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Table 1 Data collection and refinement statistics

From: Defining rules governing recognition and Fc-mediated effector functions to the HIV-1 co-receptor binding site

  Fab N12-i2-gp12093TH057-M48U1 (data set 1) Fab N12-i2-gp12093TH057-M48U1 (data set 2)
Data collection
 Wavelength, Ǻ 0.9795 0.9795
 Space group P212121 P212121
 Cell parameters
a, b, c, Å 52.7, 69.5, 213.5 52.7, 69.5, 213.5
α, β, γ, ° 90, 90, 90 90, 90, 90
  Molecules/a.u. 4 4
  Resolution, (Å) 50–3.2 (3.26–3.2) 50–3.2 (3.26–3.25)
 # of reflections
  Total 52,155 60,052
  Unique 12,129 12,777
Rmerga, % 32.1 (52.1) 29.5 (100)
Rpimb, % 15.6 (43.4) 14.8 (57.7)
  CC1/2c 0.931 (0.611) 0.96 (0.466)
I/σ 6.2 (1.1) 7.0 (1.25)
  Completeness, % 88.5 (66.9) 96.9 (97.7)
  Redundancy 4.3 (1.9) 4.7 (4.6)
Refinement statistics
 Resolution, Å 50.0–3.2 50.0–3.25
Rd, % 24.1 23.6
Rfreee, % 30.1 28.3
 # of atoms   
  Protein 6130 6130
  Ligand 190 190
 Overall B value (Å)2
  Protein 81 80
  Ligand 74 71
 Root mean square deviation
  Bond lengths, Å 0.003 0.004
  Bond angles, ° 0.7 0.8
 Ramachandranf   
  Favored, % 90.1 90.2
  Allowed, % 98.5 98.3
  Outliers, % 1.5 1.7
PDB ID 6W4M
  1. Values in parentheses are for highest-resolution shell
  2. aRmerge = ∑│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
  3. bRpim = as defined by Weiss [39]
  4. cCC1/2 = as defined by Karplus and Diederichs [40]
  5. dR = ∑║Fo│ − │ Fc║/∑│Fo │, where Fo and Fc are the observed and calculated structure factors, respectively
  6. eRfree = defined by Brünger [41]
  7. fCalculated with MolProbity