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BMRB: 15338

2JRP

NMR Structure of Protein YfgJ from Salmonella Typhimurium. Northeast Structural Genomics Target StR86.

Authors

Ding, K., Ramelot, T.A., Cort, J.R., Wang, H., Nwosu, C., Cunningham, K., Owens, L., Ma, L., Xiao, R., Liu, J., Baran, M.C., Swapna, G.V.T., Acton, T.B., Rost, B., Montelione, G.T., Kennedy, M.A.

Assembly

YfgJ monomer

Entity

1. protein (polymer, Thiol state: free and other bound), 81 monomers, 9144.318 Da Detail

MEITCPVCHH ALERNGDTAH CETCAKDFSL QALCPDCRQP LQVLKACGAV DYFCQNGHGL ISKKRVNFVI SDQLEHHHHH H

2. ZN (non-polymer), 65.409 × 2 Da

Total weight

9275.137 Da

Max. entity weight

9144.318 Da

Entity Connection

na 8 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	na	sing	1:CYS5:SG	2:ZN1:ZN
2	na	sing	1:CYS8:SG	2:ZN1:ZN
3	na	sing	1:CYS21:SG	2:ZN1:ZN
4	na	sing	1:CYS24:SG	2:ZN1:ZN
5	na	sing	1:CYS34:SG	2:ZN1:ZN
6	na	sing	1:CYS37:SG	2:ZN1:ZN
7	na	sing	1:CYS54:SG	2:ZN1:ZN
8	na	sing	1:HIS58:NE2	2:ZN1:ZN

Source organism

Salmonella enterica subsp. enterica serovar Typhimurium

Exptl. method

solution NMR

Refine. method

DGSA-distance geometry simulated annealing

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 91.6 %, Completeness (bb): 96.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.6 % (838 of 915)	91.5 % (433 of 473)	92.7 % (330 of 356)	87.2 % (75 of 86)
Backbone	96.7 % (464 of 480)	97.5 % (159 of 163)	96.7 % (231 of 239)	94.9 % (74 of 78)
Sidechain	88.1 % (451 of 512)	88.4 % (274 of 310)	90.7 % (176 of 194)	12.5 % (1 of 8)
Aromatic	59.0 % (46 of 78)	59.0 % (23 of 39)	59.0 % (23 of 39)
Methyl	100.0 % (78 of 78)	100.0 % (39 of 39)	100.0 % (39 of 39)

1. protein

MEITCPVCHH ALERNGDTAH CETCAKDFSL QALCPDCRQP LQVLKACGAV DYFCQNGHGL ISKKRVNFVI SDQLEHHHHH H

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

Sample #2

Solvent system 100% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
9	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
10	NH4OAc	natural abundance	20 (±1.0) mM
11	NaCl	natural abundance	100 (±5.0) mM
12	DTT	natural abundance	10 (±1.0) mM
13	CaCl2	natural abundance	5 (±1.0) mM
14	NaN3	natural abundance	0.02 (±0.001) %
15	D2O		100 %

Sample #3

Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
16	protein	[U-5% 13C; U-100% 15N]	1.7 (±0.2) mM
17	NH4OAc	natural abundance	20 (±1.0) mM
18	NaCl	natural abundance	100 (±5.0) mM
19	DTT	natural abundance	10 (±1.0) mM
20	CaCl2	natural abundance	5 (±1.0) mM
21	NaN3	natural abundance	0.02 (±0.001) %
22	H2O		95 %
23	D2O		5 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.03 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.03 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -0.04 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.52 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2JRP, Strand ID: A Detail

Release date

2007-08-01

Citation

NMR Structure of Protein YfgJ from Salmonella Typhimurium
Ding, K., Ramelot, T.A., Cort, J.R., Wang, H., Nwosu, C., Cunningham, K., Owens, L., Ma, L., Xiao, R., Liu, J., Baran, M.C., Swapna, G.V.T., Acton, T.B., Rost, B., Montelione, G.T., Kennedy, M.A.

Related entities 1. protein, : 1 : 7 entities Detail

Experiments performed 16 experiments Detail

1 2D 1H-15N HSQC

Instrument

Varian INOVA - 750 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

2 2D 1H-13C HSQC (aliph)

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

3 2D 1H-13C HSQC

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
16	protein	[U-5% 13C; U-100% 15N]	1.7 (±0.2) mM
17	NH4OAc	natural abundance	20 (±1.0) mM
18	NaCl	natural abundance	100 (±5.0) mM
19	DTT	natural abundance	10 (±1.0) mM
20	CaCl2	natural abundance	5 (±1.0) mM
21	NaN3	natural abundance	0.02 (±0.001) %
22	H2O		95 %
23	D2O		5 %

4 3D HNCO

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

5 3D CBCA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

6 3D HNCACB

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

7 3D HBHA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

8 3D HNHA

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

9 3D HCCH-TOCSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

10 3D C(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

11 3D 1H-15N NOESY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

12 3D 1H-13C NOESY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

13 3D 1H-13C NOESY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
9	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
10	NH4OAc	natural abundance	20 (±1.0) mM
11	NaCl	natural abundance	100 (±5.0) mM
12	DTT	natural abundance	10 (±1.0) mM
13	CaCl2	natural abundance	5 (±1.0) mM
14	NaN3	natural abundance	0.02 (±0.001) %
15	D2O		100 %

14 3D aromatic 1H-13C NOESY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
9	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
10	NH4OAc	natural abundance	20 (±1.0) mM
11	NaCl	natural abundance	100 (±5.0) mM
12	DTT	natural abundance	10 (±1.0) mM
13	CaCl2	natural abundance	5 (±1.0) mM
14	NaN3	natural abundance	0.02 (±0.001) %
15	D2O		100 %

15 4D 1H-13C NOESY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
9	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
10	NH4OAc	natural abundance	20 (±1.0) mM
11	NaCl	natural abundance	100 (±5.0) mM
12	DTT	natural abundance	10 (±1.0) mM
13	CaCl2	natural abundance	5 (±1.0) mM
14	NaN3	natural abundance	0.02 (±0.001) %
15	D2O		100 %

16 2D 1H-13C HSQC (arom)

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±1) atm, Temperature 293 (±1) K, pH 4.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	protein	[U-100% 13C; U-100% 15N]	1 (±0.2) mM
2	NH4OAc	natural abundance	20 (±1.0) mM
3	NaCl	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	10 (±1.0) mM
5	CaCl2	natural abundance	5 (±1.0) mM
6	NaN3	natural abundance	0.02 (±0.001) %
7	H2O		95 %
8	D2O		5 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_15338_2jrp.nef
Input source #2: Coordindates	2jrp.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	True (see coodinates for details)
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Error

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:22:GLU:OE1	2:1:ZN:ZN	unknown	unknown	n/a
1:22:GLU:OE2	2:1:ZN:ZN	unknown	unknown	n/a
1:23:THR:O	2:1:ZN:ZN	unknown	unknown	n/a
1:23:THR:OG1	2:1:ZN:ZN	unknown	unknown	n/a
1:58:HIS:ND1	2:2:ZN:ZN	unknown	unknown	n/a
1:59:GLY:O	2:2:ZN:ZN	unknown	unknown	n/a
1:8:CYS:SG	2:1:ZN:ZN	unknown	unknown	n/a
1:54:CYS:SG	2:2:ZN:ZN	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	1	ZN	ZINC ION	Distance restraints
B	2	ZN	ZINC ION	None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70--------80-
MEITCPVCHHALERNGDTAHCETCAKDFSLQALCPDCRQPLQVLKACGAVDYFCQNGHGLISKKRVNFVISDQLEHHHHHH
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MEITCPVCHHALERNGDTAHCETCAKDFSLQALCPDCRQPLQVLKACGAVDYFCQNGHGLISKKRVNFVISDQLEHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	81	0	0	100.0

Content subtype: combined_15338_2jrp.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	8		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	834		100.0 (chain: A, length: 81)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Error	26 (1)	undefined	14.8 (chain: A, length: 81), 50.0 (chain: B, length: 2)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	738 (1)	noe	87.7 (chain: A, length: 81)
3	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	22 (1)	hbond	17.3 (chain: A, length: 81)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 81, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 430
  - ¹³C chemical shifts: 330
  - ¹⁵N chemical shifts: 74
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	473	430	90.9
¹³C chemical shifts	356	330	92.7
¹⁵N chemical shifts	89	74	83.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	163	158	96.9
¹³C chemical shifts	162	154	95.1
¹⁵N chemical shifts	78	73	93.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	310	272	87.7
¹³C chemical shifts	194	176	90.7
¹⁵N chemical shifts	11	1	9.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	40	39	97.5
¹³C chemical shifts	40	39	97.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	23	59.0
¹³C chemical shifts	39	23	59.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Error
- Experiment type: undefined
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 81, Sequence coverage: 14.8%
  - Entity_assembly_ID: B, Chain length: 2, Sequence coverage: 50.0%
- Total number of restraints: 26
- Weight of restraints: 1.0 (26)
- Potential type of restraints: square-well-parabolic (26)
- Range of distance target values: 2.1, 11.99 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: OK
  - Experiment type: noe
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 81, Sequence coverage: 87.7%
  - Total number of restraints: 738
  - Weight of restraints: 1.0 (738)
  - Potential type of restraints: square-well-parabolic (738)
  - Range of distance target values: 2.4, 3.4 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
      None
  - Distance restraints on contact map
  - Saveframe: CNS/XPLOR_distance_constraints_3
    - Status: Warning
    - Experiment type: hbond
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 81, Sequence coverage: 17.3%
    - Total number of restraints: 22
    - Weight of restraints: 1.0 (22)
    - Potential type of restraints: square-well-parabolic (22)
    - Range of distance target values: 2.0, 3.0 (Å)
    - Histogram of distance target values
    - Distance restraints per residue
      - Chain_ID: A
      - Chain_ID: B
        None
    - Distance restraints on contact map

Keywords two-zinc binding protein

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Found 1 Document (0.697 seconds)

BMRB: 15338

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. protein, : 1 : 7 entities Detail

Experiments performed 16 experiments Detail

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NMR combined restraints 5 contents Detail