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- PDB-1vwq: STREPTAVIDIN-CYCLO-[5-S-VALERAMIDE-HPQGPPC]K-NH2, PH 2.5, I4122 C... -

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Basic information

Entry
Database: PDB / ID: 1vwq
TitleSTREPTAVIDIN-CYCLO-[5-S-VALERAMIDE-HPQGPPC]K-NH2, PH 2.5, I4122 COMPLEX
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 / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
PENTANOIC ACID / Streptavidin
Similarity search - Component
Biological speciesStreptomyces avidinii (bacteria)
Bothrops insularis (golden lancehead)
MethodX-RAY DIFFRACTION / Resolution: 1.7 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, 1997-
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

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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
hetero molecules


Theoretical massNumber of molelcules
Total (without water)13,9303
Polymers13,8282
Non-polymers1021
Water1,15364
1
B: STREPTAVIDIN
P: PEPTIDE LIGAND CONTAINING HPQ
hetero molecules

B: STREPTAVIDIN
P: PEPTIDE LIGAND CONTAINING HPQ
hetero molecules

B: STREPTAVIDIN
P: PEPTIDE LIGAND CONTAINING HPQ
hetero molecules

B: STREPTAVIDIN
P: PEPTIDE LIGAND CONTAINING HPQ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)55,72112
Polymers55,3128
Non-polymers4094
Water1448
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)58.100, 58.100, 174.490
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-518-

HOH

21B-518-

HOH

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Components

#1: Protein STREPTAVIDIN /


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


Mass: 863.017 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bothrops insularis (golden lancehead)
#3: Chemical ChemComp-LEA / PENTANOIC ACID / VALERIC ACID / Valeric acid


Mass: 102.132 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C5H10O2
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 64 / 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: 2.66 Å3/Da / Density % sol: 33.3 %
Crystal growpH: 2.5
Details: SYNTHETIC MOTHER LIQUOR = 75 % SATURATED AMMONIUM SULFATE, 25 % 1.0 M SODIUM FORMATE ADJUSTED TO PH 2.5.
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: RIGAKU RAXIS IV / Detector: IMAGE PLATE
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionNum. obs: 28160 / Redundancy: 4.5 % / Rmerge(I) obs: 0.107
Reflection
*PLUS
Highest resolution: 1.33 Å / Num. measured all: 127962

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Processing

Software
NameVersionClassification
X-PLORmodel building
X-PLORrefinement
BIOTEX(MSC)data reduction
X-PLORphasing
RefinementResolution: 1.7→7.5 Å / σ(F): 2.5
Details: THE FOLLOWING ATOMS HAD WEAK DENSITY AND OCCUPANCIES WERE REFINED: 13, 14, 15, (MAIN CHAIN OF GLN 24), (SIDE CHAIN OF GLN 24), (N, HN, CA, HA1, HA2 OF GLY 26), (MAIN CHAIN OF ALA 35), (SIDE ...Details: THE FOLLOWING ATOMS HAD WEAK DENSITY AND OCCUPANCIES WERE REFINED: 13, 14, 15, (MAIN CHAIN OF GLN 24), (SIDE CHAIN OF GLN 24), (N, HN, CA, HA1, HA2 OF GLY 26), (MAIN CHAIN OF ALA 35), (SIDE CHAIN OF ALA 35), (MAIN CHAIN AND CB, HB1, HB2 OF ASP 36), (CG, OD1, AND OD2 OF ASP 36), 46, 47, 48, 49, 50, (MAIN CHAIN AND CB, HB1, HB2 OF GLU 51), (CG, HG1, HG2, CD, OE1, OE2 OF GLU 51), (SIDE CHAIN OF SER 52), (TERMINUS OF ARG 53), 99, 100, (N AND HN OF GLU 101), (CG, HG1, HG2, CD, OE1, OE2 OF GLU 101), TERMINUS OF ARG 103, (N, HN, CA, HA OF GLU 116), (CB, HB1, HB2, CG, HG1, HG2 OF GLU 116), (CD, OE1, OE2 OF GLU 116), (N, HN, CA, HA OF ALA 117), (CB, HB1, HB2, HB3 OF ALA 117), LYS 121 FROM CG OUTWARD, LYS 132 SIDE CHAIN, (LYS P 9 AND NH2 P 10). DISCRETELY DISORDERED ENTIRE RESIDUES WHOSE OCCUPANCIES AND STRUCTURES WERE SIMULTANEOUSLY REFINED ARE: 60, 61, 62, 63, 64, 65, 66, 67, 68, 69. DISCRETELY DISORDERED SIDE CHAINS WHOSE OCCUPANCIES AND STRUCTURES WERE SIMULTANEOUSLY REFINED ARE: ARG 84, GLN 107. RESIDUES 60 - 69 WERE REFINED IN 2 CONFORMATIONS BECAUSE UPON PROTONATION OF ASP 61 AT LOW PH, ASP 61 UNDERGOES A LARGE SHIFT IN CONFORMATION AND CHANGE IN HYDROGEN BONDING. THE LOOP COMPRISING RESIDUES 61 - 69 ALSO UNDERGO CORRESPONDING CONFORMATIONAL CHANGES. HOWEVER SOME OF THESE RESIDUES ARE DISORDERED AND NOT VISIBLE IN EITHER CONFORMATION. DISORDERED WATERS ARE HOH 166 WHICH IS CLOSE TO A SYMMETRY-RELATED EQUIVALENT OF HOH 354; HOH 148 WHICH OCCUPIES THE SPACE AVAILABLE WHEN ASP 61 IS IN CONFORMATION 2; HOH 279, HOH 305, HOH 313, HOH 516, HOH 526, HOH 532 WHICH ARE CLOSE TO SYMMETRY-RELATED EQUIVALENTS OF THEMSELVES; NO ENERGY INTERACTIONS INVOLVING HOH 279, HOH 305, HOH 313, HOH 516, HOH 526, HOH 532 WERE TURNED ON DURING REFINEMENT. THE FOLLOWING ATOMS HAD WEAK DENSITY AND OCCUPANCIES WERE REFINED: 13, 14, 15, (MAIN CHAIN OF GLN 24), (SIDE CHAIN OF GLN 24), (N, HN, CA, HA1, HA2 OF GLY 26), (MAIN CHAIN OF ALA 35), (SIDE CHAIN OF ALA 35), (MAIN CHAIN AND CB, HB1, HB2 OF ASP 36), (CG, OD1, AND OD2 OF ASP 36), 46, 47, 48, 49, 50, (MAIN CHAIN AND CB, HB1, HB2 OF GLU 51), (CG, HG1, HG2, CD, OE1, OE2 OF GLU 51), (SIDE CHAIN OF SER 52), (TERMINUS OF ARG 53), 99, 100, (N AND HN OF GLU 101), (CG, HG1, HG2, CD, OE1, OE2 OF GLU 101), TERMINUS OF ARG 103, (N, HN, CA, HA OF GLU 116), (CB, HB1, HB2, CG, HG1, HG2 OF GLU 116), (CD, OE1, OE2 OF GLU 116), (N, HN, CA, HA OF ALA 117), (CB, HB1, HB2, HB3 OF ALA 117), LYS 121 FROM CG OUTWARD, LYS 132 SIDE CHAIN, (LYS P 9 AND NH2 P 10). RESIDUES 60 - 69 WERE REFINED IN 2 CONFORMATIONS BECAUSE UPON PROTONATION OF ASP 61 AT LOW PH, ASP 61 UNDERGOES A LARGE SHIFT IN CONFORMATION AND CHANGE IN HYDROGEN BONDING. THE LOOP COMPRISING RESIDUES 61 - 69 ALSO UNDERGO CORRESPONDING CONFORMATIONAL CHANGES. HOWEVER SOME OF THESE RESIDUES ARE DISORDERED AND NOT VISIBLE IN EITHER CONFORMATION.
RfactorNum. reflection% reflection
Rfree0.223 -10 %
Rwork0.195 --
obs0.195 11983 71.6 %
Refinement stepCycle: LAST / Resolution: 1.7→7.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2017 0 14 192 2223
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.017
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_deg4.3
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d25.3
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: 1.7→1.78 Å / % reflection obs: 60.5 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1I4VAL25_PARMALLH3X.PROI4VAL25_TOPALLH6X_BAK.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_deg25.3

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