TABLE 3.
Data collection and refinement statistics
| Parameter | Result(s) for:
|
||
|---|---|---|---|
| 2219 + MN peptide on beamline SSRL 9-2 | 2219 + UR29 peptide on beamline ALS 5.0.1 | 2219 + UG1033 peptide on beamline SSRL-11-1 | |
| Wavelength (Å) | 1.033 | 1.000 | 0.984 |
| Resolution (Å)a | 2.30 (2.34-2.30) | 2.0 (2.03-2.00) | 2.35 (2.39-2.35) |
| Space group; cell dimension a, b, c (Å) | P41212; 60.5, 60.5, 275.2 | P212121; 62.9, 94.4, 96.7 | P212121; 62.7, 96.9, 97.0 |
| No. of observations | 125,481 (6,361) | 189,728 (9,361) | 93,252 (3,432) |
| No. of unique reflections | 23,835 (1,162) | 39,609 (1,963) | 24,986 (1,118) |
| Completeness (%) | 99.8 (100.0) | 99.9 (100.0) | 98.6 (92.8) |
| Rsym (%)b | 8.6 (52.5) | 6.9 (61.2) | 5.7 (48.8) |
| Avg I/σ | 22.0 (3.5) | 19.7 (2.6) | 31.9 (2.4) |
| Refinement statistics for all reflections of >0.0 σF | |||
| Resolution (Å) | 69.0-2.3 | 67.4-2.0 | 31.3-2.35 |
| No. of reflections (working) | 22,624 | 37,576 | 23,732 |
| No. of reflections (test) | 1,195 | 1,982 | 1,208 |
| Rcryst (%)c | 21.7 | 20.6 | 21.2 |
| Rfree (%)d | 26.7 | 23.8 | 24.4 |
| No. of Fab atoms | 3,315 | 3,315 | 3,315 |
| No. of peptide atoms | 137 | 137 | 128 |
| No. of water molecules | 191 | 123 | 60 |
| Avg B value (Å2) for: | |||
| Variable | 34.7 | 42.1 | 70.5 |
| Constant | 34.9 | 42.5 | 71.1 |
| Peptide | 35.5 | 43.4 | 74.0 |
| Wilson B value (Å2) | 30.8 | 33.6 | 56.0 |
| Ramachandran plots (%) for: | |||
| Most favored | 92.1 | 90.3 | 88.7 |
| Additionally allowed | 6.6 | 8.4 | 10.5 |
| Generously allowed | 0.8 | 0.5 | 0.0 |
| Disallowede | 0.5 | 0.8 | 0.8 |
| Root mean square deviations | |||
| Bond length (Å) | .013 | .020 | .013 |
| Angle (Å) | 1.46 | 1.73 | 1.33 |
a
Numbers in parentheses are for the highest-resolution shell of data.
b
Rsym = Σhkl = ∑hkl|I− <I>|/Σhkl|I|.
c
Rcryst = Σhkl = ∑hkl|Fobs − Fcalc|/Σhkl |Fobs|.
d
Rfree is the same as Rcryst except for 5% of the data excluded from the refinement.
e
Residue AsnL51 is in a conserved γ turn almost always found in Fab structures, SerH128 is in a disordered region of the heavy chain, and AspL151 is in clear density and is the i + 1 residue in a type II′ turn.