eF-site ID 3pvn-FGHIJKLMNO PDB Code 3pvn Chain F, G, H, I, J, K, L, M, N, O click to enlarge Title Triclinic form of Human C-Reactive Protein in complex with Zinc Classification IMMUNE SYSTEM Compound C-reactive protein Source Homo sapiens (Human) (CRP_HUMAN) Sequence F:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP G:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP H:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP I:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP J:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP K:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP L:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP M:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP N:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP O:  QTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFY TELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGS EILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKS LKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVN MWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFT KPQLWP Description Functional site 1) chain F residue 60 type sequence D description BINDING SITE FOR RESIDUE CA F 5011 source : BC3 2) chain F residue 138 type sequence E description BINDING SITE FOR RESIDUE CA F 5012 source : BC4 3) chain G residue 60 type sequence D description BINDING SITE FOR RESIDUE CA G 5013 source : BC5 4) chain G residue 61 type sequence N description BINDING SITE FOR RESIDUE CA G 5013 source : BC5 5) chain G residue 138 type sequence E description BINDING SITE FOR RESIDUE CA G 5013 source : BC5 6) chain G residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA G 5013 source : BC5 7) chain G residue 140 type sequence D description BINDING SITE FOR RESIDUE CA G 5013 source : BC5 8) chain G residue 138 type sequence E description BINDING SITE FOR RESIDUE CA G 5014 source : BC6 9) chain G residue 140 type sequence D description BINDING SITE FOR RESIDUE CA G 5014 source : BC6 10) chain G residue 147 type sequence E description BINDING SITE FOR RESIDUE CA G 5014 source : BC6 11) chain G residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA G 5014 source : BC6 12) chain G residue 38 type sequence H description BINDING SITE FOR RESIDUE ZN G 6002 source : BC7 13) chain H residue 60 type sequence D description BINDING SITE FOR RESIDUE CA H 5015 source : BC8 14) chain H residue 61 type sequence N description BINDING SITE FOR RESIDUE CA H 5015 source : BC8 15) chain H residue 138 type sequence E description BINDING SITE FOR RESIDUE CA H 5015 source : BC8 16) chain H residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA H 5015 source : BC8 17) chain H residue 140 type sequence D description BINDING SITE FOR RESIDUE CA H 5015 source : BC8 18) chain H residue 138 type sequence E description BINDING SITE FOR RESIDUE CA H 5016 source : BC9 19) chain H residue 140 type sequence D description BINDING SITE FOR RESIDUE CA H 5016 source : BC9 20) chain H residue 147 type sequence E description BINDING SITE FOR RESIDUE CA H 5016 source : BC9 21) chain H residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA H 5016 source : BC9 22) chain I residue 60 type sequence D description BINDING SITE FOR RESIDUE CA I 5017 source : CC1 23) chain I residue 61 type sequence N description BINDING SITE FOR RESIDUE CA I 5017 source : CC1 24) chain I residue 138 type sequence E description BINDING SITE FOR RESIDUE CA I 5017 source : CC1 25) chain I residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA I 5017 source : CC1 26) chain I residue 140 type sequence D description BINDING SITE FOR RESIDUE CA I 5017 source : CC1 27) chain I residue 138 type sequence E description BINDING SITE FOR RESIDUE CA I 5018 source : CC2 28) chain I residue 140 type sequence D description BINDING SITE FOR RESIDUE CA I 5018 source : CC2 29) chain I residue 147 type sequence E description BINDING SITE FOR RESIDUE CA I 5018 source : CC2 30) chain I residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA I 5018 source : CC2 31) chain J residue 140 type sequence D description BINDING SITE FOR RESIDUE CA J 5019 source : CC3 32) chain M residue 16 type sequence D description BINDING SITE FOR RESIDUE CA J 5019 source : CC3 33) chain J residue 60 type sequence D description BINDING SITE FOR RESIDUE CA J 5020 source : CC4 34) chain J residue 61 type sequence N description BINDING SITE FOR RESIDUE CA J 5020 source : CC4 35) chain J residue 138 type sequence E description BINDING SITE FOR RESIDUE CA J 5020 source : CC4 36) chain J residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA J 5020 source : CC4 37) chain J residue 140 type sequence D description BINDING SITE FOR RESIDUE CA J 5020 source : CC4 38) chain K residue 60 type sequence D description BINDING SITE FOR RESIDUE CA K 5021 source : CC5 39) chain K residue 61 type sequence N description BINDING SITE FOR RESIDUE CA K 5021 source : CC5 40) chain K residue 138 type sequence E description BINDING SITE FOR RESIDUE CA K 5021 source : CC5 41) chain K residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA K 5021 source : CC5 42) chain K residue 140 type sequence D description BINDING SITE FOR RESIDUE CA K 5021 source : CC5 43) chain K residue 138 type sequence E description BINDING SITE FOR RESIDUE CA K 5022 source : CC6 44) chain K residue 140 type sequence D description BINDING SITE FOR RESIDUE CA K 5022 source : CC6 45) chain K residue 147 type sequence E description BINDING SITE FOR RESIDUE CA K 5022 source : CC6 46) chain K residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA K 5022 source : CC6 47) chain L residue 60 type sequence D description BINDING SITE FOR RESIDUE CA L 5023 source : CC7 48) chain L residue 61 type sequence N description BINDING SITE FOR RESIDUE CA L 5023 source : CC7 49) chain L residue 138 type sequence E description BINDING SITE FOR RESIDUE CA L 5023 source : CC7 50) chain L residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA L 5023 source : CC7 51) chain L residue 140 type sequence D description BINDING SITE FOR RESIDUE CA L 5023 source : CC7 52) chain L residue 138 type sequence E description BINDING SITE FOR RESIDUE CA L 5024 source : CC8 53) chain L residue 140 type sequence D description BINDING SITE FOR RESIDUE CA L 5024 source : CC8 54) chain L residue 147 type sequence E description BINDING SITE FOR RESIDUE CA L 5024 source : CC8 55) chain L residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA L 5024 source : CC8 56) chain L residue 38 type sequence H description BINDING SITE FOR RESIDUE ZN L 6003 source : CC9 57) chain L residue 206 type sequence P description BINDING SITE FOR RESIDUE ZN L 6003 source : CC9 58) chain M residue 60 type sequence D description BINDING SITE FOR RESIDUE CA M 5025 source : DC1 59) chain M residue 61 type sequence N description BINDING SITE FOR RESIDUE CA M 5025 source : DC1 60) chain M residue 138 type sequence E description BINDING SITE FOR RESIDUE CA M 5025 source : DC1 61) chain M residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA M 5025 source : DC1 62) chain M residue 140 type sequence D description BINDING SITE FOR RESIDUE CA M 5025 source : DC1 63) chain M residue 138 type sequence E description BINDING SITE FOR RESIDUE CA M 5026 source : DC2 64) chain M residue 140 type sequence D description BINDING SITE FOR RESIDUE CA M 5026 source : DC2 65) chain M residue 147 type sequence E description BINDING SITE FOR RESIDUE CA M 5026 source : DC2 66) chain M residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA M 5026 source : DC2 67) chain N residue 60 type sequence D description BINDING SITE FOR RESIDUE CA N 5027 source : DC3 68) chain N residue 61 type sequence N description BINDING SITE FOR RESIDUE CA N 5027 source : DC3 69) chain N residue 138 type sequence E description BINDING SITE FOR RESIDUE CA N 5027 source : DC3 70) chain N residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA N 5027 source : DC3 71) chain N residue 140 type sequence D description BINDING SITE FOR RESIDUE CA N 5027 source : DC3 72) chain N residue 138 type sequence E description BINDING SITE FOR RESIDUE CA N 5028 source : DC4 73) chain N residue 140 type sequence D description BINDING SITE FOR RESIDUE CA N 5028 source : DC4 74) chain N residue 147 type sequence E description BINDING SITE FOR RESIDUE CA N 5028 source : DC4 75) chain N residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA N 5028 source : DC4 76) chain O residue 60 type sequence D description BINDING SITE FOR RESIDUE CA O 5029 source : DC5 77) chain O residue 61 type sequence N description BINDING SITE FOR RESIDUE CA O 5029 source : DC5 78) chain O residue 138 type sequence E description BINDING SITE FOR RESIDUE CA O 5029 source : DC5 79) chain O residue 139 type sequence Q description BINDING SITE FOR RESIDUE CA O 5029 source : DC5 80) chain O residue 140 type sequence D description BINDING SITE FOR RESIDUE CA O 5029 source : DC5 81) chain O residue 138 type sequence E description BINDING SITE FOR RESIDUE CA O 5030 source : DC6 82) chain O residue 140 type sequence D description BINDING SITE FOR RESIDUE CA O 5030 source : DC6 83) chain O residue 147 type sequence E description BINDING SITE FOR RESIDUE CA O 5030 source : DC6 84) chain O residue 150 type sequence Q description BINDING SITE FOR RESIDUE CA O 5030 source : DC6 85) chain F residue 147 type sequence E description BINDING SITE FOR RESIDUE CA P 5031 source : DC7 86) chain F residue 147 type sequence E description BINDING SITE FOR RESIDUE CA P 5032 source : DC8 87) chain G residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 88) chain G residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 89) chain G residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 90) chain G residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 91) chain G residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 92) chain H residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 93) chain H residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 94) chain H residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 95) chain H residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 96) chain H residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 97) chain H residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 98) chain I residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 99) chain I residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 100) chain I residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 101) chain I residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 102) chain I residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 103) chain I residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 104) chain J residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 105) chain J residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 106) chain J residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 107) chain J residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 108) chain J residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 109) chain J residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 110) chain K residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 111) chain K residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 112) chain K residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 113) chain K residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 114) chain K residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 115) chain K residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 116) chain L residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 117) chain L residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 118) chain L residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 119) chain L residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 120) chain L residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 121) chain L residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 122) chain M residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 123) chain M residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 124) chain M residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 125) chain M residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 126) chain M residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 127) chain M residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 128) chain N residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 129) chain N residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 130) chain N residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 131) chain N residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 132) chain N residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 133) chain N residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 134) chain O residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 135) chain O residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 136) chain O residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 137) chain O residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 138) chain O residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 139) chain O residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 140) chain F residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 141) chain F residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 142) chain F residue 138 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 143) chain F residue 139 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 144) chain F residue 140 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 145) chain F residue 150 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 146) chain G residue 60 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01172 source Swiss-Prot : SWS_FT_FI1 147) chain F residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 148) chain J residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 149) chain K residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 150) chain L residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 151) chain M residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 152) chain N residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 153) chain O residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 154) chain G residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 155) chain H residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2 156) chain I residue 1 type MOD_RES sequence Q description Pyrrolidone carboxylic acid => ECO:0000269|PubMed:762075 source Swiss-Prot : SWS_FT_FI2

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