Header list of 1waz.pdb file
Complete list - 3 20 Bytes
HEADER TRANSPORT PROTEIN 28-OCT-04 1WAZ
TITLE NMR STRUCTURE DETERMINATION OF THE BACTERIAL MERCURY TRANSPORTER,
TITLE 2 MERF, IN MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MERF;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HELIX-LOOP-HELIX CORE, RESIDUES 24-69;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MORGANELLA MORGANII;
SOURCE 3 ORGANISM_TAXID: 582;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: C43;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET31B/MERF
KEYWDS PROTEIN STRUCTURE, RESIDUAL DIPOLAR COUPLING, POLYTOPIC MEMBRANE
KEYWDS 2 PROTEIN, TRANSPORT PROTEIN, ANTIBIOTIC RESISTANCE, MERCURY
KEYWDS 3 DETOXIFICATION
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR S.C.HOWELL,M.F.MESLEH,S.J.OPELLA
REVDAT 3 03-APR-19 1WAZ 1 SOURCE
REVDAT 2 24-FEB-09 1WAZ 1 VERSN
REVDAT 1 11-APR-05 1WAZ 0
JRNL AUTH S.C.HOWELL,M.F.MESLEH,S.J.OPELLA
JRNL TITL NMR STRUCTURE DETERMINATION OF A MEMBRANE PROTEIN WITH TWO
JRNL TITL 2 TRANSMEMBRANE HELICES IN MICELLES: MERF OF THE BACTERIAL
JRNL TITL 3 MERCURY DETOXIFICATION SYSTEM
JRNL REF BIOCHEMISTRY V. 44 5196 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15794657
JRNL DOI 10.1021/BI048095V
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.9.4
REMARK 3 AUTHORS : C.D.SCHWIETERS, J.J.KUSZEWSKI, N.TJ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 BIOCHEMISTRY CITATION ABOVE.
REMARK 4
REMARK 4 1WAZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1290021447.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 333.0
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D20,500MM SDS,
REMARK 210 10MM PHOSPHATE PH6.0, 0.7MM
REMARK 210 SAMPLE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCA; 1H15N-HSQC; 2D- 1H15N
REMARK 210 -HMQC-NOESY; 1H15N- IPAP-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR-NIH
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H-15N RESIDUAL DIPOLAR
REMARK 210 COUPLINGS FROM TWO NON-DEGENERATE ORIENTATIONS.
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: CLOSE CONTACTS
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
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 1 THR A 40 37.37 -142.46
REMARK 500 1 LEU A 43 129.49 -174.98
REMARK 500 1 ASP A 44 -178.21 -67.08
REMARK 500 1 VAL A 46 -145.59 -99.12
REMARK 500 2 THR A 40 38.40 -147.94
REMARK 500 2 ASP A 44 -167.27 -78.05
REMARK 500 2 VAL A 46 -147.40 -103.87
REMARK 500 3 LEU A 43 129.96 -174.73
REMARK 500 3 ASP A 44 -178.00 -66.96
REMARK 500 3 VAL A 46 -157.36 -91.98
REMARK 500 3 GLN A 67 138.28 -172.73
REMARK 500 4 THR A 40 38.71 -148.86
REMARK 500 4 VAL A 46 -145.51 -102.69
REMARK 500 5 LEU A 43 127.65 -173.45
REMARK 500 5 ASP A 44 -178.14 -68.87
REMARK 500 5 VAL A 46 -146.90 -98.14
REMARK 500 6 THR A 40 39.80 -151.16
REMARK 500 6 VAL A 46 -146.05 -102.31
REMARK 500 7 THR A 40 37.75 -144.09
REMARK 500 7 LEU A 43 128.63 -175.54
REMARK 500 7 ASP A 44 -175.56 -69.86
REMARK 500 7 VAL A 46 -147.22 -95.91
REMARK 500 8 THR A 40 37.56 -140.22
REMARK 500 8 LEU A 43 128.67 -174.26
REMARK 500 8 VAL A 46 -155.91 -93.15
REMARK 500 9 THR A 40 38.35 -147.04
REMARK 500 9 LEU A 43 142.88 -176.14
REMARK 500 9 VAL A 46 -135.41 -105.17
REMARK 500 9 ALA A 68 -164.62 -73.83
REMARK 500 10 LEU A 43 131.15 -175.89
REMARK 500 10 VAL A 46 -138.43 -100.49
REMARK 500 10 ALA A 68 -158.83 -84.34
REMARK 500 11 THR A 40 37.60 -140.91
REMARK 500 11 LEU A 43 127.66 -173.81
REMARK 500 11 ASP A 44 -176.39 -68.28
REMARK 500 11 VAL A 46 -145.82 -99.07
REMARK 500 12 THR A 40 37.68 -143.74
REMARK 500 12 LEU A 43 130.89 -175.41
REMARK 500 12 ASP A 44 -175.98 -68.66
REMARK 500 12 VAL A 46 -155.76 -92.36
REMARK 500 13 LEU A 43 130.85 -173.69
REMARK 500 13 VAL A 46 -143.07 -101.35
REMARK 500 14 LEU A 43 129.51 -175.33
REMARK 500 14 VAL A 46 -136.53 -103.45
REMARK 500 15 THR A 40 38.45 -147.05
REMARK 500 15 LEU A 43 144.71 -176.62
REMARK 500 15 VAL A 46 -134.25 -104.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 64 0.28 SIDE CHAIN
REMARK 500 1 ARG A 66 0.29 SIDE CHAIN
REMARK 500 2 ARG A 64 0.23 SIDE CHAIN
REMARK 500 2 ARG A 66 0.26 SIDE CHAIN
REMARK 500 3 ARG A 64 0.28 SIDE CHAIN
REMARK 500 3 ARG A 66 0.26 SIDE CHAIN
REMARK 500 4 ARG A 64 0.27 SIDE CHAIN
REMARK 500 4 ARG A 66 0.25 SIDE CHAIN
REMARK 500 5 ARG A 64 0.31 SIDE CHAIN
REMARK 500 5 ARG A 66 0.24 SIDE CHAIN
REMARK 500 6 ARG A 64 0.23 SIDE CHAIN
REMARK 500 6 ARG A 66 0.20 SIDE CHAIN
REMARK 500 7 ARG A 64 0.30 SIDE CHAIN
REMARK 500 7 ARG A 66 0.30 SIDE CHAIN
REMARK 500 8 ARG A 64 0.22 SIDE CHAIN
REMARK 500 8 ARG A 66 0.32 SIDE CHAIN
REMARK 500 9 ARG A 64 0.27 SIDE CHAIN
REMARK 500 9 ARG A 66 0.29 SIDE CHAIN
REMARK 500 10 ARG A 64 0.18 SIDE CHAIN
REMARK 500 10 ARG A 66 0.32 SIDE CHAIN
REMARK 500 11 ARG A 64 0.28 SIDE CHAIN
REMARK 500 11 ARG A 66 0.32 SIDE CHAIN
REMARK 500 12 ARG A 64 0.27 SIDE CHAIN
REMARK 500 12 ARG A 66 0.21 SIDE CHAIN
REMARK 500 13 ARG A 64 0.27 SIDE CHAIN
REMARK 500 13 ARG A 66 0.31 SIDE CHAIN
REMARK 500 14 ARG A 64 0.32 SIDE CHAIN
REMARK 500 14 ARG A 66 0.20 SIDE CHAIN
REMARK 500 15 ARG A 64 0.30 SIDE CHAIN
REMARK 500 15 ARG A 66 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FRAGMENT USED IN THIS EXPERIMENT COMPRISES RESIDUES 24-69
DBREF 1WAZ A 24 69 UNP Q56446 Q56446 24 69
SEQRES 1 A 46 THR PRO VAL LEU VAL ILE LEU LEU GLY VAL VAL GLY LEU
SEQRES 2 A 46 SER ALA LEU THR GLY TYR LEU ASP TYR VAL LEU LEU PRO
SEQRES 3 A 46 ALA LEU ALA ILE PHE ILE GLY LEU THR ILE TYR ALA ILE
SEQRES 4 A 46 GLN ARG LYS ARG GLN ALA ASP
HELIX 1 1 THR A 24 LEU A 39 1 16
HELIX 2 2 PRO A 49 GLN A 67 1 19
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
Complete list - 3 20 Bytes