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Biological Magnetic Resonance Data Bank


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BMRB Entry 15356

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15356
MolProbity Validation Chart

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Title: Solution NMR Structure of Human Myeloid Differentiation Primary Response (MyD88). Northeast Structural Genomics target HR2869A.

Deposition date: 2007-06-29 Original release date: 2007-07-24

Authors: Rossi, Paolo; Ramelot, Theresa; Ciano, Melissa; Ho, Chi-Kent; Ma, Li-Chung; Xiao, Rong; Acton, Thomas; Kennedy, Michael; Tong, Liang; Montelione, Gaetano

Citation: Rossi, Paolo; Xiao, Rong; Acton, Thomas; Tong, Liang; Montelione, Gaetano. "Solution NMR Structure of Human Myeloid Differentiation Primary Response (MyD88). Northeast Structural Genomics target HR2869A."  Not known ., .-..

Assembly members:
HR2869A, polymer, 160 residues, 18769.064 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
HR2869A: MGITTLDDPLGHMPERFDAF ICYCPSDIQFVQEMIRQLEQ TNYRLKLCVSDRDVLPGTCV WSIASELIEKRCRRMVVVVS DDYLQSKECDFQTKFALSLS PGAHQKRLIPIKYKAMKKEF PSILRFITVCDYTNPCTKSW FWTRLAKALSLPLEHHHHHH

Data typeCount
13C chemical shifts708
15N chemical shifts155
1H chemical shifts1140

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR2869A1

Entities:

Entity 1, HR2869A 160 residues - 18769.064 Da.

Native sequence numbering 146-296 (excluding cloning artifacts and C-term His tag)

1   METGLYILETHRTHRLEUASPASPPROLEU
2   GLYHISMETPROGLUARGPHEASPALAPHE
3   ILECYSTYRCYSPROSERASPILEGLNPHE
4   VALGLNGLUMETILEARGGLNLEUGLUGLN
5   THRASNTYRARGLEULYSLEUCYSVALSER
6   ASPARGASPVALLEUPROGLYTHRCYSVAL
7   TRPSERILEALASERGLULEUILEGLULYS
8   ARGCYSARGARGMETVALVALVALVALSER
9   ASPASPTYRLEUGLNSERLYSGLUCYSASP
10   PHEGLNTHRLYSPHEALALEUSERLEUSER
11   PROGLYALAHISGLNLYSARGLEUILEPRO
12   ILELYSTYRLYSALAMETLYSLYSGLUPHE
13   PROSERILELEUARGPHEILETHRVALCYS
14   ASPTYRTHRASNPROCYSTHRLYSSERTRP
15   PHETRPTHRARGLEUALALYSALALEUSER
16   LEUPROLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: entity, [U-5% 13C; U-100% 15N], 0.8 mM; DTT 10 mM; ammonium acetate 40 mM; acetonitrile 5%

sample_2: entity, [U-100% 13C; U-100% 15N], 0.8 mM; DTT 10 mM; ammonium acetate 40 mM; acetonitrile 5%

sample_3: entity, [U-100% 13C; U-100% 15N], 0.8 mM; DTT 10 mM; ammonium acetate 40 mM; acetonitrile 5%

sample_conditions_1: pH: 5.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC stereospecific VLsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
H/D exchsample_2isotropicsample_conditions_1
HETnoesample_3isotropicsample_conditions_1
T1/T2sample_3isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution

AutoAssign v1.14, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

SPARKY v2.110, Goddard - data analysis

NMRPipe v2005, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v1.3, Bruker Biospin - collection

Molmol v2K.2, Koradi, Billeter and Wuthrich - visualization

PSVS v1.3, Bhattacharya and Montelione - validation

ProcheckNMR, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Th - validation

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

X-PLOR NIH v2.11.2, Schwieters, Kuszewski, Tjandra and Clore - refinement

MolProbity, Richardson - validation

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 11078
PDB
DBJ BAE89833 BAG55247 BAG55248 BAG55249 BAG55250
GB AAB49967 AAC50954 AAH13589 AAP36040 AAP36509
REF NP_001123935 NP_001124153 NP_001166039 NP_001266118 NP_001266529
SP B3Y678 B3Y679 B3Y680 B3Y681 B3Y682

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts