HEADER TRANSPORT PROTEIN 17-MAY-00 1F0Z
TITLE SOLUTION STRUCTURE OF THIS, THE SULFUR CARRIER PROTEIN IN E.COLI
TITLE 2 THIAMIN BIOSYNTHESIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIS PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: SULFUR CARRIER PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCLK413
KEYWDS UBIQUITIN FOLD, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR C.WANG,J.XI,T.P.BEGLEY,L.K.NICHOLSON
REVDAT 3 16-FEB-22 1F0Z 1 REMARK
REVDAT 2 24-FEB-09 1F0Z 1 VERSN
REVDAT 1 10-JAN-01 1F0Z 0
JRNL AUTH C.WANG,J.XI,T.P.BEGLEY,L.K.NICHOLSON
JRNL TITL SOLUTION STRUCTURE OF THIS AND IMPLICATIONS FOR THE
JRNL TITL 2 EVOLUTIONARY ROOTS OF UBIQUITIN.
JRNL REF NAT.STRUCT.BIOL. V. 8 47 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11135670
JRNL DOI 10.1038/83041
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, X-PLOR 3.851
REMARK 3 AUTHORS : VARIAN ASSOCIATES (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 882 RESTRAINTS, 802 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 64 DIHEDRAL ANGLE RESTRAINTS, 16 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1F0Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000011111.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.6
REMARK 210 IONIC STRENGTH : 25 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM THIS NA; 25 MM SODIUM
REMARK 210 PHOSPHATE, 5 MM DTT, 5 MG/ML
REMARK 210 PEPSTATIN, 50 MICROM EDTA, 50
REMARK 210 MICROM CHLORAMPHENICOL; 1 MM
REMARK 210 THIS U-15N; 25 MM SODIUM
REMARK 210 PHOSPHATE, 5 MM DTT, 5 MG/ML
REMARK 210 PEPSTATIN, 50 MICROM EDTA, 50
REMARK 210 MICROM CHLORAMPHENICOL; 1 MM
REMARK 210 THIS U-15N, 13C; 25 MM SODIUM
REMARK 210 PHOSPHATE, 5 MM DTT, 5 MG/ML
REMARK 210 PEPSTATIN, 50 MICROM EDTA, 50
REMARK 210 MICROM CHLORAMPHENICOL; 1 MM
REMARK 210 THIS U-15N, 13C; 25 MM SODIUM
REMARK 210 PHOSPHATE, 5 MM DTT, 5 MG/ML
REMARK 210 PEPSTATIN, 50 MICROM EDTA, 50
REMARK 210 MICROM CHLORAMPHENICOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY; HNHA;
REMARK 210 HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, PIPP 1, X-PLOR
REMARK 210 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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 O GLN A 45 H GLN A 48 1.50
REMARK 500 O LEU A 22 H GLN A 27 1.53
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 ASP A 7 19.49 57.62
REMARK 500 1 CYS A 12 -158.80 -134.45
REMARK 500 1 THR A 17 -169.03 -52.11
REMARK 500 1 ASP A 26 33.58 94.57
REMARK 500 1 ARG A 28 -111.25 -113.94
REMARK 500 1 GLN A 29 -74.46 -154.66
REMARK 500 1 GLN A 38 0.28 82.52
REMARK 500 1 ARG A 43 -59.30 -20.95
REMARK 500 1 TRP A 46 -33.63 -39.95
REMARK 500 1 VAL A 62 153.75 56.98
REMARK 500 2 ASP A 7 18.82 56.53
REMARK 500 2 CYS A 12 -149.76 -152.02
REMARK 500 2 THR A 17 -165.12 -60.78
REMARK 500 2 ASP A 26 32.94 80.39
REMARK 500 2 ARG A 28 -101.34 -85.87
REMARK 500 2 GLN A 29 -64.41 170.87
REMARK 500 2 ASN A 37 19.68 54.84
REMARK 500 2 GLN A 38 1.61 88.86
REMARK 500 2 ARG A 43 -60.10 -19.99
REMARK 500 2 VAL A 62 128.84 -178.17
REMARK 500 3 ASP A 7 17.27 57.87
REMARK 500 3 CYS A 12 -149.01 -149.48
REMARK 500 3 THR A 17 -166.88 -59.09
REMARK 500 3 ASP A 26 22.96 104.70
REMARK 500 3 GLN A 29 47.85 74.64
REMARK 500 3 ASN A 37 18.32 58.84
REMARK 500 3 GLN A 38 3.75 91.50
REMARK 500 3 ARG A 43 -60.88 -25.23
REMARK 500 4 CYS A 12 -159.11 -139.82
REMARK 500 4 THR A 17 -164.75 -55.62
REMARK 500 4 ASP A 26 39.30 92.92
REMARK 500 4 GLN A 29 63.43 76.56
REMARK 500 4 GLN A 38 -3.92 85.95
REMARK 500 4 ARG A 43 -41.24 -23.67
REMARK 500 4 HIS A 49 79.62 -105.23
REMARK 500 4 VAL A 62 151.28 -49.13
REMARK 500 5 ASP A 7 19.95 56.50
REMARK 500 5 THR A 17 -166.00 -58.66
REMARK 500 5 ASP A 26 36.39 79.43
REMARK 500 5 ARG A 28 -114.36 -93.63
REMARK 500 5 GLN A 29 -56.18 174.35
REMARK 500 5 GLN A 38 11.03 84.88
REMARK 500 5 ARG A 43 -62.18 -22.67
REMARK 500 5 VAL A 62 152.28 53.11
REMARK 500 6 CYS A 12 -156.06 -139.80
REMARK 500 6 THR A 17 -165.57 -51.48
REMARK 500 6 ASP A 26 36.56 84.72
REMARK 500 6 ALA A 30 -34.89 -31.23
REMARK 500 6 ARG A 43 -53.85 -23.85
REMARK 500 6 TRP A 46 -30.91 -39.87
REMARK 500
REMARK 500 THIS ENTRY HAS 205 RAMACHANDRAN OUTLIERS.
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 28 0.30 SIDE CHAIN
REMARK 500 1 ARG A 43 0.30 SIDE CHAIN
REMARK 500 2 ARG A 28 0.32 SIDE CHAIN
REMARK 500 2 ARG A 43 0.21 SIDE CHAIN
REMARK 500 3 ARG A 28 0.08 SIDE CHAIN
REMARK 500 3 ARG A 43 0.24 SIDE CHAIN
REMARK 500 4 ARG A 28 0.17 SIDE CHAIN
REMARK 500 4 ARG A 43 0.15 SIDE CHAIN
REMARK 500 5 ARG A 28 0.32 SIDE CHAIN
REMARK 500 5 ARG A 43 0.32 SIDE CHAIN
REMARK 500 6 ARG A 28 0.21 SIDE CHAIN
REMARK 500 6 ARG A 43 0.28 SIDE CHAIN
REMARK 500 7 ARG A 28 0.28 SIDE CHAIN
REMARK 500 7 ARG A 43 0.28 SIDE CHAIN
REMARK 500 8 ARG A 28 0.27 SIDE CHAIN
REMARK 500 8 ARG A 43 0.31 SIDE CHAIN
REMARK 500 9 ARG A 43 0.30 SIDE CHAIN
REMARK 500 10 ARG A 28 0.32 SIDE CHAIN
REMARK 500 10 ARG A 43 0.28 SIDE CHAIN
REMARK 500 11 ARG A 28 0.28 SIDE CHAIN
REMARK 500 11 ARG A 43 0.32 SIDE CHAIN
REMARK 500 12 ARG A 28 0.23 SIDE CHAIN
REMARK 500 12 ARG A 43 0.30 SIDE CHAIN
REMARK 500 13 ARG A 28 0.23 SIDE CHAIN
REMARK 500 13 ARG A 43 0.18 SIDE CHAIN
REMARK 500 14 ARG A 28 0.30 SIDE CHAIN
REMARK 500 14 ARG A 43 0.26 SIDE CHAIN
REMARK 500 15 ARG A 28 0.20 SIDE CHAIN
REMARK 500 15 ARG A 43 0.15 SIDE CHAIN
REMARK 500 16 ARG A 28 0.31 SIDE CHAIN
REMARK 500 16 ARG A 43 0.14 SIDE CHAIN
REMARK 500 17 ARG A 28 0.32 SIDE CHAIN
REMARK 500 17 ARG A 43 0.31 SIDE CHAIN
REMARK 500 18 ARG A 28 0.21 SIDE CHAIN
REMARK 500 18 ARG A 43 0.27 SIDE CHAIN
REMARK 500 19 ARG A 28 0.26 SIDE CHAIN
REMARK 500 19 ARG A 43 0.32 SIDE CHAIN
REMARK 500 20 ARG A 28 0.32 SIDE CHAIN
REMARK 500 20 ARG A 43 0.32 SIDE CHAIN
REMARK 500 21 ARG A 28 0.18 SIDE CHAIN
REMARK 500 21 ARG A 43 0.26 SIDE CHAIN
REMARK 500 22 ARG A 28 0.25 SIDE CHAIN
REMARK 500 22 ARG A 43 0.30 SIDE CHAIN
REMARK 500 23 ARG A 28 0.29 SIDE CHAIN
REMARK 500 23 ARG A 43 0.16 SIDE CHAIN
REMARK 500 24 ARG A 28 0.28 SIDE CHAIN
REMARK 500 24 ARG A 43 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1F0Z A 1 66 UNP O32583 THIS_ECOLI 1 66
SEQRES 1 A 66 MET GLN ILE LEU PHE ASN ASP GLN ALA MET GLN CYS ALA
SEQRES 2 A 66 ALA GLY GLN THR VAL HIS GLU LEU LEU GLU GLN LEU ASP
SEQRES 3 A 66 GLN ARG GLN ALA GLY ALA ALA LEU ALA ILE ASN GLN GLN
SEQRES 4 A 66 ILE VAL PRO ARG GLU GLN TRP ALA GLN HIS ILE VAL GLN
SEQRES 5 A 66 ASP GLY ASP GLN ILE LEU LEU PHE GLN VAL ILE ALA GLY
SEQRES 6 A 66 GLY
HELIX 1 1 THR A 17 ASP A 26 1 10
HELIX 2 2 PRO A 42 ALA A 47 1 6
SHEET 1 A 3 ALA A 9 MET A 10 0
SHEET 2 A 3 ILE A 3 PHE A 5 -1 O ILE A 3 N MET A 10
SHEET 3 A 3 ASP A 55 ILE A 57 1 O ASP A 55 N LEU A 4
SHEET 1 B 3 GLN A 39 VAL A 41 0
SHEET 2 B 3 ALA A 32 ILE A 36 -1 O LEU A 34 N VAL A 41
SHEET 3 B 3 LEU A 59 GLN A 61 -1 N PHE A 60 O ALA A 33
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
