HEADER MEMBRANE PROTEIN 23-SEP-14 2MV6
TITLE SOLUTION STRUCTURE OF THE TRANSMEMBRANE DOMAIN AND THE JUXTA-MEMBRANE
TITLE 2 DOMAIN OF THE ERYTHROPOIETIN RECEPTOR IN MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERYTHROPOIETIN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 237-284;
COMPND 5 SYNONYM: EPO-R;
COMPND 6 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: EPOR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET29B
KEYWDS MICELLES, TRANSMEMBRANE DOMAIN, ERYTHROPOIETIN RECEPTOR, MEMBRANE
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Q.LI,Y.WONG,Q.HUANG,C.KANG
REVDAT 1 10-DEC-14 2MV6 0
JRNL AUTH Q.LI,Y.L.WONG,Q.HUANG,C.KANG
JRNL TITL STRUCTURAL INSIGHT INTO THE TRANSMEMBRANE DOMAIN AND THE
JRNL TITL 2 JUXTAMEMBRANE REGION OF THE ERYTHROPOIETIN RECEPTOR IN
JRNL TITL 3 MICELLES.
JRNL REF BIOPHYS.J. V. 107 2325 2014
JRNL REFN ISSN 0006-3495
JRNL PMID 25418301
JRNL DOI 10.1016/J.BPJ.2014.10.013
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING WAS STARTED WITH
REMARK 3 3500 AND COOL DOWN TO 100 K WITH 15,000 STEPS. STRUCTURE WAS
REMARK 3 ENERGY MINIMIZED WITH POWELL ENERGY MINIMIZATION.
REMARK 4
REMARK 4 2MV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-14.
REMARK 100 THE RCSB ID CODE IS RCSB104084.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20 MM SODIUM PHOSPHATE, 10 V/V
REMARK 210 D2O, 250 MM DPC, 0.5 MM [U-99%
REMARK 210 15N] PROTEIN, 90% H2O/10% D2O;
REMARK 210 0.5-1 MM [U-100% 13C; U-100% 15N]
REMARK 210 PROTEIN, 10 % D2O, 20 MM SODIUM
REMARK 210 PHOSPHATE, 200-400 MM DPC, 1 MM
REMARK 210 DTT, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCACB; 3D
REMARK 210 CBCA(CO)NH; 3D HBHA(CO)NH; 3D 1H-
REMARK 210 15N NOESY; 3D HNCO; 3D HCACO
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, X-PLOR_NIH, NMRPIPE,
REMARK 210 NMRVIEW, TOPSPIN
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 : STRUCTURES WITH THE LOWEST ENERGY
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 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 SER A 2 19.95 -159.73
REMARK 500 1 LEU A 8 101.25 55.65
REMARK 500 1 SER A 11 -7.27 -59.23
REMARK 500 1 ASP A 12 -45.27 -133.87
REMARK 500 1 LEU A 13 85.33 -53.04
REMARK 500 2 LEU A 13 83.49 -68.87
REMARK 500 2 TRP A 48 65.38 -157.90
REMARK 500 3 SER A 2 -177.73 51.19
REMARK 500 3 LEU A 7 -169.60 -102.10
REMARK 500 3 LEU A 8 80.94 64.98
REMARK 500 3 SER A 11 1.36 -69.06
REMARK 500 3 LEU A 13 91.94 -56.98
REMARK 500 4 VAL A 5 82.32 40.23
REMARK 500 4 THR A 9 95.65 -30.88
REMARK 500 4 LEU A 13 109.91 -40.60
REMARK 500 5 SER A 2 -53.80 -163.74
REMARK 500 5 GLU A 3 54.60 -143.54
REMARK 500 5 LEU A 13 75.75 -65.86
REMARK 500 6 ASP A 12 -37.04 -139.58
REMARK 500 6 LEU A 13 82.26 -54.66
REMARK 500 7 SER A 2 -126.28 -66.76
REMARK 500 7 TRP A 48 63.53 -154.26
REMARK 500 8 GLU A 3 52.92 -151.80
REMARK 500 8 LEU A 7 -29.30 -36.92
REMARK 500 8 THR A 9 92.19 -29.09
REMARK 500 8 LEU A 13 81.92 -60.77
REMARK 500 9 SER A 2 -70.06 -135.06
REMARK 500 9 VAL A 5 -19.58 -166.00
REMARK 500 9 SER A 6 90.66 -177.48
REMARK 500 9 TRP A 48 61.53 -150.82
REMARK 500 10 SER A 6 -35.34 -143.10
REMARK 500 10 LEU A 7 108.95 -51.65
REMARK 500 10 SER A 11 -9.32 -56.75
REMARK 500 10 ASP A 12 -44.52 -145.13
REMARK 500 10 LEU A 13 85.02 -64.27
REMARK 500 11 SER A 2 91.32 -175.85
REMARK 500 11 GLU A 3 54.44 -145.95
REMARK 500 11 LEU A 8 175.29 51.22
REMARK 500 11 TRP A 48 73.64 -152.14
REMARK 500 12 SER A 2 29.96 47.14
REMARK 500 13 SER A 2 -0.60 -165.95
REMARK 500 13 LEU A 7 132.96 -39.68
REMARK 500 13 ASP A 12 -41.28 -148.13
REMARK 500 13 LEU A 13 95.85 -61.75
REMARK 500 14 SER A 2 16.18 -142.02
REMARK 500 14 PRO A 4 109.92 -46.47
REMARK 500 14 LEU A 7 156.41 57.27
REMARK 500 14 ASP A 12 -38.54 -147.07
REMARK 500 14 LEU A 13 92.10 -46.02
REMARK 500 15 SER A 2 4.23 -154.48
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 25079 RELATED DB: BMRB
DBREF 2MV6 A 2 49 UNP P19235 EPOR_HUMAN 237 284
SEQADV 2MV6 MET A 1 UNP P19235 INITIATING METHIONINE
SEQRES 1 A 49 MET SER GLU PRO VAL SER LEU LEU THR PRO SER ASP LEU
SEQRES 2 A 49 ASP PRO LEU ILE LEU THR LEU SER LEU ILE LEU VAL VAL
SEQRES 3 A 49 ILE LEU VAL LEU LEU THR VAL LEU ALA LEU LEU SER HIS
SEQRES 4 A 49 ARG ARG ALA LEU LYS GLN LYS ILE TRP PRO
HELIX 1 1 ASP A 14 TRP A 48 1 35
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
