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- PDB-2h1n: 3.0 A X-ray structure of putative oligoendopeptidase F: crystals ... -

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Basic information

Entry
Database: PDB / ID: 2h1n
Title3.0 A X-ray structure of putative oligoendopeptidase F: crystals grown by vapor diffusion technique
ComponentsOligoendopeptidase F
KeywordsHYDROLASE / STRUCTURAL GENOMICS / PROTEIN STRUCTURE INITIATIVE / MIDWEST CENTER FOR STRUCTURAL GENOMICS / MCSG / PSI
Function / homology
Function and homology information


peptide metabolic process / Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / metalloendopeptidase activity / proteolysis / metal ion binding
Similarity search - Function
Peptidase M3B, oligoendopeptidase-related / Neurolysin; domain 3 - #30 / Peptidase M3A/M3B catalytic domain / Peptidase M3A/M3B / Peptidase family M3 / Neurolysin; domain 3 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Unknown ligand / Oligoendopeptidase F
Similarity search - Component
Biological speciesGeobacillus stearothermophilus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3 Å
AuthorsGerdts, C.J. / Tereshko, V. / Dementieva, I. / Collart, F. / Joachimiak, A. / Kossiakoff, A. / Ismagilov, R.F. / Midwest Center for Structural Genomics (MCSG)
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2006
Title: Time-Controlled Microfluidic Seeding in nL-Volume Droplets To Separate Nucleation and Growth Stages of Protein Crystallization.
Authors: Gerdts, C.J. / Tereshko, V. / Yadav, M.K. / Dementieva, I. / Collart, F. / Joachimiak, A. / Stevens, R.C. / Kuhn, P. / Kossiakoff, A. / Ismagilov, R.F.
History
DepositionMay 16, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 13, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Version format compliance
Remark 999SEQUENCE At the time of processing, the sequence of this protein is not available at the UNP ...SEQUENCE At the time of processing, the sequence of this protein is not available at the UNP sequence database. Residues -2 to 0 are cloning artifacts.
Remark 300BIOMOLECULE: 1, 2 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 ...BIOMOLECULE: 1, 2 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAIN(S). EACH CHAIN REPRESENTS ONE BIOLOGICAL UNIT. THE OLIGOMERIZATION IS UNKNOWN.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Oligoendopeptidase F
B: Oligoendopeptidase F
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,12010
Polymers133,9902
Non-polymers1318
Water1086
1
A: Oligoendopeptidase F
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,0605
Polymers66,9951
Non-polymers654
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Oligoendopeptidase F
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,0605
Polymers66,9951
Non-polymers654
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)119.987, 119.987, 249.747
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31A
41B
51A
61B
71A
81B
91A
101B
111A
121B
131A
141B
151A
161B
171A
181B

NCS domain segments:

Ens-ID: 1 / Refine code: 2

Dom-IDComponent-IDBeg label comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LYSPHEAA2 - 275 - 30
21LYSPHEBB2 - 275 - 30
32GLYLEUAA31 - 3534 - 38
42GLYLEUBB31 - 3534 - 38
53ILETYRAA43 - 9146 - 94
63ILETYRBB43 - 9146 - 94
74LYSGLYAA110 - 211113 - 214
84LYSGLYBB110 - 211113 - 214
95PHEALAAA215 - 319218 - 322
105PHEALABB215 - 319218 - 322
116LYSASNAA323 - 376326 - 379
126LYSASNBB323 - 376326 - 379
137PROILEAA378 - 480381 - 483
147PROILEBB378 - 480381 - 483
158TYRASPAA481 - 489484 - 492
168TYRASPBB481 - 489484 - 492
179TYRLEUAA490 - 564493 - 567
189TYRLEUBB490 - 564493 - 567

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Components

#1: Protein Oligoendopeptidase F


Mass: 66994.828 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Geobacillus stearothermophilus (bacteria)
Gene: GK0963 / Plasmid: PMCSG7 / Production host: Escherichia coli (E. coli)
References: UniProt: Q5L1D2*PLUS, Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-UNL / UNKNOWN LIGAND


Num. of mol.: 6 / Source method: obtained synthetically
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 3.87 Å3/Da / Density % sol: 68.24 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7
Details: Hampton research SaltRX condition #96: 0.1M Bis-Tris Propane buffer, 60% Tascimate, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.00

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 0.9793
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Apr 1, 2006 / Details: ADJUSTABLE FOCUSING MIRRORS. K-B GEOMETRY
RadiationMonochromator: DOUBLE CRYSTAL SI (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 42052 / % possible obs: 98.7 % / Observed criterion σ(I): 0 / Redundancy: 5.6 % / Rmerge(I) obs: 0.047 / Net I/σ(I): 17.6
Reflection shellResolution: 3→3.11 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 2.1 / % possible all: 98.3

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
HKL-2000data reduction
HKL-2000data scaling
SOLVEphasing
RefinementMethod to determine structure: SAD / Resolution: 3→20 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.934 / SU B: 28.048 / SU ML: 0.225 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 1.222 / ESU R Free: 0.315
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. WE HAVE DETECTED THE DIFFERENCE ELECTRON DENSITY AT >2.5 SIGMA LEVEL IN THE CENTER GROOVE OF THE MOLECULE. WE HAVE USED TASCIMATE (THE ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. WE HAVE DETECTED THE DIFFERENCE ELECTRON DENSITY AT >2.5 SIGMA LEVEL IN THE CENTER GROOVE OF THE MOLECULE. WE HAVE USED TASCIMATE (THE HAMPTON RESEARCH PROPRIETARY MIXTURE OF ORGANIC ACIDS) FOR CRYSTALLIZATION. IT IS LIKELY THAT ONE OF THE ORGANIC ACIDS OR THEIR MIXTURE ENTERS THE GROOVE IN THE SOLUTION AND HELPS TO STABILIZE THE CLOSED CONFORMATION OF OLIGOENDOPEPTIDASE F IN THE CRYSTAL FORM. WE DID NOT ATTEMPT TO INTERPRET THE DIFFERENCE DENSITY AND USED THE UNKNOWN LIGAND TYPE (UNL) WITH OCCUPANCY=0 IN THE COORDINATE FILE TO INDICATE THIS FACT.
RfactorNum. reflection% reflectionSelection details
Rfree0.211 2088 5 %RANDOM
Rwork0.185 ---
obs0.186 39493 98.2 %-
all-41581 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 63.66 Å2
Baniso -1Baniso -2Baniso -3
1-0.67 Å20.34 Å20 Å2
2--0.67 Å20 Å2
3----1.01 Å2
Refinement stepCycle: LAST / Resolution: 3→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9358 0 14 6 9378
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0219614
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.0471.87813008
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.87151130
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.90923.358536
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.001151592
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.3741582
X-RAY DIFFRACTIONr_chiral_restr0.0750.21316
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.027612
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2250.24227
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3220.26669
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1230.2227
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1920.233
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1850.23
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.5371.55772
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.73329068
X-RAY DIFFRACTIONr_scbond_it1.23834393
X-RAY DIFFRACTIONr_scangle_it1.8574.53940
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Auth asym-ID: A / Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

NumberTypeRms dev position (Å)Weight position
2112tight positional0.030.05
2245medium positional0.270.5
2112tight thermal0.040.5
2245medium thermal0.392
LS refinement shellResolution: 3→3.08 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.335 147 -
Rwork0.293 2775 -
obs--95.93 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.26030.19920.45450.85540.01421.2128-0.03380.04440.29720.0576-0.1018-0.0266-0.3695-0.14060.1356-0.0290.09250.0478-0.1634-0.0368-0.063641.525932.2999104.2833
20.6552-0.24360.24541.4361-0.48630.80060.0616-0.1022-0.11840.074-0.04530.06750.144-0.2512-0.0163-0.1471-0.12320.0711-0.0387-0.0423-0.14892.214783.9083111.8808
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA0 - 5643 - 567
2X-RAY DIFFRACTION1AC - G601 - 6071
3X-RAY DIFFRACTION2BB0 - 5643 - 567
4X-RAY DIFFRACTION2BD - J701 - 7071

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