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2tmp

N-TERMINAL DOMAIN OF TISSUE INHIBITOR OF METALLOPROTEINASE-2 (N-TIMP-2), NMR, 49 STRUCTURES

Method: SOLUTION NMR Dmax: 53.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TISSUE INHIBITOR OF METALLOPROTEINASES-2

Homo sapiens

UniProt P16035

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 27–153 Fragment：N-TERMINAL DOMAIN, RESIDUES 1-127 Mutation：A21T No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.7；308 K；Ionic strength (raw mmCIF value) 125 mM；Pressure 1 NMR sample composition：AQUEOUS Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 2TMP Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BR9 HUMAN TISSUE INHIBITOR OF METALLOPROTEINASE-2 Deposited 1998-08-28 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 27–220（194 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 2.10 Å R-free 0.271
1GXD proMMP-2/TIMP-2 complex Deposited 2002-04-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 27–220（194 aa）
Not recorded SO4 SULFATE ION × 1 ZN ZINC ION × 2 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；pH 8.50
Resolution 3.10 Å R-free 0.333
1GXD proMMP-2/TIMP-2 complex Deposited 2002-04-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 27–220（194 aa）
Not recorded SO4 SULFATE ION × 1 ZN ZINC ION × 2 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；pH 8.50
Resolution 3.10 Å R-free 0.333
4ILW Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor of metalloproteinases-2 (TIMP-2) Deposited 2013-01-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 27–220（194 aa） Fragment：Tissue inhibitor of metalloproteinases-2
Not recorded ZN ZINC ION × 2 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；298 K；0.1 M HEPES pH 7.5, 25 % (w/v) PEG 2000 MME, VAPOR DIFFUSION, temperature 298K
Resolution 2.10 Å R-free 0.263
4ILW Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor of metalloproteinases-2 (TIMP-2) Deposited 2013-01-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 27–220（194 aa） Fragment：Tissue inhibitor of metalloproteinases-2
Not recorded ZN ZINC ION × 2 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；298 K；0.1 M HEPES pH 7.5, 25 % (w/v) PEG 2000 MME, VAPOR DIFFUSION, temperature 298K
Resolution 2.10 Å R-free 0.263

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIMP2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–127； UniProt 27–153

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.

SAXS scattering curve SAXS Profile

SAXS profile for 2tmp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2tmp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2tmp
Deposition date deposition_date1998-05-26
Structure title titleN-TERMINAL DOMAIN OF TISSUE INHIBITOR OF METALLOPROTEINASE-2 (N-TIMP-2), NMR, 49 STRUCTURES
Keywords keywordsTIMP, METALLOPROTEINASE INHIBITOR, OB PROTEIN FOLD, METALLOPROTEASE INHIBITOR; METALLOPROTEASE INHIBITOR
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.32 Å
Radius of gyration Rg (electron density) rg_electron14.09 Å
Forward intensity I(0) i06594330000.00
Molecular weight molecular_weight689590.0 kDa
Excluded volume excluded_volume860850 ų
Envelope volume envelope_volume24300 ų
Hydration-shell volume shell_volume13659 ų
Envelope diameter envelope_diameter50.8 Å
Shell Rg shell_rg20.85 Å
Envelope Rg envelope_rg15.57 Å
Shape Rg shape_rg14.06 Å
Total Rg total_rg14.21 Å
Total atoms total_atoms95942
Residues n_residues6223
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax53.8 Å
Rg (real space) rg_real14.28 Å
Rg uncertainty (real space) rg_real_error0.51 Å
I(0) (real space) i0_real6.5940e+09
I(0) uncertainty (real space) i0_real_error7.9830e+07
Rg (reciprocal space) rg_reciprocal14.29 Å
I(0) (reciprocal space) i0_reciprocal6594000000.0000
Solution quality estimate total_estimate0.7291
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary16.3 Å
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.305
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha300700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.530; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.902; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2tmpa_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.3 — TIMP-like
Family Family familyb.40.3.1 — Tissue inhibitor of metalloproteinases, TIMP

CATH v4.4 (1 domains)

Domain ID domain_id2tmpA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily120 —
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8. Citations (5)

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9. Files and Curves (10)