Resonance assignments for stromelysin complexed with a beta-sulfonyl hydroxamate
inhibitor

Resonance assignments for stromelysin complexed with a beta-sulfonyl hydroxamate inhibitor.

The NMRPipe system is a UNIX software environment of processing, graphics, and
analysis tools designed to meet current routine and research-oriented
multidimensional processing requirements, and to anticipate and accommodate
future demands and developments. The system is based on UNIX pipes, which allow
programs running simultaneously to exchange streams of data under user control.
In an NMRPipe processing scheme, a stream of spectral data flows through a
pipeline of processing programs, each of which performs one component of the
overall scheme, such as Fourier transformation or linear prediction. Complete
multidimensional processing schemes are constructed as simple UNIX shell
scripts. The processing modules themselves maintain and exploit accurate
records of data sizes, detection modes, and calibration information in all
dimensions, so that schemes can be constructed without the need to explicitly
define or anticipate data sizes or storage details of real and imaginary
channels during processing. The asynchronous pipeline scheme provides other
substantial advantages, including high flexibility, favorable processing
speeds, choice of both all-in-memory and disk-bound processing, easy adaptation
to different data formats, simpler software development and maintenance, and
the ability to distribute processing tasks on multi-CPU computers and computer
networks.

Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A.
NMRPipe: a multidimensional spectral processing system based on UNIX pipes.
J Biomol NMR. 1995 Nov;6(3):277-93.

NMRPipe: a multidimensional spectral processing system based on UNIX pipes.

Moseley HN, Monleon D, Montelione GT.
Automatic determination of protein backbone resonance assignments from triple
resonance nuclear magnetic resonance data.
Methods Enzymol. 2001;339:91-108.

Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.

X-Ray Structure Of Human Stromelysin Catalytic Domain Complexed With Non-Peptide Inhibitors: Implications For Inhibitor Selecti

Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors

Solution Structure Of The Catalytic Domain Of Human Stromelysin-1 Complexed To A Potent Non-Peptidic Inhibitor, Nmr, 20 Structu

Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors

Human Stromelysin-1 Catalytic Domain Complexed With Ro-26-2812

Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812

X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectiv

Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution

Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor.

Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor.

Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor.

Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor

Heterocycle-Based Mmp Inhibitor With P2'substituents

A Carboxylic Acid Based Inhibitor In Complex With Mmp3

X-ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin

Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-764,

Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings

Crystal Structure Of Stromelysin Catalytic Domain

Crystal Structure Of Fibroblast Stromelysin-1: The C-Truncated Human Proenzyme

Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-702,

Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Ensemble Of 2

Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Average Of 20

Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-142372

Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor

Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydro

Solution Structure Of Matrix Metalloproteinase 3 (mmp-3) In The Presence Of N-hydroxy-2-[n-(2-hydroxyethyl)biphenyl-4- Sulfonam

Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of 3-4'-Cyanobyphenyl-4-Yloxy)-N- Hdydroxypropionamide

Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor

Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-141803

Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methoxy-N-(Pyridine-3-Ylmethyl)phenylsulfonamido)acetamide

Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methylphenylsulfonamido)acetamide

Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The Thiadiazole Inhibitor Ipnu-107859, Nmr,

Structure Of Mmp3 Complexed With A Platinum-based Inhibitor.

Structure Of Mmp3 Complexed With Nngh Inhibitor

matrix metalloproteinase 3 preproprotein variant [Homo sapiens]

prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]

matrix metalloproteinase-3 [Homo sapiens]

stromelysin catalytic domain [synthetic construct]

Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]

stromelysin-1 preproprotein [Homo sapiens]

PREDICTED: stromelysin-1 [Nomascus leucogenys]

PREDICTED: stromelysin-1 [Gorilla gorilla gorilla]

RecName: Full=Stromelysin-1; Short=SL-1; AltName: Full=Matrix metalloproteinase-3; Short=MMP-3; AltName: Full=Transin-1; Flags:

Goddard and Kneller, University of California, San Francisco.

Licensed from Geneformatics (http://www.geneformatics.com).