Header list of 1bbn.pdb file
Complete list - 12 20 Bytes
HEADER CYTOKINE 01-MAY-92 1BBN
TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4
TITLE 2 BY MULTI-DIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE
TITLE 3 SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-4;
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 GENE: POTENTIAL
KEYWDS CYTOKINE
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,B.POWERS,D.S.GARRETT,A.M.GRONENBORN
REVDAT 2 24-FEB-09 1BBN 1 VERSN
REVDAT 1 31-OCT-93 1BBN 0
JRNL AUTH R.POWERS,D.S.GARRETT,C.J.MARCH,E.A.FRIEDEN,
JRNL AUTH 2 A.M.GRONENBORN,G.M.CLORE
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN
JRNL TITL 2 INTERLEUKIN-4 BY MULTIDIMENSIONAL HETERONUCLEAR
JRNL TITL 3 MAGNETIC RESONANCE SPECTROSCOPY.
JRNL REF SCIENCE V. 256 1673 1992
JRNL REFN ISSN 0036-8075
JRNL PMID 1609277
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.POWERS,D.S.GARRETT,C.J.MARCH,E.A.FRIEDEN,
REMARK 1 AUTH 2 A.M.GRONENBORN,G.M.CLORE
REMARK 1 TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN
REMARK 1 TITL 2 INTERLEUKIN-4 BY MULTIDIMENSIONAL HETERONUCLEAR
REMARK 1 TITL 3 MAGNETIC RESONANCE SPECTROSCOPY
REMARK 1 REF SCIENCE V. 256 1673 1992
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.POWERS,D.S.GARRETT,C.J.MARCH,E.A.FRIEDEN,
REMARK 1 AUTH 2 A.M.GRONENBORN,G.M.CLORE
REMARK 1 TITL 1H, 15N, 13C AND 13CO ASSIGNMENTS OF HUMAN
REMARK 1 TITL 2 INTERLEUKIN-4 USING THREE-DIMENSIONAL DOUBLE-AND
REMARK 1 TITL 3 TRIPLE-RESONANCE HETERONUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 4 SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 31 4334 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.S.GARRETT,R.POWERS,C.J.MARCH,E.A.FRIEDEN,
REMARK 1 AUTH 2 G.M.CLORE,A.M.GRONENBORN
REMARK 1 TITL DETERMINATION OF THE SECONDARY STRUCTURE AND
REMARK 1 TITL 2 FOLDING TOPOLOGY OF HUMAN INTERLEUKIN-4 USING
REMARK 1 TITL 3 THREE-DIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 4 SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 31 4347 1992
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 823 INTERPROTON DISTANCE
REMARK 3 RESTRAINTS FROM NOE MEASUREMENTS; 98 HYDROGEN-BONDING
REMARK 3 DISTANCE RESTRAINTS FOR 49 HYDROGEN-BONDS IDENTIFIED ON
REMARK 3 THE BASIS OF THE NOE AND AMIDE PROTON EXCHANGE DATA, AS
REMARK 3 WELL AS THE INITIAL STRUCTURE CALCULATIONS; AND 101 PHI
REMARK 3 AND 82 PSI BACKBONE TORSION ANGLE RESTRAINTS DERIVED FROM
REMARK 3 COUPLING CONSTANTS, NOE DATA, AND 13C SECONDARY CHEMICAL
REMARK 3 SHIFTS.
REMARK 3
REMARK 3 THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID
REMARK 3 METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED
REMARK 3 ANNEALING METHOD (M. NILGES, G. M. CLORE, AND A. M.
REMARK 3 GRONENBORN FEBS LETT. 229, 317-324 (1988)).
REMARK 3
REMARK 3 DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL
REMARK 3 STATISTICS ARE GIVEN IN REFERENCE 1 (I.E. AGREEMENT WITH
REMARK 3 EXPERIMENTAL RESTRAINTS, DEVIATIONS FROM IDEALITY FOR BOND
REMARK 3 LENGTHS, ANGLES, PLANES AND CHIRALITY, NON-BONDED CONTACTS,
REMARK 3 ATOMIC RMS DIFFERENCES BETWEEN THE CALCULATED STRUCTURES.
REMARK 3
REMARK 3 RESIDUES 1 - 6 AND 132 - 133 AT THE N- AND C-TERMINI ARE
REMARK 3 DISORDERED.
REMARK 3
REMARK 3 THE RESTRAINED MINIMIZED AVERAGE STRUCTURE IS PRESENTED IN
REMARK 3 THIS ENTRY. THIS WAS OBTAINED BY AVERAGING THE COORDINATES
REMARK 3 OF THE INDIVIDUAL STRUCTURES AND SUBJECTING THE RESULTING
REMARK 3 COORDINATES TO RESTRAINED MINIMIZATION. MODELS 1 - 22,
REMARK 3 PRESENTED IN PROTEIN DATA BANK ENTRY 1BCN, REPRESENT THE
REMARK 3 INDIVIDUAL MODELS.
REMARK 3
REMARK 3 THE (SA)R RESTRAINED MINIMIZED MEAN STRUCTURE WAS DERIVED
REMARK 3 BY AVERAGING THE COORDINATES OF THE INDIVIDUAL SA
REMARK 3 STRUCTURES (BEST FITTED TO RESIDUES 7 - 131), AND
REMARK 3 SUBJECTING THE RESULTING COORDINATES TO RESTRAINED
REMARK 3 MINIMIZATION. THE QUANTITY PRESENTED IN COLUMNS 61 - 66 IN
REMARK 3 THIS ENTRY REPRESENTS THE ATOMIC RMS DEVIATIONS OF THE 22
REMARK 3 INDIVIDUAL SA STRUCTURES ABOUT THE MEAN STRUCTURE.
REMARK 4
REMARK 4 1BBN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 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 ALA A 2 -42.10 -177.99
REMARK 500 ALA A 4 -168.16 -177.83
REMARK 500 LYS A 6 95.39 -55.30
REMARK 500 CYS A 7 -32.26 -179.28
REMARK 500 ILE A 9 -64.84 -90.97
REMARK 500 GLN A 24 70.30 -103.46
REMARK 500 LYS A 25 53.26 -116.68
REMARK 500 THR A 26 -46.38 -136.68
REMARK 500 GLU A 30 45.31 -95.61
REMARK 500 VAL A 33 -145.05 -123.85
REMARK 500 LYS A 41 -70.79 -124.34
REMARK 500 LEU A 70 -70.92 -55.79
REMARK 500 ALA A 72 34.21 -158.67
REMARK 500 ASN A 101 -78.71 -121.83
REMARK 500 PRO A 104 86.04 -57.55
REMARK 500 LYS A 106 -36.26 -158.88
REMARK 500 ALA A 108 140.15 -176.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BCN RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE NUMBERING SCHEME IN THIS STRUCTURE INCLUDES THE
REMARK 999 FOUR-RESIDUE SEQUENCE GLU-ALA-GLU-ALA AT THE N-TERMINUS OF
REMARK 999 THE RECOMBINANT PROTEIN WHICH IS NOT PART OF THE NATURAL
REMARK 999 HUMAN IL-4; THE NATURAL IL-4 SEQUENCE THEREFORE STARTS AT
REMARK 999 RESIDUE 5. IN ADDITION, THE TWO POTENTIAL N-LINKED
REMARK 999 GLYCOSYLATION SITES AT ASN 42 AND ASN 109 HAVE BEEN
REMARK 999 CHANGED TO ASP BY SITE DIRECTED MUTAGENESIS TO PREVENT
REMARK 999 HYPERGLYCOSYLATION IN THE YEAST HOST.
DBREF 1BBN A 5 133 UNP P05112 IL4_HUMAN 25 153
SEQADV 1BBN ASP A 42 UNP P05112 ASN 62 CONFLICT
SEQADV 1BBN ASP A 109 UNP P05112 ASN 129 CONFLICT
SEQRES 1 A 133 GLU ALA GLU ALA HIS LYS CYS ASP ILE THR LEU GLN GLU
SEQRES 2 A 133 ILE ILE LYS THR LEU ASN SER LEU THR GLU GLN LYS THR
SEQRES 3 A 133 LEU CYS THR GLU LEU THR VAL THR ASP ILE PHE ALA ALA
SEQRES 4 A 133 SER LYS ASP THR THR GLU LYS GLU THR PHE CYS ARG ALA
SEQRES 5 A 133 ALA THR VAL LEU ARG GLN PHE TYR SER HIS HIS GLU LYS
SEQRES 6 A 133 ASP THR ARG CYS LEU GLY ALA THR ALA GLN GLN PHE HIS
SEQRES 7 A 133 ARG HIS LYS GLN LEU ILE ARG PHE LEU LYS ARG LEU ASP
SEQRES 8 A 133 ARG ASN LEU TRP GLY LEU ALA GLY LEU ASN SER CYS PRO
SEQRES 9 A 133 VAL LYS GLU ALA ASP GLN SER THR LEU GLU ASN PHE LEU
SEQRES 10 A 133 GLU ARG LEU LYS THR ILE MET ARG GLU LYS TYR SER LYS
SEQRES 11 A 133 CYS SER SER
HELIX 1 1 ILE A 9 LEU A 21 1 13
HELIX 2 2 THR A 44 HIS A 62 1 19
HELIX 3 3 HIS A 63 LYS A 65 5 3
HELIX 4 4 ASP A 66 GLY A 71 1 6
HELIX 5 5 ALA A 74 GLY A 99 1 26
HELIX 6 6 THR A 112 SER A 129 1 18
SHEET 1 A 2 VAL A 33 THR A 34 0
SHEET 2 A 2 GLN A 110 SER A 111 -1 O SER A 111 N VAL A 33
SSBOND 1 CYS A 7 CYS A 131 1555 1555 2.02
SSBOND 2 CYS A 28 CYS A 69 1555 1555 2.02
SSBOND 3 CYS A 50 CYS A 103 1555 1555 2.01
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 - 12 20 Bytes