BMRB: 5171

NMR Structure of BPTI Mutant G37A

Authors

Battiste, J.L., Li, R., Woodward, C.

Assembly

BPTI G37A, TRYPSIN INHIBITOR

Entity

1. BPTI G37A, TRYPSIN INHIBITOR (polymer, Thiol state: all disulfide bound), 58 monomers, 6531.511 Da Detail

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGACRA KRNNFKSAED CMRTCGGA

Formula weight

6531.511 Da

Entity Connection

disulfide 3 Detail

---

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS5:SG	1:CYS55:SG
2	disulfide	sing	1:CYS14:SG	1:CYS38:SG
3	disulfide	sing	1:CYS30:SG	1:CYS51:SG

Exptl. method

NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 93.1 %, Completeness: 81.0 %, Completeness (bb): 89.7 % Detail

Download

• NMR-STAR v3.1 (partial)
• BMRB/XML (partial)
• CSV
• TSV

Polymer type: polypeptide(L)

	Total	1H
All	81.0 % (285 of 352)	81.0 % (285 of 352)
Backbone	89.7 % (105 of 117)	89.7 % (105 of 117)
Sidechain	76.6 % (180 of 235)	76.6 % (180 of 235)
Aromatic	11.1 % (4 of 36)	11.1 % (4 of 36)
Methyl	95.0 % (19 of 20)	95.0 % (19 of 20)

1. BPTI

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGACRA KRNNFKSAED CMRTCGGA

Show sample condition

Sample

Pressure 1 atm, Temperature 298 K, pH 4.6

#	Name	Isotope labeling	Type	Concentration
1	BPTI			5 mM
2	H2O			90 %
3	D2O			10 %

Hide sample codition

Protein Blocks Logo

Calculated from 1 models in PDB: 1JV9, Strand ID: A Detail

---

Release date

2001-10-02

Citation

A highly destabilizing mutation, G37A, of the bovine pancreatic trypsin inhibitor retains the average native conformation but greatly increases local flexibility
Battiste, J.L., Li, R., Woodward, C.
Biochemistry (2002), 41, 2237-2245, PubMed 11841215 , DOI 10.1021/bi011693e , Abstract

Related entities 1. BPTI G37A, TRYPSIN INHIBITOR, : 1 : 1 : 73 : 287 entities Detail

Interaction partners 1. BPTI G37A, TRYPSIN INHIBITOR, : 8 interactors Detail

Experiments performed 2 experiments Detail