Header list of 1fox.pdb file
Complete list - b 23 2 Bytes
HEADER RIBOSOMAL PROTEIN 13-SEP-96 1FOX
TITLE NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL
TITLE 2 PROTEIN L11, 33 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L11-C76;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CARBOXYL-TERMINAL DOMAIN OF PROTEIN L11, RESIDUES THR 59 TO
COMPND 5 ASP 133;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: BINDS SPECIFICALLY TO RNA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1422;
SOURCE 4 CELL_LINE: BL21;
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_PLASMID: DERIVED FROM PET11A
KEYWDS RIBOSOMAL PROTEIN, RNA-BINDING DOMAIN, L11-C76, ALPHA-HELICAL
KEYWDS 2 PROTEIN, HOMEODOMAIN FOLD
EXPDTA SOLUTION NMR
NUMMDL 33
AUTHOR M.A.MARKUS,A.P.HINCK,S.HUANG,D.E.DRAPER,D.A.TORCHIA
REVDAT 3 23-FEB-22 1FOX 1 REMARK
REVDAT 2 24-FEB-09 1FOX 1 VERSN
REVDAT 1 12-MAR-97 1FOX 0
JRNL AUTH M.A.MARKUS,A.P.HINCK,S.HUANG,D.E.DRAPER,D.A.TORCHIA
JRNL TITL HIGH RESOLUTION SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN
JRNL TITL 2 L11-C76, A HELICAL PROTEIN WITH A FLEXIBLE LOOP THAT BECOMES
JRNL TITL 3 STRUCTURED UPON BINDING TO RNA.
JRNL REF NAT.STRUCT.BIOL. V. 4 70 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 8989327
JRNL DOI 10.1038/NSB0197-70
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.XING,D.GUHA THAKURTA,D.E.DRAPER
REMARK 1 TITL THE RNA BINDING DOMAIN OF RIBOSOMAL PROTEIN L11 IS
REMARK 1 TITL 2 STRUCTURALLY SIMILAR TO HOMEODOMAINS
REMARK 1 REF NAT.STRUCT.BIOL. V. 4 24 1997
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.XING,D.E.DRAPER
REMARK 1 TITL COOPERATIVE INTERACTIONS OF RNA AND THIOSTREPTON ANTIBIOTIC
REMARK 1 TITL 2 WITH TWO DOMAINS OF RIBOSOMAL PROTEIN L11
REMARK 1 REF BIOCHEMISTRY V. 35 1581 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FOX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173359.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.10
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N HSQC; 13C HSQC; HNCACB;
REMARK 210 CBCA(CO)NH; HCACO; C(CO)NH;
REMARK 210 H(CCO)NH; HCCH-TOCSY; HMBC; HNHA;
REMARK 210 HNHB; HCACB-COSY; (13CO)SED CT
REMARK 210 HSQC; (15N) SED CT HSQC; (13C-
REMARK 210 13C) LRC; (13C-1H) LRC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DGSA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 33
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATIONS OVER 0.3 A, NO
REMARK 210 ANGLE VIOLATIONS OVER 5 DEG
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: BUFFER: 10 MM K2HPO4, 25 MM KCL, 2MM MGCL2
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 PHE A 3 -171.94 67.16
REMARK 500 1 LEU A 14 -75.69 -44.83
REMARK 500 1 ALA A 18 -75.53 -61.60
REMARK 500 1 GLU A 26 84.47 -157.89
REMARK 500 1 PRO A 27 -159.16 -78.10
REMARK 500 1 ARG A 29 99.67 57.00
REMARK 500 1 LYS A 36 167.50 -45.00
REMARK 500 1 LYS A 39 -60.10 -95.00
REMARK 500 1 SER A 55 -179.86 -170.73
REMARK 500 1 GLU A 64 -72.83 -81.32
REMARK 500 1 ALA A 67 30.97 -89.83
REMARK 500 1 ARG A 68 -53.56 -137.97
REMARK 500 2 THR A 2 135.43 172.98
REMARK 500 2 ILE A 4 72.91 44.58
REMARK 500 2 SER A 22 83.88 54.80
REMARK 500 2 ASN A 28 42.71 166.20
REMARK 500 2 ASN A 30 -81.94 -44.72
REMARK 500 2 LYS A 31 124.02 63.81
REMARK 500 2 ARG A 68 -35.14 -131.45
REMARK 500 3 THR A 2 -48.40 -142.48
REMARK 500 3 PHE A 3 36.48 -146.40
REMARK 500 3 GLU A 21 -81.72 -99.96
REMARK 500 3 SER A 22 -38.90 -179.67
REMARK 500 3 GLU A 26 80.10 51.58
REMARK 500 3 LYS A 36 160.13 -49.13
REMARK 500 3 LEU A 51 -76.09 -104.56
REMARK 500 3 ASN A 52 -24.59 160.47
REMARK 500 3 SER A 55 -166.50 -170.79
REMARK 500 4 PHE A 3 38.84 -163.64
REMARK 500 4 LYS A 6 40.96 -106.22
REMARK 500 4 GLU A 21 -173.09 -60.30
REMARK 500 4 SER A 24 47.25 -159.79
REMARK 500 4 PRO A 27 44.09 -80.51
REMARK 500 4 ASN A 30 68.67 60.03
REMARK 500 4 LYS A 31 40.88 -144.03
REMARK 500 4 VAL A 32 43.42 -96.74
REMARK 500 4 ALA A 67 31.68 -90.16
REMARK 500 4 ARG A 68 -51.62 -138.84
REMARK 500 5 PHE A 3 51.15 -154.81
REMARK 500 5 ILE A 4 146.32 179.76
REMARK 500 5 LYS A 6 -167.33 169.60
REMARK 500 5 ALA A 11 35.71 -90.20
REMARK 500 5 VAL A 12 -38.24 -149.14
REMARK 500 5 GLU A 21 -30.53 175.90
REMARK 500 5 SER A 24 67.25 -117.33
REMARK 500 5 GLU A 26 82.70 59.89
REMARK 500 5 ASN A 28 -95.07 -158.58
REMARK 500 5 ARG A 29 -65.23 -128.55
REMARK 500 5 LYS A 31 48.30 179.46
REMARK 500 5 ASN A 52 19.31 55.46
REMARK 500
REMARK 500 THIS ENTRY HAS 332 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 29 0.27 SIDE CHAIN
REMARK 500 1 ARG A 37 0.26 SIDE CHAIN
REMARK 500 1 ARG A 41 0.23 SIDE CHAIN
REMARK 500 1 ARG A 61 0.32 SIDE CHAIN
REMARK 500 1 ARG A 68 0.32 SIDE CHAIN
REMARK 500 2 ARG A 29 0.22 SIDE CHAIN
REMARK 500 2 ARG A 37 0.26 SIDE CHAIN
REMARK 500 2 ARG A 41 0.25 SIDE CHAIN
REMARK 500 2 ARG A 61 0.25 SIDE CHAIN
REMARK 500 2 ARG A 68 0.20 SIDE CHAIN
REMARK 500 3 ARG A 29 0.29 SIDE CHAIN
REMARK 500 3 ARG A 37 0.30 SIDE CHAIN
REMARK 500 3 ARG A 41 0.21 SIDE CHAIN
REMARK 500 3 ARG A 61 0.16 SIDE CHAIN
REMARK 500 3 ARG A 68 0.27 SIDE CHAIN
REMARK 500 4 ARG A 29 0.25 SIDE CHAIN
REMARK 500 4 ARG A 37 0.23 SIDE CHAIN
REMARK 500 4 ARG A 41 0.26 SIDE CHAIN
REMARK 500 4 ARG A 61 0.28 SIDE CHAIN
REMARK 500 4 ARG A 68 0.20 SIDE CHAIN
REMARK 500 5 ARG A 29 0.24 SIDE CHAIN
REMARK 500 5 ARG A 37 0.17 SIDE CHAIN
REMARK 500 5 ARG A 41 0.15 SIDE CHAIN
REMARK 500 5 ARG A 61 0.17 SIDE CHAIN
REMARK 500 6 ARG A 29 0.10 SIDE CHAIN
REMARK 500 6 ARG A 37 0.22 SIDE CHAIN
REMARK 500 6 ARG A 41 0.09 SIDE CHAIN
REMARK 500 6 ARG A 61 0.31 SIDE CHAIN
REMARK 500 6 ARG A 68 0.29 SIDE CHAIN
REMARK 500 7 ARG A 29 0.31 SIDE CHAIN
REMARK 500 7 ARG A 37 0.17 SIDE CHAIN
REMARK 500 7 ARG A 41 0.28 SIDE CHAIN
REMARK 500 7 ARG A 61 0.19 SIDE CHAIN
REMARK 500 7 ARG A 68 0.14 SIDE CHAIN
REMARK 500 8 ARG A 29 0.28 SIDE CHAIN
REMARK 500 8 ARG A 37 0.11 SIDE CHAIN
REMARK 500 8 ARG A 41 0.21 SIDE CHAIN
REMARK 500 8 ARG A 68 0.30 SIDE CHAIN
REMARK 500 9 ARG A 29 0.21 SIDE CHAIN
REMARK 500 9 ARG A 37 0.29 SIDE CHAIN
REMARK 500 9 ARG A 41 0.24 SIDE CHAIN
REMARK 500 9 ARG A 61 0.27 SIDE CHAIN
REMARK 500 9 ARG A 68 0.31 SIDE CHAIN
REMARK 500 10 ARG A 29 0.31 SIDE CHAIN
REMARK 500 10 ARG A 37 0.32 SIDE CHAIN
REMARK 500 10 ARG A 41 0.30 SIDE CHAIN
REMARK 500 10 ARG A 61 0.26 SIDE CHAIN
REMARK 500 10 ARG A 68 0.26 SIDE CHAIN
REMARK 500 11 ARG A 29 0.08 SIDE CHAIN
REMARK 500 11 ARG A 37 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 158 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FOW RELATED DB: PDB
DBREF 1FOX A 2 76 UNP P56210 RL11_BACST 59 133
SEQRES 1 A 76 MET THR PHE ILE THR LYS THR PRO PRO ALA ALA VAL LEU
SEQRES 2 A 76 LEU LYS LYS ALA ALA GLY ILE GLU SER GLY SER GLY GLU
SEQRES 3 A 76 PRO ASN ARG ASN LYS VAL ALA THR ILE LYS ARG ASP LYS
SEQRES 4 A 76 VAL ARG GLU ILE ALA GLU LEU LYS MET PRO ASP LEU ASN
SEQRES 5 A 76 ALA ALA SER ILE GLU ALA ALA MET ARG MET ILE GLU GLY
SEQRES 6 A 76 THR ALA ARG SER MET GLY ILE VAL VAL GLU ASP
HELIX 1 A1 ALA A 10 ALA A 18 1 9
HELIX 2 A2 ARG A 37 LEU A 46 1 10
HELIX 3 A3 ILE A 56 THR A 66 1CSI RANGE: GLU 57 TO SER 69 11
SHEET 1 B1 2 THR A 34 LYS A 36 0
SHEET 2 B1 2 VAL A 73 GLU A 75 1 O VAL A 73 N ILE A 35
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