  O  ILE A 265   N  PHE A 253
SHEET    1   F 5 THR A 268  GLY A 269  0
SHEET    2   F 5 THR A 311  LEU A 316  1  O  ILE A 314   N  THR A 268
SHEET    3   F 5 PRO A 301  ASN A 306 -1  N  ASN A 306   O  THR A 311
SHEET    4   F 5 THR A 286  ARG A 292 -1  N  ILE A 287   O  LEU A 305
SHEET    5   F 5 GLU A 275  PHE A 281 -1  N  GLU A 275   O  ARG A 292
SHEET    1   G 4 PHE A 352  ARG A 356  0
SHEET    2   G 4 ILE A 361  ARG A 367 -1  O  TRP A 364   N  VAL A 353
SHEET    3   G 4 MET A 375  TYR A 383 -1  O  TYR A 380   N  TYR A 365
SHEET    4   G 4 THR A 395  PRO A 406 -1  O  SER A 397   N  LEU A 379
SSBOND   1 CYS A   87    CYS A  420                          1555   1555  2.04
SSBOND   2 CYS A  122    CYS A  127                          1555   1555  2.04
SSBOND   3 CYS A  182    CYS A  229                          1555   1555  2.03
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  2.04
CISPEP   1 GLN A  138    PRO A  139          0        -0.70
CISPEP   2 THR A  325    PRO A  326          0         0.10
SITE     1 AC1 12 ARG A 116  GLU A 117  ASP A 149  ARG A 150
SITE     2 AC1 12 ARG A 154  TRP A 177  GLU A 226  GLU A 275
SITE     3 AC1 12 GLU A 276  ARG A 292  ARG A 374  TYR A 409
CRYST1  124.360  124.360   71.470  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      0.008041  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008041  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013992        0.00000
      
PROCHECK
Go to PROCHECK summary
 References