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. 2017 Jun 20;112(12):2479–2493. doi: 10.1016/j.bpj.2017.04.054

Table 1.

Summary of the Data Set in which the Density Maps Are Simulated

Dataa Set ID Source Model
Target Model
Sequenceg Identity (%)
Protein Nameb PDB IDc Residued ID Lengthe (Amino Acids) Helix Residuesf Percentge Protein Name PDB ID Residue ID Length (Amino Acids) Helix Residues Percentage
1 Adenylate kinase 4AKE [A] 1–214 214 0.459 Adenylate kinase 1AKE [A] 1–214 214 0.593 100.00
2 Triacylglycerol acylhydrolase 3TGL [A] 5–269 265 0.4 Triacylglycerol acylhydrolase 4TGL [A] 5–269 264 0.381 98.86
3 Maltodextrin binding protein 1OMP [A] 1–369 369 0.513 Maltodextrin binding protein 1ANF [A] 1–369 369 0.459 100.00
4 Aspartate aminotransferase 9AAT [A] 3–410 401 0.476 Aspartate aminotransferase 1AMA [A] 3–410 401 0.506 100.00
5 GroEL 1OEL [A] 2–525 524 0.534 60 kDa chaperonin 2C7C [A] 2–525 524 0.595 99.23
6 Lactoferrin 1LFG [A] 1–691 691 0.421 Lactoferrin 1LFH [A] 1–691 691 0.421 99.69
a

The data we use in each test.

b

Protein name.

c

Protein PDB ID and chain ID.

d

The amino acid residues we use to evaluate RMSDs.

e

The number of amino acid residues in the sequence.

f

The percentage of helix residues.

g

The sequence identity between the source model and target model.