Header list of 1je4.pdb file
Complete list - 27 202 Bytes
HEADER ANTIVIRAL PROTEIN 15-JUN-01 1JE4
TITLE SOLUTION STRUCTURE OF THE MONOMERIC VARIANT OF THE CHEMOKINE MIP-1BETA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACROPHAGE INFLAMMATORY PROTEIN 1-BETA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MIP-1BETA, T-CELL ACTIVATION PROTEIN 2, ACT-2, LYMPHOCYTE
COMPND 5 ACTIVATION GENE-1 PROTEIN, LAG-1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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: PET32
KEYWDS MIP-1BETA, CHEMOKINE, MACROPHAGE INFLAMMATORY PROTEIN, ANTIVIRAL
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR S.KIM,S.JAO,J.S.LAURENCE,P.J.LIWANG
REVDAT 3 27-OCT-21 1JE4 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1JE4 1 VERSN
REVDAT 1 03-OCT-01 1JE4 0
JRNL AUTH S.KIM,S.JAO,J.S.LAURENCE,P.J.LIWANG
JRNL TITL STRUCTURAL COMPARISON OF MONOMERIC VARIANTS OF THE CHEMOKINE
JRNL TITL 2 MIP-1BETA HAVING DIFFERING ABILITY TO BIND THE RECEPTOR
JRNL TITL 3 CCR5.
JRNL REF BIOCHEMISTRY V. 40 10782 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11535053
JRNL DOI 10.1021/BI011065X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.S.LAURENCE,C.BLANPAIN,J.W.BURGNER,M.PARMENTIER,P.J.LIWANG
REMARK 1 TITL CC CHEMOKINE MIP-1BETA CAN FUNCTION AS A MONOMER AND DEPENDS
REMARK 1 TITL 2 ON PHE13 FOR RECEPTOR BINDING
REMARK 1 REF BIOCHEMISTRY V. 39 3401 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI9923196
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.J.LODI,D.S.GARRETT,J.KUSZEWSKI,M.L.TSANG,J.A.WEATHERBEE,
REMARK 1 AUTH 2 W.J.LEONARD,A.M.GRONENBORN,G.M.CLORE
REMARK 1 TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF THE BETA CHEMOKINE
REMARK 1 TITL 2 HMIP-1BETA BY MULTIDIMENSIONAL NMR
REMARK 1 REF SCIENCE V. 263 1762 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, CNS 1.0
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURE IS BASED ON A TOTAL 940 RESTRAINTS, 851
REMARK 3 DISTANCE CONSTRAINTS, 69 DIHEDRAL ANGLE RESTRAINTS, 20 DISTANCE
REMARK 3 RESTRAINTS FOR 10 HYDROGEN BONDS.
REMARK 4
REMARK 4 1JE4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013670.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 2.5
REMARK 210 IONIC STRENGTH : 20MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-2MM MIP-1B F13A U-15N, 13C;
REMARK 210 20MM NA-PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.0
REMARK 210 METHOD USED : THE INITIAL FOLD WAS OBTAINED BY
REMARK 210 DISTANCE GEOMETRY AND FURTHER
REMARK 210 REFINED BY 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 STANDARD 3D 15N OR 13C
REMARK 210 EDITED NMR EXPERIMENTS.
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 ASP A 6 58.19 -147.62
REMARK 500 ALA A 10 32.26 -165.58
REMARK 500 ALA A 17 37.86 -97.14
REMARK 500 PHE A 24 30.74 -97.26
REMARK 500 VAL A 26 -64.25 -90.03
REMARK 500 SER A 32 -170.09 -60.33
REMARK 500 ASP A 53 109.08 -57.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HUM RELATED DB: PDB
REMARK 900 1HUM IS THE DIMERIC MIP-1BETA WILD-TYPE PROTEIN.
REMARK 900 RELATED ID: 1VMP RELATED DB: PDB
REMARK 900 1VMP BINDS TO CCR5 WHICH IS A NATURAL RECEPTOR OF MIP-1BETA.
DBREF 1JE4 A 1 69 UNP P13236 CCL4_HUMAN 24 92
SEQADV 1JE4 ALA A 13 UNP P13236 PHE 36 ENGINEERED MUTATION
SEQRES 1 A 69 ALA PRO MET GLY SER ASP PRO PRO THR ALA CYS CYS ALA
SEQRES 2 A 69 SER TYR THR ALA ARG LYS LEU PRO ARG ASN PHE VAL VAL
SEQRES 3 A 69 ASP TYR TYR GLU THR SER SER LEU CYS SER GLN PRO ALA
SEQRES 4 A 69 VAL VAL PHE GLN THR LYS ARG SER LYS GLN VAL CYS ALA
SEQRES 5 A 69 ASP PRO SER GLU SER TRP VAL GLN GLU TYR VAL TYR ASP
SEQRES 6 A 69 LEU GLU LEU ASN
HELIX 1 1 PRO A 21 ASN A 23 5 3
HELIX 2 2 GLU A 56 LEU A 68 1 13
SHEET 1 A 3 VAL A 25 GLU A 30 0
SHEET 2 A 3 VAL A 40 THR A 44 -1 N VAL A 41 O TYR A 29
SHEET 3 A 3 CYS A 51 ALA A 52 -1 O ALA A 52 N VAL A 40
SSBOND 1 CYS A 11 CYS A 35 1555 1555 2.03
SSBOND 2 CYS A 12 CYS A 51 1555 1555 2.03
CRYST1 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
Complete list - 27 202 Bytes