Header list of 1ovy.pdb file
Complete list - b 23 2 Bytes
HEADER RIBOSOME 27-MAR-03 1OVY
TITLE SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN L18 FROM BACILLUS
TITLE 2 STEAROTHERMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 50S RIBOSOMAL PROTEIN L18;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1422;
SOURCE 4 GENE: RPLR;
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: PET13A
KEYWDS RIBOSOMAL PROTEIN, RIBOSOME
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.F.TURNER,P.B.MOORE
REVDAT 3 23-FEB-22 1OVY 1 REMARK
REVDAT 2 24-FEB-09 1OVY 1 VERSN
REVDAT 1 17-FEB-04 1OVY 0
JRNL AUTH C.F.TURNER,P.B.MOORE
JRNL TITL THE SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN L18 FROM
JRNL TITL 2 BACILLUS STEAROTHERMOPHILUS
JRNL REF J.MOL.BIOL. V. 335 679 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 14687565
JRNL DOI 10.1016/J.JMB.2003.11.018
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97.0, CNS 1.0, ARIA 1.2
REMARK 3 AUTHORS : BIOSYM/MSI (FELIX), BRUNGER, A.T. ET AL. (CNS),
REMARK 3 LINGE, J.P. & NILGES, M. (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2272 RESTRAINTS. 1188 ARE
REMARK 3 UNAMBIGUOUS DISTANCE CONSTRAINTS, 913 ARE AMBIGUOUS DISTANCE
REMARK 3 CONSTRAINTS, 128 ARE DIHEDRAL ANGLE RESTRAINTS, AND 43 ARE HYDROGEN
REMARK 3 BOND RESTRAINTS.
REMARK 4
REMARK 4 1OVY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018719.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 12MM KH2PO4; 8MM NAH2PO4; 200MM
REMARK 210 NACL, 5MM MGCL2
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM L18 U-15N; 20MM PHOSPHATE
REMARK 210 BUFFER; 200MM NACL; 5MM MGCL2;
REMARK 210 1.5MM L18 U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER; 200MM NACL;
REMARK 210 5MM MGCL2; 1MM L18; 20MM
REMARK 210 PHOSPHATE BUFFER; 200MM NACL;
REMARK 210 5MM MGCL2
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 : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.93, CNS 1.0, ARIA 1.2
REMARK 210 METHOD USED : ARIA WAS USED TO SELECT AND
REMARK 210 ASSIGN PEAK LISTS FROM NOESY
REMARK 210 EXPERIMENTS. CNS AS MODIFIED FOR
REMARK 210 USE WITH ARIA WAS USED FOR
REMARK 210 STRUCTURE CALCULATION USING
REMARK 210 TORSION ANGLE SIMULATED
REMARK 210 ANNEALING.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: THIS 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 VAL A 5
REMARK 465 ASP A 6
REMARK 465 ARG A 7
REMARK 465 ASN A 8
REMARK 465 ALA A 9
REMARK 465 VAL A 10
REMARK 465 ARG A 11
REMARK 465 LYS A 12
REMARK 465 LYS A 13
REMARK 465 ARG A 14
REMARK 465 HIS A 15
REMARK 465 ALA A 16
REMARK 465 ARG A 17
REMARK 465 ILE A 18
REMARK 465 ARG A 19
REMARK 465 LYS A 20
REMARK 465 LYS A 21
REMARK 465 ILE A 22
REMARK 465 PHE A 23
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 9 TYR A 100 CE1 TYR A 100 CZ 0.147
REMARK 500 9 TYR A 100 CZ TYR A 100 CE2 -0.148
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 25 16.06 -146.87
REMARK 500 1 THR A 26 -40.60 -177.28
REMARK 500 1 ARG A 28 83.03 171.94
REMARK 500 1 ARG A 30 169.55 177.72
REMARK 500 1 ASN A 37 -93.80 66.63
REMARK 500 1 ASP A 46 158.36 -47.14
REMARK 500 1 ASP A 47 -115.61 -95.54
REMARK 500 1 LYS A 49 -60.31 -102.98
REMARK 500 1 SER A 50 171.16 167.95
REMARK 500 1 ALA A 51 -159.74 166.22
REMARK 500 1 SER A 55 -139.99 176.45
REMARK 500 1 SER A 57 -167.59 -160.05
REMARK 500 1 ASP A 66 128.01 65.89
REMARK 500 1 SER A 67 -36.60 174.97
REMARK 500 1 LYS A 88 -71.32 -51.56
REMARK 500 1 ILE A 90 -43.89 -161.54
REMARK 500 1 ASP A 96 -85.36 -68.39
REMARK 500 1 ARG A 97 -39.85 -138.09
REMARK 500 1 TYR A 100 -176.58 46.84
REMARK 500 1 TYR A 102 125.55 94.51
REMARK 500 1 HIS A 103 -34.79 175.01
REMARK 500 2 THR A 26 49.78 -167.94
REMARK 500 2 GLU A 27 -91.90 -171.97
REMARK 500 2 PRO A 29 162.65 -39.94
REMARK 500 2 ASN A 37 -88.52 58.17
REMARK 500 2 ASP A 46 165.83 -46.41
REMARK 500 2 ASP A 47 -70.51 -146.86
REMARK 500 2 LYS A 49 61.93 -117.48
REMARK 500 2 SER A 50 60.90 37.59
REMARK 500 2 ALA A 51 -158.97 -61.83
REMARK 500 2 VAL A 54 -152.95 -177.61
REMARK 500 2 SER A 55 -137.92 178.33
REMARK 500 2 LEU A 59 -30.40 -38.10
REMARK 500 2 ASP A 60 74.44 92.38
REMARK 500 2 LYS A 61 -71.73 -89.19
REMARK 500 2 ASP A 66 137.48 60.64
REMARK 500 2 SER A 67 -34.45 171.86
REMARK 500 2 PHE A 95 98.08 -51.03
REMARK 500 2 ASP A 96 -142.52 25.74
REMARK 500 2 TYR A 100 58.77 179.39
REMARK 500 2 LEU A 101 -61.94 68.56
REMARK 500 2 TYR A 102 178.04 122.65
REMARK 500 2 HIS A 103 -24.16 112.63
REMARK 500 3 THR A 26 -31.85 164.25
REMARK 500 3 GLU A 27 -76.45 -79.56
REMARK 500 3 ARG A 28 85.11 -161.69
REMARK 500 3 ARG A 30 165.18 177.77
REMARK 500 3 ASN A 37 96.20 -56.43
REMARK 500 3 LYS A 38 14.29 92.37
REMARK 500 3 ASP A 46 156.23 -45.44
REMARK 500
REMARK 500 THIS ENTRY HAS 229 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 3 TYR A 41 0.09 SIDE CHAIN
REMARK 500 8 TYR A 41 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OVY A 1 120 UNP P09415 RL18_BACST 1 120
SEQRES 1 A 120 MET ILE THR LYS VAL ASP ARG ASN ALA VAL ARG LYS LYS
SEQRES 2 A 120 ARG HIS ALA ARG ILE ARG LYS LYS ILE PHE GLY THR THR
SEQRES 3 A 120 GLU ARG PRO ARG LEU SER VAL PHE ARG SER ASN LYS HIS
SEQRES 4 A 120 ILE TYR ALA GLN ILE ILE ASP ASP THR LYS SER ALA THR
SEQRES 5 A 120 ILE VAL SER ALA SER THR LEU ASP LYS GLU PHE GLY LEU
SEQRES 6 A 120 ASP SER THR ASN ASN ILE GLU ALA ALA LYS LYS VAL GLY
SEQRES 7 A 120 GLU LEU VAL ALA LYS ARG ALA LEU GLU LYS GLY ILE LYS
SEQRES 8 A 120 GLN VAL VAL PHE ASP ARG GLY GLY TYR LEU TYR HIS GLY
SEQRES 9 A 120 ARG VAL LYS ALA LEU ALA ASP ALA ALA ARG GLU ALA GLY
SEQRES 10 A 120 LEU GLU PHE
HELIX 1 1 ASN A 70 GLY A 89 1 20
HELIX 2 2 VAL A 106 LEU A 118 1 13
SHEET 1 A 3 LEU A 31 SER A 36 0
SHEET 2 A 3 HIS A 39 ILE A 45 -1 O GLN A 43 N SER A 32
SHEET 3 A 3 ILE A 53 ALA A 56 -1 O ALA A 56 N ALA A 42
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