Header list of 1n88.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSLATION 20-NOV-02 1N88
TITLE NMR STRUCTURE OF THE RIBOSOMAL PROTEIN L23 FROM THERMUS THERMOPHILUS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSOMAL PROTEIN L23;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
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: PET11C
KEYWDS NMR SPECTROSCOPY, PROTEIN STRUCTURE, L23, RIBOSOME, TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 29
AUTHOR A.OHMAN,A.RAK,M.DONTSOVA,M.B.GARBER,T.HARD
REVDAT 3 23-FEB-22 1N88 1 REMARK
REVDAT 2 24-FEB-09 1N88 1 VERSN
REVDAT 1 10-JUN-03 1N88 0
JRNL AUTH A.OHMAN,A.RAK,M.DONTSOVA,M.B.GARBER,T.HARD
JRNL TITL NMR STRUCTURE OF THE RIBOSOMAL PROTEIN L23 FROM THERMUS
JRNL TITL 2 THERMOPHILUS.
JRNL REF J.BIOMOL.NMR V. 26 131 2003
JRNL REFN ISSN 0925-2738
JRNL PMID 12766408
JRNL DOI 10.1023/A:1023502307069
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISTANCE RESTRAINTS: 1660
REMARK 3 DIHEDRAL ANGLE RESTRAINTS: 61
REMARK 4
REMARK 4 1N88 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017641.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.1
REMARK 210 IONIC STRENGTH : 0.2M LICL2
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8MM L23 U-15N,13C; 50MM
REMARK 210 KH2PO4, PH=5.1, 200MM LICL2;
REMARK 210 0.8MM L23 U-15N; 50MM KH2PO4, PH=
REMARK 210 5.1, 200MM LICL2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY;
REMARK 210 CBCANH,CBCA(CO)NH,HNCO,HNCA,HN(CO)CA,C(CO)NH,HC(CO)NH,HCCH-COSY,
REMARK 210 HCCH-TOCSY; 3D_15N-SEPARATED_NOESY; 2D 15N-HSQC,3D 15N-DIPSI-
REMARK 210 HSQC; 2D 1H-DQF-COSY, 2D 1H-CLEAN-TOCSY, 2D 1H-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, NMRPIPE 2.1, ANSIG
REMARK 210 1.02, AQUA 3.2, TALOS
REMARK 210 1999.019.15.47, MOLMOL 2K.1
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 29
REMARK 210 CONFORMERS, SELECTION CRITERIA : ACCEPT.INP (XPLOR), LOW ENERGY
REMARK 210 AND GOOD RAMACHANDRAN BEHAVIOUR.
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: 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 57 H LYS A 78 1.46
REMARK 500 O ASN A 55 H ILE A 80 1.48
REMARK 500 H VAL A 59 O ARG A 76 1.49
REMARK 500 O SER A 14 H TYR A 18 1.49
REMARK 500 H ASN A 55 O ILE A 80 1.53
REMARK 500 H VAL A 52 O GLN A 82 1.56
REMARK 500 O ALA A 17 H PHE A 21 1.57
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 THR A 3 -104.87 -108.64
REMARK 500 1 TYR A 5 -139.92 -52.83
REMARK 500 1 VAL A 7 -109.11 -51.41
REMARK 500 1 LEU A 9 -93.60 -75.42
REMARK 500 1 ALA A 22 -38.26 -38.31
REMARK 500 1 LYS A 33 -34.18 179.30
REMARK 500 1 ALA A 34 92.49 -44.27
REMARK 500 1 VAL A 49 -163.94 -116.88
REMARK 500 1 LYS A 53 119.11 169.68
REMARK 500 1 LYS A 62 -79.43 -45.14
REMARK 500 1 LYS A 64 32.94 38.56
REMARK 500 1 ARG A 65 -49.47 -160.56
REMARK 500 1 LEU A 66 104.45 53.56
REMARK 500 1 ARG A 68 -173.07 -51.80
REMARK 500 1 TYR A 69 102.76 -42.26
REMARK 500 1 LEU A 70 40.36 -157.31
REMARK 500 1 LYS A 72 142.10 65.84
REMARK 500 1 ARG A 73 103.91 -42.59
REMARK 500 1 PRO A 74 -166.48 -77.16
REMARK 500 1 ALA A 84 178.79 -57.34
REMARK 500 1 LYS A 88 105.55 179.68
REMARK 500 2 LYS A 2 76.71 -64.76
REMARK 500 2 THR A 3 -97.41 -120.59
REMARK 500 2 TYR A 5 -28.30 -34.04
REMARK 500 2 ASP A 6 -51.27 -164.00
REMARK 500 2 LEU A 9 -97.47 -79.04
REMARK 500 2 TYR A 18 -38.62 -139.18
REMARK 500 2 LYS A 33 -33.88 179.73
REMARK 500 2 ALA A 34 95.46 -42.42
REMARK 500 2 THR A 35 134.27 -39.39
REMARK 500 2 ALA A 46 -67.44 -104.23
REMARK 500 2 VAL A 49 -158.98 -123.56
REMARK 500 2 LYS A 53 119.85 169.12
REMARK 500 2 LEU A 66 100.10 -41.79
REMARK 500 2 TYR A 69 113.65 50.72
REMARK 500 2 LYS A 72 111.52 56.77
REMARK 500 2 ARG A 73 77.27 44.16
REMARK 500 2 PRO A 74 -165.01 -77.40
REMARK 500 2 ALA A 84 179.03 -49.16
REMARK 500 2 LYS A 88 108.56 179.43
REMARK 500 2 ILE A 89 91.62 -51.11
REMARK 500 3 THR A 3 -105.71 -108.87
REMARK 500 3 TYR A 5 -140.46 -52.54
REMARK 500 3 ASP A 6 -58.43 -29.87
REMARK 500 3 VAL A 7 -109.49 -52.71
REMARK 500 3 LEU A 9 -88.22 -92.06
REMARK 500 3 LYS A 33 -33.65 179.48
REMARK 500 3 ALA A 34 93.61 -42.36
REMARK 500 3 VAL A 49 -162.36 -115.29
REMARK 500 3 LYS A 53 123.40 -173.15
REMARK 500
REMARK 500 THIS ENTRY HAS 532 RAMACHANDRAN OUTLIERS.
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 1 ARG A 60 0.31 SIDE CHAIN
REMARK 500 1 ARG A 65 0.24 SIDE CHAIN
REMARK 500 1 ARG A 68 0.20 SIDE CHAIN
REMARK 500 1 ARG A 76 0.31 SIDE CHAIN
REMARK 500 2 ARG A 60 0.32 SIDE CHAIN
REMARK 500 2 ARG A 65 0.29 SIDE CHAIN
REMARK 500 2 ARG A 68 0.21 SIDE CHAIN
REMARK 500 2 ARG A 73 0.32 SIDE CHAIN
REMARK 500 2 ARG A 76 0.24 SIDE CHAIN
REMARK 500 3 ARG A 60 0.31 SIDE CHAIN
REMARK 500 3 ARG A 65 0.18 SIDE CHAIN
REMARK 500 3 ARG A 68 0.25 SIDE CHAIN
REMARK 500 3 ARG A 73 0.28 SIDE CHAIN
REMARK 500 3 ARG A 76 0.15 SIDE CHAIN
REMARK 500 4 ARG A 60 0.18 SIDE CHAIN
REMARK 500 4 ARG A 65 0.26 SIDE CHAIN
REMARK 500 4 ARG A 68 0.09 SIDE CHAIN
REMARK 500 4 ARG A 73 0.29 SIDE CHAIN
REMARK 500 4 ARG A 76 0.32 SIDE CHAIN
REMARK 500 5 ARG A 60 0.21 SIDE CHAIN
REMARK 500 5 ARG A 65 0.23 SIDE CHAIN
REMARK 500 5 ARG A 68 0.27 SIDE CHAIN
REMARK 500 5 ARG A 73 0.08 SIDE CHAIN
REMARK 500 5 ARG A 76 0.26 SIDE CHAIN
REMARK 500 6 ARG A 60 0.29 SIDE CHAIN
REMARK 500 6 ARG A 65 0.20 SIDE CHAIN
REMARK 500 6 ARG A 68 0.16 SIDE CHAIN
REMARK 500 6 ARG A 73 0.32 SIDE CHAIN
REMARK 500 6 ARG A 76 0.28 SIDE CHAIN
REMARK 500 7 ARG A 60 0.22 SIDE CHAIN
REMARK 500 7 ARG A 65 0.26 SIDE CHAIN
REMARK 500 7 ARG A 68 0.28 SIDE CHAIN
REMARK 500 7 ARG A 73 0.20 SIDE CHAIN
REMARK 500 7 ARG A 76 0.28 SIDE CHAIN
REMARK 500 8 ARG A 60 0.23 SIDE CHAIN
REMARK 500 8 ARG A 65 0.26 SIDE CHAIN
REMARK 500 8 ARG A 68 0.30 SIDE CHAIN
REMARK 500 8 ARG A 73 0.32 SIDE CHAIN
REMARK 500 8 ARG A 76 0.29 SIDE CHAIN
REMARK 500 9 ARG A 60 0.17 SIDE CHAIN
REMARK 500 9 ARG A 65 0.32 SIDE CHAIN
REMARK 500 9 ARG A 68 0.10 SIDE CHAIN
REMARK 500 9 ARG A 73 0.31 SIDE CHAIN
REMARK 500 9 ARG A 76 0.29 SIDE CHAIN
REMARK 500 10 ARG A 60 0.24 SIDE CHAIN
REMARK 500 10 ARG A 65 0.23 SIDE CHAIN
REMARK 500 10 ARG A 68 0.17 SIDE CHAIN
REMARK 500 10 ARG A 73 0.30 SIDE CHAIN
REMARK 500 10 ARG A 76 0.24 SIDE CHAIN
REMARK 500 11 ARG A 60 0.28 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 140 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6700 RELATED DB: BMRB
REMARK 900 BMRB ENTRY FOR PRESENT STRUCTURE.
DBREF 1N88 A 1 96 UNP Q9RA57 RL23_THETH 1 96
SEQRES 1 A 96 MET LYS THR ALA TYR ASP VAL ILE LEU ALA PRO VAL LEU
SEQRES 2 A 96 SER GLU LYS ALA TYR ALA GLY PHE ALA GLU GLY LYS TYR
SEQRES 3 A 96 THR PHE TRP VAL HIS PRO LYS ALA THR LYS THR GLU ILE
SEQRES 4 A 96 LYS ASN ALA VAL GLU THR ALA PHE LYS VAL LYS VAL VAL
SEQRES 5 A 96 LYS VAL ASN THR LEU HIS VAL ARG GLY LYS LYS LYS ARG
SEQRES 6 A 96 LEU GLY ARG TYR LEU GLY LYS ARG PRO ASP ARG LYS LYS
SEQRES 7 A 96 ALA ILE VAL GLN VAL ALA PRO GLY GLN LYS ILE GLU ALA
SEQRES 8 A 96 LEU GLU GLY LEU ILE
HELIX 1 1 SER A 14 ALA A 22 1 9
HELIX 2 2 THR A 35 PHE A 47 1 13
HELIX 3 3 ILE A 89 GLY A 94 1 6
SHEET 1 A 4 ILE A 8 PRO A 11 0
SHEET 2 A 4 LYS A 25 VAL A 30 -1 O TRP A 29 N LEU A 9
SHEET 3 A 4 ARG A 76 VAL A 83 -1 O LYS A 77 N VAL A 30
SHEET 4 A 4 VAL A 51 VAL A 59 -1 N VAL A 52 O GLN A 82
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 - b 23 2 Bytes