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- PDB-1vwd: STREPTAVIDIN-CYCLO-AC-[CHPQFC]-NH2, PH 3.0 -

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Basic information

Entry
Database: PDB / ID: 1vwd
TitleSTREPTAVIDIN-CYCLO-AC-[CHPQFC]-NH2, PH 3.0
Components
  • PEPTIDE LIGAND CONTAINING HPQ
  • STREPTAVIDIN
KeywordsCOMPLEX (BIOTIN-BINDING PROTEIN/PEPTIDE) / COMPLEX (BIOTIN-BINDING PROTEIN-PEPTIDE) / CYCLIC PEPTIDE DISCOVERED BY PHAGE DISPLAY / COMPLEX (BIOTIN-BINDING PROTEIN-PEPTIDE) complex
Function / homology
Function and homology information


biotin binding / extracellular region
Similarity search - Function
Avidin-like / Avidin-like, conserved site / Avidin-like domain signature. / Avidin / : / Avidin/streptavidin / Avidin-like superfamily / Avidin family / Avidin-like domain profile. / Lipocalin ...Avidin-like / Avidin-like, conserved site / Avidin-like domain signature. / Avidin / : / Avidin/streptavidin / Avidin-like superfamily / Avidin family / Avidin-like domain profile. / Lipocalin / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Biological speciesStreptomyces avidinii (bacteria)
MethodX-RAY DIFFRACTION / Resolution: 1.87 Å
AuthorsKatz, B.A. / Cass, R.T.
Citation
Journal: J.Biol.Chem. / Year: 1997
Title: In crystals of complexes of streptavidin with peptide ligands containing the HPQ sequence the pKa of the peptide histidine is less than 3.0.
Authors: Katz, B.A. / Cass, R.T.
#1: Journal: J.Am.Chem.Soc. / Year: 1996
Title: Structure-Based Design Tools: Structural and Thermodynamic Comparison with Biotin of a Small Molecule that Binds Streptavidin with Micromolar Affinity
Authors: Katz, B.A. / Liu, B. / Cass, R.T.
#2: Journal: J.Am.Chem.Soc. / Year: 1996
Title: Preparation of a Protein-Dimerizing Ligand by Topochemistry and Structure-Based Design
Authors: Katz, B.A.
#3: Journal: J.Biol.Chem. / Year: 1995
Title: Topochemical Catalysis Achieved by Structure-Based Ligand Design
Authors: Katz, B.A. / Cass, R.T. / Liu, B. / Arze, R. / Collins, N.
#4: Journal: Chem.Biol. / Year: 1995
Title: Topochemistry for Preparing Ligands that Dimerize Receptors
Authors: Katz, B.A. / Stroud, R.M. / Collins, N. / Liu, B. / Arze, R.
#5: Journal: Biochemistry / Year: 1995
Title: Binding to Protein Targets of Peptidic Leads Discovered by Phage Display: Crystal Structures of Streptavidin-Bound Linear and Cyclic Peptide Ligands Containing the Hpq Sequence
Authors: Katz, B.A.
#6: Journal: J.Am.Chem.Soc. / Year: 1995
Title: Structure-Based Design of High Affinity Streptavidin Binding Cyclic Peptide Ligands Containing Thioether Cross-Links
Authors: Katz, B.A. / Johnson, C.R. / Cass, R.T.
History
DepositionMar 3, 1997Processing site: BNL
Revision 1.0Mar 18, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 16, 2011Group: Atomic model
Revision 2.0Oct 30, 2024Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_conn / struct_site
Item: _atom_site.occupancy / _database_2.pdbx_DOI ..._atom_site.occupancy / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
B: STREPTAVIDIN
P: PEPTIDE LIGAND CONTAINING HPQ


Theoretical massNumber of molelcules
Total (without water)13,7242
Polymers13,7242
Non-polymers00
Water1,11762
1
B: STREPTAVIDIN
P: PEPTIDE LIGAND CONTAINING HPQ

B: STREPTAVIDIN
P: PEPTIDE LIGAND CONTAINING HPQ

B: STREPTAVIDIN
P: PEPTIDE LIGAND CONTAINING HPQ

B: STREPTAVIDIN
P: PEPTIDE LIGAND CONTAINING HPQ


Theoretical massNumber of molelcules
Total (without water)54,8968
Polymers54,8968
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation15_555y,x,-z1
crystal symmetry operation10_555-x,-y,z1
crystal symmetry operation8_555-y,-x,-z1
Unit cell
Length a, b, c (Å)59.100, 59.100, 176.580
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number98
Space group name H-MI4122
Components on special symmetry positions
IDModelComponents
11B-467-

HOH

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Components

#1: Protein STREPTAVIDIN


Mass: 12965.025 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptomyces avidinii (bacteria) / References: UniProt: P22629
#2: Protein/peptide PEPTIDE LIGAND CONTAINING HPQ


Mass: 758.911 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 62 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.81 Å3/Da / Density % sol: 37.7 %
Crystal growpH: 3
Details: SYNTHETIC MOTHER LIQUOR = 75 % SATURATED AMMONIUM SULFATE, 25 % 1.0 M POTASSIUM ACETATE ADJUSTED TO PH 3.0.
Crystal grow
*PLUS
Temperature: 20 ℃ / pH: 4.5 / Method: vapor diffusion, hanging drop / Details: Pahler, A., (1987) J. Biol. Chem., 262, 13933.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formulaDetails
110-20 mg/mlprotein1drop
250 mMpotassium acetate1drop
3200 mM1dropNaClpH4.5
430 %satammonium sulfate1reservoir
550 mMpotassium acetate1reservoir
6200 mM1reservoirNaCl

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Data collection

DiffractionMean temperature: 293 K
Diffraction sourceWavelength: 1.5418
DetectorType: SIEMENS / Detector: AREA DETECTOR
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionNum. obs: 12200 / Redundancy: 4 % / Rmerge(I) obs: 0.06
Reflection
*PLUS
Highest resolution: 1.81 Å / Num. measured all: 49331 / Rmerge(I) obs: 0.06

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Processing

Software
NameClassification
SADIEdata collection
SAINTdata scaling
X-PLORmodel building
X-PLORrefinement
SADIEdata reduction
SAINTdata reduction
X-PLORphasing
RefinementResolution: 1.87→7.5 Å / σ(F): 2
Details: THE FOLLOWING ATOMS HAD WEAK DENSITY AND OCCUPANCIES WERE REFINED: 13, 14, 15, SIDE CHAIN OF GLN 24, TERMINUS OF ASP 36, 46, SIDE CHAIN OF 47, 48, 49, 50, 51 (EXCLUDING C AND O), TERMINUS OF ...Details: THE FOLLOWING ATOMS HAD WEAK DENSITY AND OCCUPANCIES WERE REFINED: 13, 14, 15, SIDE CHAIN OF GLN 24, TERMINUS OF ASP 36, 46, SIDE CHAIN OF 47, 48, 49, 50, 51 (EXCLUDING C AND O), TERMINUS OF ARG 53, 64, 65, 66, 67, 100 AND N OF 101, SIDE CHAIN OF 101, TERMINUS OF ARG 103, TERMINUS OF GLU 116, TERMINUS OF LYS 121, ACE P 0 AND CYS P 1, CYS P 6 AND NH2 P 7. DISCRETELY DISORDERED SIDE CHAINS WHOSE OCCUPANCIES AND STRUCTURES WERE SIMULTANEOUSLY REFINED ARE 43, 73, 84, 87, 107, 132. DISORDERED WATERS ARE HOH 207 WHICH IS CLOSE TO A SYMMETRY-RELATED EQUIVALENT OF HOH 354; HOH 331 WHICH OCCUPIES SPACE AVAILABLE WHEN LYS 132 IS IN DISCRETE CONFORMATION NO. 1; HOH 426 WHICH OCCUPIES SPACE AVAILABLE WHEN ARG 84 IS IN DISCRETE CONFORMATION NO. 2. HOH 279, HOH 305, HOH 313, AND HOH 485 ARE CLOSE TO SYMMETRY-RELATED EQUIVALENTS OF THEMSELVES, RESPECTIVELY. NO ENERGY INTERACTIONS INVOLVING HOH 279, HOH 305, HOH 313 OR HOH 485 WERE TURNED ON DURING REFINEMENT. THE FOLLOWING ATOMS HAD WEAK DENSITY AND OCCUPANCIES WERE REFINED: 13, 14, 15, SIDE CHAIN OF GLN 24, TERMINUS OF ASP 36, 46, SIDE CHAIN OF 47, 48, 49, 50, 51 (EXCLUDING C AND O), TERMINUS OF ARG 53, 64, 65, 66, 67, 100 AND N OF 101, SIDE CHAIN OF 101, TERMINUS OF ARG 103, TERMINUS OF GLU 116, TERMINUS OF LYS 121, ACE P 0 AND CYS P 1, CYS P 6 AND NH2 P 7.
RfactorNum. reflection% reflection
Rfree0.209 -10 %
Rwork0.179 --
obs0.179 10462 79.3 %
Refinement stepCycle: LAST / Resolution: 1.87→7.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1053 0 0 62 1115
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.018
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg3
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d28.4
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
LS refinement shellResolution: 1.87→1.95 Å / % reflection obs: 36.4 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1A16PH3_PARAM19XB2_KBCO.PRA16PH3_TOPH19XB2_KBCO.PRO
X-RAY DIFFRACTION2PARAM11_UCSF.WATTOPH19.PEP
X-RAY DIFFRACTION3PARAM19XB2_KBCO.PROTOPH19XB2_KBCO.PRO
Software
*PLUS
Name: X-PLOR / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg28.4

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