HEADER LIGASE 01-MAR-07 2JO9
TITLE MOUSE ITCH 3RD WW DOMAIN COMPLEX WITH THE EPSTEIN-BARR VIRUS LATENT
TITLE 2 MEMBRANE PROTEIN 2A DERIVED PEPTIDE EEPPPPYED
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ITCHY E3 UBIQUITIN PROTEIN LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: WW 3 DOMAIN, SEQUENCE DATABASE RESIDUES 399-432;
COMPND 5 EC: 6.3.2.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LATENT MEMBRANE PROTEIN 2;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: SEQUENCE DATABASE RESIDUES 54-62;
COMPND 11 SYNONYM: TERMINAL PROTEIN;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ITCH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PETM30;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHEIZED. THE SEQUENCE
SOURCE 14 OF THE PEPTIDE IS NATURALLY FOUND IN EPSTEIN-BARR VIRUS.
KEYWDS ITCH, WW, COMPLEX, EPSTEIN-BARR VIRUS, LMP2A, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.J.MACIAS,A.Z.SHAW,P.MARTIN-MALPARTIDA,B.MORALES,L.RUIZ,X.RAMIREZ-
AUTHOR 2 ESPAIN,F.YRAOLA,M.ROYO
REVDAT 5 20-DEC-23 2JO9 1 REMARK
REVDAT 4 09-MAR-22 2JO9 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2JO9 1 VERSN
REVDAT 2 08-MAY-07 2JO9 1 JRNL
REVDAT 1 17-APR-07 2JO9 0
JRNL AUTH B.MORALES,X.RAMIREZ-ESPAIN,A.Z.SHAW,P.MARTIN-MALPARTIDA,
JRNL AUTH 2 F.YRAOLA,E.SANCHEZ-TILLO,C.FARRERA,A.CELADA,M.ROYO,
JRNL AUTH 3 M.J.MACIAS
JRNL TITL NMR STRUCTURAL STUDIES OF THE ITCHWW3 DOMAIN REVEAL THAT
JRNL TITL 2 PHOSPHORYLATION AT T30 INHIBITS THE INTERACTION WITH
JRNL TITL 3 PPXY-CONTAINING LIGANDS
JRNL REF STRUCTURE V. 15 473 2007
JRNL REFN ISSN 0969-2126
JRNL PMID 17437719
JRNL DOI 10.1016/J.STR.2007.03.005
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TOPSPIN, ARIA
REMARK 3 AUTHORS : BRUKER BIOSPIN (TOPSPIN), LINGE, O'DONOGHUE AND
REMARK 3 NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ARIA 1.2 SOFTWARE USED, ALL NOES
REMARK 3 MANUALLY ASSIGNED
REMARK 4
REMARK 4 2JO9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000100081.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 0.4
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM [U-100% 15N] WW3, 3.0 MM
REMARK 210 LIGAND, 20 MM SODIUM PHOSPHATE,
REMARK 210 100 MM NACL, 0.02% V/V SODIUM
REMARK 210 AZIDE, 90% H2O/10% D2O; 1.0 MM
REMARK 210 [U-100% 13C; U-100% 15N] WW3,
REMARK 210 3.0 MM LIGAND, 20 MM SODIUM
REMARK 210 PHOSPHATE, 100 MM NACL, 0.02% V/
REMARK 210 V SODIUM AZIDE, 90% H2O/10% D2O;
REMARK 210 1.0 MM WW3, 3.0 MM LIGAND, 20 MM
REMARK 210 SODIUM PHOSPHATE, 100 MM NACL,
REMARK 210 0.02% V/V SODIUM AZIDE, 90% H2O/
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D CBCA(CO)NH; 3D CBCANH; 2D 1H
REMARK 210 -15N HSQC; 3D 1H-15N NOESY; 3D
REMARK 210 1H-15N TOCSY; 3D 1H-13C NOESY;
REMARK 210 3D 1H-13C TOCSY; 2D 1H-1H NOESY;
REMARK 210 2D 1H-1H TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, ARIA
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 1
REMARK 465 ALA A 2
REMARK 465 MET A 3
REMARK 465 GLY A 4
REMARK 465 ARG A 36
REMARK 465 SER A 37
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-10
REMARK 470 RES CSSEQI ATOMS
REMARK 470 PRO A 35 O
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 11 HE2 HIS A 25 1.59
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 16 -51.47 -29.31
REMARK 500 1 ASN A 17 -80.92 -90.58
REMARK 500 1 ARG A 28 65.01 60.25
REMARK 500 1 GLU B 108 110.44 -163.43
REMARK 500 2 SER A 16 -52.83 -29.13
REMARK 500 2 ASN A 17 -80.41 -90.79
REMARK 500 3 SER A 16 -57.29 -29.08
REMARK 500 3 ASN A 17 -80.48 -90.78
REMARK 500 3 ARG A 28 70.69 58.10
REMARK 500 3 GLU B 108 -80.44 -70.45
REMARK 500 4 SER A 16 -55.69 -29.34
REMARK 500 4 ASN A 17 -80.50 -90.79
REMARK 500 5 SER A 16 -51.42 -29.50
REMARK 500 5 ASN A 17 -81.07 -90.58
REMARK 500 5 ARG A 28 32.63 73.39
REMARK 500 5 GLU B 108 -31.34 -155.04
REMARK 500 6 SER A 16 -53.59 -29.66
REMARK 500 6 ASN A 17 -80.65 -90.64
REMARK 500 6 TYR B 107 -83.88 -78.06
REMARK 500 6 GLU B 108 81.10 48.84
REMARK 500 7 SER A 16 -58.77 -29.17
REMARK 500 7 ASN A 17 -80.43 -90.74
REMARK 500 8 SER A 16 -59.88 -28.88
REMARK 500 8 ASN A 17 -80.26 -90.51
REMARK 500 9 SER A 16 -53.83 -29.23
REMARK 500 9 ASN A 17 -80.82 -90.59
REMARK 500 9 ARG A 28 31.46 72.13
REMARK 500 10 SER A 16 -57.02 -29.00
REMARK 500 10 ASN A 17 -81.14 -90.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 8 GLY A 9 1 134.20
REMARK 500 GLY A 18 ARG A 19 1 -147.77
REMARK 500 PRO A 8 GLY A 9 2 134.78
REMARK 500 GLY A 18 ARG A 19 2 -149.85
REMARK 500 PRO A 8 GLY A 9 3 133.35
REMARK 500 ASP A 15 SER A 16 3 -144.84
REMARK 500 PRO A 8 GLY A 9 4 137.63
REMARK 500 ASP A 15 SER A 16 4 -147.86
REMARK 500 PRO A 8 GLY A 9 5 137.51
REMARK 500 GLY A 18 ARG A 19 5 -146.77
REMARK 500 PRO A 8 GLY A 9 6 136.90
REMARK 500 ASP A 15 SER A 16 6 -148.48
REMARK 500 PRO A 8 GLY A 9 7 135.37
REMARK 500 ASP A 15 SER A 16 7 -139.72
REMARK 500 PRO A 8 GLY A 9 8 131.94
REMARK 500 ASP A 15 SER A 16 8 -141.61
REMARK 500 PRO A 8 GLY A 9 9 136.66
REMARK 500 ASP A 15 SER A 16 9 -145.04
REMARK 500 PRO A 8 GLY A 9 10 138.12
REMARK 500 ASP A 15 SER A 16 10 -146.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JOC RELATED DB: PDB
DBREF 2JO9 A 4 37 UNP Q8C863 ITCH_MOUSE 399 432
DBREF 2JO9 B 101 109 UNP P13285 LMP2_EBV 54 62
SEQADV 2JO9 GLY A 1 UNP Q8C863 CLONING ARTIFACT
SEQADV 2JO9 ALA A 2 UNP Q8C863 CLONING ARTIFACT
SEQADV 2JO9 MET A 3 UNP Q8C863 CLONING ARTIFACT
SEQRES 1 A 37 GLY ALA MET GLY PRO LEU PRO PRO GLY TRP GLU LYS ARG
SEQRES 2 A 37 THR ASP SER ASN GLY ARG VAL TYR PHE VAL ASN HIS ASN
SEQRES 3 A 37 THR ARG ILE THR GLN TRP GLU ASP PRO ARG SER
SEQRES 1 B 9 GLU GLU PRO PRO PRO PRO TYR GLU ASP
SHEET 1 A 3 TRP A 10 THR A 14 0
SHEET 2 A 3 VAL A 20 ASN A 24 -1 O TYR A 21 N ARG A 13
SHEET 3 A 3 ILE A 29 GLN A 31 -1 O GLN A 31 N PHE A 22
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
