Deposited unit | A: ATP-dependent zinc metalloprotease FtsH B: ATP-dependent zinc metalloprotease FtsH C: ATP-dependent zinc metalloprotease FtsH D: ATP-dependent zinc metalloprotease FtsH hetero molecules
| Theoretical mass | Number of molelcules |
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Total (without water) | 214,694 | 14 |
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Polymers | 212,545 | 4 |
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Non-polymers | 2,149 | 10 |
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Water | 72 | 4 |
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1 | A: ATP-dependent zinc metalloprotease FtsH B: ATP-dependent zinc metalloprotease FtsH hetero molecules A: ATP-dependent zinc metalloprotease FtsH B: ATP-dependent zinc metalloprotease FtsH hetero molecules A: ATP-dependent zinc metalloprotease FtsH B: ATP-dependent zinc metalloprotease FtsH hetero molecules
| Theoretical mass | Number of molelcules |
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Total (without water) | 322,308 | 24 |
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Polymers | 318,818 | 6 |
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Non-polymers | 3,490 | 18 |
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Water | 54 | 3 |
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Type | Name | Symmetry operation | Number |
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identity operation | 1_555 | x,y,z | 1 | crystal symmetry operation | 2_675 | -y+1,x-y+2,z | 1 | crystal symmetry operation | 3_465 | -x+y-1,-x+1,z | 1 |
Buried area | 24850 Å2 |
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ΔGint | -237 kcal/mol |
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Surface area | 105390 Å2 |
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Method | PISA |
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2 | C: ATP-dependent zinc metalloprotease FtsH D: ATP-dependent zinc metalloprotease FtsH hetero molecules C: ATP-dependent zinc metalloprotease FtsH D: ATP-dependent zinc metalloprotease FtsH hetero molecules C: ATP-dependent zinc metalloprotease FtsH D: ATP-dependent zinc metalloprotease FtsH hetero molecules
| Theoretical mass | Number of molelcules |
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Total (without water) | 321,773 | 18 |
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Polymers | 318,818 | 6 |
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Non-polymers | 2,956 | 12 |
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Water | 108 | 6 |
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Type | Name | Symmetry operation | Number |
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identity operation | 1_555 | x,y,z | 1 | crystal symmetry operation | 2_675 | -y+1,x-y+2,z | 1 | crystal symmetry operation | 3_465 | -x+y-1,-x+1,z | 1 |
Buried area | 24490 Å2 |
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ΔGint | -330 kcal/mol |
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Surface area | 106230 Å2 |
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Method | PISA |
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Unit cell | Length a, b, c (Å) | 197.550, 197.550, 323.920 |
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Angle α, β, γ (deg.) | 90.000, 90.000, 120.000 |
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Int Tables number | 155 |
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Space group name H-M | H32 |
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Noncrystallographic symmetry (NCS) | NCS domain: ID | Ens-ID | Details |
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1 | 1 | (chain A and (resid 150 through 161 or resid 163...2 | 1 | (chain B and ((resid 150 through 151 and (name N...3 | 1 | (chain C and (resid 150 through 154 or (resid 155...4 | 1 | (chain D and ((resid 150 through 151 and (name N... | | | |
NCS domain segments: Ens-ID: 1 Dom-ID | Component-ID | Beg auth comp-ID | Beg label comp-ID | End auth comp-ID | End label comp-ID | Selection details | Auth asym-ID | Label asym-ID | Auth seq-ID | Label seq-ID |
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1 | 1 | METMETGLUGLU(chain A and (resid 150 through 161 or resid 163...AA150 - 161 | 21 - 32 | 1 | 2 | VALVALVALVAL(chain A and (resid 150 through 161 or resid 163...AA163 - 219 | 34 - 90 | 1 | 3 | GLYGLYMETMET(chain A and (resid 150 through 161 or resid 163...AA221 - 227 | 92 - 98 | 1 | 4 | PHEPHEPHEPHE(chain A and (resid 150 through 161 or resid 163...AA228 | 99 | 1 | 5 | METMETLYSLYS(chain A and (resid 150 through 161 or resid 163...AA150 - 607 | 21 - 478 | 1 | 6 | METMETLYSLYS(chain A and (resid 150 through 161 or resid 163...AA150 - 607 | 21 - 478 | 1 | 7 | METMET | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | |
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