Header list of 1nd9.pdb file
Complete list - 23 20 Bytes
HEADER TRANSLATION 09-DEC-02 1ND9
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL SUBDOMAIN OF TRANSLATION
TITLE 2 INITIATION FACTOR IF2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSLATION INITIATION FACTOR IF-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: K12;
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: PET15B
KEYWDS IF2, TRANSLATION, INITIATION FACTOR
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR B.S.LAURSEN,K.K.MORTENSEN,H.U.SPERLING-PETERSEN,D.W.HOFFMAN
REVDAT 4 23-FEB-22 1ND9 1 REMARK
REVDAT 3 24-FEB-09 1ND9 1 VERSN
REVDAT 2 25-JAN-05 1ND9 1 JRNL
REVDAT 1 04-MAR-03 1ND9 0
JRNL AUTH B.S.LAURSEN,K.K.MORTENSEN,H.U.SPERLING-PETERSEN,D.W.HOFFMAN
JRNL TITL A CONSERVED STRUCTURAL MOTIF AT THE N TERMINUS OF BACTERIAL
JRNL TITL 2 TRANSLATION INITIATION FACTOR IF2
JRNL REF J.BIOL.CHEM. V. 278 16320 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12600987
JRNL DOI 10.1074/JBC.M212960200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 1.0, CNS 1.1
REMARK 3 AUTHORS : HARE RESEARCH INC. (FELIX), BRUNGER, A.T., ADAMS,
REMARK 3 P.D., CLORE, G.M., DELANO, W.L., GROS, P., GROSSE-
REMARK 3 KUNSTLEVE, R.W., JIANG, J.S., KUSZEWSKI, J.,
REMARK 3 NILGES, M., PANNU, N.S., READ, R.J., RICE, L.M.,
REMARK 3 SIMONSON, T. AND WARREN, G.L. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 996 RESTRAINTS, 918 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 63 DIHEDRAL ANGLE RESTRAINTS,15 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1ND9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017779.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 308
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 10 MM PHOSPHATE; 10 MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM IF2 (RES 2-157); 10 MM
REMARK 210 PHOSPHATE BUFFER; 2MM IF2 (RES 2-
REMARK 210 157); 10 MM PHOSPHATE BUFFER;
REMARK 210 2MM IF2 (RES 2-157); 15N; 10 MM
REMARK 210 PHOSPHATE BUFFER; 2MM IF2 (RES 2-
REMARK 210 157); 15N;13C; 10 MM PHOSPHATE
REMARK 210 BUFFER; 2MM IF2 (RES 2-157); K-
REMARK 210 15N; 10 MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.0, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 HA PHE A 24 HB1 ALA A 27 1.33
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 LYS A 7 -64.25 97.30
REMARK 500 1 GLU A 12 -71.55 -33.71
REMARK 500 1 GLN A 14 -48.59 84.23
REMARK 500 1 SER A 16 -89.22 -131.91
REMARK 500 1 ALA A 27 -77.40 -54.16
REMARK 500 1 ALA A 33 43.13 96.40
REMARK 500 1 ASP A 34 105.04 61.35
REMARK 500 1 ASP A 35 -109.08 166.71
REMARK 500 1 LYS A 42 -25.62 -32.73
REMARK 500 1 GLN A 43 -13.67 -47.75
REMARK 500 2 LYS A 7 -77.27 97.89
REMARK 500 2 GLU A 12 -71.54 -30.24
REMARK 500 2 GLN A 14 -28.32 84.79
REMARK 500 2 SER A 16 -89.27 -127.94
REMARK 500 2 GLN A 22 -70.22 -61.15
REMARK 500 2 ALA A 27 -72.75 -44.39
REMARK 500 2 ALA A 33 55.17 91.74
REMARK 500 2 ASP A 34 102.87 58.26
REMARK 500 2 ASP A 35 -141.09 175.86
REMARK 500 2 LYS A 42 -48.63 11.61
REMARK 500 2 GLN A 43 -19.79 -39.98
REMARK 500 2 LEU A 49 -70.02 -50.32
REMARK 500 3 LYS A 7 -71.47 96.01
REMARK 500 3 GLU A 12 -72.52 -34.46
REMARK 500 3 GLN A 14 -52.52 81.30
REMARK 500 3 SER A 16 -91.00 -129.76
REMARK 500 3 ALA A 27 -74.57 -48.23
REMARK 500 3 ALA A 33 55.08 89.16
REMARK 500 3 ASP A 34 97.73 58.53
REMARK 500 3 ASP A 35 -113.26 173.24
REMARK 500 3 LYS A 42 -30.53 -24.73
REMARK 500 3 GLN A 43 -16.86 -44.28
REMARK 500 3 LEU A 49 -70.15 -56.66
REMARK 500 4 LYS A 7 -73.38 103.12
REMARK 500 4 GLU A 12 -67.61 -27.04
REMARK 500 4 GLN A 14 113.88 81.72
REMARK 500 4 SER A 16 -99.76 -130.17
REMARK 500 4 GLN A 22 -70.40 -61.45
REMARK 500 4 ALA A 27 -75.12 -49.50
REMARK 500 4 ALA A 33 48.40 91.04
REMARK 500 4 ASP A 34 109.09 59.85
REMARK 500 4 ASP A 35 -105.46 163.09
REMARK 500 4 LYS A 42 -53.83 9.12
REMARK 500 4 GLN A 43 -23.28 -37.88
REMARK 500 4 ASP A 47 -70.29 -57.14
REMARK 500 4 LEU A 49 -70.02 -53.98
REMARK 500 5 LYS A 7 -79.34 96.84
REMARK 500 5 GLN A 14 -32.01 86.49
REMARK 500 5 SER A 16 -88.31 -129.60
REMARK 500 5 GLN A 22 -70.28 -63.04
REMARK 500
REMARK 500 THIS ENTRY HAS 105 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ND9 A 2 50 UNP P0A705 IF2_ECOLI 2 50
SEQRES 1 A 49 THR ASP VAL THR ILE LYS THR LEU ALA ALA GLU ARG GLN
SEQRES 2 A 49 THR SER VAL GLU ARG LEU VAL GLN GLN PHE ALA ASP ALA
SEQRES 3 A 49 GLY ILE ARG LYS SER ALA ASP ASP SER VAL SER ALA GLN
SEQRES 4 A 49 GLU LYS GLN THR LEU ILE ASP HIS LEU ASN
HELIX 1 1 LYS A 7 GLN A 14 1 8
HELIX 2 2 SER A 16 GLY A 28 1 13
HELIX 3 3 GLN A 40 LYS A 42 5 3
HELIX 4 4 GLN A 43 ASN A 50 1 8
SHEET 1 A 2 ASP A 3 VAL A 4 0
SHEET 2 A 2 VAL A 37 SER A 38 -1 O VAL A 37 N VAL A 4
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 - 23 20 Bytes