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PDBsum entry 2vn1

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Isomerase PDB id
2vn1
Jmol
Contents
Protein chains
123 a.a.
Ligands
FK5 ×2
Waters ×162
HEADER    ISOMERASE                               30-JAN-08   2VN1
TITLE     CRYSTAL STRUCTURE OF THE FK506-BINDING DOMAIN OF PLASMODIUM
TITLE    2 FALCIPARUM FKBP35 IN COMPLEX WITH FK506
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 70 KDA PEPTIDYLPROLYL ISOMERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: FK506-BINDING DOMAIN, RESIDUES 1-127;
COMPND   5 SYNONYM: PLASMODIUM FALCIPARUM FKBP35;
COMPND   6 EC: 5.2.1.8;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE   3 ORGANISM_TAXID: 36329;
SOURCE   4 STRAIN: 3D7;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET29B
KEYWDS    FKBP, FK506, ISOMERASE, TPR REPEAT,  PLASMODIUM FALCIPARUM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.KOTAKA,R.ALAG,H.YE,P.R.PREISER,H.S.YOON,J.LESCAR
REVDAT   3   24-FEB-09 2VN1    1       VERSN
REVDAT   2   17-JUN-08 2VN1    1       JRNL
REVDAT   1   20-MAY-08 2VN1    0
JRNL        AUTH   M.KOTAKA,H.YE,R.ALAG,G.HU,Z.BOZDECH,P.R.PREISER,
JRNL        AUTH 2 H.S.YOON,J.LESCAR
JRNL        TITL   CRYSTAL STRUCTURE OF THE FK506 BINDING DOMAIN OF
JRNL        TITL 2 PLASMODIUM FALCIPARUM FKBP35 IN COMPLEX WITH
JRNL        TITL 3 FK506.
JRNL        REF    BIOCHEMISTRY                  V.  47  5951 2008
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   18465874
JRNL        DOI    10.1021/BI800004U
REMARK   2
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.2
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 : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.65
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1800752.84
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 14825
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) : 0.194
REMARK   3   FREE R VALUE                     : 0.250
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.9
REMARK   3   FREE R VALUE TEST SET COUNT      : 733
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.50
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2269
REMARK   3   BIN R VALUE           (WORKING SET) : 0.275
REMARK   3   BIN FREE R VALUE                    : 0.348
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.7
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 113
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.033
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1938
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 114
REMARK   3   SOLVENT ATOMS            : 162
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 30.5
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.5
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 6.66
REMARK   3    B22 (A**2) : 6.66
REMARK   3    B33 (A**2) : -13.31
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28
REMARK   3   ESD FROM SIGMAA              (A) : 0.33
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.3
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.6
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.74
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 5.07  ; 4.00
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.52  ; 8.00
REMARK   3   SIDE-CHAIN BOND              (A**2) : 10.05 ; 8.00
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 11.91 ; 12.00
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.4
REMARK   3   BSOL        : 40.8564
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  : FK5_PRODRG.PAR
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : FK5_PRODRG.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK   4
REMARK   4 2VN1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JAN-08.
REMARK 100 THE PDBE ID CODE IS EBI-35137.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14883
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.35
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 20.7
REMARK 200  R MERGE                    (I) : 0.10
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 41.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.38
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 8.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MR. BUMP
REMARK 200 STARTING MODEL: PDB ENTRY 1YAT
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.6
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.7M NA MALONATE, PH5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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       83.99500
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.53200
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.53200
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      125.99250
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.53200
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.53200
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       41.99750
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.53200
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.53200
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      125.99250
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.53200
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.53200
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       41.99750
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       83.99500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE:  1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE:  2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     THR A     2
REMARK 465     THR A     3
REMARK 465     GLU A     4
REMARK 465     GLN A     5
REMARK 465     GLU A     6
REMARK 465     MET B     1
REMARK 465     THR B     2
REMARK 465     THR B     3
REMARK 465     GLU B     4
REMARK 465     GLN B     5
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     GLU B 129    CA   C    O    CB   CG   CD   OE1  OE2
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 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    GLU A   8      110.82   -168.08
REMARK 500    PHE B   7      -38.80   -139.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FK5 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FK5 B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FBN   RELATED DB: PDB
REMARK 900  PLASMODIUM FALCIPARUM PUTATIVE FK506-BINDING
REMARK 900  PROTEINPFL2275C, C-TERMINAL TPR-CONTAINING
REMARK 900  DOMAIN
DBREF  2VN1 A    1   127  UNP    Q8I4V8   Q8I4V8_PLAF7     1    127
DBREF  2VN1 A  128   129  PDB    2VN1     2VN1           128    129
DBREF  2VN1 B    1   127  UNP    Q8I4V8   Q8I4V8_PLAF7     1    127
DBREF  2VN1 B  128   129  PDB    2VN1     2VN1           128    129
SEQRES   1 A  129  MET THR THR GLU GLN GLU PHE GLU LYS VAL GLU LEU THR
SEQRES   2 A  129  ALA ASP GLY GLY VAL ILE LYS THR ILE LEU LYS LYS GLY
SEQRES   3 A  129  ASP GLU GLY GLU GLU ASN ILE PRO LYS LYS GLY ASN GLU
SEQRES   4 A  129  VAL THR VAL HIS TYR VAL GLY LYS LEU GLU SER THR GLY
SEQRES   5 A  129  LYS VAL PHE ASP SER SER PHE ASP ARG ASN VAL PRO PHE
SEQRES   6 A  129  LYS PHE HIS LEU GLU GLN GLY GLU VAL ILE LYS GLY TRP
SEQRES   7 A  129  ASP ILE CYS VAL SER SER MET ARG LYS ASN GLU LYS CYS
SEQRES   8 A  129  LEU VAL ARG ILE GLU SER MET TYR GLY TYR GLY ASP GLU
SEQRES   9 A  129  GLY CYS GLY GLU SER ILE PRO GLY ASN SER VAL LEU LEU
SEQRES  10 A  129  PHE GLU ILE GLU LEU LEU SER PHE ARG GLU LEU GLU
SEQRES   1 B  129  MET THR THR GLU GLN GLU PHE GLU LYS VAL GLU LEU THR
SEQRES   2 B  129  ALA ASP GLY GLY VAL ILE LYS THR ILE LEU LYS LYS GLY
SEQRES   3 B  129  ASP GLU GLY GLU GLU ASN ILE PRO LYS LYS GLY ASN GLU
SEQRES   4 B  129  VAL THR VAL HIS TYR VAL GLY LYS LEU GLU SER THR GLY
SEQRES   5 B  129  LYS VAL PHE ASP SER SER PHE ASP ARG ASN VAL PRO PHE
SEQRES   6 B  129  LYS PHE HIS LEU GLU GLN GLY GLU VAL ILE LYS GLY TRP
SEQRES   7 B  129  ASP ILE CYS VAL SER SER MET ARG LYS ASN GLU LYS CYS
SEQRES   8 B  129  LEU VAL ARG ILE GLU SER MET TYR GLY TYR GLY ASP GLU
SEQRES   9 B  129  GLY CYS GLY GLU SER ILE PRO GLY ASN SER VAL LEU LEU
SEQRES  10 B  129  PHE GLU ILE GLU LEU LEU SER PHE ARG GLU LEU GLU
HET    FK5  A 501      57
HET    FK5  B 501      57
HETNAM     FK5 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN
FORMUL   3  FK5    2(C44 H69 N O12)
FORMUL   4  HOH   *162(H2 O1)
HELIX    1   1 GLY A   29  ILE A   33  5                                   5
HELIX    2   2 ILE A   75  SER A   83  1                                   9
HELIX    3   3 SER A   97  GLY A  100  5                                   4
HELIX    4   4 GLY B   29  ILE B   33  5                                   5
HELIX    5   5 ILE B   75  SER B   83  1                                   9
HELIX    6   6 SER B   97  GLY B  100  5                                   4
SHEET    1  AA 6 GLU A   8  GLU A  11  0
SHEET    2  AA 6 VAL A  18  LYS A  24 -1  O  LYS A  20   N  VAL A  10
SHEET    3  AA 6 LYS A  90  ILE A  95 -1  O  LYS A  90   N  LEU A  23
SHEET    4  AA 6 LEU A 116  ARG A 126 -1  O  LEU A 116   N  ILE A  95
SHEET    5  AA 6 GLU A  39  LEU A  48 -1  O  GLU A  39   N  ARG A 126
SHEET    6  AA 6 PHE A  65  HIS A  68 -1  O  PHE A  65   N  VAL A  42
SHEET    1  AB 6 GLU A   8  GLU A  11  0
SHEET    2  AB 6 VAL A  18  LYS A  24 -1  O  LYS A  20   N  VAL A  10
SHEET    3  AB 6 LYS A  90  ILE A  95 -1  O  LYS A  90   N  LEU A  23
SHEET    4  AB 6 LEU A 116  ARG A 126 -1  O  LEU A 116   N  ILE A  95
SHEET    5  AB 6 GLU A  39  LEU A  48 -1  O  GLU A  39   N  ARG A 126
SHEET    6  AB 6 VAL A  54  SER A  57 -1  N  PHE A  55   O  GLY A  46
SHEET    1  BA 6 LYS B   9  GLU B  11  0
SHEET    2  BA 6 VAL B  18  LYS B  24 -1  O  LYS B  20   N  VAL B  10
SHEET    3  BA 6 LYS B  90  ILE B  95 -1  O  LYS B  90   N  LEU B  23
SHEET    4  BA 6 LEU B 116  ARG B 126 -1  O  LEU B 116   N  ILE B  95
SHEET    5  BA 6 GLU B  39  LEU B  48 -1  O  GLU B  39   N  ARG B 126
SHEET    6  BA 6 PHE B  65  HIS B  68 -1  O  PHE B  65   N  VAL B  42
SHEET    1  BB 6 LYS B   9  GLU B  11  0
SHEET    2  BB 6 VAL B  18  LYS B  24 -1  O  LYS B  20   N  VAL B  10
SHEET    3  BB 6 LYS B  90  ILE B  95 -1  O  LYS B  90   N  LEU B  23
SHEET    4  BB 6 LEU B 116  ARG B 126 -1  O  LEU B 116   N  ILE B  95
SHEET    5  BB 6 GLU B  39  LEU B  48 -1  O  GLU B  39   N  ARG B 126
SHEET    6  BB 6 VAL B  54  SER B  57 -1  N  PHE B  55   O  GLY B  46
SITE     1 AC1 23 TYR A  44  PHE A  55  ASP A  56  ARG A  61
SITE     2 AC1 23 PHE A  65  GLU A  73  VAL A  74  ILE A  75
SITE     3 AC1 23 TRP A  78  TYR A 101  ILE A 110  PHE A 118
SITE     4 AC1 23 HOH A2062  HOH A2063  HOH A2064  HOH A2065
SITE     5 AC1 23 HOH A2066  HIS B  43  SER B  57  PHE B  59
SITE     6 AC1 23 ASP B  60  LYS B  90  GLU B 119
SITE     1 AC2 21 HIS A  43  SER A  57  PHE A  59  ASP A  60
SITE     2 AC2 21 LYS A  90  GLU A 119  TYR B  44  PHE B  55
SITE     3 AC2 21 ASP B  56  ARG B  61  PHE B  65  GLU B  73
SITE     4 AC2 21 VAL B  74  ILE B  75  TRP B  78  GLY B 100
SITE     5 AC2 21 TYR B 101  PHE B 118  HOH B2094  HOH B2095
SITE     6 AC2 21 HOH B2096
CRYST1   63.064   63.064  167.990  90.00  90.00  90.00 P 43 21 2    16
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      0.015857  0.000000  0.000000        0.00000
SCALE2      0.000000  0.015857  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005953        0.00000
MTRIX1   1 -0.722400 -0.691500  0.003500       22.20110    1
MTRIX2   1  0.691400 -0.722300 -0.014600       54.69900    1
MTRIX3   1  0.012600 -0.008100  0.999900       21.28020    1
      
PROCHECK
Go to PROCHECK summary
 References