Header list of 1fh1.pdb file
Complete list - 23 202 Bytes
HEADER LIPID BINDING PROTEIN 30-JUL-00 1FH1
TITLE BACKBONE FOLD OF NODF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NODULATION PROTEIN F;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NODF;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOBIUM LEGUMINOSARUM;
SOURCE 3 ORGANISM_TAXID: 384;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PMP2301
KEYWDS ROOT NODULATION FACTOR, PROTEIN BACKBONE FOLD, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR C.A.FOWLER,F.TIAN,H.M.AL-HASHIMI,J.H.PRESTEGARD
REVDAT 3 23-FEB-22 1FH1 1 REMARK
REVDAT 2 24-FEB-09 1FH1 1 VERSN
REVDAT 1 17-JAN-01 1FH1 0
JRNL AUTH C.A.FOWLER,F.TIAN,H.M.AL-HASHIMI,J.H.PRESTEGARD
JRNL TITL RAPID DETERMINATION OF PROTEIN FOLDS USING RESIDUAL DIPOLAR
JRNL TITL 2 COUPLINGS.
JRNL REF J.MOL.BIOL. V. 304 447 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11090286
JRNL DOI 10.1006/JMBI.2000.4199
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.GHOSE,O.GEIGER,J.H.PRESTEGARD
REMARK 1 TITL NMR INVESTIGATIONS OF THE STRUCTURAL PROPERTIES OF THE
REMARK 1 TITL 2 NODULATION PROTEIN, NODF, FROM RHIZOBIUM LEGUMINOSARUM AND
REMARK 1 TITL 3 ITS HOMOLOGY WITH ESCHERICIA COLI ACYL CARRIER PROTEIN
REMARK 1 REF FEBS LETT. V. 388 66 1996
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/0014-5793(96)00512-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98, POSE
REMARK 3 AUTHORS : MSI (FELIX), FOWLER (POSE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SECONDARY STRUCTURAL ELEMENTS (3
REMARK 3 HELICES) WERE IDENTIFIED. THESE WERE SPLIT INTO SMALLER
REMARK 3 FRAGMENTS AND INDIVIDUAL FRAGMENTS WERE ORIENTED USING RESIDUAL
REMARK 3 DIPOLAR COUPLING DATA AND THE PROGRAM ORDERTEN_SVD (LOSONCZI, ET
REMARK 3 AL., J. MAGN. RES., 138, 334-342, 1999). THE FRAGMENTS WERE
REMARK 3 REASSEMBLED AND THEN POSITIONED SPATIALLY BY TRANSLATION USING A
REMARK 3 LIMITED SET OF NOES TO PRODUCE A BACKBONE FOLD OF THE NODF
REMARK 3 PROTEIN. THERE ARE N-CA-C ANGLE ERRORS (AS COMPARED TO THE
REMARK 3 STANDARD DICTIONARY) AT RESIDUES 13 AND 80. RESIDUE 80 LIES
REMARK 3 SOMEWHAT OUTSIDE ALLOWED RAMACHANDRAN SPACE. THESE SITES ARE
REMARK 3 POSITIONS WHERE ORIENTED HELICAL FRAGMENTS WERE REASSEMBLED INTO
REMARK 3 COMPLETE HELICES DURING DETERMINATION OF OF THE BACKBONE FOLD
REMARK 3 AND ANY SMALLER LOCAL DISTORTIONS FROM IDEALITY ARE EXPECTED TO
REMARK 3 CONCENTRATE HERE. THE STRUCTURE PRESENTED HERE CONTAINS ONLY
REMARK 3 COORDINATES FOR BACKBONE ATOMS INVOLVED IN SECONDARY STRUCTURE.
REMARK 3 THE STRUCTURE IS THE AVERAGE OF AN ENSEMBLE WITH A HEAVY ATOM
REMARK 3 RMSD OF 2.4 ANGSTROMS. CB POSITIONS COME FROM POLYALANINE
REMARK 3 HELICES USED TO MODEL THE BACKBONE.
REMARK 4
REMARK 4 1FH1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011579.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 6.1; 6.1
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.5 MM NODF ISOTROPIC U-15N,13C
REMARK 210 200 MM PHOSPHATE BUFFER, PH 6.1;
REMARK 210 1.0 MM NODF ALIGNED U-15N,13C
REMARK 210 200 MM PHOSPHATE BUFFER, PH 6.1
REMARK 210 20 MG/ML PF1 BACTERIOPHAGE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ORDERTEN_SVD, POSE
REMARK 210 METHOD USED : OTHER
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: ASSIGNMENTS WERE MADE USING DOUBLE AND TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY. DIPOLAR COUPLINGS WERE MEASURED AND USED TO
REMARK 210 PRODUCE THE PROTEIN BACKBONE FOLD.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ASP A 3
REMARK 465 GLN A 4
REMARK 465 LYS A 18
REMARK 465 ALA A 19
REMARK 465 GLU A 20
REMARK 465 ASN A 21
REMARK 465 GLY A 22
REMARK 465 GLU A 23
REMARK 465 ARG A 24
REMARK 465 THR A 25
REMARK 465 SER A 26
REMARK 465 VAL A 27
REMARK 465 ALA A 28
REMARK 465 LEU A 29
REMARK 465 GLY A 30
REMARK 465 GLU A 31
REMARK 465 ILE A 32
REMARK 465 THR A 33
REMARK 465 THR A 34
REMARK 465 ASP A 35
REMARK 465 THR A 36
REMARK 465 GLU A 37
REMARK 465 LEU A 38
REMARK 465 THR A 39
REMARK 465 SER A 40
REMARK 465 LEU A 41
REMARK 465 GLY A 42
REMARK 465 ILE A 43
REMARK 465 ASP A 44
REMARK 465 SER A 45
REMARK 465 TYR A 59
REMARK 465 GLY A 60
REMARK 465 ILE A 61
REMARK 465 LYS A 62
REMARK 465 ILE A 63
REMARK 465 GLU A 64
REMARK 465 MET A 65
REMARK 465 ASN A 66
REMARK 465 THR A 67
REMARK 465 ALA A 68
REMARK 465 ASP A 69
REMARK 465 ALA A 70
REMARK 465 TRP A 71
REMARK 465 SER A 72
REMARK 465 ASN A 73
REMARK 465 LEU A 74
REMARK 465 ASN A 75
REMARK 465 LEU A 87
REMARK 465 LEU A 88
REMARK 465 THR A 89
REMARK 465 LYS A 90
REMARK 465 GLU A 91
REMARK 465 VAL A 92
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 RES CSSEQI ATOMS
REMARK 470 LEU A 5 CG CD1 CD2
REMARK 470 THR A 6 OG1 CG2
REMARK 470 LEU A 7 CG CD1 CD2
REMARK 470 GLU A 8 CG CD OE1 OE2
REMARK 470 ILE A 9 CG1 CG2 CD1
REMARK 470 ILE A 10 CG1 CG2 CD1
REMARK 470 SER A 11 OG
REMARK 470 ILE A 13 CG1 CG2 CD1
REMARK 470 ASN A 14 CG OD1 ND2
REMARK 470 LYS A 15 CG CD CE NZ
REMARK 470 LEU A 16 CG CD1 CD2
REMARK 470 VAL A 17 CG1 CG2
REMARK 470 LEU A 46 CG CD1 CD2
REMARK 470 LEU A 48 CG CD1 CD2
REMARK 470 ASP A 50 CG OD1 OD2
REMARK 470 VAL A 51 CG1 CG2
REMARK 470 LEU A 52 CG CD1 CD2
REMARK 470 TRP A 53 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 53 CZ3 CH2
REMARK 470 ASP A 54 CG OD1 OD2
REMARK 470 LEU A 55 CG CD1 CD2
REMARK 470 GLU A 56 CG CD OE1 OE2
REMARK 470 GLN A 57 CG CD OE1 NE2
REMARK 470 LEU A 58 CG CD1 CD2
REMARK 470 ASN A 76 CG OD1 ND2
REMARK 470 ILE A 77 CG1 CG2 CD1
REMARK 470 ASP A 79 CG OD1 OD2
REMARK 470 VAL A 80 CG1 CG2
REMARK 470 VAL A 81 CG1 CG2
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 VAL A 84 CG1 CG2
REMARK 470 ARG A 85 CG CD NE CZ NH1 NH2
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 LEU A 7 CB ILE A 10 1.11
REMARK 500 O LEU A 52 H GLU A 56 1.34
REMARK 500 O VAL A 81 H VAL A 84 1.35
REMARK 500 O GLU A 8 H SER A 11 1.45
REMARK 500 O VAL A 81 N ALA A 83 1.74
REMARK 500 O GLU A 8 N SER A 11 1.88
REMARK 500 O LEU A 7 CA ILE A 10 1.95
REMARK 500 C GLU A 8 N ILE A 10 2.05
REMARK 500 O LEU A 7 N ILE A 10 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ILE A 9 N - CA - C ANGL. DEV. = -25.9 DEGREES
REMARK 500 ILE A 13 N - CA - CB ANGL. DEV. = -23.0 DEGREES
REMARK 500 ILE A 13 N - CA - C ANGL. DEV. = 43.9 DEGREES
REMARK 500 ASP A 50 N - CA - C ANGL. DEV. = 29.4 DEGREES
REMARK 500 TRP A 53 N - CA - CB ANGL. DEV. = 20.1 DEGREES
REMARK 500 VAL A 80 N - CA - CB ANGL. DEV. = -52.0 DEGREES
REMARK 500 VAL A 80 N - CA - C ANGL. DEV. = 43.5 DEGREES
REMARK 500 GLU A 82 N - CA - CB ANGL. DEV. = -19.1 DEGREES
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 ASP A 50 -89.30 -99.36
REMARK 500 TRP A 53 -80.70 -44.84
REMARK 500 VAL A 80 7.41 145.50
REMARK 500 GLU A 82 -24.02 -22.06
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FH1 A 1 92 UNP P04685 NODF_RHILV 1 92
SEQRES 1 A 92 MET ALA ASP GLN LEU THR LEU GLU ILE ILE SER ALA ILE
SEQRES 2 A 92 ASN LYS LEU VAL LYS ALA GLU ASN GLY GLU ARG THR SER
SEQRES 3 A 92 VAL ALA LEU GLY GLU ILE THR THR ASP THR GLU LEU THR
SEQRES 4 A 92 SER LEU GLY ILE ASP SER LEU GLY LEU ALA ASP VAL LEU
SEQRES 5 A 92 TRP ASP LEU GLU GLN LEU TYR GLY ILE LYS ILE GLU MET
SEQRES 6 A 92 ASN THR ALA ASP ALA TRP SER ASN LEU ASN ASN ILE GLY
SEQRES 7 A 92 ASP VAL VAL GLU ALA VAL ARG GLY LEU LEU THR LYS GLU
SEQRES 8 A 92 VAL
HELIX 1 1 LEU A 5 VAL A 17 1 13
HELIX 2 2 ASP A 50 LEU A 58 1 9
HELIX 3 3 VAL A 81 GLY A 86 1 6
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
Complete list - 23 202 Bytes