ID,Name,Type,Details,Sf_ID,Entry_ID,Study_list_ID
1,"Signal assignments and chemical-shift structural analysis of uniformly 13C, 
15N-labeled peptide, mastoparan-X, by multidimensional solid-state NMR under 
magic-angle spinning",Structure analysis,,14,10001,1
1,NMR measurement of bovine beta-lactoglobulin at neutral pH,Structure analysis,,171,10010,1
1,Actin-binding domain of troponin TnI-TnC-TnT2 ternary complex,Structure analysis,,212,10012,1
1,,Structure analysis,,368,10019,1
1,"Signal assignment and secondary structure analysis of H+-ATP synthase subunit c
by magic-angle spinning solid-state NMR",,,407,10021,1
1,Solution structure of the Rhodobacter sphaeroides PufX protein,Structure analysis,,470,10024,1
,characterization of PCP in the D1 state,Structure analysis,characterization of PCP-0SH in the D1 state was examined by using H/D exchange experiments.,1052,10052,1
1,Study of ineteraction between LolA and LolB,Protein-Protein Interaction,"The data from this entries has been used to investigate an interaction between
LolA and LolB",1590,10078,1
1,Study of ineteraction between LolB and LolA,Protein-Protein Interaction,"The data from this entries were used to investigate an interaction between LolA
and LolB",1967,10096,1
1,,,,55226,16792,1
1,,,,69492,17524,1
1,,,,71211,17612,1
1,,,,73791,17747,1
1,,,,73946,17753,1
1,,,,76780,17900,1
1,pH-dependent chemical shifts of the ionizable amino acids,pH-dependent chemical shifts,,126185,25295,1
1,pH-dependent chemical shifts of the ionizable amino acids,pH-dependent chemical shifts,,126590,25316,1
1,pH-dependent chemical shifts of the ionizable amino acids,pH-dependent chemical shifts,,126609,25317,1
1,pH-dependent chemical shifts of the ionizable amino acids,pH-dependent chemical shifts,,126628,25318,1
1,pH-dependent chemical shifts of the ionizable amino acids,pH-dependent chemical shifts,,126647,25319,1
1,pH-dependent chemical shifts of the ionizable amino acids,pH-dependent chemical shifts,,126666,25320,1
1,pH-dependent chemical shifts of the ionizable amino acids,pH-dependent chemical shifts,,126685,25321,1
1,pH-dependent chemical shifts of the ionizable amino acids,pH-dependent chemical shifts,,126704,25322,1
1,pH-dependent chemical shifts of the ionizable amino acids,pH-dependent chemical shifts,,126723,25323,1
1,Structural Study of Human Macrophage Metalloelastase (MMP-12) in its inhibitor-free state,Structure analysis,"The data from the entries that make up this study are used to determine the
structure of MMP-12 without inhibitor bound.",136265,25859,1
1,Structural basis of detection and signaling of DNA single-strand breaks by human PARP 1,,,136756,25888,1
1,Structural basis of detection and signaling of DNA single-strand breaks by human PARP 1,,,136798,25889,1
1,Structural basis of detection and signaling of DNA single-strand breaks by human PARP 1,,,136822,25890,1
1,Structural basis of detection and signaling of DNA single-strand breaks by human PARP 1,,,136847,25891,1
1,Structural basis of detection and signaling of DNA single-strand breaks by human PARP 1,,,136873,25892,1
1,Structural basis of detection and signaling of DNA single-strand breaks by human PARP 1,,,136898,25893,1
1,Structural basis of detection and signaling of DNA single-strand breaks by human PARP 1,,,136921,25894,1
1,Structural basis of detection and signaling of DNA single-strand breaks by human PARP 1,,,136949,25895,1
1,NMR solution structure of crambin in DPC micelles,Structure analysis,,247766,6504,1
,"NMR assignment of the holo-acyl carrier protein (PfACP) from malaria parasite
Plasmodium falciparum",,,248031,6516,1
1,Characterization of an amyloid fibril intermediate,Structure analysis,Data from the entries were used to assign residues for H/D exchange and stability studies at pH 4.0.,248108,6521,1
2,Characterization of an amyloid fibril intermediate,Structure analysis,Data from the entries were used to assign residues at pH 6.0.,248108,6521,1
1,Characterization of an amyloid fibril intermediate,Structure analysis,Data from these entries were used to assign residues for H/D exchange and stability studies at pH 4.0,248127,6522,1
2,Characterization of an amyloid fibril intermediate,Structure analysis,Data from these entries were used to assign residues for H/D exchange and stability studies at pH 6.0,248127,6522,1
1,Human apolipoprotein E N-terminal domain NMR chemical shift,Structure analysis,This is the chemical shift assignment of human apoE N-terminal domain (Backbone + Cbeta),248144,6524,1
1,Solution structure of the KH-QUA2 region of the Xenopus STAR/GSG Quaking protein.,Structure analysis,,248180,6526,1
,Investigation of km23,Structure analysis,The data from the entries that make up this study were used to determine the structure of of km23,248193,6527,1
1,Structural analysis of the interaction between RPA32C and Tag-OBD,,,248347,6535,1
1,Designed Ligand Binds to (CAG)n Trinucleotide Repeats by Inducing Base Flipping,Structure analysis,The data from the entries that make up this study were used to determine the structure,248379,6537,1
1,Comparison of the oxidized and reduced form of the human ADAP hSH3-1 domain,Structure analysis,,248408,6539,1
1,Investigation of structure of oxidized ArsC in solution,Structure analysis,"The data from the entries that make up this study were used to determine the
structure of oxidized ArsC",248877,6563,1
1,Solution structure and automated disulfide bond determination of Crotamine,Structure analysis,,249111,6576,1
1,Investigation of Bacillus stearothermophilus IF2 subdomains,Structure analysis,"The data from the entries that make up this study were used to study
structure-function relations of Bacillus stearothermophilus IF2.",249131,6577,1
,Structure determination of Bcl-xl/Bad-BH3 peptide complex,,,249172,6578,1
1,Structure determination ecBMPR-II,Structure analysis,ecBMPR-II structure is going to be solved using solution NMR spectroscopy,249258,6582,1
1,Investigation of of human apolipoprotein A-I in lipid-mimetic solution,Structure analysis,The data from the entries that make up this study were used to determine the structure of A-I apolipoprotein,249366,6587,1
1,Investigation of of human apolipoprotein A-I(1-186) in lipid-mimetic solution,Structure analysis,The data from the entries that make up this study were used to determine the structure of A-I(1-186) apolipoprotein,249379,6588,1
1,Three-dimensional solution structure of the Chromo 2 domain of cpSRP43,Structure analysis,,249457,6592,1
1,Three-dimensional solution structure of the chromo 3 domain of cpSRP43,Structure analysis,,249471,6593,1
1,solution structure of scRPA70A and its interaction with ssDNA and other protein,Structure analysis,The data were used to determine the structure of scRPA70A,249738,6606,1
1,Structure of Bacillus subtilis SSD domain,Structure analysis,,249886,6615,1
1,peptide P5 encompassing G6-V32 region of the N-terminal of trialysin,Structure analysis,"The data from the entries were used to explain differences in activities of
peptides from the same protein domain in a structural basis.",249900,6616,1
1,peptide P6 encompassing F1-V32 region of the N-terminal of trialysin,Structure analysis,"The data from the entries were used to explain differences in activities of
peptides from the same protein domain in a structural basis.",249934,6618,1
1,peptide P7 encompassing F1-S27 region of the N-terminal of trialysin,Structure analysis,"The data from the entries were used to explain differences in activities of
peptides from the same protein domain in a structural basis.",249952,6619,1
,NMR solution structure of murine p22HBP,Structure analysis,NMR solution structure of murine p22HBP,249983,6620,1
1,"1H, 15N, and 13C Resonance Assignments of Human Interleukin-2",Chemical shift assignment,,250015,6621,1
1,NMR structure of PcFK1,Structure analysis,,250265,6636,1
,,Structure analysis,,250396,6642,1
,"1H, 13C and 15N backbone and side chain resonance assignments of Haloferax
volcanii DHFR1",Structure analysis,,250435,6645,1
1,comparison of one- and two-zinc finger protein domains,Structure analysis,"structural comparison of one- and two-zinc finger protein domains using
chemical shift data, in which the two fingers form a stable interacting motif",250489,6648,1
,Study of fragments from the N-terminal region of Sticholisin protein,Structure analysis,Studies of peptide structure in SDS micelles,250557,6650,1
1,Study of fragments from the N-terminal region of Sticholisin protein,Structure analysis,Studies of peptide structure in SDS micelles,250581,6651,1
1,comparison of one- and two-zinc finger protein domains,Structure analysis,"structural comparison of one- and two-zinc finger protein domains using
chemical shift data, in which the two fingers form a stable interacting motif",250624,6653,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250776,6659,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250805,6660,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250821,6661,1
1,"Solution Structure of HndAc : A Thioredoxin-like Domain Involved in the
NADP-reducing Hydrogenase Complex.",Structure analysis,"The data from the entries that make up this study were used to determine the
structure of HndAc.",254057,6836,1
1,"Dynamics and structural study of PSE-4, a 29.5 kDa class A beta-lactamase from Pseudomonas aeruginosa",Dynamics,,254102,6838,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250837,6662,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250853,6663,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250869,6664,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250885,6665,1
1,Structure determination,Structure analysis,Resonance assignments used for structure determination,254173,6840,1
1,Structure of the recombinant Crassostrea gigas defensin,Structure analysis,The structure of the recmbinant Crassostrea gigas defensin has been determined by NMR,254323,6849,1
1,MBP immunodomiant peptide in 100mM KCl,Structure analysis,structure analysis of an immunodominat peptide of MBP (FF2) in 100mM KCl,254446,6857,1
2,MBP immunodomiant peptide in 30% TFE-d2,Structure analysis,structure analysis of an immunodominat peptide of MBP (FF2) in 30% TFE-d2,254446,6857,1
3,MBP immunodomiant peptide in 100mM DPC-d38,Structure analysis,structure analysis of an immunodominat peptide of MBP (FF2) in 100mM DPC-d38,254446,6857,1
1,peptide P2 encompassing K21-K47 region of the N-terminal of trialysin,Structure analysis,"The data from the entries were used to explain differences in activities of
peptides from the same protein domain in a structural basis.",254490,6859,1
1,egg case silk,Structure analysis,,254586,6864,1
1,structure of calcium-free rat beta-parvalbumin (oncomodulin),Structure analysis,,262591,7322,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250901,6666,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250917,6667,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250933,6668,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250949,6669,1
1,Structure determination of P.falciparum TRAP-TSR domain,Structure analysis,The data from the entry were used to determine the structure of P.falciparum TRAP-TSR domain,254600,6865,1
1,Assignment of chemical shifts,Structure analysis,Determination of the structure of the Ig1 module of FGFR1,255001,6885,1
,Solution Structure of dNedd4 WW3* - Comm PY Motif Complex,"Structure, binding experiments on wildtype and mutant proteins and ligands",,255050,6890,1
1,comparison of one- and two-zinc finger protein domains,Structure analysis,"structural comparison of one- and two-zinc finger protein domains using chemical
shift data, in which the two fingers form a stable interacting motif",255363,6905,1
1,Investigation of solution structure of human metallothionein-3,Structure analysis,,255422,6909,1
1,Pfu pop5 backbone assignments,Structure analysis,"Backbone assignments of Pyrococcus furiosus Pop5 (PF1378), an archaeal RNase P protein.",255550,6917,1
1,"1H, 13C and 15N resonance assignments of the region 655-775 of the human MAN1",Structure analysis,"The data from this entry     
 that make up this study were used to determine the structure of region 655-775 of the C-terminal domain of human MAN1.",255578,6919,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250981,6670,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",250997,6671,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",251013,6672,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",251029,6673,1
1,discrepin,structure study,The data from this entry were used to determine solution structure of discrepin,255652,6924,1
1,NMR assignment of Kid toxin,Structure analysis,"The data from the entries that make up this study were used to determine the
secondary structure of the bacterial toxin Kid.",255669,6925,1
,Investigation of Wzb from E. coli,Structure analysis,The data from the entry that make up this study were used to determine the structure of Wzb.,255791,6934,1
1,Structure analysis of region 51-160 of human KIN17 protein,Structure analysis,"The data from the entries that make up this study were used to determine the
structure of region 51-160 of human KIN17",255839,6938,1
1,Investigation of the conformation of the XAO peptide at 5oC using NMR.,Structure analysis,Chemical shifts data for the XAO peptide [Ac-Dab-Dab-(Ala)7-Orn-Orn-NH2 where Dab is diaminobutyric acid and Orn is ornithine).,255885,6941,1
1,Structural investigation of the N-terminal region of the human eIF5,Structure analysis,The data from the chemical shift entry were used to determine the structure of the N-terminal domain of eIF5,255929,6944,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",251045,6674,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",251061,6675,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",251077,6676,1
,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",251093,6677,1
1,E. coli Fur,monomer/dimer comparison,monomeric and dimeric species of the E. coli Fur protein were assigned and compared,255976,6947,1
1,E. coli Fur,monomer/dimer comparison,monomeric and dimeric species of the E. coli Fur protein were assigned and compared,255996,6948,1
1,Structure Determination of Rpa2829: Northeast Structural Genomics Target RpR43,Structure analysis,,256224,6964,1
1,"1H, 13C and 15N assignment of C', CA, CB, N, HN, HA and HB of intrinsically disordered alpha-synuclein",Structure analysis,"1H, 13C and 15N assignment of C', CA, CB, N, HN, HA and HB of intrinsically disordered alpha-synuclein through new NMR experiments",256295,6968,1
,Investigation of SARS-CoV S2-HR2 domain in its trimeric stae,Structure analysis,,256310,6969,1
1,NMR study of the activated form of the small Rho-GTPase Rac1,,"1H, 15N, 13C assignments for the activated form of the small Rho-GTPase Rac1",256323,6970,1
1,Solution Structure of TA0895,Structure analysis,,256477,6982,1
1,Investigation of colicin immunity proteins and their noncognate complexes with the colicin E9 DNase domain,Structure analysis,Including structure determination of Im2 by multinuclear nmr,262605,7323,1
1,"Changes in hydrogen bond strengths explain variations in the reduction
potentials of a series of rubredoxin mutants",Mutant comparison,"The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent
system for testing ideas concerning the ways in which a protein sequence of an
iron-sulfur protein can modulate the reduction potential of the active site
iron. Mutations at two residues (valine-8 and valine-44) are known to affect
the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic
results that have allowed us to determine with unprecedented accuracy the
lengths (and therefore the strengths) of all six key hydrogen bonds between
protein backbone amides and the sulfur atoms of the four cysteine residues that
ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine
mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths
(or strengths) of the hydrogen bonds are inferred from the level of
trans-hydrogen-bond electron spin delocalization from the iron atom. The
aggregate lengths of these six hydrogen bonds, as reported by the electron spin
delocalization effect on the nitrogen-15 chemical shifts, are shorter in both
oxidation states in mutants with higher reduction potential than in those with
lower reduction potential, and the differences in the aggregate hydrogen bond
strengths upon reduction of CpRd correlate linearly with the published
reduction potentials for the 10 proteins, which span 126 mV. Sequence effects
on the reduction potential can be explained fully, in the case of these CpRd
variants, by their effects on hydrogen bonds.",251109,6678,1
1,G311,Structure analysis,,251125,6679,1
,A219 solution structure determination.,Structure analysis,"The data from the entries that make up this study were used to determine the
structure of A219 mutant protein.",251154,6680,1
1,PSI AB box,Structure analysis,PSI AB box complex with U1-70k protein proline-rich peptide,251350,6690,1
1,PSI AB box,Structure analysis,PSI AB box complex with U1-70k protein proline-rich peptide,251383,6691,1
1,Solution structure of the BLUF domain of AppA 5-125,Structure analysis,,251413,6692,1
1,assignment,Mutant comparison,assignment only,251512,6696,1
1,NMR Chemical Shift Assignment of La3+ monosubstituted Calbindin D9k.,Structure analysis,"The native metal ion (Ca2+) in the second site of calbindin D9k has been
substituted here by La3+, in order to have a diamagnetic homologous to the
paramagnetic system (Tm3+ monosubstituted calbindin D9k)with the same electric
charges.",251554,6699,1
,Drosophila (d)TAF1 was studied in complex with TATA-binding protein (TBP),Structural analysis,The data were used to study the structure of dTAF1 in complex with TBP,251576,6700,1
1,Interaction study between yTAF1(10-73)and TBP,,,251591,6702,1
1,"1H, 13C, and 15N Chemical Shift Assignments for Human Ubc7",Structure analysis,"1H, 13C, and 15N chemical shift assignments for human ubiquitin-conjugating
enzyme, Ubc7",251676,6711,1
1,Dengue Envelop protein Domain III,Structure analysis,"N15, C13 and H1 chemical shift assignment",251988,6725,1
,,Structure analysis,,252003,6726,1
1,NMR studies of RP2,Structure analysis,Resonance assignments of C-terminal domian of RP2,252318,6744,1
,NMR assignment of human HnRNP F,Structure analysis,,252334,6745,1
1,Investigation of the PH-PDZ tandem of alpha syntrophin,Structure analysis,"The data from the entries that make up this study were used to determine the
structure of alpha syntrophin",252461,6752,1
1,the joined PH domain of alpha-syntrophin,Structure analysis,,252475,6753,1
1,"solution structure of TA0743  
from thermoplasma acidophilum",Structure analysis,"the data from the entries that make up this study were used to determine the
structure of TA0743",252502,6755,1
1,magnesium ion titration,chemical shift mapping,The RNA was titrated with 0-12 mM MgCl2 and the chemical shifts plotted against the metal ion concentration. Affinity constants (log Ka values) were calculated from Levenberg-Marquardt nonlinear least-squares regression for a single binding isotherm.,252515,6756,1
,"NMR structure and molecular dynamics of the in-plane membrane anchor domain of
the NonStructural Protein 5A (NS5A) from Bovine Viral Diarrhea Virus (BVDV)",Structure analysis,"This study concerns the 3D structure analysis of the [1-28] N-terminal sequence
of NS5A in 50% TFE or 100 mM SDS.",252534,6757,1
1,NEAT domain structural studies,Structure analysis,"The data in this study will be used for structure determination of the NEAT
domain",252593,6759,1
1,Solution structure of pa0128,Structure analysis,"Solution structure calculation of a hypothetical - phn-A like protein pa0128
from Pseudomonas aeruginosa",252707,6766,1
1,"Solution Structure of a Hypothetical Protein (NE2066) from
Nitrosomonas_europaea",Structure analysis,,252738,6769,1
1,Investigation of bombinin H2 in DPC micelles,Structure analysis,,252808,6774,1
1,Investigation of bombinin H4 in DPC micelles,Structure analysis,,252821,6775,1
,Structural studies of the kinase inducible domain of CREB,Structure analysis,,253007,6784,1
,Structural analysis of the catalytic antibody 6D9 using NMR,Structure analysis,,253032,6785,1
1,Structure of the C2A domain of rabphilin 3A,Structure analysis,The data from the entries that make up this study were used to determine the structure of the C2A domain of rabphilin,253087,6787,1
,Conformational studies of the Ser133-phosphorylated kinase inducible domain of CREB,Structure analysis,,253103,6788,1
5991,Structures of Allatostatin Family Members AST5 and AST8 from 2D NMR Data,Structure analysis,"NMR strucutre of Dip-Allatostatin 5 and Dip-Allatostatin 8 are determined. AST5
has a sequence of DRLYSFGL-NH2 and AST8 has a sequence of GGSLYSFGL-NH2 and yet
they have basically opposite functionality.",253186,6791,1
1,backbone chemical shifts,Structure analysis,,253483,6809,1
1,Pharmacophore analysis of the Human Rhinovirus 3C Protease,,,253774,6823,1
1,backbone assignment of apo-MazF(E24A),Interactions with different ligands,"The data from the entries that make up this study were used to determine the
interactions of MazF(E24A) with the antitoxin peptide as well as a nucleotide
substrate.",253885,6828,1
1,"Solution structures of the Chitin-binding Domain of Hyperthermophilic Chitinase
from Pyrococcus furiosus",Structure analysis,"The data from the entries that make up this study were used to determine the
structure of Chitin-binding Domain of Hyperthermophilic Chitinase",253900,6829,1
1,"Comparative NMR study on the impact of point mutations on protein stability of
Pseudomonas mendocina lipase",Mutant comparison,,253962,6832,1
1,backbone assignment of MazF(E24A) bound with MazEp(54-77),Interactions with different ligands,The data from the entries that make up this study were used to determine the interactions of MazF(E24A) with MazEp(54-77),253986,6833,1
1,"Backbone NMR assignments and H/D exchange studies on the azide- and
cyanide-inhibited forms of P. aeruginosa heme oxygenase.",Structure analysis,"Chemical shifts and H/D exchange data were used in a comparison study to assess
the differences in structure and dynamic behavior occurring when azide or
cyanide are bound to the heme in pa-HO.",256495,6983,1
1,NMR charateriztion of the human Hexim1 TBD,Structure analysis,The data from the entries that make up this study were used to determine the structure of human Hexim1 TBD.,256528,6985,1
1,NMR STRUCTURAL AND BINDING STUDIES OF THE PTB DOMAIN OF TENSIN,Structure analysis,,256548,6986,1
1,"Backbone NMR assignments and H/D exchange studies on the azide- and
cyanide-inhibited forms of P. aeruginosa heme oxygenase.",Structure analysis,"Chemical shifts and H/D exchange data were used in a comparison study to assess
the differences in structure and dynamic behavior occurring when azide or
cyanide are bound to the heme in pa-HO.",256564,6987,1
1,"Solution Structure of the Ubiquitin-Associated Domain of Human BMSC-UbP and its
Complex with Ubiquitin",Structure analysis,"The data from the entries that make up this study were used to determine the
solution structure of Human BMSC-UbP UBA domain",256582,6988,1
1,Solution Structure of Ribosomal Protein S24E from Thermoplasma acidophilum.,Structure analysis,"This study were used to determine the structure of Ribosomal Protein S24E from
Thermoplasma acidophilum.",256596,6989,1
1,"Investigation of cerato-platanin, a phytotoxic toxin",Structure analysis,The data from the entries that make up this study were used to determine the structure of cerato-platanin protein,256626,6990,1
1,investigation of structural changes of TFCD upon phosphorylation,Structure analysis,"The data from the entries that make up this study were used to determine the
structure of unphosphorylated Tissue Factor Cytoplasmic Domain.",256642,6991,1
1,Three dimensional structure of the bacterial cell wall peptidoglycan,Structure analysis,NMR solution structure of the bacterial cell wall peptidoglycan,256658,6992,1
1,"Phosphorylation of the Cytoplasmic Domain of the Tissue Factor and its Role in
Modulating Structure and Binding Affinity.",Structure analysis,"The data from the entries that make up this study were used to determine the
structure of double phosphorylated(SEP253 and SEP258) Tissue Factor Cytoplasmic
Domain.",256679,6993,1
1,"Phosphorylation of the Cytoplasmic Domain of the Tissue Factor and its Role in
Modulating Structure and Binding Affinity.",Structure analysis,"The data from the entries that make up this study were used to determine the
structure of single phosphorylated(SEP253) Tissue Factor Cytoplasmic Domain.",256715,6996,1
1,"Phosphorylation of the Cytoplasmic Domain of the Tissue Factor and its Role in
Modulating Structure and Binding Affinity.",Structure analysis,"The data from the entries that make up this study were used to determine the
structure of single phosphorylated(SEP258) Tissue Factor Cytoplasmic Domain.",256750,6998,1
,Solution structure of the Ede1 UBA-ubiquitin complex,Structure analysis,"The data from the entries that make up this study were used to determine the
structure of the Ede1 UBA-ubiquitin complex",256838,7002,1
1,Study of complexes of Bcl-2 family proteins,Structure analysis,,257047,7013,1
,,Structure analysis,,257155,7019,1
1,"Structural, Biochemical and Dynamic Characterizations of the hRPB8 Subunit of Human RNA Polymerases",Structure analysis,,257168,7020,1
1,NMR signal assignment,NMR signal assignment,NMR signal assignment,257232,7023,1
1,"Structure insight into Binding diversity of SH3 domain of human NCK2 adaptor
protein",Structure analysis,"The data from the entries that make up this study were used to determine the
structure of SH3 domain",257433,7035,1
1,NMR chemical shift assignments and structure determination of Xanthomonas campestris XCC1710,Structure analysis,structure determination of this protein,257553,7054,1
1,Assignment of chemical shifts of Peptidyl-tRNA hydrolase (PTH) from Mycobacterium tuberculosis H37Rv.,Structure analysis,The assigned chemical shifts would be used for structural studies.,257572,7055,1
1,Solution structure of Calponin Homology domain of Human MICAL-1,Structure analysis,"The data from the entries that make up this study were used to determine the
structure of Calponin Homology domain of Human MICAL-1",257638,7058,1
1,Investigation of PZA-resistance by Mycobacterium Tuberculosis,Structure analysis,The data from the entries that make up this study were used to determine the structure of Pyrazinamidase.,257670,7059,1
1,NMR assignment of Kis antitoxin,Structure analysis,"The data from the entries that make up this study were used to determine the
secondary structure of the bacterial antitoxin Kis.",257937,7071,1
1,Solution structure of human GOPC PDZ domain,Structure analysis,The data from the entries that make up this study were used to determine the structure of human GOPC PDZ domain,257959,7072,1
1,Structure Determination of a New Protein PF1455 from Backbone-Centered NMR Data and NMR-Assisted Structure Prediction,Structure analysis,,257987,7073,1
1,Structure of an unique DNA-binding protein form prococcus furiosus,Structure analysis,"NMR study of the structure of Pf0610, a metal-chelating DNA-binding protein.",258004,7074,1
,"Solution structure of conserved unknown protein RPA2825 from Rhodopseudomonas
palustris (Northeast Structural Genomics Consortium Target RpT4; Ontario Centre
for Structural Proteomics Target RP2812)",Structure analysis,"The data from this entry is used in the calculation of Solution structure of
conserved unknown protein RPA2825 from Rhodopseudomonas palustris; Northeast
Structural Genomics Consortium Target RpT4; Ontario Centre for Structural
Proteomics Target rp2812.",258070,7079,1
1,Structure determination of the LANP N-terminal domain,Structure analysis,The data from the entries that make up this study were used to determine the structure of the LANP N-terminal domain,258116,7081,1
1,Structural determination of PutA45,Structure analysis,,258149,7082,1
,Structural Study of Human Macrophage Metalloelastase (MMP-12) in its inhibitor-free state,Structure analysis,"The data from the entries that make up this study are used to determine the
structure of MMP-12 without inhibitor bound.",258298,7089,1
2,Investigation of beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and MgF3-,Structure analysis,"The data from the entry was used to determine the backbone assignment and
19F-1H NOEs for a structural study of the beta phosphoglucomutase
glucose-6-phosphate MgF3- ternary complex",260797,7234,1
1,Investigation of beta phosphoglucomutase in the open state,Structure analysis,The data from the entry was used to determine the backbone assignment of beta phosphoglucomutase,260826,7235,1
1,"Solution structure of a purine rich hexaloop hairpin belonging to PGY/MDR1 mRNA
and targeted by antisense oligonucleotides",Structure analysis,"A preferential target of antisense oligonucleotides directed against human
PGY/MDR1 mRNA is a hairpin containing a stem with a G.U wobble pair, capped by
the purine-rich 5'r(GGGAUG)3' hexaloop. This hairpin is studied by
multidimensional NMR and restrained molecular dynamics, with special emphasis
on the conformation of south sugars and non standard phosphate linkages
evidenced in both the stem and the loop. The hairpin is found to be highly
structured. The G.U wobble pair, a strong counterion binding site, displays
structural particularities that are characteristic of this type of mismatch.
The upper part of the stem undergoes distortions that optimize its interactions
with the beginning of the loop. The loop adopts a new fold in which the
single-stranded GGGA purine tract is structured in A-like conformation stacked
in continuity of the stem and displays an extensive hydrogen bonding surface
for recognition. The remarkable hairpin stability results from classical inter-
and intra-strand interactions reinforced by numerous hydrogen bonds involving
unusual backbone conformations and ribose 2'-hydroxyl groups. Overall, this
work emphasizes numerous features that account for the well-ordered structure
of the whole hairpin and highlights the loop properties that facilitate
interaction with antisense oligonucleotides.",258319,7090,1
1,"Chemical shift assignment of monomeric chorimate mutase from methanococcus
jannaschii in a complex with a transition state analog",,,258358,7093,1
,NMR solution structure of the Acylphosphatase from Eschaerichia Coli,Structure analysis,The chemical shifts entries were used to determine the structure of the Acylphosphatase from Eschaerichia Coli.,258375,7094,1
1,Assignment of chemical shifts of the NCAM F3 module 2,Structure analysis,"The data from the entries that make up this study were used to determine the
structure of he NCAM F3 module 2.",258538,7104,1
1,RGS18 Structure,Structure analysis,Determination of the RGS18 structure in solution,258567,7106,1
6960,,,,258631,7110,1
1,Chemical shift assignment of multicrystalline ubiquitin,solid state NMR assignment,"this data include the chemical shift assignment of multicrystallline ubiquitin
including the stereospecific assignment of isopropylgroups (Val, Leu) and the
assignments of the aromatic side chains",258650,7111,1
,,Structure analysis,,258871,7124,1
,Solution Structure of Crk Sh3 domain,Structure analysis,,258975,7129,1
1,Backbone NMR assignment of the 29.6 kDa Rhodanese protein from Azotobacter vinelandii,Backbone assignment,The data from the entries that make up this study were used to assign the backbone resonances of Rhodanese,258992,7130,1
,Solution structure of IGF2R domain11,Structure analysis,,259004,7131,1
1,NMR assignment for the CheA P1 phosphotransfer domain from Thermotoga maritima,Protein-protein interaction study,"The data was used to monitor binding to a CheA catalytic domain construct, P3P4",259022,7132,1
1,"NMR assignment for the CheA P4 catalytic domain from Thermotoga maritima, in the context of P3P4.",Protein-protein interaction study,"The data was used to monitor binding to a CheA phosphotransfer domain construct, P1",259035,7133,1
,RBP unfolded in 8M urea at pH 2 and 20C,denatured state of RBP,"Investigation of human serum retinol-binding protein unfolded in 8M urea at pH
2 and 20C. This is part of a detailed study of the unfolding in urea of the RBP
molten globule at pH 2.",259205,7149,1
1,Structure determination of DLC2-SAM in solution,Structure analysis,The data from the entries that make up this study were used to determine structure,259240,7151,1
1,Structure determination of the hZnF2 NUP153 zinc-finger and its interactions with Ran,Structure analysis,,259343,7158,1
2,Structure determination of the hZnF2 NUP153 zinc-finger and its interactions with Ran,Interactions with different ligands,,259343,7158,1
,,Interactions with different ligands,the data were used to study binding to the calnexin P-domain,259405,7162,1
1,Solution structure of Urm1 and its implications for the evolution of protein modifiers,Structure analysis,The data from the entries that make up this study were used to determine the structure of Urm1.,259421,7165,1
1,Study of CNPase family proteins,Structure analysis,,259449,7167,1
1,The structure and function of a novel two-site calcium-binding fragment of calmodulin,Structure analysis,The data from the entries that make up this study were used to determine the structure of a novel fragment of calmodulin including residues 46-113.,259819,7190,1
,"Solution structure of hypothetical protein PA1123 from Pseudomonas aeruginosa
(Northeast Structural Genomics Consortium Target PaT4; Ontario Centre for
Structural Proteomics Target PA1123)",Structure analysis,"The data from this entry is used in the calculation of  Solution structure of a
hypothetical protein PA1123, from Pseudomonas aeruginosa; Northeast Structural
Genomics Consortium Target PaT4; Ontario Centre for Structural Proteomics
Target PA1123.",259872,7193,1
1,Structural analysis of dSUMO,Structure analysis,"The data from the entries that make up this study will be used to determine the
structure of SUMO protein from drosophila",259976,7202,1
1,Determination of solution structure of Homeodomain-only protein (HOP),Structure analysis,,259996,7203,1
1,Resonance assignment of PilP pilot protein,NMR assignment,"1H, 13C and 15N - resonance assignments for PilP fragment, residues 69-181.",260156,7209,1
1,Expression in Pichia pastoris and Backbone Dynamics of Dendroaspin and Erabutoxin b: Motion Variability within Three-fingered Toxins,Structure analysis,The data from the entries that make up this study were used to determine backbone dynamics of recombinant Erabutoxin b.,260213,7211,1
1,Investigation of J1 in aqueous solution,Structure analysis,,260235,7212,1
1,Investigation of J1cc in aqueous solution,Structure analysis,,260257,7213,1
1,Investigation of J3 in aqueous solution,Structure analysis,,260279,7214,1
1,Investigation of J7 in aqueous solution,Structure analysis,,260301,7215,1
1,pH titration of Link_TSG6,pH titration,chemical shifts of amide H and N-H nuclei in Link_TSG6 at a range of pH values,260429,7221,1
2,pH titration of HA8-bound Link_TSG6,pH titration,chemical shifts of amide H and N-H nuclei in Link_TSG6 in compelx with HA8 at a range of pH values,260429,7221,1
1,pH titration of Link_TSG6,pH titration,chemical shifts of amide H and N-H nuclei in Link_TSG6 at a range of pH values,260478,7222,1
2,pH titration of HA8-bound Link_TSG6,pH titration,chemical shifts of amide H and N-H nuclei in Link_TSG6 in compelx with HA8 at a range of pH values,260478,7222,1
1,Investigation of beta phosphoglucomutase in the open state,Structure analysis,The data from the entry was used to determine the backbone assignment of beta phosphoglucomutase,260797,7234,1
2,Investigation of beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and MgF3-,Structure analysis,"The data from the entry was used to determine the backbone assignment and
19F-1H NOEs for a structural study of the beta phosphoglucomutase
glucose-6-phosphate MgF3- ternary complex",260826,7235,1
1,NMR Investigation of Tyr105 Mutants in TEM-1 beta-lactamase,Mutant comparison,"Backbone 1H, 15N and 13C' assignments of mutants Y105W, Y105G, Y105N and Y105D of TEM-1 beta-lactamase",260850,7236,1
1,NMR Investigation of Tyr105 Mutants in TEM-1 beta-lactamase,Mutant comparison,"Backbone 1H, 15N and 13C' assignments of mutants Y105W, Y105G, Y105N and Y105D of TEM-1 beta-lactamase",260870,7237,1
1,NMR Investigation of Tyr105 Mutants in TEM-1 beta-lactamase,Mutant comparison,"Backbone 1H, 15N and 13C' assignments of mutants Y105W, Y105G, Y105N and Y105D of TEM-1 beta-lactamase",260890,7238,1
1,NMR Investigation of Tyr105 Mutants in TEM-1 beta-lactamase,Mutant comparison,"Backbone 1H, 15N and 13C' assignments of mutants Y105W, Y105G, Y105N and Y105D of TEM-1 beta-lactamase",260910,7239,1
1,Protein-peptide complex structure determination,Structure analysis,Protein-peptide complex structure determination using NMR,260959,7241,1
1,Human Uroporphyrinogen III synthase: High Affinity Purification,NMR Resonance Assignments and Localization of the Active Site,NMR Resonance-Perturcation Studies Do Not Spupport a Cylosolic Heme Enzyme Complex,260975,7242,1
1,Structure-function study of TM VII of NHE1 isoform of Na+/H+ exchanger.,Structure analysis,"The entires making up this deposition were used to determine the structure of
the 7th transmembrane segment of the mammalian Na+/H+ exchanger, isoform 1 in
DPC micelles.",261037,7245,1
1,,Structure analysis,,261079,7247,1
1,Investigation of p53 tetramerization domain,Mutant comparison,"The data from the entries that make up this study were used to compare the
structure of p53 tetramerization domain mutants.",261174,7251,1
1,Investigation of p53 tetramerization domain,Mutant comparison,"The data from the entries that make up this study were used to compare the
structure of p53 tetramerization domain mutants.",261192,7252,1
1,Investigation of p53 tetramerization domain,Mutant comparison,"The data from the entries that make up this study were used to compare the
structure of p53 tetramerization domain mutants.",261210,7253,1
1,Investigation of p53 tetramerization domain,Mutant comparison,"The data from the entries that make up this study were used to compare the
structure of p53 tetramerization domain mutants.",261228,7254,1
1,Investigation of p53 tetramerization domain,Mutant comparison,"The data from the entries that make up this study were used to compare the
structure of p53 tetramerization domain mutants.",261246,7255,1
1,NN-BP-6,Structure analysis,NMR structure of the N-terminal subdomain of IGFBP-6(1-45IGFBP-6),261417,7262,1
1,"Catalytic domain of the beta-1,4-glycosidase Cex from Cellulomonas fimi",Interactions with different ligands,The catalytic domain of Cex was compared in its apo- and 2-fluorocellobiosyl-enzyme intermediate states,261457,7264,1
,,Structure analysis,,261518,7269,1
,,Structure analysis,,261532,7270,1
007,"Investigation of Group 5 allergen, Blo t 5 from Blomia tropicalis.",Structure analysis,The data from the entries that make up this study were used to determine the structure of Blo t 5,261654,7276,1
1,Chemical shift assignment of GB1 domain of protein G,Structure analysis,"The data from this study were used to determine the change in structure of
protein G with pressure based on chemical shift changes.",261745,7280,1
1,"NMR STRUCTURE OF PROTEIN YJBR FROM ESCHERICHIA COLI;NORTHEAST STRUCTURAL
GENOMICS CONSORTIUM TARGET ER226",Structure analysis,"The data from the entries that make up this study were used to determine the NMR
structure of protein yjbR",261759,7281,1
1,Structure of a double dockerin domain,Structure analysis,,261825,7285,1
1,"NMR Assignment of CG7054, a PEBP from drosophila melanogaster",Structure analysis,"The data from the entries that make up this study were used to determine the
structure of CG7054",261851,7286,1
1,Structure and function of BRD7 bromodomain,Structure analysis,The data from the chemical shifts were used to determine the structure of BRD7 bromodomain.,261880,7287,1
1,Dimer of transmembrane domain of pro-apoptotic protein BNIP3,Structure analysis,This data were used to determine the structure of TM BNIP3 dimer,261907,7288,1
1,ALP folding by asp,Structure analysis,Investigation of folding of internal part of ALP. Structure induced by aspartic acid.,261989,7292,1
1,NMR study of the bacillomycin Lc in DMSO,Structure analysis,The data from the entries that make up this study were used to determine the structure of the bacillomycin Lc,262031,7294,1
1,NMR study of a synthetic analogue of bacillomycine Lc,Structure analysis,"The data from the entries that make up this study were used to determine the
structure of the synthetic analogue SCP [cyclo
(Asp1-Tyr2-Asn3-Ser4-Gln5-Ser6-Thr7-betaAla8)] of the bacillomycin Lc",262057,7295,1
,Ubp-M Znf-UBP domain,Structure analysis,This study determines the structure of Znf-UBP domain of Ubp-M/USP16.,262129,7298,1
1,solution structure of mouse Cripto CFC domain,Structure analysis,An extensive conformational study by NMR of the chemically synthesized CFC domain (96-134 residues) of mouse Cripto,262154,7299,1
1,Determination of the solution structure of the COMMD1 N-terminal domain,Structure analysis,The chemical shifts deposited here where part of the structure determination of the COMMD1 N-terminal domain,262172,7300,1
1,Structural characteristation of the folding intermediate of the colicin inhibitor protein Im7.,structural and dynamic analysis,The data from the entries that make up this study were used to characterise the conformational properties of the trapped on-pathway folding intermediate of bacterial immunity protein Im7.,262484,7316,1
1,Structural characteristation of the folding intermediate of the colicin inhibitor protein Im7.,structural and dynamic analysis,The data from the entries that make up this study were used to characterise the conformational properties of the trapped on-pathway folding intermediate of bacterial immunity protein Im7.,262502,7317,1
1,Structural characteristation of the folding intermediate of the colicin inhibitor protein Im7.,structural and dynamic analysis,The data from the entries that make up this study were used to characterise the conformational properties of the trapped on-pathway folding intermediate of bacterial immunity protein Im7.,262520,7318,1
1,PufX structure,Structure analysis,The solution structure of the PufX polypeptide from Rhodobacter sphaeroides,262558,7320,1
1,NMR analysis of LDLa module from the GPCR RXFP1,Structure analysis,The data from the entries were used to assign the resonances and determine the structure of the LDLa module of RXFP1,262573,7321,1
1,"Structural Analysis of the  NUDIX domain of budding yeast Dcp2 , residues 100-245",Structure analysis,"The data from this study were used to determine the structure of the NUDIX
domain of yeast Dcp2 residues 100-245 as a C-terminal fusion to the B1 domain
of protein G",262650,7325,1
1,Resonance Assignment,Structure analysis,Assignment of backbone spins and extracting secondary structure information using Chemical Shift Indexing (CSI),262896,7358,1
1,Actin-binding domain of troponin TnI-TnC-TnT2 ternary complex,Structure analysis,,264962,9500,1