HEADER CYTOKINE 22-JAN-91 6I1B
TITLE HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN-1 BETA IN
TITLE 2 SOLUTION BY THREE-AND FOUR-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE
TITLE 3 SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-1 BETA;
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
KEYWDS CYTOKINE
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,A.M.GRONENBORN
REVDAT 3 16-MAR-22 6I1B 1 REMARK
REVDAT 2 24-FEB-09 6I1B 1 VERSN
REVDAT 1 15-OCT-92 6I1B 0
JRNL AUTH G.M.CLORE,P.T.WINGFIELD,A.M.GRONENBORN
JRNL TITL HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN 1
JRNL TITL 2 BETA IN SOLUTION BY THREE- AND FOUR-DIMENSIONAL NUCLEAR
JRNL TITL 3 MAGNETIC RESONANCE SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 30 2315 1991
JRNL REFN ISSN 0006-2960
JRNL PMID 2001363
JRNL DOI 10.1021/BI00223A005
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.M.CLORE,L.E.KAY,A.BAX,A.M.GRONENBORN
REMARK 1 TITL FOUR-DIMENSIONAL 13C(SLASH)13C-EDITED NUCLEAR OVERHAUSER
REMARK 1 TITL 2 ENHANCEMENT SPECTROSCOPY OF A PROTEIN IN SOLUTION:
REMARK 1 TITL 3 APPLICATION TO INTERLEUKIN-1BETA
REMARK 1 REF BIOCHEMISTRY V. 30 12 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.E.KAY,G.M.CLORE,A.BAX,A.M.GRONENBORN
REMARK 1 TITL FOUR-DIMENSIONAL HETERONUCLEAR TRIPLE-RESONANCE NMR
REMARK 1 TITL 2 SPECTROSCOPY OF INTERLEUKIN-1BETA IN SOLUTION
REMARK 1 REF SCIENCE V. 249 411 1990
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH G.M.CLORE,A.BAX,P.C.DRISCOLL,P.T.WINGFIELD,A.M.GRONENBORN
REMARK 1 TITL ASSIGNMENT OF THE SIDE-CHAIN 1H AND 13C RESONANCES OF
REMARK 1 TITL 2 INTERLEUKIN-1BETA USING DOUBLE-AND TRIPLE-RESONANCE
REMARK 1 TITL 3 HETERONUCLEAR THREE-DIMENSIONAL NMR SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 29 8172 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.M.CLORE,P.C.DRISCOLL,P.T.WINGFIELD,A.M.GRONENBORN
REMARK 1 TITL ANALYSIS OF THE BACKBONE DYNAMICS OF INTERLEUKIN-1BETA USING
REMARK 1 TITL 2 TWO-DIMENSIONAL INVERSE DETECTED HETERONUCLEAR 15N-1H NMR
REMARK 1 TITL 3 SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 29 7387 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.M.CLORE,A.BAX,P.T.WINGFIELD,A.M.GRONENBORN
REMARK 1 TITL IDENTIFICATION AND LOCALIZATION OF BOUND INTERNAL WATER IN
REMARK 1 TITL 2 THE SOLUTION STRUCTURE OF INTERLEUKIN 1BETA BY HETERONUCLEAR
REMARK 1 TITL 3 THREE-DIMENSIONAL 1H ROTATING-FRAME OVERHAUSER 15N-1H
REMARK 1 TITL 4 MULTIPLE QUANTUM COHERENCE NMR SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 29 5671 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 6
REMARK 1 AUTH G.M.CLORE,P.C.DRISCOLL,P.T.WINGFIELD,A.M.GRONENBORN
REMARK 1 TITL LOW RESOLUTION STRUCTURE OF INTERLEUKIN-1BETA IN SOLUTION
REMARK 1 TITL 2 DERIVED FROM 1H-15N HETERONUCLEAR THREE-DIMENSIONAL NUCLEAR
REMARK 1 TITL 3 MAGNETIC RESONANCE SPECTROSCOPY
REMARK 1 REF J.MOL.BIOL. V. 214 811 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 7
REMARK 1 AUTH P.C.DRISCOLL,A.M.GRONENBORN,P.T.WINGFIELD,G.M.CLORE
REMARK 1 TITL DETERMINATION OF THE SECONDARY STRUCTURE AND MOLECULAR
REMARK 1 TITL 2 TOPOLOGY OF INTERLEUKIN-1BETA BY USE OF TWO-AND
REMARK 1 TITL 3 THREE-DIMENSIONAL HETERONUCLEAR 15N-1H NMR SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 29 4668 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 8
REMARK 1 AUTH P.C.DRISCOLL,G.M.CLORE,D.MARION,P.T.WINGFIELD,A.M.GRONENBORN
REMARK 1 TITL COMPLETE RESONANCE ASSIGNMENT FOR THE POLYPEPTIDE BACKBONE
REMARK 1 TITL 2 OF INTERLEUKIN 1BETA USING THREE-DIMENSIONAL HETERONUCLEAR
REMARK 1 TITL 3 NMR SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 29 3542 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 9
REMARK 1 AUTH D.MARION,P.C.DRISCOLL,L.E.KAY,P.T.WINGFIELD,A.BAX,
REMARK 1 AUTH 2 A.M.GRONENBORN,G.M.CLORE
REMARK 1 TITL OVERCOMING THE OVERLAP PROBLEM IN THE ASSIGNMENT OF 1H NMR
REMARK 1 TITL 2 SPECTRA OF LARGER PROTEINS BY USE OF THREE-DIMENSIONAL
REMARK 1 TITL 3 HETERONUCLEAR 1H-15N HARTMANN-HAHN-MULTIPLE QUANTUM
REMARK 1 TITL 4 COHERENCE AND NUCLEAR OVERHAUSER-MULTIPLE QUANTUM COHERENCE
REMARK 1 TITL 5 SPECTROSCOPY: APPLICATION TO INTERLEUKIN 1BETA
REMARK 1 REF BIOCHEMISTRY V. 28 6150 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 2630 INTERPROTON DISTANCE
REMARK 3 RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 114 HYDROGEN
REMARK 3 BONDING DISTANCE RESTRAINTS FOR 57 HYDROGEN-BONDS
REMARK 3 IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON
REMARK 3 EXCHANGE DATA, AS WELL AS THE INITIAL STRUCTURE
REMARK 3 CALCULATIONS; 36 DISTANCE RESTRAINTS RELATING TO NH-H2O-CO
REMARK 3 BRIDGING HYDROGEN BONDS INVOLVING 7 BOUND WATER MOLECULES
REMARK 3 AND IDENTIFIED FROM ROE MEASUREMENTS; AND 152 PHI AND 115
REMARK 3 PSI BACKBONE TORSION ANGLE RESTRAINTS AND 99 CHI SIDE CHAIN
REMARK 3 TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTRAINTS
REMARK 3 AND NOE DATA. THE LATTER ARE OBTAINED USING THE
REMARK 3 CONFORMATIONAL GRID SEARCH PROGRAM "STEREOSEARCH" (M.
REMARK 3 NILGES, G. M. CLORE, AND A. M. GRONENBORN (1990)
REMARK 3 BIOPOLYMERS 29, 813-822). THE METHOD USED TO DETERMINE THE
REMARK 3 STRUCTURES IS THE HYBRID METRIC MATRIX DISTANCE
REMARK 3 GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD (M. NILGES,
REMARK 3 G. M. CLORE, AND A. M. GRONENBORN, (1990) FEBS LETT. 229,
REMARK 3 317-324).
REMARK 3
REMARK 3 A TOTAL OF 32 STRUCTURES WERE CALCULATED. THIS ENTRY
REMARK 3 REPRESENTS THE RESTRAINED MINIMIZED AVERAGE STRUCTURE. IT
REMARK 3 WAS OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL
REMARK 3 STRUCTURES AND SUBJECTING THE RESULTING COORDINATES TO
REMARK 3 RESTRAINED MINIMIZATION.
REMARK 3
REMARK 3 THE QUANTITY PRESENTED IN THE B-VALUE FIELD IN THIS
REMARK 3 COORDINATE FILE REPRESENTS THE ATOMIC RMS DEVIATION OF THE
REMARK 3 INDIVIDUAL STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS.
REMARK 4
REMARK 4 6I1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179834.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
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: 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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 30 CG HIS A 30 ND1 -0.115
REMARK 500 TRP A 120 CG TRP A 120 CD2 -0.106
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TRP A 120 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 120 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP A 120 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 TRP A 120 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 DEGREES
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 2 34.35 -74.46
REMARK 500 CYS A 8 144.97 -171.69
REMARK 500 GLN A 15 4.75 82.70
REMARK 500 GLU A 50 84.92 -67.28
REMARK 500 SER A 52 -150.47 -128.35
REMARK 500 ASN A 66 39.67 -91.43
REMARK 500 ASP A 75 45.51 85.20
REMARK 500 ALA A 115 -19.14 -48.41
REMARK 500 ASN A 119 -9.72 84.10
REMARK 500 ALA A 127 161.95 -48.41
REMARK 500 ASN A 129 78.56 51.94
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 4 0.10 SIDE CHAIN
REMARK 500 ARG A 11 0.32 SIDE CHAIN
REMARK 500 ARG A 98 0.29 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7I1B RELATED DB: PDB
DBREF 6I1B A 1 153 UNP P01584 IL1B_HUMAN 117 269
SEQRES 1 A 153 ALA PRO VAL ARG SER LEU ASN CYS THR LEU ARG ASP SER
SEQRES 2 A 153 GLN GLN LYS SER LEU VAL MET SER GLY PRO TYR GLU LEU
SEQRES 3 A 153 LYS ALA LEU HIS LEU GLN GLY GLN ASP MET GLU GLN GLN
SEQRES 4 A 153 VAL VAL PHE SER MET SER PHE VAL GLN GLY GLU GLU SER
SEQRES 5 A 153 ASN ASP LYS ILE PRO VAL ALA LEU GLY LEU LYS GLU LYS
SEQRES 6 A 153 ASN LEU TYR LEU SER CYS VAL LEU LYS ASP ASP LYS PRO
SEQRES 7 A 153 THR LEU GLN LEU GLU SER VAL ASP PRO LYS ASN TYR PRO
SEQRES 8 A 153 LYS LYS LYS MET GLU LYS ARG PHE VAL PHE ASN LYS ILE
SEQRES 9 A 153 GLU ILE ASN ASN LYS LEU GLU PHE GLU SER ALA GLN PHE
SEQRES 10 A 153 PRO ASN TRP TYR ILE SER THR SER GLN ALA GLU ASN MET
SEQRES 11 A 153 PRO VAL PHE LEU GLY GLY THR LYS GLY GLY GLN ASP ILE
SEQRES 12 A 153 THR ASP PHE THR MET GLN PHE VAL SER SER
FORMUL 2 HOH *7(H2 O)
HELIX 1 1 GLN A 32 GLN A 39 5 8
HELIX 2 2 GLU A 96 PHE A 99 5 4
SHEET 1 A 6 LEU A 110 SER A 114 0
SHEET 2 A 6 PHE A 101 GLU A 105 -1 N ASN A 102 O GLU A 113
SHEET 3 A 6 ILE A 56 LEU A 62 -1 O ILE A 56 N LYS A 103
SHEET 4 A 6 PHE A 42 PHE A 46 -1 N SER A 43 O GLY A 61
SHEET 5 A 6 SER A 5 ARG A 11 -1 O LEU A 6 N MET A 44
SHEET 6 A 6 THR A 147 PHE A 150 -1 O THR A 147 N ARG A 11
SHEET 1 B 3 SER A 17 GLY A 22 0
SHEET 2 B 3 GLU A 25 LEU A 29 -1 O GLU A 25 N GLY A 22
SHEET 3 B 3 MET A 130 PRO A 131 -1 O MET A 130 N ALA A 28
SHEET 1 C 2 LEU A 67 LEU A 73 0
SHEET 2 C 2 PRO A 78 SER A 84 -1 O THR A 79 N VAL A 72
SHEET 1 D 2 TYR A 121 SER A 123 0
SHEET 2 D 2 PHE A 133 GLY A 135 -1 O PHE A 133 N SER A 123
CISPEP 1 TYR A 90 PRO A 91 0 -0.33
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
