HEADER RIBOSOME 26-APR-99 1CK2
TITLE YEAST (SACCHAROMYCES CEREVISIAE) RIBOSOMAL PROTEIN L30
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 60S RIBOSOMAL PROTEIN L30;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RL30_YEAST;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: THIS ENTRY, 1CK2, IS THE REPLACEMENT OF 1CN6 CITED IN
COMPND 7 THE PRIMARY REFERENCE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 ORGANELLE: RIBOSOME, 60S SUBUNIT;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 7 GENE: RPL30;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PMALC-L30;
SOURCE 13 OTHER_DETAILS: RECOMBINANT EXPRESSION AS A C-TERMINAL MALTOSE-
SOURCE 14 BINDING PROTEIN FUSION IN ESCHERICHIA COLI STRAIN JM109 HOSTING
SOURCE 15 PLASMID PMALC-30
KEYWDS RIBOSOMAL PROTEIN, AUTO-REGULATION OF PRE-MRNA SPLICING AND MRNA
KEYWDS 2 TRANSLATION, RIBOSOME
EXPDTA SOLUTION NMR
AUTHOR H.MAO,J.R.WILLAMSON
REVDAT 6 27-DEC-23 1CK2 1 REMARK
REVDAT 5 16-FEB-22 1CK2 1 REMARK
REVDAT 4 24-FEB-09 1CK2 1 VERSN
REVDAT 3 25-JUL-06 1CK2 1 COMPND DBREF REMARK
REVDAT 2 01-APR-03 1CK2 1 JRNL
REVDAT 1 14-OCT-99 1CK2 0
JRNL AUTH H.MAO,J.R.WILLIAMSON
JRNL TITL LOCAL FOLDING COUPLED TO RNA BINDING IN THE YEAST RIBOSOMAL
JRNL TITL 2 PROTEIN L30
JRNL REF J.MOL.BIOL. V. 292 345 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10493880
JRNL DOI 10.1006/JMBI.1999.3044
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.D.DABEVA,J.R.WARNER
REMARK 1 TITL THE YEAST RIBOSOMAL PROTEIN L32 AND ITS GENE
REMARK 1 REF J.BIOL.CHEM. V. 262 16055 1987
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,
REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISTANCE INTRARESIDUE NOES 720
REMARK 3 INTERRESIDUE NOES 698 SEQUENTIAL (|I-J|=1) 291 SHORT-RANGE (|I-J|
REMARK 3 <=4) 149, LONG-RANGE (|I-J|>4) 258, HYDROGEN BONDS 62. TOTAL
REMARK 3 1418, TORSION BACKBONE PHI 80, SIDECHAIN KAI1 59, TOTAL 139
REMARK 4
REMARK 4 1CK2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000941.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 300 MM
REMARK 210 PRESSURE : 1 ATOM
REMARK 210 SAMPLE CONTENTS : 10% WATER/90% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; HNCA; HNCO;
REMARK 210 HN(CO)CA; CBCA(CO)NH; HCCHTOCSY;
REMARK 210 NOESYHSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : VARIAN INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRDRAW, NMRPIPE
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMIC
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: MEAN STRUCTURE. THIS STRUCTURE WAS DETERMINED USING TRIPLE
REMARK 210 -RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED L30 PROTEIN.
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 OE2 GLU A 8 HG SER A 9 1.35
REMARK 500 OE2 GLU A 57 HH TYR A 69 1.37
REMARK 500 OE2 GLU A 55 HH TYR A 59 1.37
REMARK 500 HH TYR A 27 OE1 GLU A 55 1.38
REMARK 500 HG SER A 20 OD2 ASP A 97 1.40
REMARK 500 OD2 ASP A 99 HG1 THR A 103 1.42
REMARK 500 HG SER A 98 OD1 ASP A 99 1.47
REMARK 500 O SER A 29 HG SER A 33 1.49
REMARK 500 O VAL A 50 HG SER A 54 1.52
REMARK 500 O TYR A 59 HG SER A 63 1.53
REMARK 500 O LEU A 25 HG SER A 29 1.57
REMARK 500 OG SER A 63 HG1 THR A 65 1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ALA A 2 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
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 SER A 20 -12.04 -149.92
REMARK 500 ALA A 45 57.91 -114.53
REMARK 500 ASN A 47 75.40 -61.89
REMARK 500 ASN A 74 -88.71 -131.32
REMARK 500 ASN A 75 13.94 -170.39
REMARK 500 VAL A 81 -70.55 -80.58
REMARK 500 LYS A 83 -30.43 58.07
REMARK 500 LEU A 84 -60.86 -91.20
REMARK 500 ASP A 97 -85.71 -145.56
REMARK 500 ASP A 99 12.09 -52.06
REMARK 500 LEU A 104 38.72 -77.15
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CK2 A 2 105 UNP P14120 RL30_YEAST 1 104
SEQRES 1 A 104 ALA PRO VAL LYS SER GLN GLU SER ILE ASN GLN LYS LEU
SEQRES 2 A 104 ALA LEU VAL ILE LYS SER GLY LYS TYR THR LEU GLY TYR
SEQRES 3 A 104 LYS SER THR VAL LYS SER LEU ARG GLN GLY LYS SER LYS
SEQRES 4 A 104 LEU ILE ILE ILE ALA ALA ASN THR PRO VAL LEU ARG LYS
SEQRES 5 A 104 SER GLU LEU GLU TYR TYR ALA MET LEU SER LYS THR LYS
SEQRES 6 A 104 VAL TYR TYR PHE GLN GLY GLY ASN ASN GLU LEU GLY THR
SEQRES 7 A 104 ALA VAL GLY LYS LEU PHE ARG VAL GLY VAL VAL SER ILE
SEQRES 8 A 104 LEU GLU ALA GLY ASP SER ASP ILE LEU THR THR LEU ALA
HELIX 1 1 SER A 9 ILE A 18 1 10
HELIX 2 2 TYR A 27 ARG A 35 1 9
HELIX 3 3 VAL A 50 LEU A 62 1 13
HELIX 4 4 GLY A 78 VAL A 81 1 4
HELIX 5 5 ILE A 100 THR A 103 1 4
SHEET 1 A 4 LYS A 66 TYR A 69 0
SHEET 2 A 4 LEU A 41 ALA A 45 1 N ILE A 42 O LYS A 66
SHEET 3 A 4 GLY A 88 GLU A 94 -1 N ILE A 92 O LEU A 41
SHEET 4 A 4 LYS A 22 LEU A 25 -1 N THR A 24 O SER A 91
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
(ATOM LINES ARE NOT SHOWN.)
END
