Header list of 2d1u.pdb file
Complete list - p 9 2 Bytes
HEADER METAL TRANSPORT 01-SEP-05 2D1U
TITLE SOLUTION STRUCTURE OF THE PERIPLASMIC SIGNALING DOMAIN OF FECA FROM
TITLE 2 ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IRON(III) DICITRATE TRANSPORT PROTEIN FECA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PERIPLASMIC SIGNALING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: FECA;
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: PET30A
KEYWDS FECA, SURFACE SIGNALING, IRON-UPTAKE, METAL TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.GARCIA-HERRERO,H.J.VOGEL
REVDAT 3 09-SEP-20 2D1U 1 TITLE REMARK SEQADV
REVDAT 2 24-FEB-09 2D1U 1 VERSN
REVDAT 1 27-DEC-05 2D1U 0
JRNL AUTH A.GARCIA-HERRERO,H.J.VOGEL
JRNL TITL NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF THE
JRNL TITL 2 PERIPLASMIC SIGNALLING DOMAIN OF THE TONB-DEPENDENT OUTER
JRNL TITL 3 MEMBRANE TRANSPORTER FECA FROM ESCHERICHIA COLI
JRNL REF MOL.MICROBIOL. V. 58 1226 2005
JRNL REFN ISSN 0950-382X
JRNL PMID 16313612
JRNL DOI 10.1111/J.1365-2958.2005.04889.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0
REMARK 3 AUTHORS : PETER GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D1U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000024883.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 50MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM NTFECA U-15N; 50MM PHOSPHATE
REMARK 210 BUFFER; 90% H20, 10% D2O; 1MM
REMARK 210 NTFECA U-15N, 13C; 50MM
REMARK 210 PHOSPHATE BUFFER PH6; 90% H20,
REMARK 210 10% D2O; 1MM NTFECA U-15N; 50MM
REMARK 210 PHOSPHATE BUFFER; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_ROESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.0, NMRVIEW 5.0.4,
REMARK 210 NMRPIPE 2.3 REV 2004.194.17.02,
REMARK 210 XWINNMR 3.0
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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: 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: 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 PRO A 7 -164.67 -69.78
REMARK 500 1 SER A 9 118.33 179.01
REMARK 500 1 ASP A 28 97.77 -58.40
REMARK 500 1 ARG A 33 100.25 -56.38
REMARK 500 1 HIS A 41 101.43 -161.15
REMARK 500 1 ASP A 45 -175.05 -67.04
REMARK 500 1 ASN A 66 -83.19 -58.98
REMARK 500 1 LYS A 78 104.32 -52.64
REMARK 500 2 PRO A 7 -164.46 -69.80
REMARK 500 2 SER A 9 127.82 179.85
REMARK 500 2 HIS A 41 100.85 -161.00
REMARK 500 2 ASP A 45 -175.16 -60.90
REMARK 500 2 LEU A 64 -61.91 -124.33
REMARK 500 2 ALA A 76 160.96 -49.23
REMARK 500 2 LYS A 78 89.27 51.51
REMARK 500 2 GLU A 79 118.69 -178.83
REMARK 500 2 LEU A 82 74.06 -106.52
REMARK 500 2 LEU A 89 46.56 -90.14
REMARK 500 3 PRO A 7 -164.41 -69.80
REMARK 500 3 SER A 9 121.83 -173.41
REMARK 500 3 ASP A 28 102.08 -51.48
REMARK 500 3 HIS A 41 101.24 -161.44
REMARK 500 3 ASP A 45 -175.96 -59.18
REMARK 500 3 LEU A 64 -64.41 -125.14
REMARK 500 3 ASN A 66 91.34 -68.74
REMARK 500 3 ASP A 80 -176.95 -58.83
REMARK 500 3 LEU A 82 55.24 -102.70
REMARK 500 3 TRP A 88 97.94 58.59
REMARK 500 3 ASP A 91 53.77 -116.51
REMARK 500 4 PRO A 7 -160.85 -69.69
REMARK 500 4 SER A 9 117.44 -179.54
REMARK 500 4 ASP A 28 94.28 -63.97
REMARK 500 4 HIS A 41 101.01 -160.69
REMARK 500 4 ASP A 45 -174.74 -60.27
REMARK 500 4 LEU A 64 -62.38 -124.74
REMARK 500 4 ASN A 66 86.74 -68.12
REMARK 500 5 PRO A 7 -164.61 -69.76
REMARK 500 5 SER A 9 123.14 179.44
REMARK 500 5 SER A 21 -65.69 -90.92
REMARK 500 5 ASP A 28 97.81 -57.24
REMARK 500 5 HIS A 41 101.54 -162.21
REMARK 500 5 ASP A 45 -175.33 -59.65
REMARK 500 5 LEU A 64 -62.09 -123.54
REMARK 500 5 GLU A 94 129.80 -171.73
REMARK 500 5 ASN A 95 135.43 -173.19
REMARK 500 5 LEU A 97 116.03 -166.82
REMARK 500 5 GLU A 98 113.13 -164.32
REMARK 500 5 HIS A 100 -73.95 -84.21
REMARK 500 6 PRO A 7 -165.07 -69.79
REMARK 500 6 SER A 9 121.45 179.59
REMARK 500
REMARK 500 THIS ENTRY HAS 185 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6803 RELATED DB: BMRB
DBREF 2D1U A 1 96 UNP P13036 FECA_ECOLI 34 129
SEQADV 2D1U LEU A 97 UNP P13036 EXPRESSION TAG
SEQADV 2D1U GLU A 98 UNP P13036 EXPRESSION TAG
SEQADV 2D1U HIS A 99 UNP P13036 EXPRESSION TAG
SEQADV 2D1U HIS A 100 UNP P13036 EXPRESSION TAG
SEQADV 2D1U HIS A 101 UNP P13036 EXPRESSION TAG
SEQADV 2D1U HIS A 102 UNP P13036 EXPRESSION TAG
SEQADV 2D1U HIS A 103 UNP P13036 EXPRESSION TAG
SEQADV 2D1U HIS A 104 UNP P13036 EXPRESSION TAG
SEQRES 1 A 104 ALA GLN VAL ASN ILE ALA PRO GLY SER LEU ASP LYS ALA
SEQRES 2 A 104 LEU ASN GLN TYR ALA ALA HIS SER GLY PHE THR LEU SER
SEQRES 3 A 104 VAL ASP ALA SER LEU THR ARG GLY LYS GLN SER ASN GLY
SEQRES 4 A 104 LEU HIS GLY ASP TYR ASP VAL GLU SER GLY LEU GLN GLN
SEQRES 5 A 104 LEU LEU ASP GLY SER GLY LEU GLN VAL LYS PRO LEU GLY
SEQRES 6 A 104 ASN ASN SER TRP THR LEU GLU PRO ALA PRO ALA PRO LYS
SEQRES 7 A 104 GLU ASP ALA LEU THR VAL VAL GLY ASP TRP LEU GLY ASP
SEQRES 8 A 104 ALA ARG GLU ASN ASP LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 SER A 9 GLY A 22 1 14
HELIX 2 2 ASP A 28 ARG A 33 1 6
HELIX 3 3 ASP A 45 LEU A 54 1 10
SHEET 1 A 2 GLN A 2 ASN A 4 0
SHEET 2 A 2 HIS A 41 ASP A 43 -1 O GLY A 42 N VAL A 3
SHEET 1 B 3 THR A 24 LEU A 25 0
SHEET 2 B 3 SER A 68 PRO A 73 1 O TRP A 69 N THR A 24
SHEET 3 B 3 LEU A 59 PRO A 63 -1 N GLN A 60 O GLU A 72
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
Complete list - p 9 2 Bytes