1H, 15N, and 13C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state

In this protein, the heme is modified: the vinyl of pyrrole B (carbon atoms CAB
and CBB) becomes saturated. CAB carries one H (HAB2) and makes a link to NE2 of
His 117 (this should be described in the "linkages" part of the deposition).
CBB is a methyl group.

Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Wed Oct 26 08:58:22 2011

HYBRID BETWEEN B AND C TYPE HEMES (PROTOPORPHYRIN IX CONTAINING FE)

Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein.

(1)H, (15)N, and (13)C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state.

Structural and dynamic repercussions of heme binding and heme-protein cross-linking in Synechococcus sp. PCC 7002 hemoglobin.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
Characterization of the heme-histidine cross-link in cyanobacterial hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002.

Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002.

Solution Structure Of Synechococcus Sp. Pcc 7002 Hemoglobin

Crystal Structure Of The 2/2 Hemoglobin From Synechococcus Sp. Pcc 7002 In The Cyanomet State And With Covalently Attached Heme

Crystal Structure Of Synechococcus Sp. Pcc 7002 Globin At Cryogenic Temperature With Heme Modification

cyanoglobin [Synechococcus sp. PCC 7002]

group 1 hemoglobin GlbN [Synechococcus sp. NKBG042902]

DGSA-distance geometry simulated annealing, torsion angle dynamics

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax