HEADER CYTOKINE 25-FEB-00 1EIG
TITLE SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE EOTAXIN-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EOTAXIN-2;
COMPND 3 CHAIN: A;
COMPND 4 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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CHEMOKINE, CHEMOTACTIC CYTOKINE, EOSINOPHIL CHEMOATTRACTANT, CYTOKINE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR K.L.MAYER,M.J.STONE
REVDAT 4 16-FEB-22 1EIG 1 REMARK
REVDAT 3 24-FEB-09 1EIG 1 VERSN
REVDAT 2 01-APR-03 1EIG 1 JRNL
REVDAT 1 06-DEC-00 1EIG 0
JRNL AUTH K.L.MAYER,M.J.STONE
JRNL TITL NMR SOLUTION STRUCTURE AND RECEPTOR PEPTIDE BINDING OF THE
JRNL TITL 2 CC CHEMOKINE EOTAXIN-2.
JRNL REF BIOCHEMISTRY V. 39 8382 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10913244
JRNL DOI 10.1021/BI000523J
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR, X-PLOR 98
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1000 STEPS AT 2000K, COOLED TO 1000K
REMARK 3 FOR 3 PS (1000 STEPS AT 3 FS/STEP), SLOW COOLED FROM 1000K TO
REMARK 3 100K (6000 STEPS AT 5 FS/STEP), 200 STEPS RESTRAINED ENERGY
REMARK 3 MINIMIZATION
REMARK 4
REMARK 4 1EIG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010606.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.1
REMARK 210 IONIC STRENGTH : 20 MM ACETATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM EOTAXIN-2 U-15N/13C; 20 MM
REMARK 210 NAOAC; 1 MM EOTAXIN-2 U-15N,13C;
REMARK 210 20 MM NAOAC; 1 MM EOTAXIN-2 U-
REMARK 210 15N,13C; 20 MM NAOAC; 1 MM
REMARK 210 EOTAXIN-2 10% 13C; 20 MM NAOAC
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYINOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, X-PLOR 98
REMARK 210 METHOD USED : HYBRID DISTANCE
REMARK 210 GEOMETRY/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: THIS 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 PRO A 17 H ARG A 20 1.57
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 PRO A 4 -90.36 -71.99
REMARK 500 SER A 5 52.52 -165.30
REMARK 500 PRO A 6 -160.84 -72.25
REMARK 500 LYS A 14 -155.50 -168.37
REMARK 500 ARG A 15 -154.52 -85.60
REMARK 500 GLN A 46 102.74 -160.46
REMARK 500 LYS A 66 -70.80 -92.59
REMARK 500 GLN A 67 -71.62 -49.70
REMARK 500 LYS A 68 85.12 -62.81
REMARK 500 LYS A 69 77.95 -66.87
REMARK 500 ALA A 70 -82.65 -54.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 15 0.31 SIDE CHAIN
REMARK 500 ARG A 20 0.30 SIDE CHAIN
REMARK 500 ARG A 29 0.31 SIDE CHAIN
REMARK 500 ARG A 58 0.30 SIDE CHAIN
REMARK 500 ARG A 73 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EIH RELATED DB: PDB
REMARK 900 20 STRUCTURES
DBREF 1EIG A 1 73 UNP O00175 CCL24_HUMAN 27 99
SEQADV 1EIG SER A 47 UNP O00175 PHE 73 SEE REMARK 999
SEQRES 1 A 73 VAL VAL ILE PRO SER PRO CYS CYS MET PHE PHE VAL SER
SEQRES 2 A 73 LYS ARG ILE PRO GLU ASN ARG VAL VAL SER TYR GLN LEU
SEQRES 3 A 73 SER SER ARG SER THR CYS LEU LYS ALA GLY VAL ILE PHE
SEQRES 4 A 73 THR THR LYS LYS GLY GLN GLN SER CYS GLY ASP PRO LYS
SEQRES 5 A 73 GLN GLU TRP VAL GLN ARG TYR MET LYS ASN LEU ASP ALA
SEQRES 6 A 73 LYS GLN LYS LYS ALA SER PRO ARG
HELIX 1 1 GLN A 53 GLN A 67 1 15
SHEET 1 A 3 VAL A 21 LEU A 26 0
SHEET 2 A 3 VAL A 37 THR A 41 -1 O ILE A 38 N GLN A 25
SHEET 3 A 3 SER A 47 GLY A 49 -1 O SER A 47 N PHE A 39
SSBOND 1 CYS A 7 CYS A 32 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 48 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
