[English] 日本語
![](img/lk-miru.gif)
- PDB-1fvc: X-RAY STRUCTURES OF THE ANTIGEN-BINDING DOMAINS FROM THREE VARIAN... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1fvc | ||||||
---|---|---|---|---|---|---|---|
Title | X-RAY STRUCTURES OF THE ANTIGEN-BINDING DOMAINS FROM THREE VARIANTS OF HUMANIZED ANTI-P185-HER2 ANTIBODY 4D5 AND COMPARISON WITH MOLECULAR MODELING | ||||||
![]() |
| ||||||
![]() | IMMUNOGLOBULIN | ||||||
Function / homology | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta / : ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Eigenbrot, C. / Randal, M. / Kossiakoff, A.A. / Presta, L. | ||||||
![]() | ![]() Title: X-ray structures of the antigen-binding domains from three variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modeling. Authors: Eigenbrot, C. / Randal, M. / Presta, L. / Carter, P. / Kossiakoff, A.A. #1: ![]() Title: Humanization of an Anti-P185-Her2 Antibody for Human Cancer Therapy Authors: Carter, P. / Presta, L. / Gorman, C.M. / Ridgway, J.B. / Henner, D. / Wong, W.L.T. / Rowland, A.M. / Kotts, C. / Carver, M.E. / Shepard, H.M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 97.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 79.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 443.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 459.1 KB | Display | |
Data in XML | ![]() | 20.9 KB | Display | |
Data in CIF | ![]() | 29.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: EIGHT ATOMS HAVE BEEN ASSIGNED ZERO OCCUPANCY IN THE FINAL MODEL. THEY ARE ATOMS CG, CD, OE1, AND OE2 OF RESIDUE GLU B 1 AND ATOMS CG, CD, OE1, AND NE2 OF RESIDUE GLN C 3. 2: RESIDUES 8 AND 95 IN CHAINS A AND C ARE CIS PROLINES. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.99776, 0.03673, 0.05595), Vector: Details | THERE ARE TWO MOLECULES IN THE ASYMMETRIC UNIT. THE LIGHT AND HEAVY CHAINS OF MOLECULE 1 ARE DENOTED BY CHAIN IDENTIFIERS *A* AND *B*. THE LIGHT AND HEAVY CHAINS OF MOLECULE 2 ARE DENOTED BY THE CHAIN IDENTIFIERS *C* AND *D*. THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAINS *A* AND *B* WHEN APPLIED TO CHAINS *C* AND *D*. | |
-
Components
#1: Antibody | Mass: 11964.308 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Antibody | Mass: 13176.638 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Water | ChemComp-HOH / | Sequence details | THE RESIDUE NUMBERING IS SEQUENTIAL WITHIN EACH CHAIN. THE SEQUENTIAL NUMBERING OF THE LIGHT CHAIN ...THE RESIDUE NUMBERING IS SEQUENTIAL | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.86 % | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 15 Å / Num. obs: 18259 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.116 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.2→10 Å / Rfactor Rwork: 0.183 / Rfactor obs: 0.183 / σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 17110 / Rfactor obs: 0.183 / Rfactor Rwork: 0.183 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|