Header list of 1iti.pdb file
Complete list - b 23 2 Bytes
HEADER CYTOKINE 12-APR-93 1ITI
TITLE THE HIGH RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN
TITLE 2 INTERLEUKIN-4 DETERMINED BY MULTI-DIMENSIONAL HETERONUCLEAR MAGNETIC
TITLE 3 RESONANCE 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 INTERLEUKIN-4, CYTOKINE
EXPDTA SOLUTION NMR
NUMMDL 31
AUTHOR G.M.CLORE,B.POWERS,D.S.GARRETT,A.M.GRONENBORN
REVDAT 5 23-FEB-22 1ITI 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1ITI 1 VERSN
REVDAT 3 01-APR-03 1ITI 1 JRNL
REVDAT 2 15-FEB-01 1ITI 1 TITLE KEYWDS EXPDTA JRNL
REVDAT 1 15-JUL-93 1ITI 0
JRNL AUTH R.POWERS,D.S.GARRETT,C.J.MARCH,E.A.FRIEDEN,A.M.GRONENBORN,
JRNL AUTH 2 G.M.CLORE
JRNL TITL THE HIGH-RESOLUTION, THREE-DIMENSIONAL SOLUTION STRUCTURE OF
JRNL TITL 2 HUMAN INTERLEUKIN-4 DETERMINED BY MULTIDIMENSIONAL
JRNL TITL 3 HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 32 6744 1993
JRNL REFN ISSN 0006-2960
JRNL PMID 8329398
JRNL DOI 10.1021/BI00077A030
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.POWERS,D.S.GARRETT,C.J.MARCH,E.A.FRIEDEN,A.M.GRONENBORN,
REMARK 1 AUTH 2 G.M.CLORE
REMARK 1 TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4
REMARK 1 TITL 2 BY MULTIDIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 3 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,A.M.GRONENBORN,
REMARK 1 AUTH 2 G.M.CLORE
REMARK 1 TITL 1H, 15N, 13C AND 13CO ASSIGNMENTS OF HUMAN INTERLEUKIN-4
REMARK 1 TITL 2 USING THREE DIMENSIONAL DOUBLE-AND TRIPLE-RESONANCE
REMARK 1 TITL 3 HETERONUCLEAR MAGNETIC RESONANCE 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,D.J.MARCH.E.A.FRIEDEN,G.M.CLORE,
REMARK 1 AUTH 2 A.M.GRONENBORN
REMARK 1 TITL DETERMINATION OF THE SECONDARY STRUCTURE AND FOLDING
REMARK 1 TITL 2 TOPOLOGY OF HUMAN INTERLEUKIN-4 USING THREE-DIMENSIONAL
REMARK 1 TITL 3 HETERONUCLEAR MAGNETIC RESONANCE 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 DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL
REMARK 3 STATISTICS ARE GIVEN IN THE REFERENCE LISTED ON THE JRNL
REMARK 3 RECORDS ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS,
REMARK 3 DEVIATIONS FROM IDEALITY FOR BOND LENGTHS, ANGLES, PLANES
REMARK 3 AND CHIRALITY, NON-BONDED CONTACTS, ATOMIC RMS DIFFERENCES
REMARK 3 BETWEEN THE CALCULATED STRUCTURES).
REMARK 3
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2973 EXPERIMENTAL
REMARK 3 NMR RESTRAINTS COMPRISING: 2515 INTERPROTON DISTANCE
REMARK 3 RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 102
REMARK 3 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 51 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; AND 130 PHI, 119 PSI, 73 CHI1, 32 CHI2 AND
REMARK 3 2 CHI3 TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING
REMARK 3 CONSTANTS, NOE DATA, AND 13C SECONDARY CHEMICAL 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 [NILGES, M., CLORE, G.M. & GRONENBORN,
REMARK 3 A.M., FEBS LETT. 229, 317-324 (1988)].
REMARK 3
REMARK 3 A TOTAL OF 30 STRUCTURES WERE CALCULATED. THE ATOMIC RMS
REMARK 3 DISTRIBUTION ABOUT THE MEAN COORDINATE POSITIONS FOR
REMARK 3 RESIDUES 8 - 129 IS 0.44 (+/-0.03) ANGSTROMS FOR THE
REMARK 3 BACKBONE ATOMS, 0.83 (+/-0.03) ANGSTROMS FOR ALL ATOMS,
REMARK 3 AND 0.51 (+/-0.04) ANGSTROMS FOR ALL ATOMS EXCLUDING
REMARK 3 DISORDERED SIDE CHAINS. THE N- (RESIDUES 1 - 7) AND C-
REMARK 3 (RESIDUES 130 - 133) TERMINAL RESIDUES ARE DISORDERED.
REMARK 3
REMARK 3 THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE
REMARK 3 LISTED FIRST AS MODEL 0. THIS (SA)R RESTRAINED MINIMIZED
REMARK 3 MEAN STRUCTURE WAS DERIVED BY AVERAGING THE COORDINATES OF
REMARK 3 THE INDIVIDUAL SA STRUCTURES (BEST FITTED TO RESIDUES 8 -
REMARK 3 129) AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED
REMARK 3 MINIMIZATION. THE QUANTITY PRESENTED IN THE TEMPERATURE
REMARK 3 FACTOR FIELD (COLUMNS 61 - 66) REPRESENTS THE ATOMIC RMS
REMARK 3 DEVIATIONS OF THE 30 INDIVIDUAL SA STRUCTURES ABOUT THE
REMARK 3 MEAN STRUCTURE. RESIDUES 1 - 7 AND 130 - 133 AT THE N-
REMARK 3 AND C-TERMINI, RESPECTIVELY, ARE DISORDERED.
REMARK 4
REMARK 4 1ITI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174261.
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 : 31
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: 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
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 1 ALA A 2 -105.33 -51.80
REMARK 500 1 ALA A 4 -23.58 -169.16
REMARK 500 1 LYS A 6 25.26 -67.08
REMARK 500 1 ALA A 39 43.39 -157.69
REMARK 500 1 LYS A 41 -81.90 -130.05
REMARK 500 1 LYS A 46 -70.26 -52.72
REMARK 500 1 PHE A 59 -70.94 -83.19
REMARK 500 1 ARG A 68 -61.24 -100.25
REMARK 500 1 ALA A 72 -30.58 -138.47
REMARK 500 1 ARG A 89 -71.92 -83.71
REMARK 500 1 TRP A 95 -8.61 -56.86
REMARK 500 1 CYS A 103 65.71 -160.33
REMARK 500 1 LYS A 106 -130.13 -103.52
REMARK 500 1 ASP A 109 -105.43 -83.63
REMARK 500 1 GLU A 114 -74.83 -68.45
REMARK 500 1 TYR A 128 7.34 -65.42
REMARK 500 1 LYS A 130 -124.34 -156.61
REMARK 500 1 SER A 132 74.13 -105.38
REMARK 500 2 ALA A 4 -147.99 -159.04
REMARK 500 2 ALA A 38 27.89 -77.30
REMARK 500 2 ALA A 39 10.52 -147.75
REMARK 500 2 SER A 40 105.52 -55.62
REMARK 500 2 LYS A 41 -89.72 -145.18
REMARK 500 2 GLU A 64 -16.95 -47.27
REMARK 500 2 THR A 67 43.17 -93.13
REMARK 500 2 ARG A 68 -62.18 -95.76
REMARK 500 2 ALA A 72 -35.25 -147.37
REMARK 500 2 THR A 73 164.19 -48.11
REMARK 500 2 ARG A 89 -77.63 -90.09
REMARK 500 2 LEU A 94 -71.01 -58.35
REMARK 500 2 TRP A 95 -14.19 -48.54
REMARK 500 2 LEU A 97 -1.43 -59.83
REMARK 500 2 ALA A 98 -73.85 -81.88
REMARK 500 2 ASN A 101 -88.62 -87.66
REMARK 500 2 CYS A 103 68.20 -159.34
REMARK 500 2 LYS A 106 -106.85 -92.70
REMARK 500 2 ALA A 108 172.99 179.37
REMARK 500 2 ASP A 109 -120.54 -92.59
REMARK 500 2 LYS A 130 -115.44 -175.28
REMARK 500 2 SER A 132 56.59 -147.56
REMARK 500 3 GLN A 12 -71.00 -78.94
REMARK 500 3 ALA A 39 89.93 -165.01
REMARK 500 3 LYS A 41 -70.63 -145.70
REMARK 500 3 PHE A 59 -70.24 -83.56
REMARK 500 3 GLU A 64 -18.94 -47.58
REMARK 500 3 THR A 67 37.83 -95.69
REMARK 500 3 ARG A 68 -70.42 -93.77
REMARK 500 3 LEU A 70 -66.00 -94.52
REMARK 500 3 ARG A 89 -70.08 -76.07
REMARK 500 3 LEU A 97 -2.23 -59.06
REMARK 500
REMARK 500 THIS ENTRY HAS 655 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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.
REMARK 999 THE TWO POTENTIAL N-LINKED GLYCOSYLATION SITES AT ASN 42
REMARK 999 AND ASN 109 IN THE NATURAL SEQUENCE WERE CHANGED TO ASP TO
REMARK 999 PREVENT HYPERGLYCOSYLATION IN THE YEAST HOST.
DBREF 1ITI A 5 133 UNP P05112 IL4_HUMAN 25 153
SEQADV 1ITI ASP A 42 UNP P05112 ASN 62 CONFLICT
SEQADV 1ITI 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 ASP A 8 GLN A 24 1 17
HELIX 2 2 THR A 26 GLU A 30 5 5
HELIX 3 3 ILE A 36 SER A 40 5 5
HELIX 4 4 THR A 44 HIS A 63 1 20
HELIX 5 5 THR A 73 GLY A 99 1 27
HELIX 6 6 LEU A 113 TYR A 128 1 16
SHEET 1 A 2 THR A 32 VAL A 33 0
SHEET 2 A 2 SER A 111 THR A 112 -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 2.02
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
MODEL 1
Complete list - b 23 2 Bytes