Table 1.
Data collection and refinement statistics.
| LM/HT gp120CRF01_AE Coree—TFH-I-070-A6 | LM/HT gp120CRF01_AE Coree—TFH-I-116-D1 | LM/HT gp120CRF01_AE Coree—ZXC-I-090 | LM/HT gp120CRF01_AE Coree—ZXC-I-092 | LM/HS gp120CRF01_AE Coree—DL-I-101 | LM/HS gp120CRF01_AE Coree—DL-I-102 | |
|---|---|---|---|---|---|---|
| Data collection | ||||||
| Wavelength, Ǻ | 0.979 | 0.979 | 0.979 | 0.979 | 0.979 | 0.979 |
| Space group | P212121 | P212121 | P212121 | P212121 | P212121 | P212121 |
| Cell parameters | ||||||
| a, b, c, Å | 63.6, 66.3, 91.4 | 64.7, 66.0, 87.8 | 61.8, 65.9, 91.2 | 60.0, 65.2, 87.3 | 67.7, 66.9, 92.2 | 194.5, 86.6, 57.7 |
| α, β, γ, ° | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 909, 90 | 90, 90, 90 | 90, 90, 90 |
| Molecules/a.u. | 1 | 1 | 1 | 1 | 1 | 1 |
| Resolution, (Å) | 50–2.4 (2.44–2.4) | 50–3.5 (3.69–3.5) | 50–2.4 (2.44–2.4) | 50–2.85 (2.9–2.85) | 50–2.19 (2.23–2.19) | 50–2.6 (2.64–2.6) |
| # of reflections | ||||||
| Total | 49,666 | 11,650 | 61,106 | 34,488 | 86,920 | 39,768 |
| Unique | 13,796 | 4021 | 14,904 | 7185 | 20,214 | 10,748 |
| Rmerge a, % | 9.1 (57.9) | 22.3 (113) | 10.6 (80.1) | 12.1 (104) | 17.2 (66.5) | 15.4 (98.3) |
| Rpim b, % | 5.1 (32.3) | 14.7 (72.9) | 5.8 (71.1) | 8.2 (77.4) | 9.7 (36.4) | 9.0 (65.0) |
| CC1/2 c | 0.98 (0.71) | 0.97 (0.33) | 1.0 (0.50) | 1.0 (0.42) | 1.0 (0.65) | 0.94 (0.60) |
| I/σ | 12.3 (1.3) | 2.8 (0.6) | 14.2 (0.8) | 12.5 (0.8) | 25.5 (2.1) | 17.3 (1.1) |
| Completeness, % | 88.3 (78.2) | 80.6 (83.9) | 97.8 (86.4) | 83.3 (78.0) | 97.4 (85.0) | 86.1 (90.2) |
| Redundancy | 3.6 (3.7) | 2.9 (3.0) | 4.1 (2.7) | 4.8 (4.2) | 4.3 (3.8) | 3.7 (3.1) |
| Refinement Statistics | ||||||
| Resolution, Å | 50.0–2.4 | 50.0–3.5 | 50.0–2.4 | 50.0–2.85 | 50.0–2.19 | 50.0–2.6 |
| R d % | 22.1 | 25.6 | 24.0 | 24.2 | 20.8 | 22.1 |
| Rfree e, % | 27.4 | 30.7 | 26.7 | 29.6 | 25.5 | 27.4 |
| # of atoms | ||||||
| Protein | 2,668 | 2,640 | 2,665 | 2,675 | 2,683 | 2,668 |
| Water | 32 | – | 23 | – | 64 | 2 |
| Ligand/Ion | 212 | 184 | 211 | 186 | 193 | 186 |
| Overall B value (Å)2 | ||||||
| Protein | 52 | 82 | 62 | 73 | 53 | 85 |
| Water | 48 | – | 56 | – | 49 | 74 |
| Ligand/Ion | 70 | 96 | 74 | 86 | 63 | 102 |
| RMSD f | ||||||
| Bond lengths, Å | 0.005 | 0.004 | 0.006 | 0.009 | 0.007 | 0.012 |
| Bond angles, ° | 1.0 | 0.79 | 0.98 | 1.3 | 1.0 | 1.4 |
| Ramachandran g | ||||||
| Favored, % | 94.0 | 90.2 | 94.0 | 89.5 | 95.0 | 92.5 |
| Allowed, % | 4.2 | 7.4 | 5.4 | 9.0 | 4.7 | 7.2 |
| Outliers, % | 1.8 | 2.4 | 0.6 | 1.5 | 0.3 | 0.3 |
| PDB ID | 8GD0 | 8GJT | 8GCZ | 8GD1 | 8GD3 | 8GD5 |
Values in parentheses are for highest-resolution shell; a Rmerge = ∑│I − <I>│/∑I, where I is the observed intensity and <I> is the average intensity obtained from multiple observations of symmetry-related reflections after rejections; b Rpim = as defined in [26]; c CC1/2 = as defined by Karplus and Diederichs [27]; d R = ∑║Fo│ − │ Fc║/∑│Fo│, where Fo and Fc are the observed and calculated structure factors, respectively; e Rfree = as defined by Brünger [28]; f RMSD = root mean square deviation; g calculated with MolProbity.