HEADER RNA BINDING PROTEIN 12-MAY-03 1P9K
TITLE THE SOLUTION STRUCTURE OF YBCJ FROM E. COLI REVEALS A RECENTLY
TITLE 2 DISCOVERED ALFAL MOTIF INVOLVED IN RNA-BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORF, HYPOTHETICAL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: YBCJ;
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: PET20B
KEYWDS ALFAL MOTIF, RNA-BINDING PROTEIN, E.COLI, MONTREAL-KINGSTON BACTERIAL
KEYWDS 2 STRUCTURAL GENOMICS INITIATIVE, BSGI, STRUCTURAL GENOMICS, RNA
KEYWDS 3 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.VOLPON,C.LIEVRE,M.J.OSBORNE,S.GANDHI,P.IANNUZZI,R.LAROCQUE,A.MATTE,
AUTHOR 2 M.CYGLER,K.GEHRING,I.EKIEL,MONTREAL-KINGSTON BACTERIAL STRUCTURAL
AUTHOR 3 GENOMICS INITIATIVE (BSGI)
REVDAT 3 13-JUL-11 1P9K 1 VERSN
REVDAT 2 24-FEB-09 1P9K 1 VERSN
REVDAT 1 25-NOV-03 1P9K 0
SPRSDE 25-NOV-03 1P9K 1O09
JRNL AUTH L.VOLPON,C.LIEVRE,M.J.OSBORNE,S.GANDHI,P.IANNUZZI,
JRNL AUTH 2 R.LAROCQUE,M.CYGLER,K.GEHRING,I.EKIEL
JRNL TITL THE SOLUTION STRUCTURE OF YBCJ FROM ESCHERICHIA COLI REVEALS
JRNL TITL 2 A RECENTLY DISCOVERED ALPHAL MOTIF INVOLVED IN RNA BINDING.
JRNL REF J.BACTERIOL. V. 185 4204 2003
JRNL REFN ISSN 0021-9193
JRNL PMID 12837795
JRNL DOI 10.1128/JB.185.14.4204-4210.2003
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TALOS 2003.027.13.05, ARIA 1.1, CNS 1.1
REMARK 3 AUTHORS : BAX (TALOS), NILGES (ARIA), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1205 RESTRAINTS, 1011 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 89
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 54 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS (27 HYDROGEN BONDS), AND 51 15N-1H RESIDUAL DIPOLAR
REMARK 3 COUPLINGS.
REMARK 4
REMARK 4 1P9K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-03.
REMARK 100 THE RCSB ID CODE IS RCSB019178.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE, 300MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 4-7MM YBCJ U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 300MM NACL,
REMARK 210 15MM DTT, 1MM SODIUM AZIDE, PH
REMARK 210 6.8; 4-7MM YBCJ U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 300MM NACL,
REMARK 210 15MM DTT, 1MM SODIUM AZIDE, PH
REMARK 210 6.8, 8MG/ML OF PF1 PHAGE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; HNHA; 3D_15N
REMARK 210 -SEPARATED_NOESY; IPAP-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.31, XWINNMR 2.1, XEASY
REMARK 210 1.3.13
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR AND 3D HETERONUCLEAR TECHNIQUES.
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 HZ2 TRP A 32 HB VAL A 75 1.55
REMARK 500 HB3 GLU A 55 H THR A 56 1.56
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 SER A 2 80.29 -151.58
REMARK 500 1 MET A 3 72.91 -168.58
REMARK 500 1 MET A 7 -31.32 74.43
REMARK 500 1 SER A 8 115.99 67.72
REMARK 500 1 LYS A 17 57.40 -143.86
REMARK 500 1 HIS A 20 -170.36 171.38
REMARK 500 1 GLN A 38 -74.69 -54.91
REMARK 500 1 ALA A 42 -79.14 -74.11
REMARK 500 1 GLN A 47 -14.62 -46.33
REMARK 500 1 VAL A 48 -88.21 -74.92
REMARK 500 1 LYS A 49 128.87 -172.84
REMARK 500 1 ASP A 51 85.91 -55.66
REMARK 500 1 GLU A 55 -151.39 -106.94
REMARK 500 1 THR A 56 57.30 -166.96
REMARK 500 1 ALA A 64 -150.39 74.40
REMARK 500 1 ALA A 71 -87.01 46.67
REMARK 500 2 SER A 2 103.26 63.43
REMARK 500 2 ARG A 6 94.51 61.65
REMARK 500 2 LYS A 17 56.62 -151.06
REMARK 500 2 HIS A 20 -164.32 163.01
REMARK 500 2 ALA A 42 -79.81 -72.21
REMARK 500 2 ALA A 44 -72.18 -63.09
REMARK 500 2 GLN A 47 -9.52 -47.96
REMARK 500 2 VAL A 48 -90.67 -74.66
REMARK 500 2 LYS A 49 119.37 -167.02
REMARK 500 2 ASP A 51 98.20 -44.70
REMARK 500 2 ALA A 64 -155.01 74.48
REMARK 500 2 ALA A 71 -85.03 48.72
REMARK 500 3 SER A 2 -171.44 65.68
REMARK 500 3 ILE A 4 117.89 60.36
REMARK 500 3 HIS A 5 -60.45 -172.82
REMARK 500 3 ARG A 6 167.66 58.40
REMARK 500 3 MET A 7 -172.30 58.28
REMARK 500 3 SER A 8 161.59 67.55
REMARK 500 3 ASN A 9 -62.38 -165.46
REMARK 500 3 HIS A 20 -174.60 168.14
REMARK 500 3 LEU A 23 -39.28 -38.08
REMARK 500 3 GLN A 38 -79.42 -61.11
REMARK 500 3 ALA A 42 -79.09 -74.40
REMARK 500 3 GLN A 47 -10.88 -48.26
REMARK 500 3 VAL A 48 -96.66 -75.33
REMARK 500 3 ASP A 51 97.05 -44.79
REMARK 500 3 THR A 56 46.19 -147.29
REMARK 500 3 ALA A 64 -151.27 72.69
REMARK 500 3 ALA A 71 -85.85 47.55
REMARK 500 4 HIS A 5 139.43 64.50
REMARK 500 4 ARG A 6 71.46 -168.66
REMARK 500 4 MET A 7 -62.90 -99.48
REMARK 500 4 LYS A 17 54.72 -149.84
REMARK 500 4 HIS A 20 -165.65 162.75
REMARK 500
REMARK 500 THIS ENTRY HAS 277 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: YBCJ_ECOLI RELATED DB: TARGETDB
DBREF 1P9K A 3 79 UNP P0AAS7 YBCJ_ECOLI 1 77
SEQADV 1P9K GLY A 1 UNP P0AAS7 CLONING ARTIFACT
SEQADV 1P9K SER A 2 UNP P0AAS7 CLONING ARTIFACT
SEQRES 1 A 79 GLY SER MET ILE HIS ARG MET SER ASN MET ALA THR PHE
SEQRES 2 A 79 SER LEU GLY LYS HIS PRO HIS VAL GLU LEU CYS ASP LEU
SEQRES 3 A 79 LEU LYS LEU GLU GLY TRP SER GLU SER GLY ALA GLN ALA
SEQRES 4 A 79 LYS ILE ALA ILE ALA GLU GLY GLN VAL LYS VAL ASP GLY
SEQRES 5 A 79 ALA VAL GLU THR ARG LYS ARG CYS LYS ILE VAL ALA GLY
SEQRES 6 A 79 GLN THR VAL SER PHE ALA GLY HIS SER VAL GLN VAL VAL
SEQRES 7 A 79 ALA
HELIX 1 1 GLU A 22 GLY A 31 1 10
HELIX 2 2 LYS A 40 VAL A 48 1 9
SHEET 1 A 4 THR A 12 SER A 14 0
SHEET 2 A 4 HIS A 73 VAL A 78 1 O GLN A 76 N PHE A 13
SHEET 3 A 4 GLN A 66 PHE A 70 -1 N GLN A 66 O VAL A 77
SHEET 4 A 4 LYS A 49 VAL A 50 -1 N LYS A 49 O SER A 69
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
(ATOM LINES ARE NOT SHOWN.)
END
