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Found 1 Document (3.348 seconds)

BMRB: 19368

4BXU

Structure of Pex14 in complex with Pex5 LVxEF motif

Authors

Kooshapur, H., Meyer, H., Madl, T., Sattler, M.

Assembly

Structure of Pex14 in complex with Pex5 LVxEF motif

Entity

1. PEROXISOMAL MEMBRANE PROTEIN PEX14 (polymer, Thiol state: not present), 69 monomers, 7444.372 Da Detail

GAMATPGSEN VLPREPLIAT AVKFLQNSRV RQSPLATRRA FLKKKGLTDE EIDMAFQQSG TAADEPSSL

2. PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR (polymer, Thiol state: not present), 15 monomers, 1707.745 Da Detail

ASEDELVAEF LQDQN

Total weight

9152.117 Da

Max. entity weight

7444.372 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 100.0 %, Completeness: 73.7 %, Completeness (bb): 73.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	73.7 % (697 of 946)	83.2 % (411 of 494)	61.0 % (222 of 364)	72.7 % (64 of 88)
Backbone	73.7 % (364 of 494)	96.4 % (161 of 167)	56.5 % (140 of 248)	79.7 % (63 of 79)
Sidechain	73.9 % (393 of 532)	76.1 % (249 of 327)	73.5 % (144 of 196)	0.0 % (0 of 9)
Aromatic	0.0 % (0 of 40)	0.0 % (0 of 20)	0.0 % (0 of 20)
Methyl	83.7 % (77 of 92)	87.0 % (40 of 46)	80.4 % (37 of 46)

1. PEROXISOMAL MEMBRANE PROTEIN PEX14

GAMATPGSEN VLPREPLIAT AVKFLQNSRV RQSPLATRRA FLKKKGLTDE EIDMAFQQSG TAADEPSSL

2. PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR

ASEDELVAEF LQDQN

Show sample condition

Sample

Pressure 1 atm, Temperature 298.000 K, pH 6.500

#	Name	Isotope labeling	Type	Concentration
1	PEROXISOMAL MEMBRANE PROTEIN PEX14	[U-13C; U-15N]		0.0 ~ 0.0 mM
2	PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR	[U-13C; U-15N]		0.0 ~ 0.0 mM

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 68.0 %, Completeness (bb): 71.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	68.0 % (1287 of 1892)	72.8 % (719 of 988)	60.3 % (439 of 728)	73.3 % (129 of 176)
Backbone	71.5 % (706 of 988)	88.3 % (295 of 334)	57.3 % (284 of 496)	80.4 % (127 of 158)
Sidechain	66.4 % (706 of 1064)	64.7 % (423 of 654)	71.9 % (282 of 392)	5.6 % (1 of 18)
Aromatic	0.0 % (0 of 80)	0.0 % (0 of 40)	0.0 % (0 of 40)
Methyl	76.1 % (140 of 184)	78.3 % (72 of 92)	73.9 % (68 of 92)

1. PEROXISOMAL MEMBRANE PROTEIN PEX14

GAMATPGSEN VLPREPLIAT AVKFLQNSRV RQSPLATRRA FLKKKGLTDE EIDMAFQQSG TAADEPSSL

2. PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR

ASEDELVAEF LQDQN

Show sample condition

Sample

Pressure 1 atm, Temperature 298.000 K, pH 6.500

#	Name	Isotope labeling	Type	Concentration
1	PEROXISOMAL MEMBRANE PROTEIN PEX14	[U-13C; U-15N]		0.0 ~ 0.0 mM
2	PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR	[U-13C; U-15N]		0.0 ~ 0.0 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 4BXU, Strand ID: A, B Detail

Release date

2013-11-25

Citation

A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes
Neuhaus, A., Kooshapur, H., Wolf, J., Meyer, N., Madl, T., Saidowsky, J., Hambruch, E., Lazam, A., Jung, M., Sattler, M., Schliebs, W., Erdmann, R.
J. Biol. Chem. (2014), 289, 437-448, PubMed 24235149 , DOI 10.1074/jbc.M113.499707 , Abstract

Related entities 1. PEROXISOMAL MEMBRANE PROTEIN PEX14, : 12 entities Detail

Related entities 2. PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR, : 1 : 4 : 2 : 4 entities Detail

Interaction partners 1. PEROXISOMAL MEMBRANE PROTEIN PEX14, : 21 : 1 interactors Detail

More details for 22 interactors identified by 10 citations

Interaction partners 2. PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR, : 39 : 1 interactors Detail

More details for 40 interactors identified by 16 citations

Experiments performed 1 experiments Detail

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19368_4bxu.nef
Input source #2: Coordindates	4bxu.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	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Sequence alignments

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

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

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

--60--------70-
ASEDELVAEFLQDQN
|||||||||||||||
ASEDELVAEFLQDQN
--------10-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	69	0	0	100.0
B	B	15	0	0	100.0

Content subtype: combined_19368_4bxu.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	683		100.0 (chain: A, length: 69), 100.0 (chain: B, length: 15)
2	Assigned chemical shifts	assigned_chem_shift_list_1_2	Warning	559		100.0 (chain: A, length: 69), 100.0 (chain: B, length: 15)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	163 (1)	noe	100.0 (chain: B, length: 15)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	16 (1)	hbond	80.0 (chain: B, length: 15)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	28 (28)	.	100.0 (chain: B, length: 15)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 69, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 409
  - ¹³C chemical shifts: 212
  - ¹⁵N chemical shifts: 62
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Peptide bond of PRO
- 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
  - Chain_ID: B
Saveframe: assigned_chem_shift_list_1_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 69, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 203
  - ¹H chemical shifts: 294
  - ¹⁵N chemical shifts: 62
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Peptide bond of PRO
- 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
  - Chain_ID: B

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	408	354	86.8
¹³C chemical shifts	301	212	70.4
¹⁵N chemical shifts	75	62	82.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	137	131	95.6
¹³C chemical shifts	138	69	50.0
¹⁵N chemical shifts	64	62	96.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	271	223	82.3
¹³C chemical shifts	163	143	87.7
¹⁵N chemical shifts	11	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	40	35	87.5
¹³C chemical shifts	40	38	95.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	15	0	0.0
¹³C chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	86	55	64.0
¹³C chemical shifts	63	0	0.0
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	30	30	100.0
¹³C chemical shifts	30	0	0.0
¹⁵N chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	56	25	44.6
¹³C chemical shifts	33	0	0.0
¹⁵N chemical shifts	3	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	6	75.0
¹³C chemical shifts	8	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	5	0	0.0
¹³C chemical shifts	5	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	301	203	67.4
¹H chemical shifts	408	258	63.2
¹⁵N chemical shifts	75	62	82.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	138	69	50.0
¹H chemical shifts	137	101	73.7
¹⁵N chemical shifts	64	62	96.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	163	134	82.2
¹H chemical shifts	271	157	57.9
¹⁵N chemical shifts	11	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	40	29	72.5
¹H chemical shifts	40	30	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	15	0	0.0
¹H chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	63	0	0.0
¹H chemical shifts	86	36	41.9
¹⁵N chemical shifts	18	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	30	0	0.0
¹H chemical shifts	30	28	93.3
¹⁵N chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	33	0	0.0
¹H chemical shifts	56	8	14.3
¹⁵N chemical shifts	3	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	8	0	0.0
¹H chemical shifts	8	1	12.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	5	0	0.0
¹H chemical shifts	5	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 100.0%
- Total number of restraints: 163
- Weight of restraints: 1.0 (163)
- Potential type of restraints: square-well-parabolic (163)
- Range of distance target values: 1.3, 2.62 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
    None
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 80.0%
  - Total number of restraints: 16
  - Weight of restraints: 1.0 (16)
  - Potential type of restraints: square-well-parabolic (16)
  - Range of distance target values: 1.9, 2.85 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
      None
    - Chain_ID: B
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 15, Sequence coverage: 100.0%
- Total number of restraints: 28
- Total number of restraints per polymer type: 28
- Weight of restraints: 1.0 (28)
- Potential type of restraints: square-well-parabolic (28)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: B

Keywords NMR, peroxisome, pex, pex14, pex5, protein complex, protein transport, translocation

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Found 1 Document (3.348 seconds)

BMRB: 19368

Sample

Sample

Related entities 1. PEROXISOMAL MEMBRANE PROTEIN PEX14, : 12 entities Detail

Related entities 2. PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR, : 1 : 4 : 2 : 4 entities Detail

Interaction partners 1. PEROXISOMAL MEMBRANE PROTEIN PEX14, : 21 : 1 interactors Detail

Interaction partners 2. PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR, : 39 : 1 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

NMR combined restraints 6 contents Detail