Header list of 6i1b.pdb file
Complete list - 16 20 Bytes
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
Complete list - 16 20 Bytes