Header list of 2fz5.pdb file
Complete list - 9 20 Bytes
HEADER ELECTRON TRANSPORT 09-FEB-06 2FZ5
TITLE SOLUTION STRUCTURE OF TWO-ELECTRON REDUCED MEGASPHAERA ELSDENII
TITLE 2 FLAVODOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAVODOXIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MEGASPHAERA ELSDENII;
SOURCE 3 ORGANISM_TAXID: 907
KEYWDS ALPHA/BETA DOUBLY-WOUND TOPOLOGY, NON-COVALENTLY BOUND FMN, ELECTRON
KEYWDS 2 TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR C.P.M.VAN MIERLO,P.LIJNZAAD,J.VERVOORT,F.MUELLER,H.J.BERENDSEN,J.DE
AUTHOR 2 VLIEG
REVDAT 4 09-MAR-22 2FZ5 1 REMARK
REVDAT 3 24-FEB-09 2FZ5 1 VERSN
REVDAT 2 11-APR-06 2FZ5 1 FORMUL
REVDAT 1 14-MAR-06 2FZ5 0
JRNL AUTH C.P.M.VAN MIERLO,P.LIJNZAAD,J.VERVOORT,F.MUELLER,
JRNL AUTH 2 H.J.BERENDSEN,J.DE VLIEG
JRNL TITL TERTIARY STRUCTURE OF TWO-ELECTRON REDUCED MEGASPHAERA
JRNL TITL 2 ELSDENII FLAVODOXIN AND SOME IMPLICATIONS, AS DETERMINED BY
JRNL TITL 3 TWO-DIMENSIONAL 1H NMR AND RESTRAINED MOLECULAR DYNAMICS
JRNL REF EUR.J.BIOCHEM. V. 194 185 1990
JRNL REFN ISSN 0014-2956
JRNL PMID 2253614
JRNL DOI 10.1111/J.1432-1033.1990.TB19444.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.P.M.VAN MIERLO,F.MUELLER,J.VERVOORT
REMARK 1 TITL SECONDARY AND TERTIARY STRUCTURE CHARACTERISTICS OF
REMARK 1 TITL 2 MEGASPHAERA ELSDENII FLAVODOXIN IN THE REDUCED STATE AS
REMARK 1 TITL 3 DETERMINED BY TWO-DIMENSIONAL 1H NMR
REMARK 1 REF EUR.J.BIOCHEM. V. 189 589 1990
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 2161759
REMARK 1 DOI 10.1111/J.1432-1033.1990.TB15527.X
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.P.M.VAN MIERLO,J.VERVOORT,F.MUELLER,A.BACHER
REMARK 1 TITL A TWO-DIMENSIONAL 1H NMR STUDY ON MEGASPHAERA ELSDENII
REMARK 1 TITL 2 FLAVODOXIN IN THE REDUCED STATE: SEQUENTIAL ASSIGNMENTS
REMARK 1 REF EUR.J.BIOCHEM. V. 187 521 1990
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 2303055
REMARK 1 DOI 10.1111/J.1432-1033.1990.TB15334.X
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.P.M.VAN MIERLO,B.P.VAN DER SANDEN,P.VAN WOENSEL,F.MUELLER,
REMARK 1 AUTH 2 J.VERVOORT
REMARK 1 TITL A TWO-DIMENSIONAL 1H NMR STUDY ON MEGASPHAERA ELSDENII
REMARK 1 TITL 2 FLAVODOXIN IN THE OXIDIZED STATE AND SOME COMPARISONS WITH
REMARK 1 TITL 3 THE TWO-ELECTRON REDUCED STATE
REMARK 1 REF EUR.J.BIOCHEM. V. 194 199 1990
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 2253616
REMARK 1 DOI 10.1111/J.1432-1033.1990.TB19445.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISNMR, GROMOS
REMARK 3 AUTHORS : BRUKER (DISNMR), VAN GUNSTEREN AND BERENDSEN
REMARK 3 (GROMOS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE XRAY STRUCTURE OF THE SEMIQUINONE STATE OF CLOSTRIDIUM MP
REMARK 3 FLAVODOXIN WAS USED AS A STARTING STRUCTURE
REMARK 3 FOR RESTRAINED MOLECULAR DYNAMICS (RMD) CALCULATIONS IN VACUO (VAN
REMARK 3 MIERLO ET AL. EUR. J. BIOCHEM. 194, 185 - 198 (1990)).
REMARK 3 509 DISTANCE RESTRAINTS, 293 MEDIUM, 216 LONG-RANGE WERE USED IN
REMARK 3 REFINEMENT. ONE
REMARK 3 REPULSIVE RESTRAINT, BETWEEN N5H OF FMN AND NH OF E60 WAS
REMARK 3 INCLUDED. RMD RUN WAS OF 120 PS. DURING THE FIRST 50 PS
REMARK 3 THE FORCE CONSTANT WAS GRADUALLY INCREASED TO A HIGH VALUE OF 4000
REMARK 3 KJMOL-1NM-2. FROM 50 PS ON, THE FORCE CONSTANT WAS KEPT
REMARK 3 CONSTANT. THE TIME SPAN OF 60-120 PS, AT A TIME RESOLUTION OF 0.02
REMARK 3 PS, WAS USED FOR CALCULATING
REMARK 3 THE AVERAGE STRUCTURE. THE TIME-AVERAGED (NOT ENERGY MINIMISED)
REMARK 3 STRUCTURE HAS A POTENTIAL ENERGY
REMARK 3 -2278 +/- 122 KJMOL-1, TIME-AVERAGED SUM OF ALL VIOLATIONS IS 2.27
REMARK 3 NM, LARGEST
REMARK 3 OCCURING VIOLATION IS 66 PM
REMARK 4
REMARK 4 2FZ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036485.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 306; 310; 314; 316
REMARK 210 PH : 8.3; 8.3; 8.3; 8.3; 8.3
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL; NULL; NULL
REMARK 210 PRESSURE : NULL; NULL; NULL; NULL; NULL
REMARK 210 SAMPLE CONTENTS : 6-10 MM PROTEIN, POTASSIUM
REMARK 210 PHOSPHATE/POTASSIUM
REMARK 210 PYROPHOSPHATE 75-200 MM, PH 8.3,
REMARK 210 90% H2O, 10% D2O; 6-10 MM
REMARK 210 PROTEIN, POTASSIUM PHOSPHATE/
REMARK 210 POTASSIUM PYROPHOSPHATE 75-200
REMARK 210 MM, PH 8.3, 99.9% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; DOUBLE QUANTUM FILTERED
REMARK 210 COSY; NOESY (MIXING 200MS);
REMARK 210 NOESY (MIXING 50, 100, 150 MS);
REMARK 210 DOUBLE QUANTUM SPECTRA;
REMARK 210 HOMONUCLEAR HARTMANN HAHN
REMARK 210 TRANSFER SPECTRA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : WM; AM
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GROMOS
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 3000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NOESY SPECTRA HAD MIXING TIMES 50, 100, 150 AND 200 MS.
REMARK 210 DOUBLE QUANTUM SPECTRA HAD A DELAY OF 32 MS. HOMONUCLEAR
REMARK 210 HARTMANN HAHN TRANSFER SPECTRA (USING MLEV-17 COMPOSITE PULSE
REMARK 210 CYCLING) HAD MIXING TIMES 10-160 MS
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 TRP A 7 HG1 THR A 13 1.60
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 ASN A 118 OD1 - CG - ND2 ANGL. DEV. = -25.0 DEGREES
REMARK 500 ASN A 118 CB - CG - OD1 ANGL. DEV. = 14.1 DEGREES
REMARK 500 ASN A 118 CB - CG - ND2 ANGL. DEV. = -15.9 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 VAL A 66 -59.74 -122.38
REMARK 500 LEU A 78 59.95 -107.44
REMARK 500 LYS A 81 152.19 -49.43
REMARK 500 ILE A 112 53.61 -90.64
REMARK 500 GLU A 119 -73.62 62.31
REMARK 500 PRO A 121 -177.13 -63.04
REMARK 500 ASP A 122 -37.11 72.66
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 ARG A 35 0.11 SIDE CHAIN
REMARK 500 PHE A 70 0.08 SIDE CHAIN
REMARK 500 PHE A 71 0.08 SIDE CHAIN
REMARK 500 ASN A 118 0.16 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 TRP A 96 -10.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNR A 138
DBREF 2FZ5 A 1 137 UNP P00321 FLAV_MEGEL 1 137
SEQRES 1 A 137 MET VAL GLU ILE VAL TYR TRP SER GLY THR GLY ASN THR
SEQRES 2 A 137 GLU ALA MET ALA ASN GLU ILE GLU ALA ALA VAL LYS ALA
SEQRES 3 A 137 ALA GLY ALA ASP VAL GLU SER VAL ARG PHE GLU ASP THR
SEQRES 4 A 137 ASN VAL ASP ASP VAL ALA SER LYS ASP VAL ILE LEU LEU
SEQRES 5 A 137 GLY CYS PRO ALA MET GLY SER GLU GLU LEU GLU ASP SER
SEQRES 6 A 137 VAL VAL GLU PRO PHE PHE THR ASP LEU ALA PRO LYS LEU
SEQRES 7 A 137 LYS GLY LYS LYS VAL GLY LEU PHE GLY SER TYR GLY TRP
SEQRES 8 A 137 GLY SER GLY GLU TRP MET ASP ALA TRP LYS GLN ARG THR
SEQRES 9 A 137 GLU ASP THR GLY ALA THR VAL ILE GLY THR ALA ILE VAL
SEQRES 10 A 137 ASN GLU MET PRO ASP ASN ALA PRO GLU CYS LYS GLU LEU
SEQRES 11 A 137 GLY GLU ALA ALA ALA LYS ALA
HET FNR A 138 37
HETNAM FNR 1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-
HETNAM 2 FNR BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-
HETNAM 3 FNR RIBITOL
HETSYN FNR TWO ELECTRON REDUCED FLAVIN MONONUCLEOTIDE
FORMUL 2 FNR C17 H23 N4 O9 P
HELIX 1 1 GLY A 11 ALA A 27 1 17
HELIX 2 2 ASN A 40 SER A 46 1 7
HELIX 3 3 GLU A 63 ALA A 75 1 13
HELIX 4 4 PRO A 76 LEU A 78 5 3
HELIX 5 5 GLY A 94 THR A 107 1 14
HELIX 6 6 PRO A 125 LYS A 136 1 12
SHEET 1 A 5 VAL A 31 ARG A 35 0
SHEET 2 A 5 VAL A 2 TYR A 6 1 N VAL A 2 O GLU A 32
SHEET 3 A 5 VAL A 49 GLY A 53 1 O LEU A 51 N VAL A 5
SHEET 4 A 5 LYS A 82 TYR A 89 1 O LYS A 82 N ILE A 50
SHEET 5 A 5 THR A 110 ASN A 118 1 O VAL A 117 N TYR A 89
SITE 1 AC1 15 TRP A 7 GLY A 9 THR A 10 ASN A 12
SITE 2 AC1 15 PRO A 55 ALA A 56 MET A 57 GLY A 58
SITE 3 AC1 15 GLU A 60 SER A 88 TYR A 89 GLY A 90
SITE 4 AC1 15 TRP A 91 GLY A 92 GLU A 119
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 - 9 20 Bytes