HEADER ELECTRON TRANSPORT 12-JUL-06 2HNB
TITLE SOLUTION STRUCTURE OF A BACTERIAL HOLO-FLAVODOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN MIOC;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FLAVODOXIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
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_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21A(+)
KEYWDS ALPHA-BETA SANDWICH, FLAVODOXIN FOLD, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR Y.HU,C.JIN
REVDAT 5 09-MAR-22 2HNB 1 REMARK
REVDAT 4 24-FEB-09 2HNB 1 VERSN
REVDAT 3 15-MAY-07 2HNB 3 ATOM
REVDAT 2 15-MAY-07 2HNB 1 JRNL
REVDAT 1 19-SEP-06 2HNB 0
JRNL AUTH Y.HU,Y.LI,X.ZHANG,X.GUO,B.XIA,C.JIN
JRNL TITL SOLUTION STRUCTURES AND BACKBONE DYNAMICS OF A FLAVODOXIN
JRNL TITL 2 MIOC FROM ESCHERICHIA COLI IN BOTH APO- AND HOLO-FORMS:
JRNL TITL 3 IMPLICATIONS FOR COFACTOR BINDING AND ELECTRON TRANSFER
JRNL REF J.BIOL.CHEM. V. 281 35454 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16963438
JRNL DOI 10.1074/JBC.M607336200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), CASE, D. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HNB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038540.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 30MM NACL, 30MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HOLO-FLAVODOXIN U-15N; 30MM
REMARK 210 PHOSPHATE BUFFER NA; 30MM NACL;
REMARK 210 50MM FMN; 90% H2O, 10% D2O; 1MM
REMARK 210 HOLO-FLAVODOXIN U-15N,13C; 30MM
REMARK 210 PHOSPHATE BUFFER NA; 30MM NACL;
REMARK 210 50MM FMN; 90% H2O, 10% 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; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5, CYANA
REMARK 210 2.0
REMARK 210 METHOD USED : MOLECULAR DYNAMICS, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: 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 OD1 ASP A 79 HG SER A 81 1.55
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 1 GLU A 20 OE1 - CD - OE2 ANGL. DEV. = -45.3 DEGREES
REMARK 500 1 GLU A 20 CG - CD - OE1 ANGL. DEV. = 43.5 DEGREES
REMARK 500 1 GLU A 20 CG - CD - OE2 ANGL. DEV. = -34.5 DEGREES
REMARK 500 1 ASP A 64 OD1 - CG - OD2 ANGL. DEV. = -45.0 DEGREES
REMARK 500 1 ASP A 64 CB - CG - OD1 ANGL. DEV. = 43.2 DEGREES
REMARK 500 1 ASP A 64 CB - CG - OD2 ANGL. DEV. = -35.1 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 1 GLU A 42 2.10 -66.35
REMARK 500 1 LYS A 77 62.82 26.73
REMARK 500 1 SER A 81 10.80 -63.96
REMARK 500 1 PHE A 98 64.27 -153.04
REMARK 500 1 ILE A 130 129.46 51.72
REMARK 500 1 GLU A 132 -13.57 -148.31
REMARK 500 2 LYS A 77 66.11 37.74
REMARK 500 2 SER A 81 18.62 -61.58
REMARK 500 2 THR A 97 51.15 -119.32
REMARK 500 2 ASP A 133 72.02 -152.87
REMARK 500 3 LYS A 77 64.30 27.31
REMARK 500 3 LEU A 80 34.98 -74.66
REMARK 500 3 SER A 81 23.42 -61.75
REMARK 500 3 PHE A 98 83.36 -67.52
REMARK 500 3 ASP A 127 -130.54 -149.71
REMARK 500 3 GLU A 132 -16.32 -155.51
REMARK 500 4 THR A 35 73.15 -108.81
REMARK 500 4 LYS A 77 57.22 30.53
REMARK 500 4 SER A 81 19.97 -63.31
REMARK 500 4 SER A 92 140.92 115.01
REMARK 500 4 ARG A 93 0.84 -67.81
REMARK 500 4 ASP A 127 -54.14 -144.82
REMARK 500 4 PRO A 131 170.57 -57.55
REMARK 500 5 ASP A 96 -16.31 66.57
REMARK 500 5 THR A 97 171.66 59.78
REMARK 500 5 ILE A 102 -34.10 -141.15
REMARK 500 5 ASP A 127 -42.18 -153.03
REMARK 500 5 ILE A 130 52.83 35.61
REMARK 500 5 ASP A 133 65.50 -152.82
REMARK 500 6 LEU A 12 -30.29 -140.57
REMARK 500 6 HIS A 57 19.61 45.08
REMARK 500 6 ALA A 59 -9.09 -147.82
REMARK 500 6 LYS A 77 60.54 39.71
REMARK 500 6 SER A 81 10.95 -51.57
REMARK 500 6 ASP A 127 -7.39 -142.68
REMARK 500 6 GLU A 132 24.32 -70.95
REMARK 500 7 THR A 11 -41.40 -133.42
REMARK 500 7 SER A 81 20.00 -61.00
REMARK 500 7 ASP A 96 -47.06 -162.87
REMARK 500 7 HIS A 128 34.84 -159.76
REMARK 500 7 ASP A 129 -25.16 67.87
REMARK 500 8 ALA A 46 4.67 -69.71
REMARK 500 8 LYS A 77 57.92 31.00
REMARK 500 8 SER A 81 4.67 -57.87
REMARK 500 8 ASP A 96 -49.02 -171.61
REMARK 500 8 ASP A 129 12.77 -143.17
REMARK 500 8 ILE A 130 56.51 34.91
REMARK 500 8 ASP A 133 57.89 37.94
REMARK 500 9 HIS A 37 99.96 -69.29
REMARK 500 9 LYS A 77 59.06 36.55
REMARK 500
REMARK 500 THIS ENTRY HAS 144 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 97 PHE A 98 1 -129.44
REMARK 500 ASP A 129 ILE A 130 1 -140.88
REMARK 500 PRO A 131 GLU A 132 1 -141.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HNA RELATED DB: PDB
REMARK 900 APO-FORM OF THE SAME PROTEIN
DBREF 2HNB A 1 147 UNP P03817 MIOC_ECOLI 1 147
SEQRES 1 A 147 MET ALA ASP ILE THR LEU ILE SER GLY SER THR LEU GLY
SEQRES 2 A 147 GLY ALA GLU TYR VAL ALA GLU HIS LEU ALA GLU LYS LEU
SEQRES 3 A 147 GLU GLU ALA GLY PHE THR THR GLU THR LEU HIS GLY PRO
SEQRES 4 A 147 LEU LEU GLU ASP LEU PRO ALA SER GLY ILE TRP LEU VAL
SEQRES 5 A 147 ILE SER SER THR HIS GLY ALA GLY ASP ILE PRO ASP ASN
SEQRES 6 A 147 LEU SER PRO PHE TYR GLU ALA LEU GLN GLU GLN LYS PRO
SEQRES 7 A 147 ASP LEU SER ALA VAL ARG PHE GLY ALA ILE GLY ILE GLY
SEQRES 8 A 147 SER ARG GLU TYR ASP THR PHE CYS GLY ALA ILE ASP LYS
SEQRES 9 A 147 LEU GLU ALA GLU LEU LYS ASN SER GLY ALA LYS GLN THR
SEQRES 10 A 147 GLY GLU THR LEU LYS ILE ASN ILE LEU ASP HIS ASP ILE
SEQRES 11 A 147 PRO GLU ASP PRO ALA GLU GLU TRP LEU GLY SER TRP VAL
SEQRES 12 A 147 ASN LEU LEU LYS
HELIX 1 1 GLY A 13 GLY A 30 1 18
HELIX 2 2 LEU A 40 LEU A 44 5 5
HELIX 3 3 SER A 67 LYS A 77 1 11
HELIX 4 4 GLY A 100 GLY A 113 1 14
HELIX 5 5 PRO A 134 LYS A 147 1 14
SHEET 1 A 5 THR A 33 HIS A 37 0
SHEET 2 A 5 ILE A 4 SER A 8 1 N LEU A 6 O GLU A 34
SHEET 3 A 5 SER A 47 SER A 55 1 O LEU A 51 N ILE A 7
SHEET 4 A 5 ALA A 82 GLY A 91 1 O ARG A 84 N GLY A 48
SHEET 5 A 5 LYS A 115 GLN A 116 1 O LYS A 115 N VAL A 83
SHEET 1 B 5 THR A 33 HIS A 37 0
SHEET 2 B 5 ILE A 4 SER A 8 1 N LEU A 6 O GLU A 34
SHEET 3 B 5 SER A 47 SER A 55 1 O LEU A 51 N ILE A 7
SHEET 4 B 5 ALA A 82 GLY A 91 1 O ARG A 84 N GLY A 48
SHEET 5 B 5 LEU A 121 ASN A 124 1 O LEU A 121 N GLY A 89
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
