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PDBsum entry 1zk6

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Isomerase PDB id
1zk6
Jmol
Contents
Protein chain
91 a.a.
HEADER    ISOMERASE                               02-MAY-05   1ZK6
TITLE     NMR SOLUTION STRUCTURE OF B. SUBTILIS PRSA PPIASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FOLDASE PROTEIN PRSA;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PPIASE DOMAIN;
COMPND   5 EC: 5.2.1.8;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE   3 ORGANISM_TAXID: 1423;
SOURCE   4 GENE: PRSA;
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: PGEX-2T;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PKTH 3678
KEYWDS    ALPHA/BETA STRUCTURE, ISOMERASE
EXPDTA    SOLUTION NMR
NUMMDL    15
AUTHOR    H.TOSSAVAINEN,P.PERMI,S.L.PURHONEN,M.SARVAS,I.KILPELAINEN,
AUTHOR   2 R.SEPPALA
REVDAT   2   24-FEB-09 1ZK6    1       VERSN
REVDAT   1   28-MAR-06 1ZK6    0
JRNL        AUTH   H.TOSSAVAINEN,P.PERMI,S.L.PURHONEN,M.SARVAS,
JRNL        AUTH 2 I.KILPELAINEN,R.SEPPALA
JRNL        TITL   NMR SOLUTION STRUCTURE AND CHARACTERIZATION OF
JRNL        TITL 2 SUBSTRATE BINDING SITE OF THE PPIASE DOMAIN OF
JRNL        TITL 3 PRSA PROTEIN FROM BACILLUS SUBTILIS
JRNL        REF    FEBS LETT.                    V. 580  1822 2006
JRNL        REFN                   ISSN 0014-5793
JRNL        PMID   16516208
JRNL        DOI    10.1016/J.FEBSLET.2006.02.042
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : AMBER 8.0
REMARK   3   AUTHORS     : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,
REMARK   3                 SEIBEL,SINGH,WEINER,KOLLMAN
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1ZK6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-05.
REMARK 100 THE RCSB ID CODE IS RCSB032810.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210  EXPERIMENT TYPE                : NMR
REMARK 210  TEMPERATURE           (KELVIN) : 298
REMARK 210  PH                             : 7.0
REMARK 210  IONIC STRENGTH                 : NULL
REMARK 210  PRESSURE                       : AMBIENT
REMARK 210  SAMPLE CONTENTS                : 0.9 MM PRSA PPIASE DOMAIN
REMARK 210                                   U15N,13C; 20 MM BIS-TRIS
REMARK 210                                   BUFFER; 92% H2O, 8% D2O
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_13C-SEPARATED_NOESY, 3D_
REMARK 210                                   15N-SEPARATED_NOESY
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ, 800 MHZ
REMARK 210  SPECTROMETER MODEL             : INOVA
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN
REMARK 210
REMARK 210  STRUCTURE DETERMINATION.
REMARK 210   SOFTWARE USED                 : VNMR 6.1C, SPARKY 3.106,
REMARK 210                                   CYANA 1.0
REMARK 210   METHOD USED                   : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST
REMARK 210                                   RESTRAINT VIOLATIONS,
REMARK 210                                   STRUCTURES WITH THE LOWEST
REMARK 210                                   ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465   MODELS 1-15
REMARK 465     RES C SSSEQI
REMARK 465     GLY A   114
REMARK 465     SER A   115
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  9 ARG A 119   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 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  3 TYR A 151      -31.02   -130.16
REMARK 500  5 TYR A 151      -34.99   -134.09
REMARK 500  6 TYR A 151      -31.75   -131.38
REMARK 500  6 PRO A 191      103.00    -54.51
REMARK 500 10 THR A 185        0.15    -64.26
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1ZK6 A  116   206  UNP    P24327   PRSA_BACSU     135    225
SEQADV 1ZK6 GLY A  114  UNP  P24327              CLONING ARTIFACT
SEQADV 1ZK6 SER A  115  UNP  P24327              CLONING ARTIFACT
SEQRES   1 A   93  GLY SER GLY LYS ILE ARG ALA SER HIS ILE LEU VAL ALA
SEQRES   2 A   93  ASP LYS LYS THR ALA GLU GLU VAL GLU LYS LYS LEU LYS
SEQRES   3 A   93  LYS GLY GLU LYS PHE GLU ASP LEU ALA LYS GLU TYR SER
SEQRES   4 A   93  THR ASP SER SER ALA SER LYS GLY GLY ASP LEU GLY TRP
SEQRES   5 A   93  PHE ALA LYS GLU GLY GLN MET ASP GLU THR PHE SER LYS
SEQRES   6 A   93  ALA ALA PHE LYS LEU LYS THR GLY GLU VAL SER ASP PRO
SEQRES   7 A   93  VAL LYS THR GLN TYR GLY TYR HIS ILE ILE LYS LYS THR
SEQRES   8 A   93  GLU GLU
HELIX    1   1 ASP A  127  GLY A  141  1                                  15
HELIX    2   2 LYS A  143  SER A  152  1                                  10
HELIX    3   3 ASP A  154  GLY A  160  5                                   7
HELIX    4   4 THR A  175  LEU A  183  1                                   9
SHEET    1   A 4 ASP A 162  PHE A 166  0
SHEET    2   A 4 ILE A 118  VAL A 125 -1  N  ILE A 118   O  PHE A 166
SHEET    3   A 4 TYR A 198  GLU A 205 -1  O  LYS A 202   N  SER A 121
SHEET    4   A 4 VAL A 192  LYS A 193 -1  N  VAL A 192   O  HIS A 199
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1
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      1.000000  0.000000  0.000000        0.00000
SCALE2      0.000000  1.000000  0.000000        0.00000
SCALE3      0.000000  0.000000  1.000000        0.00000
      
PROCHECK
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