HEADER TRANSFERASE 13-JUL-15 2N58
TITLE STRUCTURE OF AN N-TERMINAL MEMBRANE-ANCHORING REGION OF THE
TITLE 2 GLYCOSYLTRANSFERASE WAAG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOPOLYSACCHARIDE CORE BIOSYNTHESIS PROTEIN RFAG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 103-132;
COMPND 5 SYNONYM: GLUCOSYLTRANSFERASE I;
COMPND 6 EC: 2.4.-.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 4 ORGANISM_TAXID: 83333
KEYWDS GLYCOSYLTRANSFERASE, WAAG, MEMBRANE, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.LIEBAU,P.PETTERSSON,S.SZPRYNGIEL,L.MALER
REVDAT 2 14-JUN-23 2N58 1 REMARK
REVDAT 1 19-AUG-15 2N58 0
JRNL AUTH J.LIEBAU,P.PETTERSSON,S.SZPRYNGIEL,L.MALER
JRNL TITL MEMBRANE INTERACTION OF THE GLYCOSYLTRANSFERASE WAAG.
JRNL REF BIOPHYS.J. V. 109 552 2015
JRNL REFN ISSN 0006-3495
JRNL PMID 26244737
JRNL DOI 10.1016/J.BPJ.2015.06.036
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1, N.A.
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2N58 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000104437.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : 50
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM PROTEIN, 50 MM [U-100%
REMARK 210 2H] DPC, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-1H NOESY; 2D 1H-13C HSQC;
REMARK 210 2D 1H-1H TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 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: 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 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 1 GLU A 3 35.24 -96.75
REMARK 500 1 ALA A 6 -70.43 -62.37
REMARK 500 1 PHE A 25 -67.07 -92.25
REMARK 500 1 ARG A 27 43.06 -103.59
REMARK 500 2 GLU A 3 -69.21 -121.76
REMARK 500 2 PHE A 25 -52.39 -140.74
REMARK 500 2 ARG A 27 -43.84 -147.46
REMARK 500 3 LYS A 9 -73.58 -122.49
REMARK 500 3 PHE A 25 -52.08 -140.95
REMARK 500 3 ARG A 27 -44.07 -147.16
REMARK 500 4 GLU A 3 70.86 -104.57
REMARK 500 4 PHE A 25 -52.16 -141.04
REMARK 500 4 ARG A 27 -44.03 -147.51
REMARK 500 5 GLU A 8 -57.65 -128.71
REMARK 500 5 PHE A 25 -52.09 -141.08
REMARK 500 5 ARG A 27 -44.68 -150.71
REMARK 500 6 LYS A 9 -74.43 -104.57
REMARK 500 6 ARG A 27 -45.95 -145.35
REMARK 500 7 ALA A 2 62.42 -102.22
REMARK 500 7 VAL A 5 43.61 -99.30
REMARK 500 7 ALA A 6 -42.69 -133.56
REMARK 500 7 LYS A 9 -69.83 -128.21
REMARK 500 7 ARG A 27 -45.15 -147.05
REMARK 500 8 VAL A 5 43.41 -93.18
REMARK 500 8 ARG A 27 -45.01 -147.01
REMARK 500 10 GLU A 3 -63.60 -101.81
REMARK 500 11 PHE A 25 -41.27 -136.17
REMARK 500 11 ARG A 27 24.64 -145.88
REMARK 500 12 LYS A 9 -71.42 -52.17
REMARK 500 12 PHE A 25 -39.66 -131.15
REMARK 500 13 ALA A 28 -72.11 -52.02
REMARK 500 14 GLU A 3 -60.40 -132.77
REMARK 500 14 LYS A 9 -74.18 -126.55
REMARK 500 14 ALA A 28 -72.36 -73.87
REMARK 500 15 VAL A 5 76.55 -119.67
REMARK 500 15 ALA A 6 -75.04 -152.93
REMARK 500 15 ALA A 28 -76.07 -60.61
REMARK 500 16 GLU A 3 65.73 -116.89
REMARK 500 16 ALA A 6 -62.57 -90.05
REMARK 500 16 LYS A 9 -72.00 -55.87
REMARK 500 16 ARG A 27 43.78 -144.71
REMARK 500 16 ALA A 28 -75.13 -88.27
REMARK 500 17 GLU A 3 -40.40 -164.22
REMARK 500 17 LYS A 4 25.41 -152.15
REMARK 500 17 ALA A 6 93.06 63.69
REMARK 500 17 LYS A 9 -42.52 -140.41
REMARK 500 17 ALA A 28 -76.03 -60.35
REMARK 500 18 GLU A 3 -62.37 -123.07
REMARK 500 18 LYS A 9 -74.26 -125.51
REMARK 500 18 PHE A 25 -54.96 -139.92
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IW1 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF RESIDUES 103-132.
REMARK 900 RELATED ID: 25699 RELATED DB: BMRB
DBREF 2N58 A 1 30 UNP P25740 RFAG_ECOLI 103 132
SEQRES 1 A 30 TYR ALA GLU LYS VAL ALA GLN GLU LYS GLY PHE LEU TYR
SEQRES 2 A 30 ARG LEU THR SER ARG TYR ARG HIS TYR ALA ALA PHE GLU
SEQRES 3 A 30 ARG ALA THR PHE
HELIX 1 1 GLU A 3 GLY A 10 1 8
HELIX 2 2 PHE A 11 LEU A 15 5 5
HELIX 3 3 THR A 16 GLU A 26 1 11
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
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END