match no.target idtarget lengthalignment lengthprobabilityE-valuecoveragematch description
11ENA_A13513199.86.8E-22[       ----------------------                    ]STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTATION WITH; HYDROLASE(PHOSPHORIC DIESTER); 2.15A {Staphylococcus aureus} SCOP: b.40.1.1
24HMJ_A14312999.82.8E-19[      -----------------------                    ]Thermonuclease (E.C.3.1.31.1); nuclease, hyperstable, pdTp, ionizable group; HET: THP; 1.35A {Staphylococcus aureus}
34QMG_D32513799.82E-18[       ----------------------                    ]Staphylococcal nuclease domain-containing protein 1; SN domains, oligonucleotide/oligosaccharide binding-fold (OB-fold); HET: SO4, GOL; 2.701A {Homo sapiens}
44QMG_C32513699.81.6E-18[       ----------------------                    ]Staphylococcal nuclease domain-containing protein 1; SN domains, oligonucleotide/oligosaccharide binding-fold (OB-fold); HET: GOL, SO4; 2.701A {Homo sapiens}
54QMG_C32513599.67.4E-17[      -----------------------                    ]Staphylococcal nuclease domain-containing protein 1; SN domains, oligonucleotide/oligosaccharide binding-fold (OB-fold); HET: GOL, SO4; 2.701A {Homo sapiens}
64QMG_D32513599.67.4E-17[      -----------------------                    ]Staphylococcal nuclease domain-containing protein 1; SN domains, oligonucleotide/oligosaccharide binding-fold (OB-fold); HET: SO4, GOL; 2.701A {Homo sapiens}
71RKN_A11010099.53E-15[       -----------------                         ]Thermonuclease (E.C.3.1.31.1); staphylococcal nuclease, folding, G88W110, HYDROLASE; NMR {Staphylococcus aureus} SCOP: b.40.1.1
83BDL_A57013799.52.8E-14[      -----------------------                    ]Staphylococcal nuclease domain-containing protein 1; Staphylococcal nuclease OB fold, Tudor; HET: CIT; 1.9A {Homo sapiens}
93UMN_B1239399.32.1E-11[                                ---------------  ]Lamin-B1; Structural Genomics Consortium, SGC, Ig-like; 2.0A {Homo sapiens}
102KPW_A1229399.32.2E-11[                                ---------------  ]Lamin-B1; PSI-2, NESG, HR5546A, Lamin-B1, GFT; NMR {Homo sapiens}
111IFR_A1219399.26.5E-11[                                ---------------  ]Lamin A/C; immunoglobulin, IMMUNE SYSTEM; 1.4A {Homo sapiens} SCOP: b.1.16.1
123GEF_D1189599.17.8E-10[                                ---------------  ]Lamin-A/C; immunoglobulin fold, lamin, Cardiomyopathy, Charcot-Marie-Tooth; 1.5A {Homo sapiens}
131UFG_A1519399.04E-09[                                ---------------  ]Lamin A; immunoglobulin like fold, nuclear lamin; NMR {Mus musculus} SCOP: b.1.16.1
143BDL_A57013098.91.6E-09[       ----------------------                    ]Staphylococcal nuclease domain-containing protein 1; Staphylococcal nuclease OB fold, Tudor; HET: CIT; 1.9A {Homo sapiens}
152LLL_A1399298.81.4E-08[                                ---------------  ]Lamin-B2; immunoglobulin-like fold, structural protein, NESG; NMR {Homo sapiens}
162HQX_B24612298.43.2E-07[       ----------------------                    ]CRYSTAL STRUCTURE OF HUMAN P100; HUMAN P100 TUDOR DOMAIN, PROTEOLYTIC; 1.42A {Homo sapiens} SCOP: b.34.9.1
175M9O_A22412398.02.8E-05[       ----------------------                    ]Staphylococcal nuclease domain-containing protein 1; Transcriptional coactivator, Structural Genomics, Structural; HET: 2MR; 1.45A {Homo sapiens}
182WAC_A21812298.02.9E-05[       ----------------------                    ]CG7008-PA; UNKNOWN FUNCTION, TUDOR, BETA-BARREL, NUCLEASE; 2.1A {DROSOPHILA MELANOGASTER}
192O4X_A21712997.94.7E-05[       ----------------------                    ]Staphylococcal nuclease domain-containing protein 1; OB fold, beta barrel, aromatic; 2.0A {Homo sapiens}
202KHS_B352597.20.00025[                         ----                    ]Thermonuclease (E.C.3.1.31.1), Nuclease; HYDROLASE, Endonuclease, Membrane, Metal-binding, Nuclease; NMR {Staphylococcus aureus}
211XQ4_A1398584.85.1[                              -------------      ]Protein apaG; all beta protein, Structural Genomics; HET: PO4; 2.7A {Bordetella pertussis} SCOP: b.1.23.1
222CO6_B2215283.72.9[                                ---------        ]PUTATIVE OUTER MEMBRANE PROTEIN, PUTATIVE; PILUS SUBUNIT, ADHESION, STRAND COMPLEMENTATION; 2.0A {SALMONELLA TYPHIMURIUM} SCOP: b.1.11.1, b.7.2.1
232CO7_B2215283.62.9[                                ---------        ]SAFA PILUS SUBUNIT, PUTATIVE FIMBRIAE; PILUS SUBUNIT, CHAPERONE, ADHESION, STRAND; HET: SO4; 1.8A {SALMONELLA TYPHIMURIUM} SCOP: b.1.11.1, b.7.2.1
243DPA_A2185483.23.6[                                  --------       ]PAPD; CHAPERONE PROTEIN; 2.5A {Escherichia coli} SCOP: b.7.2.1, b.1.11.1
251TZA_B1346282.86.1[                                  ---------      ]apaG protein; STRUCTURAL GENOMICS, PSI, Protein Structure; 2.4A {Shewanella oneidensis} SCOP: b.1.23.1
261XQ4_B1398481.45.1[                              -------------      ]Protein apaG; all beta protein, Structural Genomics; HET: PO4; 2.7A {Bordetella pertussis} SCOP: b.1.23.1
271TZA_A1346381.36.1[                                  ---------      ]apaG protein; STRUCTURAL GENOMICS, PSI, Protein Structure; 2.4A {Shewanella oneidensis} SCOP: b.1.23.1
282QSV_A2204578.66.5[                                 -------         ]Uncharacterized protein; MCSG, structural genomics, Porphyromonas gingivalis; 2.1A {Porphyromonas gingivalis}
295GHU_A2225176.08.5[                                ---------        ]Probable fimbrial chaperone YadV; CU chaperone, fimbriae, pilin, CHAPERONE; HET: ACT, PGE; 1.63A {Escherichia coli K-12}
302F1E_A1277874.123[                               ------------      ]Protein apaG; ApaG protein, Xanthomonas axonopodis pv.citri; NMR {Xanthomonas axonopodis pv. citri}
313DPA_A2185371.713[                                ---------        ]PAPD; CHAPERONE PROTEIN; 2.5A {Escherichia coli} SCOP: b.7.2.1, b.1.11.1
324DJM_D2395169.47.1[                                --------         ]E. coli chaperone DraB; DraB, Chaperone, Pili; 2.52A {Escherichia coli}
334DJM_G2395168.47.1[                                --------         ]E. coli chaperone DraB; DraB, Chaperone, Pili; 2.52A {Escherichia coli}
341XVS_A1266367.729[                                  ---------      ]Protein apaG; apaG, MCSG APC26324, Midwest Center; 2.01A {Vibrio cholerae} SCOP: b.1.23.1
352XG5_A2185267.318[                                ---------        ]CHAPERONE PROTEIN PAPD, PAP FIMBRIAL; CHAPERONE, CHAPERONE-SURFACE ACTIVE PROTEIN COMPLEX; HET: EC5, EC2; 2.0A {ESCHERICHIA COLI}
364AJY_V1636266.022[                                  ------------   ]TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE; E3 UBIQUITIN LIGASE, TRANSCRIPTION FACTOR; 1.73A {HOMO SAPIENS}
372XG5_A2185464.67.3[                                  --------       ]CHAPERONE PROTEIN PAPD, PAP FIMBRIAL; CHAPERONE, CHAPERONE-SURFACE ACTIVE PROTEIN COMPLEX; HET: EC5, EC2; 2.0A {ESCHERICHIA COLI}
381LM8_V1606264.025[                                  ------------   ]elongin B, elongin C, Von; REGULATION, tumor suppressor, oxygen sensing; 1.85A {Homo sapiens} SCOP: b.3.3.1
393Q48_A2575162.718[                                --------         ]Chaperone CupB2; Ig fold, periplasmic chaperone, CupB1; 2.5A {Pseudomonas aeruginosa}
401KIU_G2055160.436[                                --------         ]CHAPERONE PROTEIN FIMC/FIMH PROTEIN COMPLEX; adhesin-chaperone complex, mannose-bound, CHAPERONE-CELL ADHESION; HET: MMA; 3.0A {Escherichia coli} SCOP: b.7.2.1, b.1.11.1
415DFK_A2176460.020[                                 ---------       ]Probable fimbrial chaperone EcpB; chaperone usher, pilus, pili, biofilm; 2.4A {Escherichia coli}
424AY0_A2185358.624[                                ---------        ]CHAPERONE PROTEIN CAF1M; CHAPERONE, AMINO ACID MOTIFS, BACTERIAL; 1.52A {YERSINIA PESTIS}
433FLD_B1532457.36.5[                                            ---- ]Protein traI (E.C.3.6.1.-); NOVEL ALPHA/BETA CORE DOMAIN, ALTERNATIVE; HET: SO4; 2.4A {Escherichia coli K-12}
441OK0_A745556.285[                               ----------        ]ALPHA-AMYLASE INHIBITOR HOE-467A; INHIBITOR, ALPHA AMYLASE INHIBITOR; HET: GOL; 0.93A {STREPTOMYCES TENDAE} SCOP: b.5.1.1
452K6Y_A1208756.128[                                ---------------- ]Putative uncharacterized protein TTHA1943; PCuA, copper transfer protein, cis; NMR {Thermus thermophilus}
463ZJA_A1404456.139[                                       --------- ]SL3965; CHAPERONE; 1.48A {STREPTOMYCES LIVIDANS}
473BWU_C2055156.047[                                --------         ]FimD (N-Terminal Domain)/Chaperone protein FimC/the; Usher, N-terminal domain, ternary complex; HET: EDO; 1.76A {Escherichia coli} SCOP: b.7.2.1, b.1.11.1
483Q48_A2574454.717[                                  -------        ]Chaperone CupB2; Ig fold, periplasmic chaperone, CupB1; 2.5A {Pseudomonas aeruginosa}
493ZK0_A1404454.639[                                       --------- ]SCO3965; CHAPERONE, METALLOCHAPERONE; 1.7A {STREPTOMYCES LIVIDANS}
504PWW_A893953.939[        -------                                  ]OR494; Structural Genomics, PSI-Biology, Protein Structure; HET: ACY; 1.471A {synthetic construct}
515D6H_A2434953.343[                                 --------        ]CsuC, CsuA/B; archaic chaperone-usher pathway, Ig-like fold; HET: MSE; 2.4A {Acinetobacter baumannii}
525HDW_A1334752.372[                                  -------        ]F-box only protein 3; FBxo3, F-box, ApaG, FBxl2, PROTEIN; 2.0A {Homo sapiens}
534Y2O_A2316252.124[                                 ---------       ]CFA/I pili chaperone CfaA, CFA/I; Enterotoxigenic Escherichia coli, periplasmic chaperone; HET: PGE; 2.419A {Escherichia coli O78:H11 (strain H10407 / ETEC)}
545GHU_A2224551.427[                                  -------        ]Probable fimbrial chaperone YadV; CU chaperone, fimbriae, pilin, CHAPERONE; HET: ACT, PGE; 1.63A {Escherichia coli K-12}
552KER_A785551.396[                               ----------        ]Alpha-amylase inhibitor Z-2685; alpha-amylase inhibitor, Parvulustat (Z-2685), HYDROLASE; NMR {Streptomyces parvulus}
563GFU_A2245251.152[                                ---------        ]Chaperone protein faeE, FaeG; immunoglobulin like fold, Chaperone, Fimbrium; HET: SO4; 1.991A {Escherichia coli}
575AVG_A2065250.849[                                  ---------      ]Thaumatin-1; thaumatin, high-strength agarose, hydrogel, PLANT; 0.95A {Thaumatococcus daniellii}
582VHK_A2065150.849[                                  --------       ]THAUMATIN-I; KINETICS OF CRYSTALLIZATION, CHIRALITY, TEMPERATURE; HET: GOL, TLA; 0.94A {THAUMATOCOCCUS DANIELLII}
594NCD_A2466150.234[                                 ---------       ]Gram-negative pili assembly chaperone, N-terminal; immunoglobulin fold, chaperone; 2.037A {Escherichia coli}
603BWU_C2055147.472[                                  --------       ]FimD (N-Terminal Domain)/Chaperone protein FimC/the; Usher, N-terminal domain, ternary complex; HET: EDO; 1.76A {Escherichia coli} SCOP: b.7.2.1, b.1.11.1
613AIT_A745546.685[                               ----------        ]TENDAMISTAT (ENERGY MINIMIZED MODEL USING; ALPHA-AMYLASE INHIBITOR; NMR {Streptomyces tendae} SCOP: b.5.1.1
622WOO_C3294645.11.1E+02[               -------                           ]ATPASE GET3 (E.C.3.6.3.16); TAIL-ANCHORED, MEMBRANE PROTEIN, TARGETING FACTOR; 3.006A {SCHIZOSACCHAROMYCES POMBE}
635UDF_A2302544.540[        ----                                     ]Lipoprotein-releasing system transmembrane protein LolE; SSGCID, Acinetobacter baumannii, Lipoprotein-releasing system; 2.35A {Acinetobacter baumannii}
641ZEQ_X845642.769[                                ---------        ]Cation efflux system protein cusF; copper-binding, OB-fold, beta barrel, metallochaperone; 1.5A {Escherichia coli}
654B0M_M2355340.056[                                ---------        ]F1 CAPSULE-ANCHORING PROTEIN, F1 CAPSULE; PROTEIN TRANSPORT, CHAPERONE-USHER PATHWAY, PILI; 1.8A {YERSINIA PESTIS}
663O4F_C2944539.177[          -------                                ]Spermidine synthase (E.C.2.5.1.16); AMINOPROPYLTRANSFERASE, POLYAMINE SYNTHASE, ROSSMANN FOLD; HET: SO4; 2.9A {Escherichia coli}
672JQA_A1497239.052[                                  -------------- ]Hypothetical protein; COPPER BINDING PROTEIN, METAL BINDING; NMR {Deinococcus radiodurans} SCOP: b.2.10.1
683ISY_A1204239.076[                                  ------         ]Intracellular proteinase inhibitor; Intracellular proteinase inhibitor bsupi, beta; HET: PG4; 2.61A {Bacillus subtilis}
692MHG_A752238.094[        ---                                      ]Uncharacterized protein; gut microbiome, secreted protein, structural; NMR {Pseudomonas aeruginosa PAO1}
702KUT_A1224037.563[                                  ------         ]Uncharacterized protein; Structural Genomics, PSI-2, Protein Structure; NMR {Geobacter metallireducens}
711GY2_A1554636.637[                                 --------        ]RUSTICYANIN; S86D, M148L, RUSTICYANIN, MUTANT, METAL-BINDING; 1.82A {THIOBACILLUS FERROOXIDANS} SCOP: b.6.1.1
721Z9L_A1284236.51.2E+02[                                  ------         ]Vesicle-associated membrane protein-associated protein A; VAP-A, Cytoplasmic domain, PROTEIN BINDING; 1.7A {Rattus norvegicus}
732CO6_B2214135.985[                                  -------        ]PUTATIVE OUTER MEMBRANE PROTEIN, PUTATIVE; PILUS SUBUNIT, ADHESION, STRAND COMPLEMENTATION; 2.0A {SALMONELLA TYPHIMURIUM} SCOP: b.1.11.1, b.7.2.1
742QCP_X805535.51.4E+02[                                ---------        ]Cation efflux system protein cusF; silver-binding, copper-binding, beta barrel, OB-fold; HET: SO4; 1.0A {Escherichia coli str. K12 substr.}
754OLE_A1225234.771[                                  --------       ]Next to BRCA1 gene 1; Ig-like domain from next to; HET: SO4, EDO; 2.52A {Homo sapiens}
764OLE_B1225234.771[                                  --------       ]Next to BRCA1 gene 1; Ig-like domain from next to; HET: EDO, SO4; 2.52A {Homo sapiens}
773IQW_A3345834.777[             ---------                           ]Tail-anchored protein targeting factor Get3; Protein targeting, ATPase, tail-anchored protein; HET: ANP; 3.0A {Chaetomium thermophilum}
785D6H_A2435034.620[                                  --------       ]CsuC, CsuA/B; archaic chaperone-usher pathway, Ig-like fold; HET: MSE; 2.4A {Acinetobacter baumannii}
792CO7_B2214233.864[                                  -------        ]SAFA PILUS SUBUNIT, PUTATIVE FIMBRIAE; PILUS SUBUNIT, CHAPERONE, ADHESION, STRAND; HET: SO4; 1.8A {SALMONELLA TYPHIMURIUM} SCOP: b.1.11.1, b.7.2.1
803RGB_A41425233.772[      -------------------------------------------]Methane monooxygenase subunit B2 (E.C.1.14.13.25); membrane, OXIDOREDUCTASE; 2.8A {Methylococcus capsulatus}
812YS4_A1226333.51.5E+02[                                 -----------     ]Hydrocephalus-inducing protein homolog; HYDIN, PapD-like, NPPSFA, National Project; NMR {Homo sapiens}
821WIC_A1524333.31.5E+02[                                 -------         ]Hypothetical Protein RIKEN cDNA 6030424E15; beta sandwich fold, STRUCTURAL GENOMICS; NMR {Mus musculus} SCOP: b.1.11.2
834DJM_D2394132.994[                                  -------        ]E. coli chaperone DraB; DraB, Chaperone, Pili; 2.52A {Escherichia coli}
844DJM_G2394132.794[                                  -------        ]E. coli chaperone DraB; DraB, Chaperone, Pili; 2.52A {Escherichia coli}
851YEW_I3829032.785[                                 ----------------]methane monooxygenase, B subunit, methane; membrane protein, methane, beta barrel; 2.801A {Methylococcus capsulatus}
861R5E_A1153732.537[                 ------                          ]avirulence protein; three-helix bundle, omega loop, PROTEIN; NMR {Pseudomonas syringae} SCOP: a.8.8.1
872AHN_A2225031.91.1E+02[                                  --------       ]Thaumatin-like protein; Allergen, Thaumatin-like protein; 1.3A {Prunus avium}
883NRF_B1064031.61.2E+02[                                  ------         ]ApaG protein; Structural Genomics, Joint Center for; HET: MRD; 1.5A {Pseudomonas aeruginosa}
894B1L_A1652931.01.2E+02[      ----                                       ]LEVANASE (E.C.3.2.1.80); HYDROLASE, LEVAN; HET: FRU; 1.65A {BACILLUS SUBTILIS}
901WDD_A4773330.825[                        -----                    ]Ribulose bisphosphate carboxylase large chain(E.C.4.1.1.39)/Ribulose; Rubisco, Photosynthesis, alpha/beta barrel, N-methylmethionine; HET: GOL, CAP; 1.35A {Oryza sativa Japonica Group} SCOP: c.1.14.1, d.58.9.1
912E6J_A1126330.62.1E+02[                                  ----------     ]HYDIN protein; PapD, HYDIN, Structural Genomics, NPPSFA; NMR {Homo sapiens}
922WOJ_A3547830.41.3E+02[          -------------                          ]ATPASE GET3 (E.C.3.6.3.16); TAIL-ANCHORED, MEMBRANE PROTEIN, TARGETING FACTOR; HET: ALF, ADP; 1.994A {SACCHAROMYCES CEREVISIAE}
934L2J_A2064730.092[                                  ---------      ]Osmotin: antifungal laticifer protein; Osmotin-like proteins, laticifer proteins, pathogen; 1.61A {Calotropis procera}
943S5Q_A2143029.71.2E+02[      ----                                       ]Putative glycosylhydrolase; Concanavalin A-like lectins/glucanases, Structural Genomics; HET: EDO; 1.85A {Parabacteroides distasonis}
952BVU_C1264229.52.5E+02[                                  ------         ]MAJOR SPERM PROTEIN, ISOFORM ALPHA; CYTOSKETAL PROTEIN, MAJOR SPERM PROTEIN; 2.5A {ASCARIS SUUM}
963NRF_A1064028.71.2E+02[                                  ------         ]ApaG protein; Structural Genomics, Joint Center for; HET: MRD; 1.5A {Pseudomonas aeruginosa}
971DM9_A1332528.586[        ----                                     ]HYPOTHETICAL 15.5 KD PROTEIN IN; HEAT SHOCK PROTEINS, PROTEIN-RNA INTERACTIONS; HET: SO4; 2.0A {Escherichia coli} SCOP: d.66.1.3
983QFW_A3783228.453[                        -----                    ]Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit (E.C.4.1.1.39); Structural Genomics, PSI-2, Protein Structure; HET: SO4; 1.789A {Rhodopseudomonas palustris}
993QFW_B3783228.453[                        -----                    ]Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit (E.C.4.1.1.39); Structural Genomics, PSI-2, Protein Structure; HET: SO4; 1.789A {Rhodopseudomonas palustris}
1004PHZ_I4207328.286[      -----------                                ]peptide, pmoC, pmoB, pmoA; Bacterial Proteins, Binding Sites, Copper; HET: PGT; 2.59A {Methylocystis sp. ATCC 49242}
1012X3B_A3431828.11.2E+02[                                  --             ]TOXIC EXTRACELLULAR ENDOPEPTIDASE (E.C.3.4.24.39); HYDROLASE; 2.28A {AEROMONAS SALMONICIDA SUBSP. ACHROMOGENES}
1024B0M_M2354027.41.9E+02[                                  -------        ]F1 CAPSULE-ANCHORING PROTEIN, F1 CAPSULE; PROTEIN TRANSPORT, CHAPERONE-USHER PATHWAY, PILI; 1.8A {YERSINIA PESTIS}
1031OQ1_D2232827.31.1E+02[      ----                                       ]Protein yesU; Structural genomics, Singleton, PSI, Protein; HET: GOL, ACY; 1.7A {Bacillus subtilis} SCOP: b.29.1.17
1042P4V_B1583027.11E+02[       -----                                     ]Transcription elongation factor greB; Transcription, transcript cleavage, Gre-factors, RNA; 2.6A {Escherichia coli}
1053QBT_F1405326.83.2E+02[                                --------         ]Ras-related protein Rab-8A, Inositol polyphosphate; Protein transport, vesicular trafficking, GTPase; HET: SO4, GNP; 2.0A {Homo sapiens}
1064JOX_A1235526.62.9E+02[                                  --------       ]13.6 kDa insecticidal crystal protein; beta-sandwich, TOXIN; 2.15A {Bacillus thuringiensis}
1072X3C_A3431926.31.4E+02[                                  --             ]TOXIC EXTRACELLULAR ENDOPEPTIDASE (E.C.3.4.24.39); HYDROLASE; HET: SO4; 1.99A {AEROMONAS SALMONICIDA SUBSP. ACHROMOGENES}
1083IBG_D3483825.83.9E+02[                ------                           ]Arsenite translocating ATPase ArsA (E.C.3.6.3.16); nucleotide binding, hydrolase, deviant Walker; HET: ADP; 3.2A {Aspergillus fumigatus}
1091B2P_A1191825.860[                                      --         ]LECTIN; MANNOSE-BINDING LECTIN, MONOCOT, AGLUTININ, BLUEBELL; 1.7A {Hyacinthoides hispanica} SCOP: b.78.1.1
1103H43_C854225.11.6E+02[      -------                                    ]Proteasome-activating nucleotidase; Proteasome, regulatory particle, nucleosidase, ATP-binding; 2.1A {Methanocaldococcus jannaschii}
1113H43_I854225.11.6E+02[      -------                                    ]Proteasome-activating nucleotidase; Proteasome, regulatory particle, nucleosidase, ATP-binding; 2.1A {Methanocaldococcus jannaschii}
1124AY0_A2183925.02.8E+02[                                  -------        ]CHAPERONE PROTEIN CAF1M; CHAPERONE, AMINO ACID MOTIFS, BACTERIAL; 1.52A {YERSINIA PESTIS}
1133FK4_A4143424.938[                        -----                    ]RuBisCO-like protein (E.C.5.3.2.-); Structural genomics, RuBisCO-like protein. NYSGXRC; 2.0A {Bacillus cereus ATCC 14579}
1142QKW_A1641924.559[                 --                              ]Avirulence protein, Protein kinase (E.C.2.7.11.1); three-helix bundle motif, Avrpto-pto duplex; 3.2A {Pseudomonas syringae} SCOP: a.8.8.1
1153NRL_A811724.21.2E+02[        ---                                      ]uncharacterized protein RUMGNA_01417; beta protein, Structural Genomics, PSI-2; HET: SO4; 1.9A {Ruminococcus gnavus}
1163U1X_A2363024.11.7E+02[      ----                                       ]putative glycosyl hydrolase; glycosyl hydrolysis, carbohydrate metabolism,, Structural; HET: PGE; 1.7A {Parabacteroides distasonis}
1173U1X_B2363124.11.7E+02[     -----                                       ]putative glycosyl hydrolase; glycosyl hydrolysis, carbohydrate metabolism,, Structural; HET: PGE; 1.7A {Parabacteroides distasonis}
1185X8T_K1975123.958[                                       -------   ]50S ribosomal protein L31,50S ribosomal; Cryo-EM, ribosome, chloroplast ribosome; 3.3A {Spinacia oleracea}
1193KDN_C4443223.543[                        -----                    ]Ribulose bisphosphate carboxylase (E.C.4.1.1.39); ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco, Carbon dioxide; HET: CAP, MG; 2.09A {Thermococcus kodakaraensis}
1203FK4_B4143423.342[                        -----                    ]RuBisCO-like protein (E.C.5.3.2.-); Structural genomics, RuBisCO-like protein. NYSGXRC; 2.0A {Bacillus cereus ATCC 14579}
1211RBL_B4673223.352[                        -----                    ]RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (RUBISCO); LYASE(CARBON-CARBON), LYASE; HET: CAP, FMT; 2.2A {Synechococcus elongatus} SCOP: c.1.14.1, d.58.9.1
1224B1M_A1852823.21.7E+02[      ----                                       ]LEVANASE (E.C.3.2.1.80); HYDROLASE, CBM66; HET: FRU; 1.1A {BACILLUS SUBTILIS}
1233MSP_B1264223.13.1E+02[                                  ------         ]MAJOR SPERM PROTEIN; CELL MOTILITY PROTEIN, MAJOR SPERM; NMR {Ascaris suum} SCOP: b.1.11.2
1242EQU_A742223.02E+02[       ---                                       ]PHD finger protein 20-like 1; tudor domain, Structural Genomics, NPPSFA; NMR {Homo sapiens}
1251AUN_A2084922.81.5E+02[                                  ---------      ]PR-5D; ANTIFUNGAL PROTEIN, PATHOGENESIS-RELATED PROTEIN, PR-5D; 1.8A {Nicotiana tabacum} SCOP: b.25.1.1
1265VGZ_B734322.644[      -------                                    ]26S protease regulatory subunit 7; p28, 26S proteasome, regulatory particle; 3.7A {Homo sapiens}
1273G7M_A1515022.61.7E+02[                                  ---------      ]Xylanase inhibitor TL-XI; beta-sheets, Xylan degradation, HYDROLASE INHIBITOR; HET: GOL; 2.91A {Triticum aestivum}
1283U60_G2284522.01.3E+02[                                      --------   ]DNA polymerase accessory protein 44; AAA+, ATP hydrolase, sliding clamp; HET: 08T, ADP; 3.34A {Enterobacteria phage T4}
1292JV2_A832422.01.9E+02[        ---                                      ]Putative uncharacterized protein PH1500; AAA ATPASE NC-DOMAIN-LIKE, UNKNOWN FUNCTION; NMR {Pyrococcus horikoshii}
1301KIU_G2055221.41.8E+02[                                  --------       ]CHAPERONE PROTEIN FIMC/FIMH PROTEIN COMPLEX; adhesin-chaperone complex, mannose-bound, CHAPERONE-CELL ADHESION; HET: MMA; 3.0A {Escherichia coli} SCOP: b.7.2.1, b.1.11.1
1313A5U_A1302720.955[             ----                                ]Single-stranded DNA-binding protein/DNA complex; DNA binding protein, DNA damage; 2.8A {Mycobacterium smegmatis}
1323IMM_A2013020.62.1E+02[      ----                                       ]Putative secreted glycosylhydrolase; YP_001301887.1, Putative glycosyl hydrolase, Structural; 2.0A {Parabacteroides distasonis ATCC 8503}
1335MMI_K2505120.478[                                       -------   ]50S ribosomal protein L31, 50S; chloroplast, translation, ribosome, cryo-EM; HET: MG; 3.25A {Spinacia oleracea}
1345NV3_D4673220.455[                        -----                    ]Ribulose bisphosphate carboxylase large chain; beta barrel, lyase; HET: KCX, CAP; 3.39A {Rhodobacter sphaeroides}
1354UYT_A1823620.41.4E+02[        ------                                   ]FLOCCULATION PROTEIN FLO11; CELL ADHESION, ADHESIN, FLOCCULATION, HYDROPHOBIC; 1.03A {SACCHAROMYCES CEREVISIAE}
1363SJA_F3627820.43.2E+02[          -------------                          ]ATPase GET3 (E.C.3.6.-.-), Golgi to; Coiled-coil, receptor complex, TA-protein biogenesis; HET: PO4; 3.0A {Saccharomyces cerevisiae}
1373ZG9_A471520.187[                                            --   ]PENICILLIN-BINDING PROTEIN 4; PENICILLIN-BINDING PROTEIN; HET: DXF, GOL; 1.804A {LISTERIA MONOCYTOGENES}