Start2Fold

The database of hydrogen/deuterium exchange data on protein folding and stability

Entry STF0034

Borrelia burgdorferi outer surface protein A (OspA)

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Protein information

Name of the protein: Outer surface protein A
Organism: Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Number of residues: 257
Related UniProt entry:   P0CL66 (Fragment: 18 - 273)
Related PDB entry:   1OSP

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Experiment sets

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STRONG

Method: Native exchange NMR

Conditions: pH 6.0; 37.0 Celsius; Probes: 150

Related publication:
 PMID 12381326

Experiment details: "15N- and 13C, 15N-labeled OspA was prepared as described. HX was initiated by rapid buffer exchange of 15N-labeled, 1 mM OspA using a Sephadex G25 (Pharmcia) spin column to D2O buffer containing 10 mM sodium phosphate and 0 – 0.6 M Gu2HCl. This buffer contained NaCl, so that the sum of [Gu2HCl] and [NaCl] was kept at 0.65 M. Immediately following buffer exchange, a series of 1H, 15N-HSQC spectra were recorded at 37 °C on a Varian 600 spectrometer. The pH (uncorrected) of each sample was determined after NMR measurements."

Protection threshold: ΔG(HX0) > 10; m-value > 10

Sequence: KQNVSSLDEKNSVSVDLPGEMKVLVSKEKNKDGKYDLIATVDKLELKGTSDKNNGSGVLEGVKADKSKVKLTISDDLGQTTLEVFKEDGKTLVSKKVTSKDKSSTEEKFNEKGEVSEKIITRADGTRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISKSGEVSVELNDTDSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTKENTITVQQYDSNGTKLEGSAVEITKLDEIKNALK
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STRONG residues

1: K; 2: Q; 3: N; 4: V; 5: S; 6: S; 7: L; 8: D; 9: E; 10: K; 11: N; 12: S; 13: V; 14: S; 15: V; 16: D; 17: L; 18: P; 19: G; 20: E; 21: M; 22: K; 23: V; 24: L; 25: V; 26: S; 27: K; 28: E; 29: K; 30: N; 31: K; 32: D; 33: G; 34: K; 35: Y; 36: D; 37: L; 38: I; 39: A; 40: T; 41: V; 42: D; 43: K; 44: L; 45: E; 46: L; 47: K; 48: G; 49: T; 50: S; 51: D; 52: K; 53: N; 54: N; 55: G; 56: S; 57: G; 58: V; 59: L; 60: E; 61: G; 62: V; 63: K; 64: A; 65: D; 66: K; 67: S; 68: K; 69: V; 70: K; 71: L; 72: T; 73: I; 74: S; 75: D; 76: D; 77: L; 78: G; 79: Q; 80: T; 81: T; 82: L; 83: E; 84: V; 85: F; 86: K; 87: E; 88: D; 89: G; 90: K; 91: T; 92: L; 93: V; 94: S; 95: K; 96: K; 97: V; 98: T; 99: S; 100: K; 101: D;
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MEDIUM

Method: Native exchange NMR

Conditions: pH 6.0; 37.0 Celsius; Probes: 150

Related publication:
 PMID 12381326

Experiment details: "15N- and 13C, 15N-labeled OspA was prepared as described. HX was initiated by rapid buffer exchange of 15N-labeled, 1 mM OspA using a Sephadex G25 (Pharmcia) spin column to D2O buffer containing 10 mM sodium phosphate and 0 – 0.6 M Gu2HCl. This buffer contained NaCl, so that the sum of [Gu2HCl] and [NaCl] was kept at 0.65 M. Immediately following buffer exchange, a series of 1H, 15N-HSQC spectra were recorded at 37 °C on a Varian 600 spectrometer. The pH (uncorrected) of each sample was determined after NMR measurements."

Protection threshold: 7 < ΔG(HX0) < 10; m-value > 7

Sequence: KQNVSSLDEKNSVSVDLPGEMKVLVSKEKNKDGKYDLIATVDKLELKGTSDKNNGSGVLEGVKADKSKVKLTISDDLGQTTLEVFKEDGKTLVSKKVTSKDKSSTEEKFNEKGEVSEKIITRADGTRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISKSGEVSVELNDTDSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTKENTITVQQYDSNGTKLEGSAVEITKLDEIKNALK
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MEDIUM residues

102: K; 103: S; 104: S; 105: T; 106: E; 107: E; 108: K; 109: F; 110: N; 111: E; 112: K; 113: G; 114: E; 115: V; 116: S; 117: E; 118: K; 119: I; 120: I; 121: T; 122: R; 123: A; 124: D; 125: G; 126: T; 127: R; 128: L; 129: E; 130: Y; 131: T; 132: G; 133: I; 134: K; 135: S;
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WEAK

Method: Native exchange NMR

Conditions: pH 6.0; 37.0 Celsius; Probes: 150

Related publication:
 PMID 12381326

Experiment details: "15N- and 13C, 15N-labeled OspA was prepared as described. HX was initiated by rapid buffer exchange of 15N-labeled, 1 mM OspA using a Sephadex G25 (Pharmcia) spin column to D2O buffer containing 10 mM sodium phosphate and 0 – 0.6 M Gu2HCl. This buffer contained NaCl, so that the sum of [Gu2HCl] and [NaCl] was kept at 0.65 M. Immediately following buffer exchange, a series of 1H, 15N-HSQC spectra were recorded at 37 °C on a Varian 600 spectrometer. The pH (uncorrected) of each sample was determined after NMR measurements."

Protection threshold: 5 < ΔG(HX0) < 8; 5 < m-value < 6

Sequence: KQNVSSLDEKNSVSVDLPGEMKVLVSKEKNKDGKYDLIATVDKLELKGTSDKNNGSGVLEGVKADKSKVKLTISDDLGQTTLEVFKEDGKTLVSKKVTSKDKSSTEEKFNEKGEVSEKIITRADGTRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISKSGEVSVELNDTDSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTKENTITVQQYDSNGTKLEGSAVEITKLDEIKNALK
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WEAK residues

157: E; 158: K; 159: T; 160: T; 161: L; 162: V; 163: V; 164: K; 165: E; 166: G; 167: T; 168: V; 169: T; 170: L; 171: S; 172: K; 173: N; 174: I; 175: S; 176: K; 177: S; 178: G; 179: E; 180: V; 181: S; 182: V; 183: E; 184: L; 185: N; 186: D; 187: T; 188: D; 189: S; 190: S; 191: A; 192: A; 193: T; 194: K; 195: K; 196: T; 197: A; 198: A; 199: W; 200: N; 201: S; 202: G; 203: T; 204: S; 205: T; 206: L; 207: T; 208: I; 209: T; 210: V; 211: N; 212: S; 213: K; 214: K; 215: T; 216: K; 217: D; 218: L; 219: V; 220: F; 221: T; 222: K; 223: E; 224: N; 225: T; 226: I; 227: T; 228: V; 229: Q; 230: Q; 231: Y; 232: D; 233: S; 234: N; 235: G; 236: T; 237: K; 238: L; 239: E; 240: G; 241: S; 242: A; 243: V; 244: E; 245: I; 246: T; 247: K; 248: L; 249: D; 250: E; 251: I; 252: K; 253: N; 254: A; 255: L; 256: K;
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