HEADER CYTOKINE 01-MAY-01 1IJZ
TITLE SOLUTION STRUCTURE OF HUMAN IL-13
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-13;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IL-13;
COMPND 5 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: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET
KEYWDS LEFT-HANDED FOUR-HELIX BUNDLE, CYTOKINE
EXPDTA SOLUTION NMR
AUTHOR F.J.MOY,E.DIBLASIO,J.WILHELM,R.POWERS
REVDAT 3 23-FEB-22 1IJZ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1IJZ 1 VERSN
REVDAT 1 01-MAY-02 1IJZ 0
JRNL AUTH F.J.MOY,E.DIBLASIO,J.WILHELM,R.POWERS
JRNL TITL SOLUTION STRUCTURE OF HUMAN IL-13 AND IMPLICATION FOR
JRNL TITL 2 RECEPTOR BINDING.
JRNL REF J.MOL.BIOL. V. 310 219 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11419948
JRNL DOI 10.1006/JMBI.2001.4764
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, X-PLOR 3.84
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUMGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2848 RESTRAINTS, 2248 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 299 DIHEDRAL ANGLE RESTRAINTS,50 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS, 205 CA/CB CONSTRAINTS, 96 COUPLING CONSTANT
REMARK 3 CONSTRAINTS.
REMARK 3 ADDITIONALLY, A RAMACHANDRAN CONFORMATIONAL DATABASE AND RADIUS OF
REMARK 3 GYRATION
REMARK 3 TARGET FUNCTION WAS USED DURING THE REFINEMENT.
REMARK 4
REMARK 4 1IJZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013350.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 6.0; 6.0; 6.0
REMARK 210 IONIC STRENGTH : 40 MM SODIUM PHOSPHATE, 2 MM
REMARK 210 NAN3, 40 MM NACL; 40 MM SODIUM
REMARK 210 PHOSPHATE, 2 MM NAN3, 40 MM NACL;
REMARK 210 40 MM SODIUM PHOSPHATE, 2 MM
REMARK 210 NAN3, 40 MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM INTERLEUKIN-13 U-15N; 40MM
REMARK 210 PHOSPHATE BUFFER; 2MM NAN3; 40
REMARK 210 MM NACL 90% H2O, 10% D2O; PH 6.0;
REMARK 210 1MM INTERLEUKIN-13 U-15N,U-13C;
REMARK 210 40MM PHOSPHATE BUFFER; 2MM NAN3;
REMARK 210 40 MM NACL 90% H2O, 10% D2O; PH
REMARK 210 6.0; 1MM INTERLEUKIN-13 U-15N,U-
REMARK 210 13C; 40MM PHOSPHATE BUFFER; 2MM
REMARK 210 NAN3; 40 MM NACL; 100% D2O; PH
REMARK 210 6.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNCA-J; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 97.231.15.18, PIPP 4.2.8
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 O CYS A 29 H GLY A 31 1.54
REMARK 500 O ALA A 41 H MET A 43 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 LYS A 25 -80.01 -88.19
REMARK 500 ASN A 30 54.63 -69.06
REMARK 500 THR A 40 -100.03 -138.29
REMARK 500 ALA A 41 -64.82 -109.95
REMARK 500 ALA A 77 0.13 -64.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IK0 RELATED DB: PDB
REMARK 900 1IK0 CONTAINS THE ENSEMBLE STRUCTURES FOR IL-13
DBREF 1IJZ A 2 113 UNP P35225 IL13_HUMAN 21 132
SEQADV 1IJZ MET A 1 UNP P35225 CLONING ARTIFACT
SEQRES 1 A 113 MET GLY PRO VAL PRO PRO SER THR ALA LEU ARG GLU LEU
SEQRES 2 A 113 ILE GLU GLU LEU VAL ASN ILE THR GLN ASN GLN LYS ALA
SEQRES 3 A 113 PRO LEU CYS ASN GLY SER MET VAL TRP SER ILE ASN LEU
SEQRES 4 A 113 THR ALA GLY MET TYR CYS ALA ALA LEU GLU SER LEU ILE
SEQRES 5 A 113 ASN VAL SER GLY CYS SER ALA ILE GLU LYS THR GLN ARG
SEQRES 6 A 113 MET LEU SER GLY PHE CYS PRO HIS LYS VAL SER ALA GLY
SEQRES 7 A 113 GLN PHE SER SER LEU HIS VAL ARG ASP THR LYS ILE GLU
SEQRES 8 A 113 VAL ALA GLN PHE VAL LYS ASP LEU LEU LEU HIS LEU LYS
SEQRES 9 A 113 LYS LEU PHE ARG GLU GLY ARG PHE ASN
HELIX 1 1 PRO A 5 ASN A 23 1 19
HELIX 2 2 GLY A 42 ILE A 52 1 11
HELIX 3 3 CYS A 57 ALA A 59 5 3
HELIX 4 4 ILE A 60 CYS A 71 1 12
HELIX 5 5 VAL A 92 GLY A 110 1 19
SHEET 1 A 2 MET A 33 TRP A 35 0
SHEET 2 A 2 LYS A 89 GLU A 91 -1 N ILE A 90 O VAL A 34
SSBOND 1 CYS A 29 CYS A 57 1555 1555 2.02
SSBOND 2 CYS A 45 CYS A 71 1555 1555 2.02
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
(ATOM LINES ARE NOT SHOWN.)
END