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- PDB-1q2n: REFINED Solution NMR structure of the Z domain of STAPHYLOCOCCAL ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1q2n | ||||||
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Title | REFINED Solution NMR structure of the Z domain of STAPHYLOCOCCAL PROTEIN A | ||||||
![]() | IMMUNOGLOBULIN G BINDING PROTEIN A | ||||||
![]() | IMMUNE SYSTEM / IMMUNOGLOBULIN-BINDING PROTEIN / THREE-HELICAL BUNDLE STRUCTURE / RESIDUAL DIPOLAR COUPLINGS | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING WITH RESTRAINED MOLECULAR DYNAMICS, PROTOCAL USED: ANNEAL.INP | ||||||
![]() | Zheng, D. / Tashiro, M. / Aramini, J.M. / Montelione, G.T. | ||||||
![]() | ![]() Title: Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data. Authors: Zheng, D. / Aramini, J.M. / Montelione, G.T. #1: ![]() Title: The Mechanism of Binding Staphylococcal Protein a to Immunoglobin G Does not Involve Helix Unwinding Authors: Jendeberg, L. / Tashiro, M. / Tejero, R. / Lyons, B.A. / Uhlen, M. / Montelione, G.T. / Nilsson, B. #2: ![]() Title: Structures of Bacterial Immunoglobulin-Binding Domains and Their Complexes with Immunoglobulin Authors: Tashiro, M. / Montelione, G.T. #3: ![]() Title: An Improved Strategy for Determining Resonance Assignments for Isotopically Enriched Proteins and its Application to an Engineered Domain of Staphylococcal Protein A Authors: Lyons, B.A. / Tashiro, M. / Cedergren, L. / Nilsson, B. / Montelione, G.T. #4: ![]() Title: High Resolution Solution NMR Structure of the Z Domain of Staphylococcal Protein A Authors: Tashiro, M. / Tejero, R. / Zimmerman, D.E. / Celda, B. / Nilsson, B. / Montelione, G.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 184.8 KB | Display | ![]() |
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PDB format | ![]() | 153.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 351.4 KB | Display | ![]() |
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Full document | ![]() | 418.8 KB | Display | |
Data in XML | ![]() | 13.2 KB | Display | |
Data in CIF | ![]() | 20 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Antibody | Mass: 6648.316 Da / Num. of mol.: 1 / Fragment: residues 212-269 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR details | Text: NMR EXPERIMENTS CONDUCTED: 2D PFG-[15N]HSQC, 3D PFG-HNCO, 3D PFG-(HA)CA(CO)NH, 3D PFG-HA(CA)(CO)NH, 3D PFG-HA(CA)NH, 3D PFG-CBCANH, 3D PFG-CBCA(CO)NH, 3D PFG- (HA)CANH, 3D PFG-HN(CA)CO, 3D PFG- ...Text: NMR EXPERIMENTS CONDUCTED: 2D PFG-[15N]HSQC, 3D PFG-HNCO, 3D PFG-(HA)CA(CO)NH, 3D PFG-HA(CA)(CO)NH, 3D PFG-HA(CA)NH, 3D PFG-CBCANH, 3D PFG-CBCA(CO)NH, 3D PFG- (HA)CANH, 3D PFG-HN(CA)CO, 3D PFG-HCCNH-TOCSY, 3D PFG-HCC (CO)NH-TOCSY, 2D [15N]HSQC-IPAP, 3D Ca-coupled HNCO |
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Sample preparation
Details | Contents: 1mM Z domain U-15N,13C; 20mM NH4OAc buffer; 95% H2O, 5% D2O. Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 20 mM NH4OAc / pH: 6.50 / Pressure: 1 atm / Temperature: 303.00 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian MODIFIED UNITY 500 / Manufacturer: Varian / Model: MODIFIED UNITY 500 / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: SIMULATED ANNEALING WITH RESTRAINED MOLECULAR DYNAMICS, PROTOCAL USED: ANNEAL.INP Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON A TOTAL OF 769 CONFORMATIONAL RESTRAINTS. SUMMARY OF EXPERIMENTAL CONSTRAINTS: DISTANCE CONSTRAINTS: TOTAL = 536; INTRA-RESIDUE [I=J] = 224; SEQUENTIAL [(I-J)=1] ...Details: THE STRUCTURES ARE BASED ON A TOTAL OF 769 CONFORMATIONAL RESTRAINTS. SUMMARY OF EXPERIMENTAL CONSTRAINTS: DISTANCE CONSTRAINTS: TOTAL = 536; INTRA-RESIDUE [I=J] = 224; SEQUENTIAL [(I-J)=1] = 142; MEDIUM RANGE [1<(I-J)<5] 105; LONG RANGE [(I-J)>=5] = 65; NUMBER OF DISTANCE CONSTRAINTS RESIDUE = 9.2; DIHEDRAL-ANGLE CONSTRAINTS = 107 RESIDUAL DIPOLAR COUPLING CONSTRAINTS = 126 (34 N-H, 43 HA-CA, 4 TOTAL NUMBER OF CONSTRAINTS PER RESIDUE = 13.3; NUMBER OF LONG RANGE CONSTRAINTS PER RESIDUE = 3.3; NUMBER OF STRUCTURES COMPUTED = 100; NUMBER OF STRUCTURES USED = 10. AVERAGE RESIDUAL CONSTRAINT VIOLATIONS: DISTANCE VIOLATIONS 0.1-0.2 ANG = 7.7, 0. 0.8, >0.5 ANG = 0.3. AVERAGE R.M.S. DISTANCE VIOLATION = 0.03 AN AVERAGE DIHEDRAL ANGLE VIOLATIONS: >0 DEG = 0; RMSD VALUES: BACKBONE ATOMS (N,C,C') = 1.2 ANG; BACKBONE ATOMS(N,C,C') OF ORDERED RESIDUES = 0.4 ANG; ALL HEAVY = 1.7 ANG; ALL HEAVY ATOMS OF ORDERED RESIDUES = 1.0 ANG. PROCHECK USING ORDERED RESIDUES (5-36,39-57): MOST FAVORED REGIONS = 91.4%; ADDITIONAL ALLOWED REGIONS = 8.4%; GENEROUSLY ALLOWED REGIONS = 0.2%; DISALLOWED REGIONS = 0%. | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |