HEADER METAL BINDING PROTEIN, ONCOPROTEIN 04-JAN-06 2FK4
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL ZINC BINDING DOMAIN OF THE HPV16
TITLE 2 E6 ONCOPROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN E6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN PAPILLOMAVIRUS TYPE 16;
SOURCE 3 ORGANISM_TAXID: 333760;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 DE2;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ZINC BINDING DOMAIN, ONCOPROTEIN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Y.NOMINE,S.CHARBONNIER
REVDAT 4 20-OCT-21 2FK4 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2FK4 1 VERSN
REVDAT 2 25-APR-06 2FK4 1 JRNL
REVDAT 1 24-JAN-06 2FK4 0
JRNL AUTH Y.NOMINE,M.MASSON,S.CHARBONNIER,K.ZANIER,T.RISTRIANI,
JRNL AUTH 2 F.DERYCKERE,A.P.SIBLER,D.DESPLANCQ,R.A.ATKINSON,E.WEISS,
JRNL AUTH 3 G.ORFANOUDAKIS,B.KIEFFER,G.TRAVE
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF E6 ONCOPROTEIN:
JRNL TITL 2 INSIGHTS IN THE MOLECULAR PATHWAYS OF HUMAN
JRNL TITL 3 PAPILLOMAVIRUS-MEDIATED PATHOGENESIS
JRNL REF MOL.CELL V. 21 665 2006
JRNL REFN ISSN 1097-2765
JRNL PMID 16507364
JRNL DOI 10.1016/J.MOLCEL.2006.01.024
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.CHARBONNIER,L.MIGUET,N.POTIER,A.VAN DORSSELAER,
REMARK 1 AUTH 2 R.A.ATKINSON,B.KIEFFER
REMARK 1 TITL 1H AND 15N RESONANCE ASSIGNMENT, SECONDARY STRUCTURE AND
REMARK 1 TITL 2 DYNAMIC BEHAVIOUR OF THE C-TERMINAL DOMAIN OF HUMAN
REMARK 1 TITL 3 PAPILLOMAVIRUS ONCOPROTEIN E6.
REMARK 1 REF J.BIOMOL.NMR V. 31 129 2005
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 15772752
REMARK 1 DOI 10.1007/S10858-004-7802-Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH, X-PLOR NIH
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NOE DISTANCE RESTRAINTS WERE SPLIT IN
REMARK 3 TWO SETS. ONE SET INVOLVED RESIDUES THAT WERE IDENTIFIED AS
REMARK 3 BEEING AFFECTED BY CONFORMATIONAL EXCHANGE BY RELAXATION
REMARK 3 DISPERSION EXPERIMENTS. THESE DISTANCES WERE ASSIGNED AN
REMARK 3 ADDITIONAL 1A TO THE UPPER DISTANCE LIMIT. REPORTED CLOSE
REMARK 3 CONTACTS ARE DUE TO CONFORMATIONAL HETEROGENEITIES IN THE SET OF
REMARK 3 NOES. THE DYNAMICAL PROPERTIES OF THIS PROTEIN HAVE BEEN
REMARK 3 DESCRIBED IN DEPTH IN THE J. BIOMOL. NMR REFERENCE CITED ABOVE.
REMARK 4
REMARK 4 2FK4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000035972.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288; 288
REMARK 210 PH : 6.8; 6.8
REMARK 210 IONIC STRENGTH : 50 MM; 50 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM E6C U-15N; 20 MM TRIS
REMARK 210 -HCL, 50 MM NACL, 1MM DTT; 1.0
REMARK 210 MM E6C, 20 MM TRIS-HCL, 50 MM
REMARK 210 NACL, 1MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.0, XWINNMR 2.6
REMARK 210 METHOD USED : SIMULATED ANNEALING, PROTOCOL
REMARK 210 REFINE.INP
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR AND 3D 15N 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 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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 0
REMARK 465 THR A 68
REMARK 465 ARG A 69
REMARK 465 ARG A 70
REMARK 465 GLU A 71
REMARK 465 THR A 72
REMARK 465 GLN A 73
REMARK 465 LEU A 74
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 O ILE A 27 HH21 ARG A 54 1.37
REMARK 500 O CYS A 26 HE21 GLN A 30 1.49
REMARK 500 N ASN A 28 HE22 GLN A 30 1.60
REMARK 500 O ASN A 28 OE1 GLN A 30 2.16
REMARK 500 O ILE A 51 O ARG A 54 2.19
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 ASN A 28 -43.18 -130.44
REMARK 500 1 LYS A 44 71.33 173.86
REMARK 500 2 TYR A 7 17.27 -146.73
REMARK 500 2 ASN A 28 -62.10 -109.14
REMARK 500 2 LYS A 44 67.81 124.09
REMARK 500 3 LYS A 44 68.05 156.31
REMARK 500 4 ASN A 28 -40.02 -138.97
REMARK 500 4 CYS A 29 56.87 -100.54
REMARK 500 4 GLN A 30 -9.04 -32.07
REMARK 500 4 PRO A 32 150.14 -49.74
REMARK 500 4 LYS A 44 71.93 139.18
REMARK 500 4 ARG A 52 104.75 -52.42
REMARK 500 5 LEU A 23 89.11 128.09
REMARK 500 5 GLN A 30 -114.06 65.04
REMARK 500 5 PRO A 32 79.74 -56.72
REMARK 500 5 LYS A 44 66.54 131.47
REMARK 500 6 THR A 10 -38.08 -166.88
REMARK 500 6 LEU A 23 97.99 -63.91
REMARK 500 6 ARG A 25 168.00 178.61
REMARK 500 6 ASN A 28 -47.00 -135.70
REMARK 500 6 LYS A 44 79.08 113.40
REMARK 500 7 LEU A 23 103.76 122.77
REMARK 500 7 CYS A 29 60.13 -158.83
REMARK 500 7 GLN A 30 -9.36 -32.73
REMARK 500 7 LYS A 44 66.50 129.33
REMARK 500 8 THR A 10 -25.72 -38.47
REMARK 500 8 LEU A 23 87.46 129.81
REMARK 500 8 ASN A 28 -62.07 -108.67
REMARK 500 8 LYS A 44 77.58 -172.26
REMARK 500 8 ARG A 47 145.25 -172.70
REMARK 500 9 ASN A 28 -64.84 -98.34
REMARK 500 9 LYS A 44 84.34 -171.87
REMARK 500 10 LEU A 23 75.66 154.70
REMARK 500 10 LYS A 44 72.77 110.45
REMARK 500 10 ARG A 52 104.93 -52.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 26 SG
REMARK 620 2 CYS A 29 SG 108.6
REMARK 620 3 CYS A 59 SG 106.4 110.8
REMARK 620 4 CYS A 62 SG 112.0 110.1 108.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 101
DBREF 2FK4 A 3 74 UNP P03126 VE6_HPV16 87 158
SEQADV 2FK4 GLY A 0 UNP P03126 CLONING ARTIFACT
SEQADV 2FK4 ALA A 1 UNP P03126 CLONING ARTIFACT
SEQADV 2FK4 MET A 2 UNP P03126 CLONING ARTIFACT
SEQADV 2FK4 SER A 3 UNP P03126 CYS 87 ENGINEERED MUTATION
SEQADV 2FK4 SER A 20 UNP P03126 CYS 104 ENGINEERED MUTATION
SEQADV 2FK4 SER A 34 UNP P03126 CYS 118 ENGINEERED MUTATION
SEQADV 2FK4 SER A 63 UNP P03126 CYS 147 ENGINEERED MUTATION
SEQRES 1 A 75 GLY ALA MET SER TYR SER LEU TYR GLY THR THR LEU GLU
SEQRES 2 A 75 GLN GLN TYR ASN LYS PRO LEU SER ASP LEU LEU ILE ARG
SEQRES 3 A 75 CYS ILE ASN CYS GLN LYS PRO LEU SER PRO GLU GLU LYS
SEQRES 4 A 75 GLN ARG HIS LEU ASP LYS LYS GLN ARG PHE HIS ASN ILE
SEQRES 5 A 75 ARG GLY ARG TRP THR GLY ARG CYS MET SER CYS SER ARG
SEQRES 6 A 75 SER SER ARG THR ARG ARG GLU THR GLN LEU
HET ZN A 101 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLY A 8 LYS A 17 1 10
HELIX 2 2 SER A 34 LYS A 45 1 12
HELIX 3 3 GLY A 57 SER A 63 1 7
SHEET 1 A 3 TYR A 4 LEU A 6 0
SHEET 2 A 3 PHE A 48 ILE A 51 -1 O ASN A 50 N TYR A 4
SHEET 3 A 3 ARG A 54 THR A 56 -1 O THR A 56 N HIS A 49
LINK SG CYS A 26 ZN ZN A 101 1555 1555 2.30
LINK SG CYS A 29 ZN ZN A 101 1555 1555 2.29
LINK SG CYS A 59 ZN ZN A 101 1555 1555 2.29
LINK SG CYS A 62 ZN ZN A 101 1555 1555 2.30
SITE 1 AC1 5 CYS A 26 ASN A 28 CYS A 29 CYS A 59
SITE 2 AC1 5 CYS A 62
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
