Header list of 1irl.pdb file
Complete list - 3 20 Bytes
HEADER CYTOKINE 25-AUG-95 1IRL
TITLE THE SOLUTION STRUCTURE OF THE F42A MUTANT OF HUMAN INTERLEUKIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CYTOKINE
EXPDTA SOLUTION NMR
AUTHOR H.R.MOTT,B.S.BAINES,R.M.HALL,R.M.COOKE,P.C.DRISCOLL,M.P.WEIR,
AUTHOR 2 I.D.CAMPBELL
REVDAT 3 03-NOV-21 1IRL 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1IRL 1 VERSN
REVDAT 1 07-DEC-95 1IRL 0
JRNL AUTH H.R.MOTT,B.S.BAINES,R.M.HALL,R.M.COOKE,P.C.DRISCOLL,
JRNL AUTH 2 M.P.WEIR,I.D.CAMPBELL
JRNL TITL THE SOLUTION STRUCTURE OF THE F42A MUTANT OF HUMAN
JRNL TITL 2 INTERLEUKIN 2.
JRNL REF J.MOL.BIOL. V. 247 979 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7723044
JRNL DOI 10.1006/JMBI.1994.0194
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: NULL
REMARK 4
REMARK 4 1IRL 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_1000174241.
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: 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 2 102.74 -58.20
REMARK 500 THR A 3 -64.98 -107.38
REMARK 500 ILE A 24 -72.04 -88.42
REMARK 500 LYS A 32 37.51 -95.60
REMARK 500 LYS A 35 59.61 -108.95
REMARK 500 LEU A 36 41.67 -93.43
REMARK 500 THR A 41 -18.58 -49.71
REMARK 500 LYS A 43 28.94 45.99
REMARK 500 ALA A 50 60.08 -175.00
REMARK 500 ALA A 73 32.20 -96.60
REMARK 500 SER A 75 -51.87 -170.86
REMARK 500 LYS A 76 -73.78 -135.92
REMARK 500 PHE A 78 51.25 -90.33
REMARK 500 PRO A 82 86.37 -69.27
REMARK 500 LYS A 97 -79.05 -163.51
REMARK 500 GLU A 100 89.30 -11.60
REMARK 500 THR A 102 93.68 -67.27
REMARK 500 CYS A 105 98.72 -54.38
REMARK 500 ALA A 108 -170.49 -174.96
REMARK 500 ASP A 109 -53.68 86.71
REMARK 500 GLU A 110 161.11 174.46
REMARK 500 THR A 113 -154.53 -95.08
REMARK 500 CYS A 125 -70.60 -67.16
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 38 0.30 SIDE CHAIN
REMARK 500 ARG A 81 0.30 SIDE CHAIN
REMARK 500 ARG A 83 0.30 SIDE CHAIN
REMARK 500 ARG A 120 0.20 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IRL A 1 133 UNP P60568 IL2_HUMAN 21 153
SEQADV 1IRL ALA A 42 UNP P60568 PHE 62 ENGINEERED MUTATION
SEQRES 1 A 133 ALA PRO THR SER SER SER THR LYS LYS THR GLN LEU GLN
SEQRES 2 A 133 LEU GLU HIS LEU LEU LEU ASP LEU GLN MET ILE LEU ASN
SEQRES 3 A 133 GLY ILE ASN ASN TYR LYS ASN PRO LYS LEU THR ARG MET
SEQRES 4 A 133 LEU THR ALA LYS PHE TYR MET PRO LYS LYS ALA THR GLU
SEQRES 5 A 133 LEU LYS HIS LEU GLN CYS LEU GLU GLU GLU LEU LYS PRO
SEQRES 6 A 133 LEU GLU GLU VAL LEU ASN LEU ALA GLN SER LYS ASN PHE
SEQRES 7 A 133 HIS LEU ARG PRO ARG ASP LEU ILE SER ASN ILE ASN VAL
SEQRES 8 A 133 ILE VAL LEU GLU LEU LYS GLY SER GLU THR THR PHE MET
SEQRES 9 A 133 CYS GLU TYR ALA ASP GLU THR ALA THR ILE VAL GLU PHE
SEQRES 10 A 133 LEU ASN ARG TRP ILE THR PHE CYS GLN SER ILE ILE SER
SEQRES 11 A 133 THR LEU THR
HELIX 1 1 LYS A 9 ILE A 28 1 20
HELIX 2 2 LEU A 40 ALA A 42 5 3
HELIX 3 3 HIS A 55 ASN A 71 5 17
HELIX 4 4 ARG A 83 LEU A 96 5 14
HELIX 5 5 ILE A 114 SER A 130 1 17
SHEET 1 S1 2 PHE A 44 LYS A 48 0
SHEET 2 S1 2 TYR A 107 ALA A 112 -1
SSBOND 1 CYS A 58 CYS A 105 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
Complete list - 3 20 Bytes