HEADER BIOSYNTHETIC PROTEIN 30-JAN-06 2FVE
TITLE STRUCTURE OF 10:0-ACP (PROTEIN ALONE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL CARRIER PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE 3 ORGANISM_COMMON: SPINACH;
SOURCE 4 ORGANISM_TAXID: 3562;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSACP-2T
KEYWDS 4-HELIX BUNDLE, BIOSYNTHETIC PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.A.ZORNETZER,B.G.FOX,J.L.MARKLEY
REVDAT 4 09-MAR-22 2FVE 1 REMARK
REVDAT 3 24-FEB-09 2FVE 1 VERSN
REVDAT 2 02-MAY-06 2FVE 1 JRNL
REVDAT 1 11-APR-06 2FVE 0
JRNL AUTH G.A.ZORNETZER,B.G.FOX,J.L.MARKLEY
JRNL TITL SOLUTION STRUCTURES OF SPINACH ACYL CARRIER PROTEIN WITH
JRNL TITL 2 DECANOATE AND STEARATE
JRNL REF BIOCHEMISTRY V. 45 5217 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16618110
JRNL DOI 10.1021/BI052062D
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1, CYANA 2.1
REMARK 3 AUTHORS : GUNTER, P. (CYANA), GUNTER, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FVE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036357.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 287
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2 MM PROTEIN, 10 MM MES PH 6.1,
REMARK 210 100 MM NACL, 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE MOLECULAR DYNAMICS
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 ALA A 18 -175.89 -178.36
REMARK 500 1 SER A 65 -43.44 -133.08
REMARK 500 2 ALA A 18 -179.47 -178.70
REMARK 500 3 ALA A 18 -177.05 -177.69
REMARK 500 3 ALA A 61 30.59 -95.52
REMARK 500 4 ALA A 18 -176.36 -176.60
REMARK 500 5 ALA A 18 -179.48 -173.81
REMARK 500 6 ALA A 18 -173.59 -178.00
REMARK 500 6 ALA A 61 31.81 -95.52
REMARK 500 6 SER A 65 -46.83 -132.54
REMARK 500 7 ALA A 18 -175.49 -175.85
REMARK 500 7 ALA A 61 30.04 -95.44
REMARK 500 7 SER A 65 -46.86 -135.20
REMARK 500 7 LYS A 81 -72.51 -51.75
REMARK 500 9 ALA A 18 -175.51 -177.21
REMARK 500 9 ALA A 61 30.90 -95.56
REMARK 500 9 SER A 65 -47.51 -131.02
REMARK 500 10 ALA A 18 -173.00 -177.18
REMARK 500 10 ALA A 61 30.05 -95.59
REMARK 500 11 ALA A 18 -175.95 -177.05
REMARK 500 11 ALA A 36 109.96 -56.91
REMARK 500 12 ALA A 18 -168.90 -178.29
REMARK 500 12 SER A 65 -53.96 -128.63
REMARK 500 13 ALA A 18 -170.94 -178.75
REMARK 500 14 ALA A 18 -171.20 -175.73
REMARK 500 14 ALA A 61 31.09 -95.95
REMARK 500 15 ALA A 18 -178.73 -177.62
REMARK 500 15 ALA A 61 31.94 -95.45
REMARK 500 16 ALA A 18 -176.38 -177.41
REMARK 500 16 SER A 65 -49.86 -134.34
REMARK 500 17 ALA A 18 -175.64 -177.53
REMARK 500 18 SER A 65 -51.18 -126.92
REMARK 500 19 ALA A 18 -172.38 -178.32
REMARK 500 19 SER A 65 -52.80 -127.20
REMARK 500 20 ALA A 18 -172.52 -178.49
REMARK 500 20 ALA A 61 32.11 -95.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AVA RELATED DB: PDB
REMARK 900 18:0-ACP (COMPARABLE PROTEIN STRUCTURE WITH A LARGER FATTY ACID)
REMARK 900 RELATED ID: 2FVA RELATED DB: PDB
REMARK 900 18:0-ACP (SIMILAR PROTEIN STRUCTURE THAT CONTAINS THE BOUND FATTY
REMARK 900 ACID)
REMARK 900 RELATED ID: 2FVF RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THE PROTEIN HAS 100% MATCH
REMARK 999 TO THE SEQUENCE FROM GB ENTRY CAA31207
REMARK 999 (ACP-I POLYPEPTIDE, SYNTHETIC CONSTRUCT).
DBREF 2FVE A 1 82 UNP P07854 ACP1_SPIOL 57 138
SEQRES 1 A 82 ALA LYS LYS GLU THR ILE ASP LYS VAL SER ASP ILE VAL
SEQRES 2 A 82 LYS GLU LYS LEU ALA LEU GLY ALA ASP VAL VAL VAL THR
SEQRES 3 A 82 ALA ASP SER GLU PHE SER LYS LEU GLY ALA ASP SER LEU
SEQRES 4 A 82 ASP THR VAL GLU ILE VAL MET ASN LEU GLU GLU GLU PHE
SEQRES 5 A 82 GLY ILE ASN VAL ASP GLU ASP LYS ALA GLN ASP ILE SER
SEQRES 6 A 82 THR ILE GLN GLN ALA ALA ASP VAL ILE GLU GLY LEU LEU
SEQRES 7 A 82 GLU LYS LYS ALA
HELIX 1 1 LYS A 2 ALA A 18 1 17
HELIX 2 2 GLU A 30 GLY A 35 1 6
HELIX 3 3 ASP A 37 PHE A 52 1 16
HELIX 4 4 GLU A 58 GLN A 62 5 5
HELIX 5 5 THR A 66 LYS A 81 1 16
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