Study_ID,Keyword,Sf_ID,Entry_ID,Study_list_ID
1,beta-lactoglobulin,171,10010,1
1,actin,212,10012,1
1,tropomyosin,212,10012,1
1,troponin,212,10012,1
1,Fo subunit c,407,10021,1
1,MAS solid-state NMR,407,10021,1
1,folding,1052,10052,1
1,H/D exchange,1052,10052,1
1,Hyperthermophile,1052,10052,1
1,intermediate,1052,10052,1
1,PCP,1052,10052,1
1,Pyrococcus furiosus,1052,10052,1
1,pyrrolidone carboxyl peptidase,1052,10052,1
1,protein-protein interaction,1590,10078,1
1,protein-protein interaction,1967,10096,1
1,Chemical Shift Assignment,136265,25859,1
1,NMR,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
,NMR assignments,248031,6516,1
,PfACP,248031,6516,1
,phosphopantetheine moiety,248031,6516,1
,triple resonance experiments,248031,6516,1
1,p53tet,248108,6521,1
1,p53 tetramerization domain,248108,6521,1
1,Tumor suppressor protein p53 - human,248108,6521,1
1,Tetramerization domain of p53 (residues 310 - 360),248108,6521,1
1,Nuclear Magnetic Resonance,248108,6521,1
1,Hydrogen exchange studies,248108,6521,1
1,Amyloid fibrils,248108,6521,1
1,Intermediate,248108,6521,1
1,p53tet-wt,248108,6521,1
1,Amyloid fibril intermediate,248127,6522,1
1,Hydrogen exchange studies,248127,6522,1
1,Mutant p53 tetramerization domain,248127,6522,1
1,Mutant tetramerization domain of p53 (residues 310 - 360),248127,6522,1
1,Nuclear Magnetic Resonance,248127,6522,1
1,R337H,248127,6522,1
1,Tumor suppressor protein p53 - human,248127,6522,1
1,p53tet-R337H,248127,6522,1
,"13C,15N labelled protein",248180,6526,1
,NMR structure,248180,6526,1
,km23 dimer nmr structure,248193,6527,1
1,NMR derived structural model,248347,6535,1
,NMR Structure,248379,6537,1
,NMR structure,248877,6563,1
1,function,249131,6577,1
1,structure,249131,6577,1
,"cpSRP43, chromo 2 domain",249457,6592,1
,"Chromo 3 domain, cpSRP43, structure",249471,6593,1
1,NMR structure,249738,6606,1
,AAA+ superfamily,249886,6615,1
,solution structure,249886,6615,1
,SSD domain,249886,6615,1
,lytic peptides,249900,6616,1
,NMR study,249900,6616,1
,lytic peptides,249934,6618,1
,NMR study,249934,6618,1
,lytic peptides,249952,6619,1
,NMR study,249952,6619,1
,NMR structure,249983,6620,1
,p22HBP,249983,6620,1
1,IL-2,250015,6621,1
1,resonance assignments,250015,6621,1
1,PcFK1,250265,6636,1
,DHFR,250435,6645,1
,Haloferax volcanii,250435,6645,1
,halophilic enzyme,250435,6645,1
,NMR chemical shift,250435,6645,1
,two-finger,250489,6648,1
,zinc finger,250489,6648,1
,peptide-membrane interaction,250557,6650,1
,sticholysin,250557,6650,1
1,peptide-membrane interaction,250581,6651,1
1,sticholysin,250581,6651,1
,zinc finger,250624,6653,1
,one finger,250624,6653,1
,rubredoxin,250776,6659,1
,iron-sulfur protein,250776,6659,1
,reduction potential,250776,6659,1
,H-bond,250776,6659,1
,15N hyperfine shifts,250776,6659,1
,15N hyperfine shifts,250805,6660,1
,H-bond,250805,6660,1
,iron-sulfur protein,250805,6660,1
,reduction potential,250805,6660,1
,rubredoxin,250805,6660,1
,15N hyperfine shifts,250821,6661,1
,H-bond,250821,6661,1
,iron-sulfur protein,250821,6661,1
,reduction potential,250821,6661,1
,rubredoxin,250821,6661,1
,15N hyperfine shifts,250837,6662,1
,H-bond,250837,6662,1
,iron-sulfur protein,250837,6662,1
,reduction potential,250837,6662,1
,rubredoxin,250837,6662,1
,15N hyperfine shifts,250853,6663,1
,H-bond,250853,6663,1
,iron-sulfur protein,250853,6663,1
,reduction potential,250853,6663,1
,rubredoxin,250853,6663,1
,15N hyperfine shifts,250869,6664,1
,H-bond,250869,6664,1
,iron-sulfur protein,250869,6664,1
,reduction potential,250869,6664,1
,rubredoxin,250869,6664,1
,15N hyperfine shifts,250885,6665,1
,H-bond,250885,6665,1
,iron-sulfur protein,250885,6665,1
,reduction potential,250885,6665,1
,rubredoxin,250885,6665,1
,15N hyperfine shifts,250901,6666,1
,H-bond,250901,6666,1
,iron-sulfur protein,250901,6666,1
,reduction potential,250901,6666,1
,rubredoxin,250901,6666,1
,15N hyperfine shifts,250917,6667,1
,H-bond,250917,6667,1
,iron-sulfur protein,250917,6667,1
,reduction potential,250917,6667,1
,rubredoxin,250917,6667,1
,15N hyperfine shifts,250933,6668,1
,H-bond,250933,6668,1
,iron-sulfur protein,250933,6668,1
,reduction potential,250933,6668,1
,rubredoxin,250933,6668,1
,15N hyperfine shifts,250949,6669,1
,H-bond,250949,6669,1
,iron-sulfur protein,250949,6669,1
,reduction potential,250949,6669,1
,rubredoxin,250949,6669,1
,15N hyperfine shifts,250981,6670,1
,H-bond,250981,6670,1
,iron-sulfur protein,250981,6670,1
,reduction potential,250981,6670,1
,rubredoxin,250981,6670,1
,15N hyperfine shifts,250997,6671,1
,H-bond,250997,6671,1
,iron-sulfur protein,250997,6671,1
,reduction potential,250997,6671,1
,rubredoxin,250997,6671,1
,15N hyperfine shifts,251013,6672,1
,H-bond,251013,6672,1
,iron-sulfur protein,251013,6672,1
,reduction potential,251013,6672,1
,rubredoxin,251013,6672,1
,15N hyperfine shifts,251029,6673,1
,H-bond,251029,6673,1
,iron-sulfur protein,251029,6673,1
,reduction potential,251029,6673,1
,rubredoxin,251029,6673,1
,15N hyperfine shifts,251045,6674,1
,H-bond,251045,6674,1
,iron-sulfur protein,251045,6674,1
,reduction potential,251045,6674,1
,rubredoxin,251045,6674,1
,15N hyperfine shifts,251061,6675,1
,H-bond,251061,6675,1
,iron-sulfur protein,251061,6675,1
,reduction potential,251061,6675,1
,rubredoxin,251061,6675,1
,15N hyperfine shifts,251077,6676,1
,H-bond,251077,6676,1
,iron-sulfur protein,251077,6676,1
,reduction potential,251077,6676,1
,rubredoxin,251077,6676,1
,15N hyperfine shifts,251093,6677,1
,H-bond,251093,6677,1
,iron-sulfur protein,251093,6677,1
,reduction potential,251093,6677,1
,rubredoxin,251093,6677,1
1,15N hyperfine shifts,251109,6678,1
2,H-bond,251109,6678,1
3,iron-sulfur protein,251109,6678,1
4,reduction potential,251109,6678,1
5,rubredoxin,251109,6678,1
1,NMR,251125,6679,1
1,IgG-binding,251125,6679,1
1,protein G,251125,6679,1
1,phage display,251125,6679,1
,IgG binding,251154,6680,1
,NMR,251154,6680,1
,phage display,251154,6680,1
,protein A,251154,6680,1
,NMR structure,251350,6690,1
,NMR structure,251383,6691,1
,backbone and sidechain shifts,251413,6692,1
,NMR structure,251413,6692,1
1,NMR assigment,251512,6696,1
1,NMR chemical shift assignment,251554,6699,1
,dTAF1,251576,6700,1
,NMR structure,251576,6700,1
1,NMR resonance assignment,251676,6711,1
1,Ubiquitin-conjugating enzyme,251676,6711,1
1,NMR assignments,251988,6725,1
1,dengue,251988,6725,1
,CalC,252003,6726,1
,calicheamicin,252003,6726,1
,NMR,252003,6726,1
,resistance,252003,6726,1
,Self-sacrifice,252003,6726,1
,AtTRD1d,252019,6727,1
,telomere,252019,6727,1
,TRP,252019,6727,1
,NMR assignments,252318,6744,1
,alternative splicing,252334,6745,1
,NMR assigments,252334,6745,1
,NMR structure,252461,6752,1
,NMR structure,252502,6755,1
,TA0743,252502,6755,1
1,magnesium,252515,6756,1
1,metal ion binding,252515,6756,1
,in-plane membrane anchor domain,252534,6757,1
,liquid NMR,252534,6757,1
,micellar SDS,252534,6757,1
,water:TFE mixture,252534,6757,1
1,NMR structure,252593,6759,1
,NMR structure of pa0128,252707,6766,1
,Two domain protein,252707,6766,1
,Zn binding protein,252707,6766,1
,NMR structure of NE2066,252738,6769,1
,NMR structure,252808,6774,1
,NMR structure,252821,6775,1
,Assignments of the KID domain of CREB free in solution,253007,6784,1
,catalytic antibody,253032,6785,1
,Fv fragment,253032,6785,1
1,C2A rabphilin,253087,6787,1
,Assignments of the pSer133-KID domain of CREB free in solution,253103,6788,1
1,2D NMR,253186,6791,1
2,Allatostatin,253186,6791,1
3,AST,253186,6791,1
,interaction,253885,6828,1
,Chemical shift,253900,6829,1
,NMR structure,253900,6829,1
1,addiction module,253986,6833,1
1,MazE,253986,6833,1
1,MazF,253986,6833,1
1,mRNA interferase,253986,6833,1
1,NMR,253986,6833,1
,NMR structure,254057,6836,1
1,antibiotic resistance,254102,6838,1
1,class A beta-lactamase,254102,6838,1
1,liquid-state NMR,254102,6838,1
1,PSE-4,254102,6838,1
1,Pseudomonas aeruginosa,254102,6838,1
,NMR structure,254173,6840,1
1,amphipatic helix,254446,6857,1
2,immunodominant epitope,254446,6857,1
3,multiple sclerosis,254446,6857,1
,lytic peptides,254490,6859,1
,NMR study,254490,6859,1
,egg case silk,254586,6864,1
,NMR assignment,254586,6864,1
,NMR structure,254600,6865,1
,two-finger,255363,6905,1
,zinc finger,255363,6905,1
,NMR,255422,6909,1
,structures,255422,6909,1
,Archaea,255550,6917,1
,Backbone assignments,255550,6917,1
,RNase P,255550,6917,1
,NMR,255578,6919,1
,structure,255578,6919,1
,IA current,255652,6924,1
,potassium channel blocker,255652,6924,1
,scorpion toxin,255652,6924,1
,Kid toxin,255669,6925,1
,NMR assignment,255669,6925,1
,Neurabin,255772,6933,1
,PDZ,255772,6933,1
,NMR assignment,255839,6938,1
,alanine-based peptides,255885,6941,1
,chemical shift,255885,6941,1
,NMR structure,255929,6944,1
,NMR structure,256224,6964,1
,COCON,256295,6968,1
,GTPase,256323,6970,1
,NMR assignment,256323,6970,1
,MoaD,256477,6982,1
,molybdopterin,256477,6982,1
1,"protein structure, protein-ligand interactions",256548,6986,1
,NMR structure,256582,6988,1
,NMR structure,256596,6989,1
,Ribosomal protein,256596,6989,1
,NMR structure,256626,6990,1
,phytotoxin,256626,6990,1
1,Phosphorylation,256642,6991,1
1,Tissue Factor Cytoplasmic Domain,256642,6991,1
1,bacterial cell wall,256658,6992,1
1,peptidoglycan,256658,6992,1
1,NMR,256679,6993,1
1,Phosphorylation,256679,6993,1
1,Tissue Factor,256679,6993,1
1,NMR,256715,6996,1
1,Phosphorylation,256715,6996,1
1,Tissue Factor,256715,6996,1
1,NMR,256750,6998,1
1,Phosphorylation,256750,6998,1
1,Tissue Factor,256750,6998,1
,Antibody,256821,7001,1
,b-Catenin,256821,7001,1
,NMR,256821,7001,1
,peptide,256821,7001,1
,STD,256821,7001,1
,structure,256821,7001,1
,TRNOE,256821,7001,1
,NMR structure,256838,7002,1
,UBA,256838,7002,1
,ubiquitin binding domain,256838,7002,1
,hRPB8,257168,7020,1
1,NMR structure,257415,7034,1
,NMR structure,257553,7054,1
,structural genomics,257553,7054,1
,calponin homology domain,257638,7058,1
,MICAL,257638,7058,1
,NMR structure,257638,7058,1
,NMR assignment,257670,7059,1
,Pyrazinamidase,257670,7059,1
,Pyrazinamide,257670,7059,1
,PZA-resistance,257670,7059,1
,RRM,257920,7070,1
,U6 RNA,257920,7070,1
,Kis antitoxin,257937,7071,1
,NMR assignment,257937,7071,1
,GOPC,257959,7072,1
,NMR structure,257959,7072,1
,PDZ domain,257959,7072,1
,DNA-binding protein,258004,7074,1
,Metal-chelating protein,258004,7074,1
,NMR structure,258004,7074,1
,hypothetical protein RP2812,258070,7079,1
1,PutA45,258149,7082,1
,Chemical Shift Assignment,258298,7089,1
,NMR,258298,7089,1
,13C/15N-labeled RNA,258319,7090,1
,G.U wobble pair,258319,7090,1
,hairpin structure,258319,7090,1
,hexaloop,258319,7090,1
,RNA structure,258319,7090,1
,chemical shift assignment,258358,7093,1
,Acylphosphatase,258375,7094,1
,NMR structure,258375,7094,1
1,NMR structure,258538,7104,1
1,MAS,258650,7111,1
1,microcrystalline,258650,7111,1
1,solid state NMR,258650,7111,1
1,ubiquitin,258650,7111,1
,Crk SH3 domain,258975,7129,1
,NMR,258975,7129,1
,NMR structure,259004,7131,1
,autophosphorylation,259022,7132,1
,CheA,259022,7132,1
,P1,259022,7132,1
,phosphotransfer,259022,7132,1
,autophosphorylation,259035,7133,1
,CheA,259035,7133,1
,kinase,259035,7133,1
,P4,259035,7133,1
,RBP in 8M urea,259205,7149,1
1,NMR structure,259240,7151,1
,NMR,259343,7158,1
,nuclear pore,259343,7158,1
,nucleoporin,259343,7158,1
,nucleus,259343,7158,1
,NUP153,259343,7158,1
,NUP358,259343,7158,1
,pore,259343,7158,1
,RanBP2,259343,7158,1
,structure,259343,7158,1
,transport,259343,7158,1
,zinc finger,259343,7158,1
,evolution,259421,7165,1
,NMR structure,259421,7165,1
,Urm1,259421,7165,1
,tachystatin B1,259519,7171,1
,calcium,259819,7190,1
,calcium-binding,259819,7190,1
,calmodulin,259819,7190,1
1,NMR Structure in solution state,259976,7202,1
,homeodomain,259996,7203,1
,NMR structure,259996,7203,1
1,dynamics,260213,7211,1
1,erabutoxin b,260213,7211,1
1,neurotoxin,260213,7211,1
1,structure,260213,7211,1
1,three-fingered toxin,260213,7211,1
,mimotope,260235,7212,1
,mimotope,260257,7213,1
,mimotope,260279,7214,1
,mimotope,260301,7215,1
,chemical shift,260429,7221,1
,pH titration,260429,7221,1
,chemical shift,260478,7222,1
,pH titration,260478,7222,1
,active site,260797,7234,1
,MgF3- transition state analogue,260797,7234,1
,NOE directed docking of fluoride ions,260797,7234,1
,active site,260826,7235,1
,MgF3- transition state analogue,260826,7235,1
,NOE directed docking of fluoride ions,260826,7235,1
,Backbone assignment,260850,7236,1
,Class A beta-lactamase,260850,7236,1
,Mutant comparison,260850,7236,1
,TEM-1,260850,7236,1
,Tyr105,260850,7236,1
,Backbone assignment,260870,7237,1
,Class A beta-lactamase,260870,7237,1
,Mutant comparison,260870,7237,1
,TEM-1,260870,7237,1
,Tyr105,260870,7237,1
,Backbone assignment,260890,7238,1
,Class A beta-lactamase,260890,7238,1
,Mutant comparison,260890,7238,1
,TEM-1,260890,7238,1
,Tyr105,260890,7238,1
,Backbone assignment,260910,7239,1
,Class A beta-lactamase,260910,7239,1
,Mutant comparison,260910,7239,1
,TEM-1,260910,7239,1
,Tyr105,260910,7239,1
,cpSRP,260959,7241,1
,congenital,260975,7242,1
,erythropoietic,260975,7242,1
,heme biosynthesis,260975,7242,1
,porphyria,260975,7242,1
,NMR structure,261174,7251,1
,p53TD,261174,7251,1
,NMR structure,261192,7252,1
,p53TD,261192,7252,1
,NMR structure,261210,7253,1
,p53TD,261210,7253,1
,NMR structure,261228,7254,1
,p53TD,261228,7254,1
,NMR structure,261246,7255,1
,p53TD,261246,7255,1
,IGFBP-6,261417,7262,1
,Insulin like growth factors,261417,7262,1
,Glycosidase,261457,7264,1
,Glycosyl-enyzme intermediate,261457,7264,1
,Allergen,261654,7276,1
,Blomia tropicalis,261654,7276,1
,House dust mite,261654,7276,1
1,GB1,261745,7280,1
,GFT NMR,261759,7281,1
,NMR Structure,261759,7281,1
,cellulosome,261825,7285,1
,dockerin,261825,7285,1
,CG7054,261851,7286,1
,PEBP,261851,7286,1
,NMR structure,261880,7287,1
,apoptosis,261907,7288,1
,BNIP3,261907,7288,1
,dynamics,261907,7288,1
,structure,261907,7288,1
,antibiotic,262031,7294,1
,antifungal,262031,7294,1
,bacillomycin Lc,262031,7294,1
,NMR,262031,7294,1
,bacillomycin Lc,262057,7295,1
,NMR structure,262057,7295,1
,synthetic analogue,262057,7295,1
,Znf-UBP,262129,7298,1
,Integrin,262413,7313,1
,Pactolus I-domain,262413,7313,1
,Sequential backbone assignment,262413,7313,1
,conformational properties,262484,7316,1
,intermediate,262484,7316,1
,NMR,262484,7316,1
,protein folding,262484,7316,1
,SAXS,262484,7316,1
,conformational properties,262502,7317,1
,intermediate,262502,7317,1
,NMR,262502,7317,1
,protein folding,262502,7317,1
,SAXS,262502,7317,1
,conformational properties,262520,7318,1
,intermediate,262520,7318,1
,NMR,262520,7318,1
,protein folding,262520,7318,1
,SAXS,262520,7318,1
,NMR structure,262558,7320,1
1,NMR assignment,262573,7321,1
,colicin,262605,7323,1
,immunity protein,262605,7323,1
,NMR,262605,7323,1
,non cognate complexes,262605,7323,1
,resonance assignments,262605,7323,1
,NMR Structure,262650,7325,1
,Resonance Assignment,262896,7358,1
1,actin,264962,9500,1
1,tropomyosin,264962,9500,1
1,troponin,264962,9500,1