Header list of 1afj.pdb file
Complete list - b 16 2 Bytes
HEADER MERCURY DETOXIFICATION 07-MAR-97 1AFJ
TITLE STRUCTURE OF THE MERCURY-BOUND FORM OF MERP, THE PERIPLASMIC PROTEIN
TITLE 2 FROM THE BACTERIAL MERCURY DETOXIFICATION SYSTEM, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MERP;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ENTIRE PROTEIN;
COMPND 5 SYNONYM: MERCURIC TRANSPORT PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THE PROTEIN STUDIED EXCLUDES THE PRECURSOR SIGNAL
COMPND 8 SEQUENCE. THIS IS THE NATIVE FORM OF THE PROTEIN AFTER CELL
COMPND 9 PROCESSING.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI;
SOURCE 3 ORGANISM_TAXID: 623;
SOURCE 4 CELLULAR_LOCATION: PERIPLASM;
SOURCE 5 GENE: MERP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: MALTOSE BINDING PROTEIN;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSSS;
SOURCE 11 EXPRESSION_SYSTEM_GENE: MERP;
SOURCE 12 OTHER_DETAILS: MER GENES LOCATED ON TRANSPOSON TN21
KEYWDS MERCURY DETOXIFICATION, PERIPLASMIC, HEAVY METAL TRANSPORT, ALPHA-
KEYWDS 2 BETA SANDWICH
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.A.STEELE,S.J.OPELLA
REVDAT 3 16-FEB-22 1AFJ 1 REMARK LINK
REVDAT 2 24-FEB-09 1AFJ 1 VERSN
REVDAT 1 23-JUL-97 1AFJ 0
JRNL AUTH R.A.STEELE,S.J.OPELLA
JRNL TITL STRUCTURES OF THE REDUCED AND MERCURY-BOUND FORMS OF MERP,
JRNL TITL 2 THE PERIPLASMIC PROTEIN FROM THE BACTERIAL MERCURY
JRNL TITL 3 DETOXIFICATION SYSTEM.
JRNL REF BIOCHEMISTRY V. 36 6885 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9188683
JRNL DOI 10.1021/BI9631632
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE. IN SUMMARY, INITIAL CALCULATIONS WERE
REMARK 3 STARTED FROM A LINEAR POLYPEPTIDE TEMPLATE WITH RANDOM BACKBONE
REMARK 3 ANGLES. AN ITERATIVE REFINEMENT WAS EMPLOYED USING ADDITIONAL
REMARK 3 RESTRAINTS AS THE QUALITY OF THE STRUCTURES IMPROVED AND
REMARK 3 AMBIGUITIES IN THE DATA WERE RESOLVED.
REMARK 4
REMARK 4 1AFJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170753.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HMQC-NOESY; HMQC-TOCSY; HNCA;
REMARK 210 HNCOCA; CBCACONH
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 THR A 13 67.55 -179.75
REMARK 500 1 ALA A 16 -50.12 179.09
REMARK 500 1 GLU A 29 -84.85 165.45
REMARK 500 1 ASP A 35 92.99 -162.30
REMARK 500 1 VAL A 36 -164.07 -108.39
REMARK 500 1 PHE A 38 -117.20 -47.53
REMARK 500 1 GLU A 39 -28.04 -35.45
REMARK 500 1 LYS A 40 30.58 -83.19
REMARK 500 1 ARG A 41 68.29 6.14
REMARK 500 1 PHE A 47 -177.70 -171.91
REMARK 500 1 SER A 53 154.80 179.42
REMARK 500 1 PRO A 67 97.24 -52.85
REMARK 500 1 SER A 68 -161.71 -108.49
REMARK 500 1 LYS A 71 61.72 -157.89
REMARK 500 2 THR A 2 91.72 -160.03
REMARK 500 2 THR A 13 -9.94 179.90
REMARK 500 2 CYS A 14 -156.75 -163.50
REMARK 500 2 ALA A 16 -40.01 -169.94
REMARK 500 2 VAL A 28 -76.94 -52.17
REMARK 500 2 GLU A 29 -79.53 167.76
REMARK 500 2 ASP A 35 91.52 -167.40
REMARK 500 2 VAL A 36 -156.91 -108.39
REMARK 500 2 PHE A 38 -99.36 -38.20
REMARK 500 2 LYS A 40 46.51 -87.25
REMARK 500 2 ARG A 41 72.39 -6.15
REMARK 500 2 PHE A 47 -179.03 -172.50
REMARK 500 2 ASP A 49 -9.89 -59.84
REMARK 500 2 ALA A 52 -167.64 -117.71
REMARK 500 2 PRO A 67 94.90 -58.11
REMARK 500 2 SER A 68 -165.03 -108.43
REMARK 500 2 LYS A 71 42.68 -162.27
REMARK 500 3 THR A 13 71.53 179.92
REMARK 500 3 ALA A 16 -51.17 179.22
REMARK 500 3 GLU A 29 -84.42 175.27
REMARK 500 3 ASP A 35 98.69 -169.38
REMARK 500 3 VAL A 36 -157.09 -109.04
REMARK 500 3 PHE A 38 -130.01 -53.25
REMARK 500 3 GLU A 39 -38.00 -23.53
REMARK 500 3 LYS A 40 32.91 -81.24
REMARK 500 3 ARG A 41 87.50 7.50
REMARK 500 3 PHE A 47 -176.95 -172.69
REMARK 500 3 PRO A 67 95.06 -58.53
REMARK 500 3 SER A 68 -168.60 -108.94
REMARK 500 4 VAL A 9 79.52 -112.03
REMARK 500 4 MET A 12 -159.03 -139.06
REMARK 500 4 THR A 13 79.53 -179.04
REMARK 500 4 CYS A 14 -177.41 -178.60
REMARK 500 4 ALA A 16 -44.84 -177.31
REMARK 500 4 GLU A 29 -50.35 170.86
REMARK 500 4 ASP A 35 92.43 -167.92
REMARK 500
REMARK 500 THIS ENTRY HAS 290 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 73 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 CYS A 17 N 116.2
REMARK 620 3 CYS A 17 SG 176.6 62.3
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: HMA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: MERCURY BINDING CYS RESIDUES ARE CONTAINED IN
REMARK 800 THE GMTCAAC HEAVY METAL BINDING REGION (HMA).
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 73
DBREF 1AFJ A 1 72 UNP P04129 MERP_SHIFL 20 91
SEQRES 1 A 72 ALA THR GLN THR VAL THR LEU ALA VAL PRO GLY MET THR
SEQRES 2 A 72 CYS ALA ALA CYS PRO ILE THR VAL LYS LYS ALA LEU SER
SEQRES 3 A 72 LYS VAL GLU GLY VAL SER LYS VAL ASP VAL GLY PHE GLU
SEQRES 4 A 72 LYS ARG GLU ALA VAL VAL THR PHE ASP ASP THR LYS ALA
SEQRES 5 A 72 SER VAL GLN LYS LEU THR LYS ALA THR ALA ASP ALA GLY
SEQRES 6 A 72 TYR PRO SER SER VAL LYS GLN
HET HG A 73 1
HETNAM HG MERCURY (II) ION
FORMUL 2 HG HG 2+
HELIX 1 1 ILE A 19 LYS A 27 1 9
HELIX 2 2 VAL A 54 ALA A 64 1 11
SHEET 1 A 3 GLN A 3 VAL A 9 0
SHEET 2 A 3 GLU A 42 PHE A 47 -1 N PHE A 47 O GLN A 3
SHEET 3 A 3 VAL A 31 GLY A 37 -1 N GLY A 37 O GLU A 42
LINK SG CYS A 14 HG HG A 73 1555 1555 2.33
LINK N CYS A 17 HG HG A 73 1555 1555 3.01
LINK SG CYS A 17 HG HG A 73 1555 1555 2.33
SITE 1 HMA 2 CYS A 14 CYS A 17
SITE 1 AC1 3 CYS A 14 ALA A 16 CYS A 17
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 - b 16 2 Bytes