Header list of 1ily.pdb file
Complete list - b 23 2 Bytes
HEADER RNA BINDING PROTEIN 09-MAY-01 1ILY
TITLE SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN L18 OF THERMUS THERMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSOMAL PROTEIN L18;
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 ORGANELLE: RIBOSOME;
SOURCE 5 GENE: RL18;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11C
KEYWDS MIXED ALPHA/BETA, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 27
AUTHOR E.A.WOESTENENK,G.M.GONGADZE,D.V.SHCHERBAKOV,A.V.RAK,M.B.GARBER,
AUTHOR 2 T.HARD,H.BERGLUND
REVDAT 3 23-FEB-22 1ILY 1 REMARK
REVDAT 2 24-FEB-09 1ILY 1 VERSN
REVDAT 1 01-MAY-02 1ILY 0
JRNL AUTH E.A.WOESTENENK,G.M.GONGADZE,D.V.SHCHERBAKOV,A.V.RAK,
JRNL AUTH 2 M.B.GARBER,T.HARD,H.BERGLUND
JRNL TITL THE SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN L18 FROM THERMUS
JRNL TITL 2 THERMOPHILUS REVEALS A CONSERVED RNA-BINDING FOLD.
JRNL REF BIOCHEM.J. V. 363 553 2002
JRNL REFN ISSN 0264-6021
JRNL PMID 11964156
JRNL DOI 10.1042/0264-6021:3630553
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON 1925 NOE
REMARK 3 -DERIVED DISTANCE RESTRAINTS, 125 BACKBONE DIHEDRAL ANGLE
REMARK 3 RESTRAINTS, 12 CHI-1 ANGLE RESTRAINTS, 68 DISTANCE RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1ILY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013398.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.9
REMARK 210 IONIC STRENGTH : 50 MM KH2PO4, 200 MM LICL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8 MM L18 U-15N,13C; 50 MM
REMARK 210 PHOSPHATE BUFFER; 200 MM LICL;
REMARK 210 1.3 MM L18 U-15N; 50 MM
REMARK 210 PHOSPHATE BUFFER; 200 MM LICL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 2D
REMARK 210 NOESY; 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ; 500 MHZ; 700
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, ANSIG 3.3, ANSIG FOR
REMARK 210 WINDOWS, CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 27
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 O GLU A 102 H GLU A 106 1.37
REMARK 500 O GLU A 102 N GLU A 106 2.19
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 LEU A 31 -59.16 -147.60
REMARK 500 1 LYS A 56 -44.24 177.12
REMARK 500 1 ARG A 88 -39.18 -37.71
REMARK 500 1 TYR A 93 88.68 -52.11
REMARK 500 1 HIS A 94 -165.12 -103.73
REMARK 500 1 ARG A 96 -71.25 -45.77
REMARK 500 1 LYS A 98 -80.23 -66.37
REMARK 500 2 LEU A 31 -64.18 -170.52
REMARK 500 2 LEU A 47 -61.78 -104.02
REMARK 500 2 LYS A 56 62.60 3.09
REMARK 500 2 LEU A 57 171.82 -46.75
REMARK 500 2 ASN A 60 -71.32 -76.13
REMARK 500 2 LYS A 61 -41.12 -175.95
REMARK 500 2 ALA A 65 -39.32 -35.43
REMARK 500 2 ASP A 87 33.70 -150.17
REMARK 500 2 PRO A 90 37.85 -95.73
REMARK 500 2 TYR A 93 76.37 0.69
REMARK 500 2 LYS A 98 -72.10 -53.99
REMARK 500 3 LEU A 31 -58.16 -152.12
REMARK 500 3 LYS A 56 -31.98 178.99
REMARK 500 3 LYS A 58 -45.48 -132.05
REMARK 500 3 LYS A 61 -60.23 -93.65
REMARK 500 3 ALA A 65 -37.96 -35.22
REMARK 500 3 ASP A 87 45.88 -148.48
REMARK 500 3 PRO A 90 59.84 -69.50
REMARK 500 3 TYR A 93 93.15 -41.00
REMARK 500 3 LYS A 98 -80.11 -56.36
REMARK 500 4 SER A 30 -79.33 -90.25
REMARK 500 4 LEU A 31 -58.99 -153.06
REMARK 500 4 LEU A 47 -65.98 -92.86
REMARK 500 4 LYS A 56 63.73 2.17
REMARK 500 4 ASN A 60 -55.92 -133.31
REMARK 500 4 LYS A 61 -83.84 -175.54
REMARK 500 4 ALA A 65 -39.80 -33.92
REMARK 500 4 ASP A 87 40.80 -150.03
REMARK 500 4 TYR A 93 109.70 -47.33
REMARK 500 4 ARG A 96 -70.97 -76.70
REMARK 500 4 LYS A 98 -75.06 -57.96
REMARK 500 5 LEU A 23 137.62 -33.86
REMARK 500 5 SER A 30 -80.73 -89.52
REMARK 500 5 LEU A 31 -51.25 -143.90
REMARK 500 5 LEU A 47 -62.10 -98.84
REMARK 500 5 LYS A 56 -37.92 179.79
REMARK 500 5 LEU A 57 154.78 -46.39
REMARK 500 5 LYS A 58 -56.03 -127.05
REMARK 500 5 ASN A 60 -168.77 -113.26
REMARK 500 5 LYS A 61 -51.07 -155.38
REMARK 500 5 ASP A 87 56.67 -146.79
REMARK 500 5 TYR A 93 95.51 -51.18
REMARK 500 5 ARG A 96 -70.62 -62.54
REMARK 500
REMARK 500 THIS ENTRY HAS 271 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ILY A 22 111 UNP P80320 RL18_THETH 23 112
SEQRES 1 A 90 ARG LEU ARG LEU SER VAL PHE ARG SER LEU LYS HIS ILE
SEQRES 2 A 90 TYR ALA GLN ILE ILE ASP ASP GLU LYS GLY VAL THR LEU
SEQRES 3 A 90 VAL SER ALA SER SER LEU ALA LEU LYS LEU LYS GLY ASN
SEQRES 4 A 90 LYS THR GLU VAL ALA ARG GLN VAL GLY ARG ALA LEU ALA
SEQRES 5 A 90 GLU LYS ALA LEU ALA LEU GLY ILE LYS GLN VAL ALA PHE
SEQRES 6 A 90 ASP ARG GLY PRO TYR LYS TYR HIS GLY ARG VAL LYS ALA
SEQRES 7 A 90 LEU ALA GLU GLY ALA ARG GLU GLY GLY LEU GLU PHE
HELIX 1 1 SER A 52 LYS A 56 1 5
HELIX 2 2 VAL A 64 LEU A 79 1 16
HELIX 3 3 HIS A 94 GLY A 108 1 15
SHEET 1 A 4 VAL A 45 SER A 51 0
SHEET 2 A 4 ILE A 34 ASP A 40 -1 N ALA A 36 O ALA A 50
SHEET 3 A 4 ARG A 24 ARG A 29 -1 O ARG A 24 N ILE A 39
SHEET 4 A 4 ALA A 85 PHE A 86 1 O ALA A 85 N LEU A 25
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