eF-site ID 5nmf-ABCDEFGHIJ PDB Code 5nmf Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title 868 TCR in complex with HLA A02 presenting SLYNTIATL Classification IMMUNE SYSTEM Compound HLA class I histocompatibility antigen, A-2 alpha chain Source Homo sapiens (Human) (5NMF) Sequence A:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP B:  IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLL KNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDM C:  SLYNTIATL D:  KEVEQNSGPLSVPEGAIASLNCTYSDRGSQSFFWYRQYSG KSPELIMFIYSNGDKEDGRFTAQLNKASQYISLLIRDSKL SDSATYLCAVRTNSGYALNFGKGTSLLVTPHIQKPDPAVY QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVL DMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPS E:  AGVTQSPTHLIKTRGQQVTLRCSPKQGHDTVSWYQQALGQ GPQFIFQYYEEEERQRGNFPDRFSGHQFPNYSSELNVNAL LLGDSALYLCASSDTVSYEQYFGPGTRLTVTEDLKNVFPP EVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNG KEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQD PRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGR F:  GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP G:  MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM H:  SLYNTIATL I:  KEVEQNSGPLSVPEGAIASLNCTYSDRGSQSFFWYRQYSG KSPELIMFIYSNGDKEDGRFTAQLNKASQYISLLIRDSKL SDSATYLCAVRTNSGYALNFGKGTSLLVTPHIQKPDPAVY QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVL DMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPS P J:  AGVTQSPTHLIKTRGQQVTLRCSPKQGHDTVSWYQQALGQ GPQFIFQYYEEEERQRGNFPDRFSGHQFPNYSSELNVNAL LLGDSALYLCASSDTVSYEQYFGPGTRLTVTEDLKNVFPP EVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNG KEVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQD PRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRA Description Functional site 1) chain A residue 21 type sequence R description binding site for residue EDO A 301 source : AC1 2) chain B residue 51 type sequence H description binding site for residue EDO A 301 source : AC1 3) chain A residue 105 type sequence S description binding site for residue GOL A 302 source : AC2 4) chain A residue 271 type sequence T description binding site for residue SO4 A 303 source : AC3 5) chain A residue 273 type sequence R description binding site for residue SO4 A 303 source : AC3 6) chain E residue 235 type sequence A description binding site for residue SO4 A 303 source : AC3 7) chain E residue 236 type sequence E description binding site for residue SO4 A 303 source : AC3 8) chain A residue 191 type sequence H description binding site for residue SO4 A 304 source : AC4 9) chain A residue 192 type sequence H description binding site for residue SO4 A 304 source : AC4 10) chain A residue 193 type sequence A description binding site for residue SO4 A 304 source : AC4 11) chain A residue 151 type sequence H description binding site for residue SO4 A 305 source : AC5 12) chain A residue 152 type sequence V description binding site for residue SO4 A 305 source : AC5 13) chain A residue 153 type sequence A description binding site for residue SO4 A 305 source : AC5 14) chain A residue 154 type sequence E description binding site for residue SO4 A 305 source : AC5 15) chain A residue 167 type sequence W description binding site for residue SO4 A 306 source : AC6 16) chain D residue 28 type sequence R description binding site for residue SO4 A 306 source : AC6 17) chain D residue 60 type sequence R description binding site for residue EDO D 301 source : AC7 18) chain D residue 80 type sequence K description binding site for residue EDO D 301 source : AC7 19) chain D residue 7 type sequence N description binding site for residue GOL D 302 source : AC8 20) chain D residue 8 type sequence S description binding site for residue GOL D 302 source : AC8 21) chain D residue 103 type sequence K description binding site for residue GOL D 302 source : AC8 22) chain E residue 8 type sequence P description binding site for residue EDO E 301 source : AC9 23) chain E residue 10 type sequence H description binding site for residue EDO E 301 source : AC9 24) chain E residue 165 type sequence H description binding site for residue EDO E 302 source : AD1 25) chain E residue 166 type sequence S description binding site for residue EDO E 302 source : AD1 26) chain E residue 227 type sequence K description binding site for residue EDO E 303 source : AD2 27) chain E residue 15 type sequence R description binding site for residue SO4 E 304 source : AD3 28) chain E residue 84 type sequence G description binding site for residue SO4 E 304 source : AD3 29) chain E residue 17 type sequence Q description binding site for residue SO4 E 305 source : AD4 30) chain E residue 18 type sequence Q description binding site for residue SO4 E 305 source : AD4 31) chain E residue 61 type sequence P description binding site for residue SO4 E 306 source : AD5 32) chain E residue 63 type sequence R description binding site for residue SO4 E 306 source : AD5 33) chain E residue 15 type sequence R description binding site for residue SO4 E 307 source : AD6 34) chain E residue 15 type sequence R description binding site for residue SO4 E 307 source : AD6 35) chain E residue 82 type sequence L description binding site for residue SO4 E 307 source : AD6 36) chain E residue 82 type sequence L description binding site for residue SO4 E 307 source : AD6 37) chain E residue 83 type sequence L description binding site for residue SO4 E 307 source : AD6 38) chain E residue 83 type sequence L description binding site for residue SO4 E 307 source : AD6 39) chain E residue 84 type sequence G description binding site for residue SO4 E 307 source : AD6 40) chain E residue 84 type sequence G description binding site for residue SO4 E 307 source : AD6 41) chain F residue 21 type sequence R description binding site for residue EDO F 301 source : AD7 42) chain G residue 51 type sequence H description binding site for residue EDO F 301 source : AD7 43) chain F residue 35 type sequence R description binding site for residue EDO F 302 source : AD8 44) chain F residue 193 type sequence A description binding site for residue EDO F 303 source : AD9 45) chain F residue 166 type sequence E description binding site for residue EDO F 304 source : AE1 46) chain F residue 170 type sequence R description binding site for residue EDO F 304 source : AE1 47) chain F residue 87 type sequence Q description binding site for residue EDO F 305 source : AE2 48) chain F residue 88 type sequence S description binding site for residue EDO F 305 source : AE2 49) chain F residue 127 type sequence K description binding site for residue EDO F 306 source : AE3 50) chain F residue 135 type sequence A description binding site for residue EDO F 306 source : AE3 51) chain F residue 144 type sequence K description binding site for residue EDO F 306 source : AE3 52) chain F residue 86 type sequence N description binding site for residue SO4 F 307 source : AE4 53) chain J residue 164 type sequence V description binding site for residue SO4 F 307 source : AE4 54) chain J residue 165 type sequence H description binding site for residue SO4 F 307 source : AE4 55) chain J residue 166 type sequence S description binding site for residue SO4 F 307 source : AE4 56) chain F residue 131 type sequence R description binding site for residue SO4 F 308 source : AE5 57) chain F residue 151 type sequence H description binding site for residue SO4 F 308 source : AE5 58) chain F residue 153 type sequence A description binding site for residue SO4 F 308 source : AE5 59) chain F residue 154 type sequence E description binding site for residue SO4 F 308 source : AE5 60) chain F residue 127 type sequence K description binding site for residue EDO I 301 source : AE6 61) chain F residue 128 type sequence E description binding site for residue EDO I 301 source : AE6 62) chain I residue 180 type sequence S description binding site for residue EDO I 301 source : AE6 63) chain I residue 80 type sequence K description binding site for residue EDO I 302 source : AE7 64) chain I residue 81 type sequence L description binding site for residue EDO I 302 source : AE7 65) chain I residue 82 type sequence S description binding site for residue EDO I 302 source : AE7 66) chain I residue 60 type sequence R description binding site for residue GOL I 303 source : AE8 67) chain I residue 164 type sequence R description binding site for residue EDO J 301 source : AE9 68) chain J residue 168 type sequence V description binding site for residue EDO J 301 source : AE9 69) chain G residue 4 type sequence T description binding site for residue EDO J 303 source : AF1 70) chain J residue 116 type sequence K description binding site for residue EDO J 303 source : AF1 71) chain J residue 221 type sequence W description binding site for residue EDO J 303 source : AF1 72) chain J residue 222 type sequence T description binding site for residue EDO J 303 source : AF1 73) chain J residue 223 type sequence Q description binding site for residue EDO J 303 source : AF1 74) chain J residue 223 type sequence Q description binding site for residue EDO J 304 source : AF2 75) chain F residue 82 type sequence R description binding site for residue EDO J 305 source : AF3 76) chain F residue 89 type sequence E description binding site for residue EDO J 305 source : AF3 77) chain F residue 65 type sequence R description binding site for residue EDO J 306 source : AF4 78) chain F residue 72 type sequence Q description binding site for residue EDO J 306 source : AF4 79) chain J residue 50 type sequence Y description binding site for residue EDO J 306 source : AF4 80) chain J residue 55 type sequence R description binding site for residue EDO J 306 source : AF4 81) chain J residue 147 type sequence G description binding site for residue SO4 J 307 source : AF5 82) chain J residue 177 type sequence E description binding site for residue SO4 J 307 source : AF5 83) chain J residue 161 type sequence G description binding site for residue SO4 J 308 source : AF6 84) chain J residue 205 type sequence H description binding site for residue SO4 J 308 source : AF6 85) chain J residue 207 type sequence R description binding site for residue SO4 J 308 source : AF6 86) chain A residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 87) chain F residue 86 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 source Swiss-Prot : SWS_FT_FI4 88) chain B residue 19 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 89) chain G residue 58 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 90) chain G residue 91 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 91) chain G residue 94 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 92) chain B residue 41 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 93) chain B residue 48 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 94) chain B residue 58 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 95) chain B residue 91 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 96) chain B residue 94 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 97) chain G residue 19 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 98) chain G residue 41 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 99) chain G residue 48 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI3 100) chain B residue 2 type MOD_RES sequence Q description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 101) chain F residue 143 type MOD_RES sequence T description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 102) chain F residue 146 type MOD_RES sequence K description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 103) chain F residue 171 type MOD_RES sequence Y description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 104) chain G residue 2 type MOD_RES sequence Q description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 105) chain A residue 84 type MOD_RES sequence Y description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 106) chain A residue 143 type MOD_RES sequence T description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 107) chain A residue 146 type MOD_RES sequence K description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 108) chain A residue 171 type MOD_RES sequence Y description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 109) chain F residue 7 type MOD_RES sequence Y description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 110) chain F residue 73 type MOD_RES sequence T description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 111) chain F residue 84 type MOD_RES sequence Y description Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280 source Swiss-Prot : SWS_FT_FI1 112) chain B residue 1 type CARBOHYD sequence I description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI2 113) chain G residue 1 type CARBOHYD sequence I description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI2 114) chain F residue 116 type CARBOHYD sequence Y description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI2 115) chain F residue 159 type CARBOHYD sequence Y description N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443 source Swiss-Prot : SWS_FT_FI2 116) chain B residue 78-84 type prosite sequence YACRVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290 117) chain A residue 257-263 type prosite sequence YTCHVQH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH source prosite : PS00290

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