BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 08-21-2010, 11:53 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,134
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default Three-dimensional structure of the FK506 binding protein/ascomycin complex in solutio

Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR.

Related Articles Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR.

Biochemistry. 1993 Jan 26;32(3):754-65

Authors: Meadows RP, Nettesheim DG, Xu RX, Olejniczak ET, Petros AM, Holzman TF, Severin J, Gubbins E, Smith H, Fesik SW

A high-resolution three-dimensional solution structure of the FKBP/ascomycin complex has been determined using heteronuclear multidimensional nuclear magnetic resonance spectroscopy (NMR) and a distance geometry/simulated annealing protocol. A total of 43 structures of the complex, including 3 tightly bound water molecules, were obtained using 1958 experimental restraints consisting of 1724 nuclear Overhauser effect (NOE) derived distances, 66 chi 1 and 46 phi angular restraints, and 122 hydrogen bond restraints. The root mean square (rms) deviations between the 43 FKBP/ascomycin solution structures and the mean atomic coordinates were 0.43 +/- 0.08 A for the backbone heavy atoms and 0.80 +/- 0.08 A for all non-hydrogen atoms. Angular order parameters for the family of 43 conformations were calculated to determine dihedral convergence. Order parameters for phi, psi, and chi 1 angles exhibited mean values of 0.98, 0.97, and 0.95, respectively, while the mean of the chi 2 order parameter was 0.63. Comparisons were made between the FKBP/ascomycin complex and two NMR-derived solution structures of unbound FKBP and the X-ray crystal structure of an FKBP/FK506 complex. Differences were observed between the FKBP/ascomycin complex and uncomplexed FKBP for residues 33-45 and 78-92. In contrast, the NMR-derived solution structure of the FKBP/ascomycin complex and the X-ray crystal structure of the FKBP/FK506 complex were very similar. Differences between the two complexes were mainly observed in the conformations of some highly solvent exposed side chains.

PMID: 7678499 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog. Related Articles NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog. J Magn Reson B. 1994 May;104(1):77-80 Authors: Yu L, Meadows RP, Wagner R, Fesik SW
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand bi
15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition. Related Articles 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition. Biochemistry. 1994 Apr 12;33(14):4093-100 Authors: Cheng JW, Lepre CA, Moore JM Backbone dynamics of the ligand- (FK506-) bound protein FKBP-12 (107 amino acids) have been examined using 15N relaxation data derived from inverse-detected two-dimensional...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog. Related Articles NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog. J Magn Reson B. 1994 May;104(1):77-80 Authors: Yu L, Meadows RP, Wagner R, Fesik SW
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand bi
15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition. Related Articles 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition. Biochemistry. 1994 Apr 12;33(14):4093-100 Authors: Cheng JW, Lepre CA, Moore JM Backbone dynamics of the ligand- (FK506-) bound protein FKBP-12 (107 amino acids) have been examined using 15N relaxation data derived from inverse-detected two-dimensional...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the unc
15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor. Related Articles 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor. Biochemistry. 1993 Sep 7;32(35):9000-10 Authors: Cheng JW, Lepre CA, Chambers SP, Fulghum JR, Thomson JA, Moore JM Backbone dynamics of the major tacrolimus (FK506) binding protein (FKBP-12, 107 amino acids) have been studied using 15N relaxation data derived from proton-detected two-dimensional 1H-15N NMR spectroscopy....
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppres
Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppressant complex. Related Articles Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppressant complex. Biochemistry. 1993 Mar 16;32(10):2473-80 Authors: Xu RX, Meadows RP, Fesik SW From a series of 15N-resolved 3D ROESY-HMQC and 13C-resolved 3D NOESY-HMQC spectra of the FK506 binding protein (FKBP)/ascomycin complex in H2O, the locations of three tightly bound water molecules were identified. These waters are all buried within the...
nmrlearner Journal club 0 08-21-2010 11:53 PM
[NMR paper] NMR studies of an FK-506 analog, [U-13C]ascomycin, bound to FK-506-binding protein.
NMR studies of an FK-506 analog, ascomycin, bound to FK-506-binding protein. Related Articles NMR studies of an FK-506 analog, ascomycin, bound to FK-506-binding protein. J Med Chem. 1992 Jun 26;35(13):2467-73 Authors: Petros AM, Gemmecker G, Neri P, Olejniczak ET, Nettesheim D, Xu RX, Gubbins EG, Smith H, Fesik SW Multidimensional, heteronuclear NMR methods were used to determine the complete 1H and 13C resonance assignments for ascomycin bound to recombinant FKBP, including stereospecific assignment of all 22 methylene protons. The...
nmrlearner Journal club 0 08-21-2010 11:41 PM
[NMR paper] The detection of proline isomerase activity in FK506-binding protein by two-dimension
The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy. Biochem Biophys Res Commun. 1990 Aug 31;171(1):445-50 Authors: Justice RM, Kline AD, Sluka JP, Roeder WD, Rodgers GH, Roehm N, Mynderse JS 1H NMR assignments of the trans and cis isomers of...
nmrlearner Journal club 0 08-21-2010 11:04 PM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This Thread:

Posting Rules
You may not post new threads
You may not post replies
You may not post attachments
You may not edit your posts

BB code is On
Smilies are On
[IMG] code is On
HTML code is On
Trackbacks are Off
Pingbacks are Off
Refbacks are Off



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 09:43 AM.


Map