1t0w

25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina

Method: SOLUTION NMR

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Hevein

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Monomer	Protein 1 其他Polymer 1	;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HEVE_HEVBR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–32； UniProt 18–49

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1t0w
Deposition date deposition_date	2004-04-13
Structure title title	25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina
Keywords keywords	alpha-helix, anti-parallel beta-sheet, SUGAR BINDING PROTEIN; SUGAR BINDING PROTEIN
Experimental Method method	SOLUTION NMR

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1t0w__assembly_1__model_15

Assembly 1 · Model 15 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1t0w__assembly_1__model_15 | I(q)

100 plotted points; both axes use logarithmic scales.

1t0w__assembly_1__model_15 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	9.79 Å
Rg (electron density)	8.86 Å
Total Rg	10.15 Å
Atom count	529
Residues	32
Excluded volume	4842 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1t0w__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`1t0w__assembly_1__model_2`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`1t0w__assembly_1__model_3`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	4	`1t0w__assembly_1__model_4`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	5	`1t0w__assembly_1__model_5`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	6	`1t0w__assembly_1__model_6`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	7	`1t0w__assembly_1__model_7`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	8	`1t0w__assembly_1__model_8`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	9	`1t0w__assembly_1__model_9`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	10	`1t0w__assembly_1__model_10`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	11	`1t0w__assembly_1__model_11`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	12	`1t0w__assembly_1__model_12`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	13	`1t0w__assembly_1__model_13`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	14	`1t0w__assembly_1__model_14`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	15	`1t0w__assembly_1__model_15`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	16	`1t0w__assembly_1__model_16`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	17	`1t0w__assembly_1__model_17`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	18	`1t0w__assembly_1__model_18`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	19	`1t0w__assembly_1__model_19`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	20	`1t0w__assembly_1__model_20`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	21	`1t0w__assembly_1__model_21`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	22	`1t0w__assembly_1__model_22`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	23	`1t0w__assembly_1__model_23`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	24	`1t0w__assembly_1__model_24`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	25	`1t0w__assembly_1__model_25`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1t0wa_
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.1 — Plant lectins/antimicrobial peptides
Family Family family	g.3.1.1 — Hevein-like agglutinin (lectin) domain

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7. Citations (6)

;NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides ;

Chembiochem (2004)

PMID: 15368576 · DOI: 10.1002/cbic.200400025 PRIMARY

;NMR Investigations of Protein-Carbohydrate Interactions: Studies on the Relevance of Trp/Tyr Variations in Lectin Binding Sites as Deduced from Titration Microcalorimetry and NMR Studies on Hevein Domains. Determination of the NMR Structure of the Complex between Pseudohevein and N'N',N''-triacetylchitotriose ;

PROTEINS: STRUCT.,FUNCT.,GENET. (2000)

DOI: 10.1002/(SICI)1097-0134(20000801)40:2<218::AID-PROT50>3.3.CO;2-G

;Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains ;

Chem.Biol. (2000)

DOI: 10.1016/S1074-5521(00)00136-8

;NMR investigations of protein-carbohydrate interactions: refined three-dimensional structure of the complex between hevein and methyl beta-chitobioside ;

Glycobiology (1998)

DOI: 10.1093/glycob/8.6.569

H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from amaranthus caudatus

J.Mol.Biol. (1996)

DOI: 10.1006/jmbi.1996.0253

;The interaction of hevein with N-acetylglucosamine-containing oligosaccharides. Solution structure of hevein complexed to chitobiose ;

Eur.J.Biochem. (1995)

Description description	Hevein
Molecular weight formula_weight	3484.9 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	13225

Description description	;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	627.6 kDa
Source method src_method	man
Copy count entity_count	1

25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina

1. Protein Identity and Related Structures Protein Identity & Related Structures

Hevein

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1t0w__assembly_1__model_15

1t0w__assembly_1__model_15 | I(q)

1t0w__assembly_1__model_15 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 branched

6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

7. Citations (6)

25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina

1. Protein Identity and Related Structures Protein Identity & Related Structures

Hevein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1t0w__assembly_1__model_15

1t0w__assembly_1__model_15 | I(q)

1t0w__assembly_1__model_15 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 branched

6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

7. Citations (6)