HEADER VIRAL PROTEIN 04-APR-03 1OYI
TITLE SOLUTION STRUCTURE OF THE Z-DNA BINDING DOMAIN OF THE
TITLE 2 VACCINIA VIRUS GENE E3L
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DOUBLE-STRANDED RNA-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: Z-DNA BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VACCINIA VIRUS;
SOURCE 3 ORGANISM_TAXID: 10245;
SOURCE 4 GENE: E3L;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS (ALPHA+BETA) HELIX-TURN-HELIX, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.D.KAHMANN,D.A.WECKING,V.PUTTER,K.LOWENHAUPT,Y.-G.KIM,
AUTHOR 2 P.SCHMIEDER,H.OSCHKINAT,A.RICH,M.SCHADE
REVDAT 2 24-FEB-09 1OYI 1 VERSN
REVDAT 1 09-MAR-04 1OYI 0
JRNL AUTH J.D.KAHMANN,D.A.WECKING,V.PUTTER,K.LOWENHAUPT,
JRNL AUTH 2 Y.-G.KIM,P.SCHMIEDER,H.OSCHKINAT,A.RICH,M.SCHADE
JRNL TITL THE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF
JRNL TITL 2 E3L SHOWS A TYROSINE CONFORMATION THAT MAY EXPLAIN
JRNL TITL 3 ITS REDUCED AFFINITY TO Z-DNA IN VITRO.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 2712 2004
JRNL REFN ISSN 0027-8424
JRNL PMID 14981270
JRNL DOI 10.1073/PNAS.0308612100
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OYI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-03.
REMARK 100 THE RCSB ID CODE IS RCSB018802.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.2 MM U-15N E3L; 2 MM U-13C,
REMARK 210 15N E3L
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY, 3D_
REMARK 210 13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, SPARKY 3.1,
REMARK 210 DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 450
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : 20 STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: RESONANCE ASSIGNMENTS WERE OBTAINED FROM TRIPLE-
REMARK 210 RESONANCE NMR SPECTRA AND 3D 15N-SEPARATED NOESY 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 ALA A 5
REMARK 465 SER A 6
REMARK 465 LYS A 7
REMARK 465 ILE A 8
REMARK 465 TYR A 9
REMARK 465 ILE A 10
REMARK 465 ASP A 11
REMARK 465 GLU A 12
REMARK 465 GLU A 75
REMARK 465 ALA A 76
REMARK 465 ASP A 77
REMARK 465 GLU A 78
REMARK 465 ALA A 79
REMARK 465 ASP A 80
REMARK 465 ALA A 81
REMARK 465 ASP A 82
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 14 -78.40 -175.22
REMARK 500 1 ILE A 26 -100.63 -87.21
REMARK 500 1 ALA A 33 -73.55 -64.57
REMARK 500 1 GLN A 35 -81.85 -39.94
REMARK 500 1 LEU A 40 -75.29 -108.47
REMARK 500 1 ASN A 41 -47.64 176.23
REMARK 500 1 MET A 42 41.13 163.11
REMARK 500 1 GLU A 43 55.52 -90.01
REMARK 500 1 ALA A 58 16.54 86.10
REMARK 500 1 TYR A 61 -166.36 -124.75
REMARK 500 1 ASP A 64 29.71 80.36
REMARK 500 1 PHE A 71 -169.68 -113.54
REMARK 500 1 THR A 73 157.49 55.89
REMARK 500 2 SER A 14 -68.04 -176.61
REMARK 500 2 GLU A 21 -29.26 -39.05
REMARK 500 2 ILE A 26 -100.31 -55.76
REMARK 500 2 THR A 32 -157.19 -80.08
REMARK 500 2 ALA A 33 -71.18 -79.18
REMARK 500 2 GLN A 35 -78.95 -38.44
REMARK 500 2 ASN A 41 -57.20 167.39
REMARK 500 2 MET A 42 36.81 175.94
REMARK 500 2 ALA A 58 21.50 84.54
REMARK 500 2 TYR A 61 -167.12 -125.70
REMARK 500 2 ASP A 64 38.83 79.52
REMARK 500 2 PHE A 71 -169.44 -114.05
REMARK 500 2 THR A 73 72.14 40.51
REMARK 500 3 SER A 14 -65.19 172.84
REMARK 500 3 ILE A 26 -100.37 -73.04
REMARK 500 3 GLN A 35 -82.02 -37.17
REMARK 500 3 LEU A 40 -78.21 -109.76
REMARK 500 3 ASN A 41 -47.95 178.90
REMARK 500 3 MET A 42 41.66 162.71
REMARK 500 3 ALA A 58 21.24 84.98
REMARK 500 3 TYR A 61 -169.24 -126.46
REMARK 500 3 ASP A 64 20.84 82.44
REMARK 500 3 THR A 73 85.55 32.35
REMARK 500 4 SER A 14 -61.07 175.92
REMARK 500 4 ILE A 26 -101.01 -72.03
REMARK 500 4 ALA A 33 -76.20 64.12
REMARK 500 4 GLN A 35 -71.58 -37.58
REMARK 500 4 LEU A 40 -78.65 -109.83
REMARK 500 4 ASN A 41 -42.02 179.77
REMARK 500 4 MET A 42 41.04 162.97
REMARK 500 4 GLU A 43 54.97 -95.84
REMARK 500 4 LYS A 44 -19.35 -49.21
REMARK 500 5 SER A 14 -67.62 178.69
REMARK 500 5 ILE A 26 -99.97 -72.72
REMARK 500 5 LEU A 40 -80.70 -107.73
REMARK 500 5 ASN A 41 -50.86 179.62
REMARK 500 5 MET A 42 39.75 166.71
REMARK 500 5 ALA A 58 18.83 84.56
REMARK 500 5 VAL A 60 -157.58 -136.93
REMARK 500 5 TYR A 61 -174.24 -174.33
REMARK 500 5 MET A 72 76.00 -109.18
REMARK 500 5 THR A 73 68.78 30.27
REMARK 500 6 SER A 14 -79.18 169.66
REMARK 500 6 ILE A 26 -100.35 -77.18
REMARK 500 6 LEU A 40 -80.19 -108.82
REMARK 500 6 ASN A 41 -51.78 -179.06
REMARK 500 6 MET A 42 39.80 165.97
REMARK 500 6 GLU A 43 55.50 -94.82
REMARK 500 6 ALA A 58 31.10 86.00
REMARK 500 6 PHE A 71 -169.47 -116.28
REMARK 500 6 THR A 73 65.25 39.83
REMARK 500 7 SER A 14 -82.35 174.00
REMARK 500 7 ILE A 26 -101.04 -78.61
REMARK 500 7 ALA A 33 -76.40 -56.08
REMARK 500 7 GLN A 35 -78.53 -37.79
REMARK 500 7 ASN A 41 -56.69 172.35
REMARK 500 7 MET A 42 35.89 176.38
REMARK 500 7 ALA A 58 26.35 85.83
REMARK 500 7 PHE A 71 -169.47 -113.47
REMARK 500 8 SER A 14 -94.95 -120.14
REMARK 500 8 ILE A 26 -101.45 -68.11
REMARK 500 8 ALA A 33 -74.66 -43.84
REMARK 500 8 GLN A 35 -80.83 -36.05
REMARK 500 8 LEU A 40 -70.73 -113.69
REMARK 500 8 ASN A 41 -56.67 172.67
REMARK 500 8 MET A 42 36.60 177.05
REMARK 500 8 ALA A 58 23.94 85.36
REMARK 500 8 TYR A 61 -167.50 -125.20
REMARK 500 8 PHE A 71 -169.12 -115.36
REMARK 500 8 THR A 73 87.52 37.22
REMARK 500 9 SER A 14 -74.13 -158.39
REMARK 500 9 ILE A 26 -100.62 -75.86
REMARK 500 9 LEU A 40 -104.17 -104.23
REMARK 500 9 ASN A 41 25.65 -161.54
REMARK 500 9 MET A 42 41.88 75.40
REMARK 500 9 GLU A 43 59.94 -96.22
REMARK 500 9 ALA A 58 22.53 86.05
REMARK 500 9 TYR A 61 -166.97 -125.37
REMARK 500 9 ASP A 64 42.35 75.47
REMARK 500 9 THR A 73 89.29 32.24
REMARK 500 10 SER A 14 -84.13 171.91
REMARK 500 10 ILE A 26 -101.32 -68.27
REMARK 500 10 LEU A 40 -77.98 -103.70
REMARK 500 10 ASN A 41 -40.72 171.71
REMARK 500 10 MET A 42 40.73 161.84
REMARK 500 10 GLU A 43 53.21 -92.98
REMARK 500 10 TYR A 61 -168.54 -125.66
REMARK 500 10 PHE A 71 -169.24 -109.44
REMARK 500 10 THR A 73 89.40 32.73
REMARK 500 11 SER A 14 -65.28 -178.37
REMARK 500 11 ILE A 26 -100.98 -65.78
REMARK 500 11 ALA A 33 -77.25 -52.90
REMARK 500 11 GLN A 35 -85.74 -36.31
REMARK 500 11 LEU A 40 -105.16 -100.98
REMARK 500 11 ASN A 41 25.82 -163.86
REMARK 500 11 MET A 42 51.88 76.81
REMARK 500 11 GLU A 43 69.38 -110.95
REMARK 500 11 ALA A 58 15.28 89.14
REMARK 500 11 TYR A 61 -167.46 -125.26
REMARK 500 11 ASP A 64 26.29 45.63
REMARK 500 11 PHE A 71 -168.76 -117.66
REMARK 500 11 THR A 73 85.83 38.19
REMARK 500 12 SER A 14 -64.59 -175.16
REMARK 500 12 ILE A 26 -100.40 -73.85
REMARK 500 12 LEU A 40 -77.50 -102.88
REMARK 500 12 ASN A 41 -56.21 179.29
REMARK 500 12 MET A 42 36.25 175.96
REMARK 500 12 ALA A 58 22.09 84.34
REMARK 500 12 THR A 73 91.55 37.07
REMARK 500 13 SER A 14 -81.79 170.91
REMARK 500 13 ILE A 26 -96.87 -60.57
REMARK 500 13 THR A 32 -159.19 -81.33
REMARK 500 13 ALA A 33 -75.20 -69.07
REMARK 500 13 GLN A 35 -84.99 -34.71
REMARK 500 13 LEU A 40 -104.67 -102.40
REMARK 500 13 ASN A 41 25.34 -162.78
REMARK 500 13 MET A 42 51.87 76.21
REMARK 500 13 GLU A 43 68.25 -108.87
REMARK 500 13 ALA A 58 16.64 83.69
REMARK 500 13 THR A 73 90.88 37.20
REMARK 500 14 SER A 14 -92.46 175.50
REMARK 500 14 ILE A 26 -100.16 -74.77
REMARK 500 14 ALA A 33 -73.96 -57.14
REMARK 500 14 GLN A 35 -84.02 -38.12
REMARK 500 14 LEU A 40 -103.19 -97.48
REMARK 500 14 ASN A 41 24.57 -160.52
REMARK 500 14 MET A 42 39.52 77.92
REMARK 500 14 LYS A 44 -29.34 -39.53
REMARK 500 14 ALA A 58 18.32 82.11
REMARK 500 14 TYR A 61 -169.01 -126.05
REMARK 500 14 PHE A 71 -169.25 -112.74
REMARK 500 14 THR A 73 156.36 57.87
REMARK 500 15 SER A 14 -98.28 167.26
REMARK 500 15 ILE A 26 -100.18 -68.43
REMARK 500 15 LEU A 40 -103.16 -100.60
REMARK 500 15 ASN A 41 25.84 -161.85
REMARK 500 15 MET A 42 46.89 73.20
REMARK 500 15 ALA A 58 5.84 82.03
REMARK 500 15 TYR A 61 -166.54 -124.90
REMARK 500 15 ASP A 64 25.64 81.99
REMARK 500 15 THR A 73 90.23 37.45
REMARK 500 16 SER A 14 -88.83 178.51
REMARK 500 16 ILE A 26 -98.77 -61.24
REMARK 500 16 GLN A 35 -75.49 -35.70
REMARK 500 16 ASN A 41 -56.68 164.97
REMARK 500 16 MET A 42 37.70 173.04
REMARK 500 16 TYR A 61 -169.36 -127.65
REMARK 500 16 THR A 73 55.89 35.23
REMARK 500 17 SER A 14 -99.41 -172.04
REMARK 500 17 ILE A 26 -99.95 -58.78
REMARK 500 17 ALA A 33 -74.16 -58.02
REMARK 500 17 GLN A 35 -78.93 -37.50
REMARK 500 17 LEU A 40 -70.82 -110.65
REMARK 500 17 ASN A 41 -54.99 172.85
REMARK 500 17 MET A 42 37.32 173.46
REMARK 500 17 GLU A 43 55.37 -93.05
REMARK 500 17 ALA A 58 20.31 89.82
REMARK 500 17 VAL A 60 -156.82 -121.58
REMARK 500 17 TYR A 61 -173.86 -174.10
REMARK 500 17 ASP A 64 28.15 81.60
REMARK 500 17 MET A 72 72.83 -110.82
REMARK 500 17 THR A 73 73.35 38.91
REMARK 500 18 SER A 14 -59.04 179.96
REMARK 500 18 ILE A 26 -100.73 -71.65
REMARK 500 18 GLN A 35 -71.56 -36.54
REMARK 500 18 LEU A 40 -73.93 -110.65
REMARK 500 18 ASN A 41 -43.27 173.41
REMARK 500 18 MET A 42 41.07 164.33
REMARK 500 18 GLU A 43 59.38 -98.26
REMARK 500 18 ALA A 58 28.37 86.14
REMARK 500 18 ARG A 69 173.45 176.72
REMARK 500 18 MET A 72 71.19 -101.63
REMARK 500 18 THR A 73 88.31 36.29
REMARK 500 19 SER A 14 -85.74 -173.06
REMARK 500 19 ILE A 26 -100.83 -65.31
REMARK 500 19 THR A 32 -152.56 -82.88
REMARK 500 19 ALA A 33 -73.48 -72.39
REMARK 500 19 GLN A 35 -81.77 -38.39
REMARK 500 19 LEU A 40 -73.88 -110.18
REMARK 500 19 ASN A 41 -50.07 176.18
REMARK 500 19 MET A 42 39.96 167.28
REMARK 500 19 GLU A 43 55.40 -91.68
REMARK 500 19 ALA A 58 18.88 84.08
REMARK 500 19 PHE A 71 -167.77 -115.58
REMARK 500 19 THR A 73 90.09 30.09
REMARK 500 20 SER A 14 -73.32 -179.43
REMARK 500 20 ILE A 26 -100.22 -67.31
REMARK 500 20 LEU A 40 -95.68 -114.87
REMARK 500 20 ASN A 41 -56.91 -157.86
REMARK 500 20 MET A 42 40.09 172.35
REMARK 500 20 GLU A 43 48.60 -79.47
REMARK 500 20 ALA A 58 24.41 84.38
REMARK 500 20 TYR A 61 -167.28 -125.37
REMARK 500 20 ASP A 64 21.85 82.30
REMARK 500 20 PHE A 71 -169.11 -109.30
REMARK 500 20 THR A 73 156.25 56.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THESE RESIDUES ARE VECTOR-ENCODED.
DBREF 1OYI A 5 81 UNP Q86638 Q86638_9POXV 2 78
SEQADV 1OYI GLY A 1 UNP Q86638 SEE REMARK 999
SEQADV 1OYI SER A 2 UNP Q86638 SEE REMARK 999
SEQADV 1OYI HIS A 3 UNP Q86638 SEE REMARK 999
SEQADV 1OYI MET A 4 UNP Q86638 SEE REMARK 999
SEQADV 1OYI ALA A 5 UNP Q86638 SEE REMARK 999
SEQRES 1 A 82 GLY SER HIS MET ALA SER LYS ILE TYR ILE ASP GLU ARG
SEQRES 2 A 82 SER ASN ALA GLU ILE VAL CYS GLU ALA ILE LYS THR ILE
SEQRES 3 A 82 GLY ILE GLU GLY ALA THR ALA ALA GLN LEU THR ARG GLN
SEQRES 4 A 82 LEU ASN MET GLU LYS ARG GLU VAL ASN LYS ALA LEU TYR
SEQRES 5 A 82 ASP LEU GLN ARG SER ALA MET VAL TYR SER SER ASP ASP
SEQRES 6 A 82 ILE PRO PRO ARG TRP PHE MET THR THR GLU ALA ASP GLU
SEQRES 7 A 82 ALA ASP ALA ASP
HELIX 1 1 ASN A 15 GLY A 27 1 13
HELIX 2 2 ALA A 33 LEU A 40 1 8
HELIX 3 3 GLU A 43 ALA A 58 1 16
SHEET 1 A 3 ALA A 31 THR A 32 0
SHEET 2 A 3 ARG A 69 PHE A 71 -1 O TRP A 70 N ALA A 31
SHEET 3 A 3 TYR A 61 SER A 62 -1 N TYR A 61 O PHE A 71
CISPEP 1 ILE A 66 PRO A 67 1 -0.07
CISPEP 2 ILE A 66 PRO A 67 2 -0.06
CISPEP 3 ILE A 66 PRO A 67 3 0.03
CISPEP 4 ILE A 66 PRO A 67 4 0.04
CISPEP 5 ILE A 66 PRO A 67 5 0.02
CISPEP 6 ILE A 66 PRO A 67 6 0.02
CISPEP 7 ILE A 66 PRO A 67 7 0.03
CISPEP 8 ILE A 66 PRO A 67 8 0.05
CISPEP 9 ILE A 66 PRO A 67 9 -0.04
CISPEP 10 ILE A 66 PRO A 67 10 0.00
CISPEP 11 ILE A 66 PRO A 67 11 -0.05
CISPEP 12 ILE A 66 PRO A 67 12 -0.02
CISPEP 13 ILE A 66 PRO A 67 13 -0.04
CISPEP 14 ILE A 66 PRO A 67 14 0.00
CISPEP 15 ILE A 66 PRO A 67 15 -0.01
CISPEP 16 ILE A 66 PRO A 67 16 0.00
CISPEP 17 ILE A 66 PRO A 67 17 0.00
CISPEP 18 ILE A 66 PRO A 67 18 -0.03
CISPEP 19 ILE A 66 PRO A 67 19 0.00
CISPEP 20 ILE A 66 PRO A 67 20 -0.02
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
