Header list of 1c8p.pdb file
Complete list - b 16 2 Bytes
HEADER MEMBRANE PROTEIN 05-OCT-99 1C8P
TITLE NMR STRUCTURE OF THE LIGAND BINDING DOMAIN OF THE COMMON BETA-CHAIN IN
TITLE 2 THE GM-CSF, IL-3 AND IL-5 RECEPTORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOKINE RECEPTOR COMMON BETA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN 4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL: HEMOPOIETIC CELLS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PEC611
KEYWDS BETA SANDWICH, CYTOKINE RECEPTOR, FN3 DOMAIN, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR T.D.MULHERN,R.J.D'ANDREA,C.GAUNT,L.VANDELEUR,M.A.VADAS,A.F.LOPEZ,
AUTHOR 2 G.W.BOOKER,C.J.BAGLEY
REVDAT 4 16-FEB-22 1C8P 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1C8P 1 VERSN
REVDAT 2 01-APR-03 1C8P 1 JRNL
REVDAT 1 15-JUN-00 1C8P 0
SPRSDE 21-JUN-00 1C8P 1D4Q
JRNL AUTH T.D.MULHERN,A.F.LOPEZ,R.J.D'ANDREA,C.GAUNT,L.VANDELEUR,
JRNL AUTH 2 M.A.VADAS,G.W.BOOKER,C.J.BAGLEY
JRNL TITL THE SOLUTION STRUCTURE OF THE CYTOKINE-BINDING DOMAIN OF THE
JRNL TITL 2 COMMON BETA-CHAIN OF THE RECEPTORS FOR
JRNL TITL 3 GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR,
JRNL TITL 4 INTERLEUKIN-3 AND INTERLEUKIN-5.
JRNL REF J.MOL.BIOL. V. 297 989 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10736232
JRNL DOI 10.1006/JMBI.2000.3610
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.D.MULHERN,C.J.BAGLEY,C.GAUNT,A.F.LOPEZ,M.A.VADAS,
REMARK 1 AUTH 2 R.J.D'ANDREA,G.W.BOOKER
REMARK 1 TITL 1H AND 15N CHEMICAL SHIFT ASSIGNMENTS FOR DOMAIN 4 OF THE
REMARK 1 TITL 2 COMMON BETA-CHAIN OF THE IL-3, IL-5 AND GM-CSF RECEPTORS
REMARK 1 REF J.BIOMOL.NMR V. 14 281 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008360024435
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, X-PLOR 3.851
REMARK 3 AUTHORS : VARIAN AND ASSOCIATES (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 1500 UNAMBIGUOUS NOE-DERIVED DISTANCE
REMARK 3 RESTRAINTS,
REMARK 3 1034 AMBIGUOUS NOE-DERIVED DISTANCE RESTRAINTS, 42 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS
REMARK 3 AND 30 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. THE ARIA METHOD OF
REMARK 3 NILGES ET
REMARK 3 AL. (1997) WAS USED
REMARK 4
REMARK 4 1C8P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000001474.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : 0.06M
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4MM D4BC U-15N; 10MM PHOSPHATE
REMARK 210 BUFFER;90% H2O, 10% D2O; 0.4MM
REMARK 210 D4BC U-15N; 10MM PHOSPHATE
REMARK 210 BUFFER;100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS CALCULATED USING THE ARIA METHOD
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 O GLU A 67 HG1 THR A 100 1.48
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 ILE A 2 -171.94 -67.41
REMARK 500 1 MET A 4 -176.02 62.55
REMARK 500 1 PRO A 7 -177.88 -63.94
REMARK 500 1 ASP A 16 -52.62 83.24
REMARK 500 1 MET A 25 20.57 -151.45
REMARK 500 1 MET A 27 -62.36 -129.59
REMARK 500 1 ARG A 28 32.90 36.96
REMARK 500 1 TYR A 29 -78.37 -83.21
REMARK 500 1 HIS A 31 63.40 -68.86
REMARK 500 1 HIS A 34 97.12 54.65
REMARK 500 1 ARG A 41 -158.61 -104.42
REMARK 500 1 ALA A 45 -158.83 -108.99
REMARK 500 1 SER A 50 178.26 -52.60
REMARK 500 1 SER A 60 163.82 168.17
REMARK 500 1 ALA A 62 73.47 -112.61
REMARK 500 1 LEU A 63 95.81 -37.42
REMARK 500 1 ARG A 79 -152.51 -99.50
REMARK 500 1 SER A 81 74.88 -67.24
REMARK 500 1 THR A 83 -59.97 73.18
REMARK 500 1 ASN A 86 -101.74 -57.17
REMARK 500 1 TRP A 92 121.10 63.89
REMARK 500 1 GLU A 101 -162.00 40.60
REMARK 500 2 PRO A 7 -170.58 -66.76
REMARK 500 2 ASP A 14 38.21 -158.72
REMARK 500 2 ASP A 16 -63.20 175.31
REMARK 500 2 MET A 27 25.57 48.22
REMARK 500 2 GLU A 30 -176.39 -61.96
REMARK 500 2 HIS A 34 111.05 65.81
REMARK 500 2 ARG A 41 -154.75 -95.42
REMARK 500 2 ASN A 57 65.42 174.01
REMARK 500 2 SER A 60 160.16 179.09
REMARK 500 2 LEU A 63 104.24 -51.02
REMARK 500 2 PRO A 64 -62.17 -92.57
REMARK 500 2 THR A 80 65.32 -104.25
REMARK 500 2 SER A 81 74.35 -63.70
REMARK 500 2 THR A 83 -73.43 59.94
REMARK 500 2 TYR A 85 -161.42 -60.40
REMARK 500 2 ASN A 86 -106.18 -101.93
REMARK 500 2 TRP A 89 150.59 65.48
REMARK 500 2 SER A 90 -73.57 -55.19
REMARK 500 2 GLU A 91 -76.31 170.67
REMARK 500 2 TRP A 92 125.21 178.11
REMARK 500 2 GLU A 101 150.73 68.57
REMARK 500 3 MET A 4 -164.26 60.88
REMARK 500 3 PRO A 7 -166.05 -53.07
REMARK 500 3 ASP A 16 -65.01 171.93
REMARK 500 3 MET A 25 40.89 178.77
REMARK 500 3 MET A 27 -52.56 -138.40
REMARK 500 3 TYR A 29 -74.18 -53.02
REMARK 500 3 GLU A 30 -64.72 -148.97
REMARK 500
REMARK 500 THIS ENTRY HAS 444 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4308 RELATED DB: BMRB
REMARK 900 1H AND 15N CHEMICAL SHIFT DATA
DBREF 1C8P A 1 102 UNP P32927 IL3RB_HUMAN 338 438
SEQADV 1C8P MET A 1 UNP P32927 CLONING ARTIFACT
SEQRES 1 A 102 MET ILE GLN MET ALA PRO PRO SER LEU ASN VAL THR LYS
SEQRES 2 A 102 ASP GLY ASP SER TYR SER LEU ARG TRP GLU THR MET LYS
SEQRES 3 A 102 MET ARG TYR GLU HIS ILE ASP HIS THR PHE GLU ILE GLN
SEQRES 4 A 102 TYR ARG LYS ASP THR ALA THR TRP LYS ASP SER LYS THR
SEQRES 5 A 102 GLU THR LEU GLN ASN ALA HIS SER MET ALA LEU PRO ALA
SEQRES 6 A 102 LEU GLU PRO SER THR ARG TYR TRP ALA ARG VAL ARG VAL
SEQRES 7 A 102 ARG THR SER ARG THR GLY TYR ASN GLY ILE TRP SER GLU
SEQRES 8 A 102 TRP SER GLU ALA ARG SER TRP ASP THR GLU SER
HELIX 1 1 THR A 46 SER A 50 5 5
SHEET 1 A 3 SER A 8 ASP A 14 0
SHEET 2 A 3 SER A 17 GLU A 23 -1 O SER A 17 N ASP A 14
SHEET 3 A 3 SER A 60 LEU A 63 -1 O MET A 61 N LEU A 20
SHEET 1 B 4 THR A 52 GLN A 56 0
SHEET 2 B 4 THR A 35 LYS A 42 -1 N PHE A 36 O LEU A 55
SHEET 3 B 4 TYR A 72 ARG A 79 -1 O TRP A 73 N ARG A 41
SHEET 4 B 4 ARG A 96 TRP A 98 -1 O ARG A 96 N ALA A 74
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 16 2 Bytes