2K3A
NMR solution structure of Staphylococcus saprophyticus CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain protein. Northeast Structural Genomics Consortium target SyR11
Replaces: 2JRNSpectrometer
Experimental method: SOLUTION NMR
Spectrometer ID | Spectrometer maker | Spectrometer model | Spectrometer type | Spectrometer field strength |
1 | Bruker | AVANCE | Bruker Avance | 800 |
2 | Bruker | AVANCE | Bruker Avance | 600 |
Experiment
experiment id | conditions id | solution id | Experiment type |
1 | 1 | 1 | 2D 1H-15N HSQC |
10 | 1 | 1 | 3D HCCH-COSY |
11 | 1 | 1 | 3D CCH-TOCSY |
12 | 1 | 1 | 3D HN(COCA)CB |
13 | 1 | 1 | 3D HNCACO |
14 | 1 | 2 | 2D 1H-13C HSQC |
15 | 1 | 2 | T1/T2 relaxation |
16 | 1 | 2 | N15 Het-NOE |
2 | 1 | 1 | 2D 1H-13C HSQC |
3 | 1 | 1 | 3D 1H-15N NOESY |
4 | 1 | 1 | 3D 1H-13C NOESY |
5 | 1 | 1 | 3D HNCACB |
6 | 1 | 1 | 3D HNCA |
7 | 1 | 1 | 3D HNCO |
8 | 1 | 1 | 3D HBHA(CO)NH |
9 | 1 | 1 | 3D HCCH-TOCSY |
NMR Sample
conditions id | NMR sample pH | NMR sample pressure | NMR sample temperature |
1 | 6.5 | ambient | 298 |
Conformers
Conformers Calculated Total Number | 100 |
Conformers Submitted Total Number | 20 |