BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15599

Title: 1H, 13C and 15N Assignments of Human Phosphohistidine Phosphatase 1 (PHPT1)   PubMed: 18991813

Deposition date: 2007-12-18 Original release date: 2008-11-14

Authors: Gong, Weibin; Cui, Gaofeng; Jin, Changwen; Xia, Bin

Citation: Gong, Weibin; Li, Yifei; Cui, Gaofeng; Hu, Jicheng; Fang, Huaming; Jin, Changwen; Xia, Bin. "Solution structure and catalytic mechanism of human protein histidine phosphatase 1."  Biochemistry 418, 337-344 (2008).

Assembly members:
entity_phpt1_lower, polymer, 125 residues, 13833.00 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   Vector: pET28a

Entity Sequences (FASTA):
entity_phpt1_lower: MAVADLALIPDVDIDSDGVF KYVLIRVHSAPRSGAPAAES KEIVRGYKWAEYHADIYDKV SGDMQKQGCDCECLGGGRIS HQSQDKKIHVYGYSMAYGPA QHAISTEKIKAKYPDYEVTW ANDGY

Data sets:
Data typeCount
13C chemical shifts357
15N chemical shifts109
1H chemical shifts706

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PHPT1 monomer1

Entities:

Entity 1, PHPT1 monomer 125 residues - 13833.00 Da.

1   METALAVALALAASPLEUALALEUILEPRO
2   ASPVALASPILEASPSERASPGLYVALPHE
3   LYSTYRVALLEUILEARGVALHISSERALA
4   PROARGSERGLYALAPROALAALAGLUSER
5   LYSGLUILEVALARGGLYTYRLYSTRPALA
6   GLUTYRHISALAASPILETYRASPLYSVAL
7   SERGLYASPMETGLNLYSGLNGLYCYSASP
8   CYSGLUCYSLEUGLYGLYGLYARGILESER
9   HISGLNSERGLNASPLYSLYSILEHISVAL
10   TYRGLYTYRSERMETALATYRGLYPROALA
11   GLNHISALAILESERTHRGLULYSILELYS
12   ALALYSTYRPROASPTYRGLUVALTHRTRP
13   ALAASNASPGLYTYR

Samples:

sample_1: entity_phpt1_lower, [U-95% 13C; U-95% 15N], 1 mM; Tris-HCl 50 mM; NaCl 50 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.2; pressure: 1 atm; temperature: 298 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAI46371
EMBL CAB66579 CAG38512 CAL38548
GB AAF80759 AAG01156 AAH24648 AAN52504 ACJ13700
REF NP_001129333 NP_001274271 NP_054891 XP_001117869 XP_004048950
SP Q9NRX4
AlphaFold Q9NRX4

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