HEADER TRANSCRIPTION 30-MAR-07 2EQO
TITLE SOLUTION STRUCTURE OF THE STN_TRAF3IP1_ND DOMAIN OF INTERLEUKIN 13
TITLE 2 RECEPTOR ALPHA 1-BINDING PROTEIN-1 [HOMO SAPIENS]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TNF RECEPTOR-ASSOCIATED FACTOR 3-INTERACTING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: STN_TRAF3IP1_ND DOMAIN, UNP RESIDUES 1-133;
COMPND 5 SYNONYM: INTERLEUKIN 13 RECEPTOR ALPHA 1-BINDING PROTEIN 1, MIP-T3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P060925-07;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS STN_TRAF3IP1_ND DOMAIN, INTERLEUKIN 13 RECEPTOR ALPHA 1-BINDING
KEYWDS 2 PROTEIN-1 [HOMO SAPIENS], STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 3 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 4 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.DANG,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2EQO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2EQO 1 VERSN
REVDAT 1 02-OCT-07 2EQO 0
JRNL AUTH W.DANG,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE STN_TRAF3IP1_ND DOMAIN OF
JRNL TITL 2 INTERLEUKIN 13 RECEPTOR ALPHA 1-BINDING PROTEIN-1 [HOMO
JRNL TITL 3 SAPIENS]
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EQO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000026988.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9820, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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, TARGET
REMARK 210 FUNCTION
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: 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: 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 6 -60.26 -105.75
REMARK 500 1 MET A 8 98.48 -41.81
REMARK 500 1 PHE A 39 -34.24 -39.61
REMARK 500 1 PHE A 55 128.39 -34.46
REMARK 500 1 LYS A 71 -45.03 -134.76
REMARK 500 1 ASP A 74 -32.69 -35.93
REMARK 500 1 ALA A 97 133.94 -33.67
REMARK 500 2 GLU A 31 -31.71 -35.15
REMARK 500 2 PRO A 38 -172.58 -69.70
REMARK 500 2 MET A 65 -39.15 -39.56
REMARK 500 2 LYS A 71 -40.78 -130.70
REMARK 500 2 ASP A 74 -26.85 -38.79
REMARK 500 2 ALA A 97 130.92 -34.20
REMARK 500 2 LYS A 125 42.57 36.84
REMARK 500 2 ASP A 129 -46.92 -131.03
REMARK 500 3 GLN A 17 -35.02 -39.76
REMARK 500 3 GLU A 31 -30.36 -36.12
REMARK 500 3 MET A 56 41.20 72.22
REMARK 500 3 SER A 67 -36.32 -34.79
REMARK 500 3 ASP A 74 -34.42 -36.05
REMARK 500 3 ALA A 97 103.92 -34.29
REMARK 500 3 ARG A 101 -62.03 -94.54
REMARK 500 3 ASP A 129 -43.74 -133.04
REMARK 500 4 GLU A 31 -33.81 -34.42
REMARK 500 4 LYS A 32 -70.27 -68.48
REMARK 500 4 PRO A 38 -169.31 -69.71
REMARK 500 4 PHE A 55 123.64 -36.82
REMARK 500 4 MET A 65 -36.29 -37.51
REMARK 500 4 LYS A 71 -35.41 -131.02
REMARK 500 4 VAL A 87 -39.99 -39.00
REMARK 500 4 ALA A 97 118.03 -31.97
REMARK 500 4 LYS A 120 -33.43 -37.42
REMARK 500 5 SER A 2 105.90 -51.63
REMARK 500 5 SER A 3 41.92 35.41
REMARK 500 5 MET A 8 100.96 -45.01
REMARK 500 5 LYS A 22 -70.52 -81.47
REMARK 500 5 PRO A 38 -168.10 -69.75
REMARK 500 5 PHE A 55 108.17 -38.24
REMARK 500 5 MET A 56 43.38 74.07
REMARK 500 5 ASP A 129 -51.23 -121.58
REMARK 500 6 PHE A 55 119.97 -36.81
REMARK 500 6 MET A 65 -30.56 -37.82
REMARK 500 6 LYS A 71 -34.95 -131.42
REMARK 500 6 ALA A 97 115.27 -34.18
REMARK 500 7 SER A 3 86.05 -66.51
REMARK 500 7 PRO A 38 -170.95 -69.76
REMARK 500 7 ASP A 62 -38.99 -34.57
REMARK 500 7 MET A 65 -38.73 -35.98
REMARK 500 7 LYS A 71 -38.65 -130.30
REMARK 500 7 ASP A 74 -31.71 -37.79
REMARK 500
REMARK 500 THIS ENTRY HAS 157 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO003016239.1 RELATED DB: TARGETDB
DBREF 2EQO A 8 140 UNP Q8TDR0 Q8TDR0_HUMAN 1 133
SEQADV 2EQO GLY A 1 UNP Q8TDR0 EXPRESSION TAG
SEQADV 2EQO SER A 2 UNP Q8TDR0 EXPRESSION TAG
SEQADV 2EQO SER A 3 UNP Q8TDR0 EXPRESSION TAG
SEQADV 2EQO GLY A 4 UNP Q8TDR0 EXPRESSION TAG
SEQADV 2EQO SER A 5 UNP Q8TDR0 EXPRESSION TAG
SEQADV 2EQO SER A 6 UNP Q8TDR0 EXPRESSION TAG
SEQADV 2EQO GLY A 7 UNP Q8TDR0 EXPRESSION TAG
SEQRES 1 A 140 GLY SER SER GLY SER SER GLY MET ASN ALA ALA VAL VAL
SEQRES 2 A 140 ARG ARG THR GLN GLU ALA LEU GLY LYS VAL ILE ARG ARG
SEQRES 3 A 140 PRO PRO LEU THR GLU LYS LEU LEU SER LYS PRO PRO PHE
SEQRES 4 A 140 ARG TYR LEU HIS ASP ILE ILE THR GLU VAL ILE ARG MET
SEQRES 5 A 140 THR GLY PHE MET LYS GLY LEU TYR THR ASP ALA GLU MET
SEQRES 6 A 140 LYS SER ASP ASN VAL LYS ASP LYS ASP ALA LYS ILE SER
SEQRES 7 A 140 PHE LEU GLN LYS ALA ILE ASP VAL VAL VAL MET VAL SER
SEQRES 8 A 140 GLY GLU PRO LEU LEU ALA LYS PRO ALA ARG ILE VAL ALA
SEQRES 9 A 140 GLY HIS GLU PRO GLU ARG THR ASN GLU LEU LEU GLN ILE
SEQRES 10 A 140 ILE GLY LYS CYS CYS LEU ASN LYS LEU SER SER ASP ASP
SEQRES 11 A 140 ALA VAL ARG ARG VAL LEU ALA GLY GLU LYS
HELIX 1 1 ALA A 11 VAL A 23 1 13
HELIX 2 2 PHE A 39 MET A 52 1 14
HELIX 3 3 ASP A 62 ASN A 69 1 8
HELIX 4 5 LYS A 73 SER A 91 1 19
HELIX 5 6 PRO A 99 ILE A 102 1 4
HELIX 6 7 PRO A 108 LEU A 123 1 16
HELIX 7 8 ASP A 130 ALA A 137 1 8
CISPEP 1 ARG A 26 PRO A 27 1 0.00
CISPEP 2 ARG A 26 PRO A 27 2 -0.01
CISPEP 3 ARG A 26 PRO A 27 3 -0.01
CISPEP 4 ARG A 26 PRO A 27 4 0.03
CISPEP 5 ARG A 26 PRO A 27 5 0.09
CISPEP 6 ARG A 26 PRO A 27 6 -0.08
CISPEP 7 ARG A 26 PRO A 27 7 -0.09
CISPEP 8 ARG A 26 PRO A 27 8 0.05
CISPEP 9 ARG A 26 PRO A 27 9 0.08
CISPEP 10 ARG A 26 PRO A 27 10 0.00
CISPEP 11 ARG A 26 PRO A 27 11 -0.01
CISPEP 12 ARG A 26 PRO A 27 12 0.00
CISPEP 13 ARG A 26 PRO A 27 13 -0.09
CISPEP 14 ARG A 26 PRO A 27 14 -0.02
CISPEP 15 ARG A 26 PRO A 27 15 0.02
CISPEP 16 ARG A 26 PRO A 27 16 0.04
CISPEP 17 ARG A 26 PRO A 27 17 -0.01
CISPEP 18 ARG A 26 PRO A 27 18 0.00
CISPEP 19 ARG A 26 PRO A 27 19 0.05
CISPEP 20 ARG A 26 PRO A 27 20 -0.06
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
