Header list of 1jli.pdb file
Complete list - 3 20 Bytes
HEADER CYTOKINE 14-DEC-95 1JLI
TITLE HUMAN INTERLEUKIN 3 (IL-3) MUTANT WITH TRUNCATION AT BOTH N-AND C-
TITLE 2 TERMINI AND 14 RESIDUE CHANGES, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN 3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MULTI-CSF;
COMPND 5 ENGINEERED: YES;
COMPND 6 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;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM101;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMON 13302
KEYWDS HEMATOPOIETIC GROWTH FACTOR, COLONY-STIMULATING FACTOR, CYTOKINE
EXPDTA SOLUTION NMR
AUTHOR Y.FENG,B.K.KLEIN,C.A.MCWHERTER
REVDAT 4 03-NOV-21 1JLI 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1JLI 1 VERSN
REVDAT 2 01-APR-03 1JLI 1 JRNL
REVDAT 1 16-JUN-97 1JLI 0
JRNL AUTH Y.FENG,B.K.KLEIN,C.A.MCWHERTER
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE AND BACKBONE DYNAMICS
JRNL TITL 2 OF A VARIANT OF HUMAN INTERLEUKIN-3.
JRNL REF J.MOL.BIOL. V. 259 524 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8676386
JRNL DOI 10.1006/JMBI.1996.0337
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.FENG,B.K.KLEIN,L.VU,S.AYKENT,C.A.MCWHERTER
REMARK 1 TITL 1H, 13C, AND 15N NMR RESONANCE ASSIGNMENTS, SECONDARY
REMARK 1 TITL 2 STRUCTURE, AND BACKBONE TOPOLOGY OF A VARIANT OF HUMAN
REMARK 1 TITL 3 INTERLEUKIN-3
REMARK 1 REF BIOCHEMISTRY V. 34 6540 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: AS IN X-PLOR PARALLHDG.PRO STRUCTURES
REMARK 3 WERE CALCULATED USING A SIMULATED ANNEALING PROTOCOL IN X-PLOR.
REMARK 3 INPUT CONSTRAINTS ARE AS FOLLOWS: 1659 NUCLEAR OVERHAUSER
REMARK 3 ENHANCEMENT (NOE) (799 INTRA-RESIDUE; 342 SEQUENTIAL (I-J =1);
REMARK 3 236 MEDIUM-RANGE INTERRESIDUE (<1 I-J <=5); 282 LONG-RANGE
REMARK 3 INTERRESIDUE (I-J >5)); 38 PAIRS OF HYDROGEN-BOND RESTRAINTS; 76
REMARK 3 PHI TORSION ANGLE RESTRAINTS. PSEUDOATOM POSITIONS WERE USED FOR
REMARK 3 CONSTRAINTS INVOLVING METHYLENE, AROMATIC, AND METHYL PROTONS.
REMARK 3 THE COORDINATES DEPOSITED HERE ARE OBTAINED BY AVERAGING 25
REMARK 3 CONVERGED STRUCTURES PRIOR TO A RESTRAINED ENERGY MINIMIZATION.
REMARK 3 A COMPARISON OF THE FAMILY OF THE 25 STRUCTURES WITH THE
REMARK 3 AVERAGED STRUCTURE GIVES RMSD VALUES OF 0.88 ANGSTROMS FOR ALL
REMARK 3 (N,CA,C') EXCEPT RESIDUES 28 - 39, AND 0.41 ANGSTROMS FOR (N,CA,
REMARK 3 C') OF HELICAL REGIONS (RESIDUES 16 - 26, 42 - 49, 54 - 67, 72 -
REMARK 3 84, AND 104 - 122).
REMARK 4
REMARK 4 1JLI 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_1000174341.
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 ASN A 15 53.31 -150.16
REMARK 500 LEU A 27 56.50 -113.24
REMARK 500 LYS A 28 68.20 -158.44
REMARK 500 PRO A 31 -73.22 -77.64
REMARK 500 ASN A 38 88.80 -54.05
REMARK 500 ALA A 90 66.28 2.77
REMARK 500 ALA A 91 143.39 -177.16
REMARK 500 THR A 93 -45.85 -150.48
REMARK 500 PRO A 96 -164.52 -78.18
REMARK 500 ILE A 97 -171.86 -67.86
REMARK 500 LYS A 100 -161.46 -119.46
REMARK 500 TYR A 114 -84.58 -68.06
REMARK 500 ALA A 123 -74.56 -123.60
REMARK 500 GLN A 124 94.96 59.93
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JLI A 15 125 UNP P08700 IL3_HUMAN 34 144
SEQADV 1JLI ILE A 18 UNP P08700 ASN 37 ENGINEERED MUTATION
SEQADV 1JLI HIS A 25 UNP P08700 THR 44 ENGINEERED MUTATION
SEQADV 1JLI ARG A 29 UNP P08700 GLN 48 ENGINEERED MUTATION
SEQADV 1JLI ASN A 32 UNP P08700 LEU 51 ENGINEERED MUTATION
SEQADV 1JLI PRO A 37 UNP P08700 PHE 56 ENGINEERED MUTATION
SEQADV 1JLI SER A 42 UNP P08700 GLY 61 ENGINEERED MUTATION
SEQADV 1JLI MET A 45 UNP P08700 GLN 64 ENGINEERED MUTATION
SEQADV 1JLI ARG A 51 UNP P08700 ASN 70 ENGINEERED MUTATION
SEQADV 1JLI THR A 55 UNP P08700 ARG 74 ENGINEERED MUTATION
SEQADV 1JLI LEU A 59 UNP P08700 GLU 78 ENGINEERED MUTATION
SEQADV 1JLI VAL A 62 UNP P08700 ASN 81 ENGINEERED MUTATION
SEQADV 1JLI HIS A 67 UNP P08700 SER 86 ENGINEERED MUTATION
SEQADV 1JLI GLU A 69 UNP P08700 GLN 88 ENGINEERED MUTATION
SEQRES 1 A 112 ALA ASN CYS SER ILE MET ILE ASP GLU ILE ILE HIS HIS
SEQRES 2 A 112 LEU LYS ARG PRO PRO ASN PRO LEU LEU ASP PRO ASN ASN
SEQRES 3 A 112 LEU ASN SER GLU ASP MET ASP ILE LEU MET GLU ARG ASN
SEQRES 4 A 112 LEU ARG THR PRO ASN LEU LEU ALA PHE VAL ARG ALA VAL
SEQRES 5 A 112 LYS HIS LEU GLU ASN ALA SER ALA ILE GLU SER ILE LEU
SEQRES 6 A 112 LYS ASN LEU LEU PRO CYS LEU PRO LEU ALA THR ALA ALA
SEQRES 7 A 112 PRO THR ARG HIS PRO ILE HIS ILE LYS ASP GLY ASP TRP
SEQRES 8 A 112 ASN GLU PHE ARG ARG LYS LEU THR PHE TYR LEU LYS THR
SEQRES 9 A 112 LEU GLU ASN ALA GLN ALA GLN GLN
HELIX 1 1 CYS A 16 HIS A 26 1 11
HELIX 2 2 SER A 42 MET A 49 1 8
HELIX 3 3 ARG A 54 HIS A 67 1 14
HELIX 4 4 SER A 72 CYS A 84 1 13
HELIX 5 5 TRP A 104 GLN A 122 1 19
SSBOND 1 CYS A 16 CYS A 84 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