HEADER CYTOKINE 20-SEP-10 2L3O
TITLE SOLUTION STRUCTURE OF MURINE INTERLEUKIN 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 33-156;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: IL3, MCG_13767, MIL-3, RP23-309E16.5-001;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: CODONPLUS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PETNUSH HTB
KEYWDS CYTOKINE, MURINE INTERLEUKIN-3
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.YAO,I.G.YOUNG,R.S.NORTON,J.M.MURPHY
REVDAT 1 10-AUG-11 2L3O 0
JRNL AUTH S.YAO,I.G.YOUNG,R.S.NORTON,J.M.MURPHY
JRNL TITL MURINE INTERLEUKIN-3: STRUCTURE, DYNAMICS, AND
JRNL TITL 2 CONFORMATIONAL HETEROGENEITY IN SOLUTION.
JRNL REF BIOCHEMISTRY V. 50 2464 2011
JRNL REFN ISSN 0006-2960
JRNL PMID 21329364
JRNL DOI 10.1021/BI101810F
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH 2.17.0
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2L3O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB101916.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 0.020
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.15 MM [U-100% 15N] MIL-3-1, 20
REMARK 210 MM POTASSIUM PHOSPHATE-2, 95%
REMARK 210 H2O/5% D2O; 0.3 MM [U-100% 13C; U
REMARK 210 -100% 15N] MIL-3-3, 20 MM
REMARK 210 POTASSIUM PHOSPHATE-4, 95% H2O/5%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D 1H-15N NOESY;
REMARK 210 2D 1H-13C HSQC; 3D HNCO; 3D HNCA;
REMARK 210 3D HN(CO)CA; 3D CBCA(CO)NH; 3D
REMARK 210 HNCACB; 3D HCCH-TOCSY; 3D 1H-13C
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TOPSPIN 1.3, XEASY 1.3, CYANA
REMARK 210 2.1, X-PLOR_NIH 2.17.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ON THE BASIS OF STEREOCHEMISTRY
REMARK 210 AND ENERGY CONSIDERATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 30
REMARK 465 ALA A 31
REMARK 465 MET A 32
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 OE2 GLU A 49 HZ2 LYS A 53 1.52
REMARK 500 OE2 GLU A 83 HZ3 LYS A 97 1.52
REMARK 500 HG LEU A 54 HB3 ARG A 128 1.53
REMARK 500 HA LEU A 78 HD2 PHE A 81 1.53
REMARK 500 OD2 ASP A 63 HZ2 LYS A 130 1.54
REMARK 500 OG SER A 79 HZ1 LYS A 97 1.54
REMARK 500 OE1 GLU A 56 HH12 ARG A 132 1.54
REMARK 500 OG SER A 44 HZ1 LYS A 48 1.57
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 THR A 34 35.05 -90.63
REMARK 500 1 HIS A 35 -163.25 -125.17
REMARK 500 1 THR A 38 -69.62 -152.79
REMARK 500 1 THR A 40 -107.00 -143.33
REMARK 500 1 LEU A 41 62.86 -153.67
REMARK 500 1 PRO A 55 -161.76 -72.73
REMARK 500 1 GLU A 56 74.20 -115.13
REMARK 500 1 GLU A 58 41.38 -162.07
REMARK 500 1 LYS A 60 67.87 179.93
REMARK 500 1 THR A 61 -153.52 -133.08
REMARK 500 1 ASP A 62 -142.66 -119.38
REMARK 500 1 ASP A 63 -79.71 -95.27
REMARK 500 1 GLU A 64 -147.07 -164.15
REMARK 500 1 ASN A 70 147.02 -36.80
REMARK 500 1 PRO A 90 20.33 -74.09
REMARK 500 1 TYR A 94 21.44 -64.40
REMARK 500 1 VAL A 95 69.64 5.14
REMARK 500 1 THR A 109 13.59 -157.11
REMARK 500 1 ASN A 112 37.03 -69.49
REMARK 500 1 SER A 114 39.31 -155.36
REMARK 500 1 ASN A 139 -80.28 -175.17
REMARK 500 1 ASP A 140 -78.88 -167.59
REMARK 500 1 LEU A 141 25.01 -153.66
REMARK 500 1 GLU A 142 -90.63 -141.85
REMARK 500 1 PRO A 152 -80.32 -81.38
REMARK 500 1 SER A 154 -120.69 -83.07
REMARK 500 2 THR A 34 -72.69 -81.68
REMARK 500 2 ARG A 39 -142.69 -78.28
REMARK 500 2 THR A 40 -101.85 -76.78
REMARK 500 2 LEU A 41 -167.49 178.56
REMARK 500 2 ASN A 42 57.48 3.93
REMARK 500 2 GLU A 58 44.85 -90.18
REMARK 500 2 LYS A 60 95.37 0.48
REMARK 500 2 ASP A 62 -157.78 -140.68
REMARK 500 2 ASP A 63 -107.19 -70.68
REMARK 500 2 GLU A 64 -173.39 -179.10
REMARK 500 2 PRO A 66 -80.24 -86.25
REMARK 500 2 PRO A 90 25.72 -75.93
REMARK 500 2 VAL A 95 68.62 3.11
REMARK 500 2 THR A 109 -0.24 -152.03
REMARK 500 2 SER A 110 108.16 178.21
REMARK 500 2 ASN A 112 60.67 -104.40
REMARK 500 2 ASP A 113 42.78 -67.87
REMARK 500 2 SER A 114 43.01 -159.32
REMARK 500 2 ALA A 115 -130.46 -89.24
REMARK 500 2 PRO A 117 -162.61 -79.55
REMARK 500 2 LEU A 138 -36.76 -33.91
REMARK 500 2 PRO A 152 -79.75 -77.71
REMARK 500 2 ALA A 153 -167.40 -122.40
REMARK 500 3 HIS A 35 -146.79 -115.42
REMARK 500
REMARK 500 THIS ENTRY HAS 465 RAMACHANDRAN OUTLIERS.
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 1 ARG A 36 0.31 SIDE CHAIN
REMARK 500 1 ARG A 39 0.31 SIDE CHAIN
REMARK 500 1 ARG A 69 0.31 SIDE CHAIN
REMARK 500 1 ARG A 74 0.28 SIDE CHAIN
REMARK 500 1 ARG A 93 0.21 SIDE CHAIN
REMARK 500 1 ARG A 122 0.32 SIDE CHAIN
REMARK 500 1 ARG A 128 0.27 SIDE CHAIN
REMARK 500 1 ARG A 132 0.24 SIDE CHAIN
REMARK 500 1 ARG A 148 0.27 SIDE CHAIN
REMARK 500 2 ARG A 36 0.30 SIDE CHAIN
REMARK 500 2 ARG A 39 0.32 SIDE CHAIN
REMARK 500 2 ARG A 69 0.32 SIDE CHAIN
REMARK 500 2 ARG A 74 0.29 SIDE CHAIN
REMARK 500 2 ARG A 75 0.15 SIDE CHAIN
REMARK 500 2 ARG A 93 0.31 SIDE CHAIN
REMARK 500 2 ARG A 122 0.19 SIDE CHAIN
REMARK 500 2 ARG A 128 0.31 SIDE CHAIN
REMARK 500 2 ARG A 132 0.20 SIDE CHAIN
REMARK 500 2 ARG A 148 0.28 SIDE CHAIN
REMARK 500 3 ARG A 36 0.30 SIDE CHAIN
REMARK 500 3 ARG A 39 0.32 SIDE CHAIN
REMARK 500 3 ARG A 69 0.32 SIDE CHAIN
REMARK 500 3 ARG A 74 0.31 SIDE CHAIN
REMARK 500 3 ARG A 75 0.10 SIDE CHAIN
REMARK 500 3 ARG A 93 0.31 SIDE CHAIN
REMARK 500 3 ARG A 122 0.29 SIDE CHAIN
REMARK 500 3 ARG A 132 0.26 SIDE CHAIN
REMARK 500 3 ARG A 148 0.28 SIDE CHAIN
REMARK 500 4 ARG A 36 0.23 SIDE CHAIN
REMARK 500 4 ARG A 39 0.31 SIDE CHAIN
REMARK 500 4 ARG A 69 0.25 SIDE CHAIN
REMARK 500 4 ARG A 74 0.29 SIDE CHAIN
REMARK 500 4 ARG A 75 0.18 SIDE CHAIN
REMARK 500 4 ARG A 93 0.31 SIDE CHAIN
REMARK 500 4 ARG A 122 0.31 SIDE CHAIN
REMARK 500 4 ARG A 128 0.30 SIDE CHAIN
REMARK 500 4 ARG A 132 0.32 SIDE CHAIN
REMARK 500 4 ARG A 148 0.32 SIDE CHAIN
REMARK 500 5 ARG A 36 0.31 SIDE CHAIN
REMARK 500 5 ARG A 39 0.26 SIDE CHAIN
REMARK 500 5 ARG A 69 0.31 SIDE CHAIN
REMARK 500 5 ARG A 74 0.27 SIDE CHAIN
REMARK 500 5 ARG A 75 0.18 SIDE CHAIN
REMARK 500 5 ARG A 93 0.32 SIDE CHAIN
REMARK 500 5 ARG A 122 0.24 SIDE CHAIN
REMARK 500 5 ARG A 128 0.31 SIDE CHAIN
REMARK 500 5 ARG A 132 0.13 SIDE CHAIN
REMARK 500 5 ARG A 148 0.30 SIDE CHAIN
REMARK 500 6 ARG A 36 0.31 SIDE CHAIN
REMARK 500 6 ARG A 39 0.27 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 195 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 16614 RELATED DB: BMRB
REMARK 900 ENTRY CONTAINING CHEMICAL SHIFTS
DBREF 2L3O A 33 156 UNP Q5SX77 Q5SX77_MOUSE 33 156
SEQADV 2L3O GLY A 30 UNP Q5SX77 EXPRESSION TAG
SEQADV 2L3O ALA A 31 UNP Q5SX77 EXPRESSION TAG
SEQADV 2L3O MET A 32 UNP Q5SX77 EXPRESSION TAG
SEQADV 2L3O ALA A 105 UNP Q5SX77 CYS 105 ENGINEERED MUTATION
SEQRES 1 A 127 GLY ALA MET ASP THR HIS ARG LEU THR ARG THR LEU ASN
SEQRES 2 A 127 CYS SER SER ILE VAL LYS GLU ILE ILE GLY LYS LEU PRO
SEQRES 3 A 127 GLU PRO GLU LEU LYS THR ASP ASP GLU GLY PRO SER LEU
SEQRES 4 A 127 ARG ASN LYS SER PHE ARG ARG VAL ASN LEU SER LYS PHE
SEQRES 5 A 127 VAL GLU SER GLN GLY GLU VAL ASP PRO GLU ASP ARG TYR
SEQRES 6 A 127 VAL ILE LYS SER ASN LEU GLN LYS LEU ASN ALA CYS LEU
SEQRES 7 A 127 PRO THR SER ALA ASN ASP SER ALA LEU PRO GLY VAL PHE
SEQRES 8 A 127 ILE ARG ASP LEU ASP ASP PHE ARG LYS LYS LEU ARG PHE
SEQRES 9 A 127 TYR MET VAL HIS LEU ASN ASP LEU GLU THR VAL LEU THR
SEQRES 10 A 127 SER ARG PRO PRO GLN PRO ALA SER GLY SER
HELIX 1 1 CYS A 43 LEU A 54 1 12
HELIX 2 2 PRO A 66 ASN A 70 5 5
HELIX 3 3 PHE A 73 GLY A 86 1 14
HELIX 4 4 GLU A 87 VAL A 88 5 2
HELIX 5 5 ASP A 89 TYR A 94 5 6
HELIX 6 6 ILE A 96 LEU A 107 1 12
HELIX 7 7 ASP A 123 LEU A 138 1 16
SSBOND 1 CYS A 43 CYS A 106 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
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
