Header list of 1n3g.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSLATION 28-OCT-02 1N3G
TITLE SOLUTION STRUCTURE OF THE RIBOSOME-ASSOCIATED COLD SHOCK RESPONSE
TITLE 2 PROTEIN YFIA OF ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN YFIA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COLD-SHOCK PROTEIN YFIA, RIBOSOME ASSOCIATED INHIBITOR RAIA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11C
KEYWDS COLD SHOCK, TRANSLATION INHIBITOR, DSRBD, TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 29
AUTHOR A.RAK,A.KALININ,D.SHCHERBAKOV,P.BAYER
REVDAT 3 23-FEB-22 1N3G 1 REMARK
REVDAT 2 24-FEB-09 1N3G 1 VERSN
REVDAT 1 28-JAN-03 1N3G 0
JRNL AUTH A.RAK,A.KALININ,D.SHCHERBAKOV,P.BAYER
JRNL TITL SOLUTION STRUCTURE OF THE RIBOSOME-ASSOCIATED COLD SHOCK
JRNL TITL 2 RESPONSE PROTEIN YFIA OF ESCHERICHIA COL
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 299 710 2002
JRNL REFN ISSN 0006-291X
JRNL PMID 12470636
JRNL DOI 10.1016/S0006-291X(02)02721-3
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.E.AGAFONOV,V.A.KOLB,I.V.NAZIMOV,A.S.SPIRIN
REMARK 1 TITL A PROTEIN RESIDING AT THE SUBUNIT INTERFACE OF THE BACTERIAL
REMARK 1 TITL 2 RIBOSOME
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 96 12345 1999
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.96.22.12345
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.KALININ,A.RAK,D.SHCHERBAKOV,P.BAYER
REMARK 1 TITL 1H, 13C AND 15N RESONANCE ASSIGNMENTS OF THE
REMARK 1 TITL 2 RIBOSOME-ASSOCIATED COLD SHOCK RESPONSE PROTEIN YFIA OF
REMARK 1 TITL 3 ESCHERICHIA COLI
REMARK 1 REF J.BIOMOL.NMR V. 23 335 2002
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1020279728394
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.2, CNS 1.0
REMARK 3 AUTHORS : BRUKER, RHEINSTETTEN, GERMANY (XWINNMR), AXEL
REMARK 3 BRUENGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N3G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017470.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300; 300; 300
REMARK 210 PH : 6.5; 6.5; 6.5; 6.5
REMARK 210 IONIC STRENGTH : 50MM LICL, 50MM KH2PO4; 50MM
REMARK 210 LICL, 50MM KH2PO4; 50MM LICL,
REMARK 210 50MM KH2PO4; 50MM LICL, 50MM
REMARK 210 KH2PO4
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM YFIA, U-15N-13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 50MM LICL;
REMARK 210 0.5MM YFIA, U-15N; 50MM
REMARK 210 PHOSPHATE BUFFER, 50MM LICL;
REMARK 210 0.5MM YFIA, U-15N; 50MM
REMARK 210 PHOSPHATE BUFFER, 50MM LICL;
REMARK 210 0.8MM YFIA; 50MM PHOSPHATE
REMARK 210 BUFFER, 50MM LICL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; 3D_15N-SEPARATED_NOESY;
REMARK 210 3D_13C-SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DRX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE 2.03, VNMR 6.1B, AURELIA
REMARK 210 2.3
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 29
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: HYDROGEN BONDS WERE EXTRACTED FROM A SERIES OF 15N-HSQC
REMARK 210 SPECTRA RECORDED IN D2O; ASSIGNMENT WAS DONE USING TRIPLE-
REMARK 210 RESONANCE SPECTRA
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
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 MET A 3 80.42 57.74
REMARK 500 1 LYS A 8 -89.06 -74.50
REMARK 500 1 GLU A 11 -179.30 -55.86
REMARK 500 1 THR A 32 -88.26 -144.23
REMARK 500 1 HIS A 33 -23.68 150.03
REMARK 500 1 LEU A 34 94.88 24.91
REMARK 500 1 ASN A 36 75.93 -110.92
REMARK 500 1 GLN A 46 45.73 -97.81
REMARK 500 1 HIS A 67 146.40 -174.65
REMARK 500 1 HIS A 90 109.10 -55.51
REMARK 500 1 LYS A 91 40.65 -154.83
REMARK 500 1 GLU A 93 75.05 -177.19
REMARK 500 1 ARG A 95 93.70 -61.81
REMARK 500 1 ALA A 97 166.82 63.09
REMARK 500 1 ALA A 98 -167.66 62.55
REMARK 500 1 SER A 100 34.97 -95.15
REMARK 500 1 ASP A 103 111.95 -161.90
REMARK 500 1 ASN A 105 76.59 -68.23
REMARK 500 1 PHE A 106 -100.83 -85.40
REMARK 500 1 VAL A 110 77.07 58.12
REMARK 500 1 GLU A 111 -71.27 -95.37
REMARK 500 1 GLU A 112 -70.66 -149.32
REMARK 500 2 MET A 3 56.87 38.80
REMARK 500 2 LYS A 8 -78.94 -73.83
REMARK 500 2 GLN A 9 -60.01 -102.77
REMARK 500 2 GLU A 11 -166.55 -57.88
REMARK 500 2 TRP A 30 38.49 -91.51
REMARK 500 2 GLN A 31 15.04 49.23
REMARK 500 2 LEU A 34 99.66 21.26
REMARK 500 2 ASN A 36 69.26 -106.86
REMARK 500 2 GLN A 46 49.20 -101.13
REMARK 500 2 HIS A 67 126.38 -177.17
REMARK 500 2 LYS A 87 -70.25 -64.07
REMARK 500 2 HIS A 90 69.57 -67.74
REMARK 500 2 LYS A 91 35.81 176.84
REMARK 500 2 ALA A 94 -54.25 -126.69
REMARK 500 2 ARG A 95 -64.71 70.03
REMARK 500 2 PHE A 106 -117.22 -63.15
REMARK 500 2 GLU A 108 -101.13 61.48
REMARK 500 2 GLU A 109 -163.54 -69.21
REMARK 500 2 VAL A 110 133.98 74.51
REMARK 500 2 GLU A 112 34.78 -173.85
REMARK 500 3 MET A 3 91.36 -55.40
REMARK 500 3 MET A 10 95.86 -163.90
REMARK 500 3 LEU A 34 138.72 62.64
REMARK 500 3 ILE A 35 -55.87 -132.05
REMARK 500 3 ASN A 36 66.87 -111.35
REMARK 500 3 GLN A 46 47.27 -101.84
REMARK 500 3 HIS A 67 146.27 -175.62
REMARK 500 3 HIS A 90 96.04 -57.37
REMARK 500
REMARK 500 THIS ENTRY HAS 501 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5389 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT DATA FOR YFIA
DBREF 1N3G A 1 113 UNP P0AD49 YFIA_ECOLI 0 112
SEQRES 1 A 113 MET THR MET ASN ILE THR SER LYS GLN MET GLU ILE THR
SEQRES 2 A 113 PRO ALA ILE ARG GLN HIS VAL ALA ASP ARG LEU ALA LYS
SEQRES 3 A 113 LEU GLU LYS TRP GLN THR HIS LEU ILE ASN PRO HIS ILE
SEQRES 4 A 113 ILE LEU SER LYS GLU PRO GLN GLY PHE VAL ALA ASP ALA
SEQRES 5 A 113 THR ILE ASN THR PRO ASN GLY VAL LEU VAL ALA SER GLY
SEQRES 6 A 113 LYS HIS GLU ASP MET TYR THR ALA ILE ASN GLU LEU ILE
SEQRES 7 A 113 ASN LYS LEU GLU ARG GLN LEU ASN LYS LEU GLN HIS LYS
SEQRES 8 A 113 GLY GLU ALA ARG ARG ALA ALA THR SER VAL LYS ASP ALA
SEQRES 9 A 113 ASN PHE VAL GLU GLU VAL GLU GLU GLU
HELIX 1 1 THR A 13 GLU A 28 1 16
HELIX 2 2 ASP A 69 HIS A 90 1 22
HELIX 3 3 ALA A 97 LYS A 102 5 6
SHEET 1 A 4 ASN A 4 ILE A 5 0
SHEET 2 A 4 ASN A 36 GLU A 44 1 O ILE A 39 N ASN A 4
SHEET 3 A 4 GLY A 47 THR A 56 -1 O THR A 53 N HIS A 38
SHEET 4 A 4 GLY A 59 HIS A 67 -1 O HIS A 67 N PHE A 48
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