[English] 日本語
Yorodumi
- PDB-3fll: Crystal structure of E55Q mutant of nitrophorin 4 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3fll
TitleCrystal structure of E55Q mutant of nitrophorin 4
ComponentsNitrophorin-4
KeywordsTRANSPORT PROTEIN / beta barrel / lipocalin / heme / mutant / ammonia / Iron / Metal-binding / Secreted / Vasoactive / Vasodilator
Function / homology
Function and homology information


nitrite dismutase / histamine binding / nitric oxide binding / vasodilation / oxidoreductase activity / extracellular region / metal ion binding
Similarity search - Function
Nitrophorin / Nitrophorin domain / Nitrophorin / Calycin beta-barrel core domain / Calycin / Lipocalin / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
PROTOPORPHYRIN IX CONTAINING FE / AMMONIA / Nitrophorin-4
Similarity search - Component
Biological speciesRhodnius prolixus (insect)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.5 Å
AuthorsMontfort, W.R. / Weichsel, A.
Citation
Journal: J.Am.Chem.Soc. / Year: 2009
Title: Effect of mutation of carboxyl side-chain amino acids near the heme on the midpoint potentials and ligand binding constants of nitrophorin 2 and its NO, histamine, and imidazole complexes.
Authors: Berry, R.E. / Shokhirev, M.N. / Ho, A.Y. / Yang, F. / Shokhireva, T.K. / Zhang, H. / Weichsel, A. / Montfort, W.R. / Walker, F.A.
#1: Journal: Biochemistry / Year: 2001
Title: Ligand-induced heme ruffling and bent NO geometry in ultra-high-resolution structures of nitrophorin 4
Authors: Roberts, S.A. / Weichsel, A. / Qiu, Y. / Shelnutt, J.A. / Walker, F.A. / Montfort, W.R.
History
DepositionDec 18, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 10, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Oct 20, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_special_symmetry ...database_2 / pdbx_struct_special_symmetry / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Sep 6, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.4Oct 9, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Nitrophorin-4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,9253
Polymers20,2921
Non-polymers6342
Water4,396244
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)70.379, 42.838, 53.056
Angle α, β, γ (deg.)90.00, 94.20, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-210-

HOH

21A-294-

HOH

31A-450-

HOH

-
Components

#1: Protein Nitrophorin-4 / NP4


Mass: 20291.678 Da / Num. of mol.: 1 / Fragment: UNP residues 22-205 / Mutation: E55Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodnius prolixus (insect) / Plasmid: pET17B / Production host: Escherichia coli (E. coli) / Strain (production host): BL21DE3 / References: UniProt: Q94734
#2: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#3: Chemical ChemComp-NH3 / AMMONIA


Mass: 17.031 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: NH3
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 244 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 1.97 Å3/Da / Density % sol: 37.42 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.6
Details: ammonium phosphate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL9-1 / Wavelength: 0.751 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 24, 2008 / Details: mirrors
RadiationMonochromator: Si(311) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.751 Å / Relative weight: 1
ReflectionResolution: 1.5→30.6 Å / Num. obs: 23089 / % possible obs: 95.58 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.17 % / Rmerge(I) obs: 0.081 / Net I/σ(I): 10.3
Reflection shellResolution: 1.5→1.55 Å / Redundancy: 3.15 % / Rmerge(I) obs: 0.295 / Mean I/σ(I) obs: 2.7 / Num. unique all: 2527 / % possible all: 100

-
Processing

Software
NameVersionClassification
ADSCQuantumdata collection
REFMAC5.3.0037refinement
CrystalCleardata reduction
CrystalCleardata scaling
REFMAC5.3.0037phasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 1D2U

1d2u


Resolution: 1.5→30 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.943 / SU B: 1.353 / SU ML: 0.052 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.087 / ESU R Free: 0.086 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20123 1220 5 %RANDOM
Rwork0.16886 ---
all0.171 23089 --
obs0.171 23089 95.58 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 10.663 Å2
Baniso -1Baniso -2Baniso -3
1--0.04 Å20 Å20 Å2
2--0.48 Å20 Å2
3----0.45 Å2
Refinement stepCycle: LAST / Resolution: 1.5→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1476 0 44 244 1764
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0221563
X-RAY DIFFRACTIONr_bond_other_d0.0010.02992
X-RAY DIFFRACTIONr_angle_refined_deg1.5012.0382145
X-RAY DIFFRACTIONr_angle_other_deg1.4053.0032439
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.0845193
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.5125.94269
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.18315257
X-RAY DIFFRACTIONr_dihedral_angle_4_deg6.563152
X-RAY DIFFRACTIONr_chiral_restr0.0830.2227
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.021766
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02295
X-RAY DIFFRACTIONr_nbd_refined0.2230.2313
X-RAY DIFFRACTIONr_nbd_other0.190.21004
X-RAY DIFFRACTIONr_nbtor_refined0.1830.2740
X-RAY DIFFRACTIONr_nbtor_other0.0870.2829
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1580.2143
X-RAY DIFFRACTIONr_metal_ion_refined0.0050.21
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1150.214
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2030.237
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1140.238
X-RAY DIFFRACTIONr_mcbond_it1.2851.51195
X-RAY DIFFRACTIONr_mcbond_other0.2411.5384
X-RAY DIFFRACTIONr_mcangle_it1.55121518
X-RAY DIFFRACTIONr_scbond_it2.5163762
X-RAY DIFFRACTIONr_scangle_it3.244.5611
LS refinement shellResolution: 1.5→1.539 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.236 89 -
Rwork0.181 1744 -
obs-1744 98.02 %

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more