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Protein

Carbonic anhydrase 2

Gene

CA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6.By similarity3 Publications

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+22 Publications, Co2+1 PublicationNote: Zinc. Can also use cobalt(II) with lower efficiency, but not copper(II), nickel(II) and manganese(II).1 Publication

Enzyme regulationi

Activated by X-ray, histamine, L-adrenaline, L- and D-phenylalanine, L- and D-histidine, L-His-OMe and beta-Ala-His (carnosine). Competitively inhibited by saccharin, thioxolone, coumarins, 667-coumate, celecoxib (Celebrex), valdecoxib (Bextra), SC-125, SC-560, diclofenac, acetate, azide, bromide, sulfonamide derivatives such as acetazolamide (AZA), methazolamide (MZA), ethoxzolamide (EZA), dichlorophenamide (DCP), brinzolamide, dansylamide, thiabendazole-5-sulfonamide, trifluoromethane sulfonamide and N-hydroxysulfamide, fructose-based sugar sulfamate RWJ-37497, and Foscarnet (phosphonoformate trisodium salt). Repressed strongly by hydrogen sulfide(HS) and weakly by nitrate (NO3). Esterase activity weakly reduced by cyanamide. N-hydroxyurea interfers with zinc binding and inhibit activity.27 Publications

Absorptioni

Abs(max)=~550 nm10 Publications

At pH 7.0. Shows a second maximum at 618 nm.

Kineticsi

  1. KM=10 mM for CO210 Publications
  2. KM=82 mM for H2CO310 Publications
  3. KM=3 mM for 4-nitrophenyl acetate10 Publications

    pH dependencei

    Optimum pH is 6-8.10 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei62Activator3 Publications1
    Active sitei64Proton acceptor3 Publications1
    Active sitei673 Publications1
    Binding sitei67Activator3 Publications1
    Binding sitei92Activator3 Publications1
    Metal bindingi94Zinc; catalytic23 Publications1
    Metal bindingi96Zinc; catalytic22 Publications1
    Metal bindingi119Zinc; catalytic22 Publications1
    Active sitei1273 Publications1

    GO - Molecular functioni

    • arylesterase activity Source: CACAO
    • carbonate dehydratase activity Source: CACAO
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciZFISH:HS02558-MONOMER.
    BRENDAi4.2.1.1. 2681.
    ReactomeiR-HSA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
    R-HSA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
    R-HSA-1475029. Reversible hydration of carbon dioxide.
    SABIO-RKP00918.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 2 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase II
    Carbonic anhydrase C
    Short name:
    CAC
    Carbonic anhydrase II
    Short name:
    CA-II
    Gene namesi
    Name:CA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:1373. CA2.

    Subcellular locationi

    • Cytoplasm 1 Publication
    • Cell membrane 1 Publication

    • Note: Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells.

    GO - Cellular componenti

    • apical part of cell Source: UniProtKB
    • axon Source: Ensembl
    • basolateral plasma membrane Source: Ensembl
    • cytoplasm Source: UniProtKB
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • extracellular space Source: Ensembl
    • microvillus Source: Ensembl
    • myelin sheath Source: Ensembl
    • plasma membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Osteopetrosis, autosomal recessive 3 (OPTB3)5 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.
    See also OMIM:259730
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_00138192Q → P in OPTB3; in Czechoslovakia. 2 Publications1
    Natural variantiVAR_02100994H → Y in OPTB3; partial loss of activity. 1 Publication1
    Natural variantiVAR_001382107H → Y in OPTB3; frequent mutation. 4 PublicationsCorresponds to variant rs118203933dbSNPEnsembl.1
    Natural variantiVAR_021010144G → R in OPTB3; complete loss of activity. 1 Publication1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi5W → A: Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with W-64. 1 Publication1
    Mutagenesisi7Y → F: Enhanced activity. 2 Publications1
    Mutagenesisi7Y → H: Reduced proton transfer rate. 2 Publications1
    Mutagenesisi62N → A: Reduced activity. 3 Publications1
    Mutagenesisi62N → D: Strongly reduced activity. 3 Publications1
    Mutagenesisi62N → H: Reduced proton transfer; when associated with A-64. 3 Publications1
    Mutagenesisi62N → L: Reduced activity. 3 Publications1
    Mutagenesisi62N → T: Reduced activity. 3 Publications1
    Mutagenesisi62N → V: Reduced activity. 3 Publications1
    Mutagenesisi64H → A: Reduced CO(2) hydrase activity, rescued by 4-methylimidazole (4-MI). Reduced proton transfer; when associated with H-62. Enhanced proton transfer; when associated with H-67. Enhanced proton transfer capacity; when associated with H-99. 4 Publications1
    Mutagenesisi64H → G: Impaired activity, not rescued by 4-methylimidazole (4-MI). 4 Publications1
    Mutagenesisi64H → W: Impaired activity, rescued by 4-methylimidazole (4-MI). Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with A-5. 4 Publications1
    Mutagenesisi65A → F: Reduced activity. 1 Publication1
    Mutagenesisi65A → H, L or S: Normal activity. 1 Publication1
    Mutagenesisi67N → H: Enhanced proton transfer; when associated with A-64. 3 Publications1
    Mutagenesisi67N → L: Reduced activity. 3 Publications1
    Mutagenesisi67N → Q: Normal activity. 3 Publications1
    Mutagenesisi94H → C, D, E, N or Q: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding. 2 Publications1
    Mutagenesisi106E → A or Q: Strongly reduced CO(2) hydrase activity. 2 Publications1
    Mutagenesisi106E → D: Normal CO(2) hydrase activity. 2 Publications1
    Mutagenesisi117E → Q: Strongly reduced activity and sulfonamide affinity. 1 Publication1
    Mutagenesisi119H → D, N or Q: Reduced activity. 1 Publication1
    Mutagenesisi119H → E: Strongly reduced activity. 1 Publication1
    Mutagenesisi121V → A, G, I, L or S: Reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. 1 Publication1
    Mutagenesisi121V → K or R: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. 1 Publication1
    Mutagenesisi142V → F or Y: Strongly impaired activity. 1 Publication1
    Mutagenesisi142V → G: Weakly impaired activity. 1 Publication1
    Mutagenesisi142V → H: Impaired activity. 1 Publication1
    Mutagenesisi197L → A: Reduced CO(2) hydrase activity. 1 Publication1
    Mutagenesisi197L → E, H or R: Strongly reduced CO(2) hydrase activity. 1 Publication1
    Mutagenesisi197L → F: Normal activity. 1 Publication1
    Mutagenesisi198T → A, C, H or P: Strongly reduced activity. 5 Publications1
    Mutagenesisi198T → D or E: Strongly reduced activity, but enhanced zinc affinity. 5 Publications1
    Mutagenesisi198T → S or V: Reduced activity. 5 Publications1
    Mutagenesisi199T → H: Higher affinity for bicarbonate. Enhanced proton transfer capacity; when associated with A-64. 3 Publications1
    Mutagenesisi199T → S: Enhanced p-nitrophenyl acetate esterase activity, but normal CO(2) hydrase activity. 3 Publications1
    Mutagenesisi201P → A: Normal CO(2) hydrase activity, but impaired stability. 1 Publication1

    Keywords - Diseasei

    Disease mutation, Osteopetrosis

    Organism-specific databases

    DisGeNETi760.
    MalaCardsiCA2.
    MIMi259730. phenotype.
    OpenTargetsiENSG00000104267.
    Orphaneti2785. Osteopetrosis with renal tubular acidosis.
    PharmGKBiPA25989.

    Chemistry databases

    ChEMBLiCHEMBL205.
    DrugBankiDB00819. Acetazolamide.
    DB00436. Bendroflumethiazide.
    DB00562. Benzthiazide.
    DB01194. Brinzolamide.
    DB00880. Chlorothiazide.
    DB00606. Cyclothiazide.
    DB01119. Diazoxide.
    DB01144. Diclofenamide.
    DB00869. Dorzolamide.
    DB01031. Ethinamate.
    DB00695. Furosemide.
    DB00999. Hydrochlorothiazide.
    DB00774. Hydroflumethiazide.
    DB00703. Methazolamide.
    DB00232. Methyclothiazide.
    DB01325. Quinethazone.
    DB00273. Topiramate.
    DB01021. Trichlormethiazide.
    DB03904. Urea.
    DB00909. Zonisamide.

    Polymorphism and mutation databases

    BioMutaiCA2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved2 Publications
    ChainiPRO_00000774182 – 260Carbonic anhydrase 2Add BLAST259

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylserine2 Publications1
    Modified residuei2PhosphoserineBy similarity1
    Modified residuei165PhosphoserineCombined sources1
    Modified residuei172PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiP00918.
    PaxDbiP00918.
    PeptideAtlasiP00918.
    PRIDEiP00918.

    2D gel databases

    OGPiP00918.
    REPRODUCTION-2DPAGEIPI00218414.
    P00918.
    UCD-2DPAGEP00918.

    PTM databases

    iPTMnetiP00918.
    PhosphoSitePlusiP00918.

    Expressioni

    Gene expression databases

    BgeeiENSG00000104267.
    CleanExiHS_CA2.
    ExpressionAtlasiP00918. baseline and differential.
    GenevisibleiP00918. HS.

    Organism-specific databases

    HPAiCAB010102.
    HPA001550.

    Interactioni

    Subunit structurei

    Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity. Interacts with SLC26A6 isoform 4 (via C-terminus cytoplasmic domain).90 Publications

    Protein-protein interaction databases

    BioGridi107215. 14 interactors.
    IntActiP00918. 6 interactors.
    MINTiMINT-1367766.
    STRINGi9606.ENSP00000285379.

    Chemistry databases

    BindingDBiP00918.

    Structurei

    Secondary structure

    1260
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni9 – 11Combined sources3
    Turni13 – 15Combined sources3
    Helixi16 – 18Combined sources3
    Helixi21 – 24Combined sources4
    Beta strandi25 – 27Combined sources3
    Beta strandi31 – 33Combined sources3
    Turni35 – 37Combined sources3
    Beta strandi38 – 40Combined sources3
    Beta strandi42 – 44Combined sources3
    Beta strandi45 – 50Combined sources6
    Beta strandi56 – 61Combined sources6
    Beta strandi63 – 70Combined sources8
    Beta strandi73 – 75Combined sources3
    Beta strandi77 – 82Combined sources6
    Beta strandi88 – 97Combined sources10
    Beta strandi106 – 109Combined sources4
    Beta strandi115 – 124Combined sources10
    Helixi125 – 127Combined sources3
    Helixi130 – 133Combined sources4
    Beta strandi139 – 151Combined sources13
    Helixi154 – 156Combined sources3
    Helixi157 – 162Combined sources6
    Helixi163 – 165Combined sources3
    Beta strandi172 – 174Combined sources3
    Helixi180 – 183Combined sources4
    Beta strandi190 – 195Combined sources6
    Beta strandi206 – 213Combined sources8
    Beta strandi215 – 217Combined sources3
    Helixi219 – 225Combined sources7
    Turni226 – 228Combined sources3
    Beta strandi229 – 231Combined sources3
    Beta strandi233 – 235Combined sources3
    Beta strandi256 – 258Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    12CAX-ray2.40A1-260[»]
    1A42X-ray2.25A2-260[»]
    1AM6X-ray2.00A2-260[»]
    1AVNX-ray2.00A2-260[»]
    1BCDX-ray1.90A2-260[»]
    1BICX-ray1.90A2-260[»]
    1BN1X-ray2.10A2-260[»]
    1BN3X-ray2.20A2-260[»]
    1BN4X-ray2.10A2-260[»]
    1BNMX-ray2.60A2-260[»]
    1BNNX-ray2.30A2-260[»]
    1BNQX-ray2.40A2-260[»]
    1BNTX-ray2.15A2-260[»]
    1BNUX-ray2.15A2-260[»]
    1BNVX-ray2.40A2-260[»]
    1BNWX-ray2.25A2-260[»]
    1BV3X-ray1.85A2-260[»]
    1CA2X-ray2.00A2-260[»]
    1CA3X-ray2.30A1-260[»]
    1CAHX-ray1.88A2-260[»]
    1CAIX-ray1.80A2-260[»]
    1CAJX-ray1.90A2-260[»]
    1CAKX-ray1.90A2-260[»]
    1CALX-ray2.20A2-260[»]
    1CAMX-ray1.70A2-260[»]
    1CANX-ray1.90A2-260[»]
    1CAOX-ray1.90A2-260[»]
    1CAYX-ray2.10A2-260[»]
    1CAZX-ray1.90A2-260[»]
    1CCSX-ray2.35A2-260[»]
    1CCTX-ray2.20A2-260[»]
    1CCUX-ray2.25A2-260[»]
    1CILX-ray1.60A2-260[»]
    1CIMX-ray2.10A2-260[»]
    1CINX-ray2.10A2-260[»]
    1CNBX-ray2.35A2-260[»]
    1CNCX-ray2.20A2-260[»]
    1CNGX-ray1.90A2-260[»]
    1CNHX-ray2.05A2-260[»]
    1CNIX-ray1.80A2-260[»]
    1CNJX-ray1.80A2-260[»]
    1CNKX-ray2.15A2-260[»]
    1CNWX-ray2.00A1-260[»]
    1CNXX-ray1.90A1-260[»]
    1CNYX-ray2.30A1-260[»]
    1CRAX-ray1.90A2-260[»]
    1CVAX-ray2.25A2-260[»]
    1CVBX-ray2.40A2-260[»]
    1CVCX-ray2.30A2-260[»]
    1CVDX-ray2.20A5-259[»]
    1CVEX-ray2.25A2-260[»]
    1CVFX-ray2.25A2-260[»]
    1CVHX-ray2.30A5-259[»]
    1DCAX-ray2.20A1-260[»]
    1DCBX-ray2.10A1-260[»]
    1EOUX-ray2.10A1-260[»]
    1F2WX-ray1.90A2-260[»]
    1FQLX-ray2.00A1-260[»]
    1FQMX-ray2.00A1-260[»]
    1FQNX-ray2.00A1-260[»]
    1FQRX-ray2.00A1-260[»]
    1FR4X-ray1.60A1-260[»]
    1FR7X-ray1.50A/B1-260[»]
    1FSNX-ray2.00A/B1-260[»]
    1FSQX-ray2.00A/B1-260[»]
    1FSRX-ray2.00A/B1-260[»]
    1G0EX-ray1.60A1-260[»]
    1G0FX-ray1.60A1-260[»]
    1G1DX-ray2.04A2-260[»]
    1G3ZX-ray1.86A2-260[»]
    1G45X-ray1.83A2-260[»]
    1G46X-ray1.84A2-260[»]
    1G48X-ray1.86A2-260[»]
    1G4JX-ray1.84A2-260[»]
    1G4OX-ray1.96A2-260[»]
    1G52X-ray1.80A2-260[»]
    1G53X-ray1.94A2-260[»]
    1G54X-ray1.86A2-260[»]
    1H4NX-ray2.00A2-260[»]
    1H9NX-ray1.85A2-260[»]
    1H9QX-ray2.20A2-260[»]
    1HCAX-ray2.30A1-260[»]
    1HEAX-ray2.00A1-260[»]
    1HEBX-ray2.00A1-260[»]
    1HECX-ray2.00A1-260[»]
    1HEDX-ray2.00A1-260[»]
    1HVAX-ray2.30A1-260[»]
    1I8ZX-ray1.93A2-260[»]
    1I90X-ray2.00A2-260[»]
    1I91X-ray2.00A2-260[»]
    1I9LX-ray1.93A2-260[»]
    1I9MX-ray1.84A2-260[»]
    1I9NX-ray1.86A2-260[»]
    1I9OX-ray1.86A2-260[»]
    1I9PX-ray1.92A2-260[»]
    1I9QX-ray1.80A2-260[»]
    1IF4X-ray1.93A2-260[»]
    1IF5X-ray2.00A2-260[»]
    1IF6X-ray2.09A2-259[»]
    1IF7X-ray1.98A2-260[»]
    1IF8X-ray1.94A2-260[»]
    1IF9X-ray2.00A2-260[»]
    1KWQX-ray2.60A1-260[»]
    1KWRX-ray2.25A1-260[»]
    1LG5X-ray1.75A1-260[»]
    1LG6X-ray2.20A1-260[»]
    1LGDX-ray1.90A1-260[»]
    1LUGX-ray0.95A2-260[»]
    1LZVX-ray2.30A1-260[»]
    1MOOX-ray1.05A1-260[»]
    1MUAX-ray1.70A4-259[»]
    1OKLX-ray2.10A2-260[»]
    1OKMX-ray2.20A2-260[»]
    1OKNX-ray2.40A2-260[»]
    1OQ5X-ray1.50A2-259[»]
    1RAYX-ray1.80A2-260[»]
    1RAZX-ray1.90A2-260[»]
    1RZAX-ray1.90A2-260[»]
    1RZBX-ray1.80A2-260[»]
    1RZCX-ray1.90A2-260[»]
    1RZDX-ray1.90A2-260[»]
    1RZEX-ray1.90A2-260[»]
    1T9NX-ray2.00A1-259[»]
    1TB0X-ray2.00X1-259[»]
    1TBTX-ray2.00X1-259[»]
    1TE3X-ray2.00X1-260[»]
    1TEQX-ray2.00X1-260[»]
    1TEUX-ray2.00X1-260[»]
    1TG3X-ray1.80A1-260[»]
    1TG9X-ray1.90A1-260[»]
    1TH9X-ray1.63A1-260[»]
    1THKX-ray1.80A1-260[»]
    1TTMX-ray1.95A2-259[»]
    1UGAX-ray2.00A3-260[»]
    1UGBX-ray2.00A3-260[»]
    1UGCX-ray2.00A3-260[»]
    1UGDX-ray2.00A3-260[»]
    1UGEX-ray1.90A3-260[»]
    1UGFX-ray2.00A3-260[»]
    1UGGX-ray2.20A3-260[»]
    1XEGX-ray1.81A1-260[»]
    1XEVX-ray2.20A/B/C/D1-260[»]
    1XPZX-ray2.02A3-260[»]
    1XQ0X-ray1.76A2-260[»]
    1YDAX-ray2.10A2-260[»]
    1YDBX-ray1.90A2-260[»]
    1YDCX-ray1.95A2-260[»]
    1YDDX-ray2.10A2-260[»]
    1YO0X-ray1.80A1-260[»]
    1YO1X-ray1.70A1-260[»]
    1YO2X-ray1.80A1-259[»]
    1Z9YX-ray1.66A2-259[»]
    1ZE8X-ray2.00A2-260[»]
    1ZFKX-ray1.56A2-259[»]
    1ZFQX-ray1.55A2-259[»]
    1ZGEX-ray1.65A2-259[»]
    1ZGFX-ray1.75A2-259[»]
    1ZH9X-ray1.70A2-259[»]
    1ZSAX-ray2.50A2-260[»]
    1ZSBX-ray2.00A2-260[»]
    1ZSCX-ray1.80A2-260[»]
    2ABEX-ray2.00A2-259[»]
    2AW1X-ray1.46A2-260[»]
    2AX2X-ray1.50A1-259[»]
    2CA2X-ray1.90A2-260[»]
    2CBAX-ray1.54A2-260[»]
    2CBBX-ray1.67A2-260[»]
    2CBCX-ray1.88A2-260[»]
    2CBDX-ray1.67A2-260[»]
    2CBEX-ray1.82A2-260[»]
    2EU2X-ray1.15A1-260[»]
    2EU3X-ray1.60A1-260[»]
    2EZ7X-ray2.00A1-259[»]
    2F14X-ray1.71A2-259[»]
    2FMGX-ray1.60A1-259[»]
    2FMZX-ray1.60A1-259[»]
    2FNKX-ray1.80A1-260[»]
    2FNMX-ray1.80A1-260[»]
    2FNNX-ray1.80A1-260[»]
    2FOQX-ray1.25A1-259[»]
    2FOSX-ray1.10A1-259[»]
    2FOUX-ray0.99A1-259[»]
    2FOVX-ray1.15A1-259[»]
    2GD8X-ray1.46A2-259[»]
    2GEHX-ray2.00A1-259[»]
    2H15X-ray1.90A1-259[»]
    2H4NX-ray1.90A2-260[»]
    2HD6X-ray1.80A2-259[»]
    2HKKX-ray1.90A1-260[»]
    2HL4X-ray1.55A2-260[»]
    2HNCX-ray1.55A2-259[»]
    2HOCX-ray2.10A2-259[»]
    2ILIX-ray1.05A2-259[»]
    2NNGX-ray1.20A2-260[»]
    2NNOX-ray1.01A2-260[»]
    2NNSX-ray1.03A2-260[»]
    2NNVX-ray1.10A2-260[»]
    2NWOX-ray1.70A1-259[»]
    2NWPX-ray1.80A1-259[»]
    2NWYX-ray1.65A1-259[»]
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    3U3AX-ray1.55X1-260[»]