
Cap32/34


Data Collection
 
Space Group

P4_{1}

Cell Dimensions

a, b, c (Å)

124.5, 124.5, 77.5

α, β, γ (º)

90, 90, 90

Resolution Range (Å)

502.2 (2.32.2)

Number of Reflections

367874

Number of Unique Reflections

60185

Completeness (%)

99.8 (99.6)

Multiplicity

R
_{
merge
}
^{†}

14.9 (83.5)

<I/σI>

14.2 (3.8)

Refinement
 
R
_{
work
}
^{‡}

0.226

R
_{
free
}
^{§}

0.265

R.m.s. deviations
 
Bond lengths (Å)

0.008

Bond angles (°)

1.36

Ramachandran Analysis
 
Residues in most favoured regions (%)

95.9

Residues in allowed regions (%)

4.1

Outliers (%)

0

Model statistics

Protein residues:
 
No. in subunit A & B

514

Bfactor A & B (Å^{2})

15.4

Additional groups:
 
Water (No. / Bfactor)

328 / 37.9

 Values in parentheses refer to the highest resolution shell.
 ^{†}R_{
merge
} = Σ_{
hkl
}Σ_{
i
} I_{
i
}(hkl)  < I(hkl) > / Σ_{
hkl
}Σ_{
i
}I_{
i
}(hkl); where I_{
i
}(hkl) is the intensity of the i th measurement of reflection hkl and < I(hkl) > is the mean value of I_{
i
}(hkl) for all i measurements.
 ^{‡}R_{
work
} = Σ_{
hkl
}F_{
o
}F_{
c
}/ΣF_{
o
}, where F_{
o
} is the observed structure factor and F_{
c
} is the calculated structure factor.
 ^{§}R_{
free
} is the same as R_{
cryst
} except calculated with a subset, 5%, of data that are excluded from refinement calculations.