HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 19-NOV-24 9KO4 TITLE A CRYO_EM STRUCTURE OF CCR7 COMPLEX WITH CCL21 COMPND MOL_ID: 1; COMPND 2 MOLECULE: C-C MOTIF CHEMOKINE 21; COMPND 3 CHAIN: L; COMPND 4 SYNONYM: 6CKINE,BETA-CHEMOKINE EXODUS-2,SECONDARY LYMPHOID-TISSUE COMPND 5 CHEMOKINE,SLC,SMALL-INDUCIBLE CYTOKINE A21; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: C-C CHEMOKINE RECEPTOR TYPE 7; COMPND 9 CHAIN: R; COMPND 10 SYNONYM: C-C CKR-7,CC-CKR-7,CCR-7,BLR2,CDW197,EPSTEIN-BARR VIRUS- COMPND 11 INDUCED G-PROTEIN COUPLED RECEPTOR 1,EBI1,EBV-INDUCED G-PROTEIN COMPND 12 COUPLED RECEPTOR 1,MIP-3 BETA RECEPTOR; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 16 CHAIN: A; COMPND 17 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; COMPND 18 EC: 3.6.5.-; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 4; COMPND 21 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 22 BETA-1; COMPND 23 CHAIN: B; COMPND 24 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 25 ENGINEERED: YES; COMPND 26 MOL_ID: 5; COMPND 27 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 28 GAMMA-2; COMPND 29 CHAIN: G; COMPND 30 SYNONYM: G GAMMA-I; COMPND 31 ENGINEERED: YES; COMPND 32 MOL_ID: 6; COMPND 33 MOLECULE: SCFV16; COMPND 34 CHAIN: H; COMPND 35 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CCL21, SCYA21, UNQ784/PRO1600; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: CCR7, CMKBR7, EBI1, EVI1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNAI1; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: GNB1; SOURCE 27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 31 ORGANISM_COMMON: HUMAN; SOURCE 32 ORGANISM_TAXID: 9606; SOURCE 33 GENE: GNG2; SOURCE 34 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 36 MOL_ID: 6; SOURCE 37 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 38 ORGANISM_COMMON: HUMAN; SOURCE 39 ORGANISM_TAXID: 9606; SOURCE 40 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 41 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, CCR7, CCL19, MEMBRANE PROTEIN/IMMUNE SYSTEM, MEMBRANE PROTEIN- KEYWDS 2 IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Q.YUAN,J.DUAN,Y.CAO REVDAT 1 26-NOV-25 9KO4 0 JRNL AUTH Q.YUAN,J.DUAN,Y.CAO JRNL TITL A CRYO_EM STRUCTURE OF CCR7 COMPLEX WITH CCL21 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.300 REMARK 3 NUMBER OF PARTICLES : 469279 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9KO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 26-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1300053953. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : A CRYO_EM STRUCTURE OF CCR7 REMARK 245 COMPLEX WITH CCL21 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.04 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 8000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 18000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, R, A, B, G, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLN L 74 REMARK 465 LYS L 75 REMARK 465 PRO L 76 REMARK 465 ALA L 77 REMARK 465 GLN L 78 REMARK 465 GLN R 25 REMARK 465 ASP R 26 REMARK 465 GLU R 27 REMARK 465 VAL R 28 REMARK 465 THR R 29 REMARK 465 CYS R 346 REMARK 465 LEU R 347 REMARK 465 SER R 348 REMARK 465 GLN R 349 REMARK 465 GLU R 350 REMARK 465 GLN R 351 REMARK 465 LEU R 352 REMARK 465 ARG R 353 REMARK 465 GLN R 354 REMARK 465 TRP R 355 REMARK 465 SER R 356 REMARK 465 SER R 357 REMARK 465 CYS R 358 REMARK 465 ARG R 359 REMARK 465 HIS R 360 REMARK 465 ILE R 361 REMARK 465 ARG R 362 REMARK 465 ARG R 363 REMARK 465 SER R 364 REMARK 465 SER R 365 REMARK 465 MET R 366 REMARK 465 SER R 367 REMARK 465 VAL R 368 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 CYS A 3 REMARK 465 THR A 4 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLU A 58 REMARK 465 ALA A 59 REMARK 465 GLY A 60 REMARK 465 TYR A 61 REMARK 465 SER A 62 REMARK 465 GLU A 63 REMARK 465 GLU A 64 REMARK 465 GLU A 65 REMARK 465 CYS A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 ALA A 71 REMARK 465 VAL A 72 REMARK 465 VAL A 73 REMARK 465 TYR A 74 REMARK 465 SER A 75 REMARK 465 ASN A 76 REMARK 465 THR A 77 REMARK 465 ILE A 78 REMARK 465 GLN A 79 REMARK 465 SER A 80 REMARK 465 ILE A 81 REMARK 465 ILE A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 ILE A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 GLY A 89 REMARK 465 ARG A 90 REMARK 465 LEU A 91 REMARK 465 LYS A 92 REMARK 465 ILE A 93 REMARK 465 ASP A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 ASP A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 ARG A 105 REMARK 465 GLN A 106 REMARK 465 LEU A 107 REMARK 465 PHE A 108 REMARK 465 VAL A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 GLY A 112 REMARK 465 ALA A 113 REMARK 465 ALA A 114 REMARK 465 GLU A 115 REMARK 465 GLU A 116 REMARK 465 GLY A 117 REMARK 465 PHE A 118 REMARK 465 MET A 119 REMARK 465 THR A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 LEU A 123 REMARK 465 ALA A 124 REMARK 465 GLY A 125 REMARK 465 VAL A 126 REMARK 465 ILE A 127 REMARK 465 LYS A 128 REMARK 465 ARG A 129 REMARK 465 LEU A 130 REMARK 465 TRP A 131 REMARK 465 LYS A 132 REMARK 465 ASP A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 VAL A 136 REMARK 465 GLN A 137 REMARK 465 ALA A 138 REMARK 465 CYS A 139 REMARK 465 PHE A 140 REMARK 465 ASN A 141 REMARK 465 ARG A 142 REMARK 465 SER A 143 REMARK 465 ARG A 144 REMARK 465 GLU A 145 REMARK 465 TYR A 146 REMARK 465 GLN A 147 REMARK 465 LEU A 148 REMARK 465 ASN A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ALA A 152 REMARK 465 ALA A 153 REMARK 465 TYR A 154 REMARK 465 TYR A 155 REMARK 465 LEU A 156 REMARK 465 ASN A 157 REMARK 465 ASP A 158 REMARK 465 LEU A 159 REMARK 465 ASP A 160 REMARK 465 ARG A 161 REMARK 465 ILE A 162 REMARK 465 ALA A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 ASN A 166 REMARK 465 TYR A 167 REMARK 465 ILE A 168 REMARK 465 PRO A 169 REMARK 465 THR A 170 REMARK 465 GLN A 171 REMARK 465 GLN A 172 REMARK 465 ASP A 173 REMARK 465 VAL A 174 REMARK 465 LEU A 175 REMARK 465 ARG A 176 REMARK 465 THR A 177 REMARK 465 ARG A 178 REMARK 465 VAL A 179 REMARK 465 LYS A 180 REMARK 465 THR A 181 REMARK 465 LEU A 234 REMARK 465 ALA A 235 REMARK 465 GLU A 236 REMARK 465 ASP A 237 REMARK 465 GLU A 238 REMARK 465 GLU A 239 REMARK 465 MET A 240 REMARK 465 GLY B -3 REMARK 465 SER B -2 REMARK 465 LEU B -1 REMARK 465 LEU B 0 REMARK 465 GLN B 1 REMARK 465 SER B 2 REMARK 465 GLU B 3 REMARK 465 LEU B 4 REMARK 465 ASP B 5 REMARK 465 GLN B 6 REMARK 465 LEU B 7 REMARK 465 ARG B 8 REMARK 465 GLN B 9 REMARK 465 GLU B 10 REMARK 465 ALA B 11 REMARK 465 GLU B 12 REMARK 465 GLN B 13 REMARK 465 LEU B 14 REMARK 465 LYS B 15 REMARK 465 ASN B 16 REMARK 465 GLN B 17 REMARK 465 ILE B 18 REMARK 465 ARG B 19 REMARK 465 ASP B 20 REMARK 465 ALA B 21 REMARK 465 ARG B 22 REMARK 465 LYS B 23 REMARK 465 ALA B 24 REMARK 465 CYS B 25 REMARK 465 ALA B 26 REMARK 465 ASP B 27 REMARK 465 ALA B 28 REMARK 465 THR B 29 REMARK 465 LEU B 30 REMARK 465 SER B 31 REMARK 465 GLN B 32 REMARK 465 ILE B 33 REMARK 465 THR B 34 REMARK 465 ASN B 35 REMARK 465 ASN B 36 REMARK 465 GLY B 341 REMARK 465 SER B 342 REMARK 465 SER B 343 REMARK 465 GLY B 344 REMARK 465 GLY B 345 REMARK 465 GLY B 346 REMARK 465 GLY B 347 REMARK 465 SER B 348 REMARK 465 GLY B 349 REMARK 465 GLY B 350 REMARK 465 GLY B 351 REMARK 465 GLY B 352 REMARK 465 SER B 353 REMARK 465 SER B 354 REMARK 465 GLY B 355 REMARK 465 VAL B 356 REMARK 465 SER B 357 REMARK 465 GLY B 358 REMARK 465 TRP B 359 REMARK 465 ARG B 360 REMARK 465 LEU B 361 REMARK 465 PHE B 362 REMARK 465 LYS B 363 REMARK 465 LYS B 364 REMARK 465 ILE B 365 REMARK 465 SER B 366 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 ASN G 5 REMARK 465 THR G 6 REMARK 465 ALA G 7 REMARK 465 SER G 8 REMARK 465 ILE G 9 REMARK 465 ALA G 10 REMARK 465 GLN G 11 REMARK 465 ALA G 12 REMARK 465 ARG G 13 REMARK 465 LYS G 14 REMARK 465 LEU G 15 REMARK 465 VAL G 16 REMARK 465 GLU G 17 REMARK 465 GLN G 18 REMARK 465 LEU G 19 REMARK 465 LYS G 20 REMARK 465 MET G 21 REMARK 465 GLU G 22 REMARK 465 ALA G 23 REMARK 465 ASN G 24 REMARK 465 ILE G 25 REMARK 465 ASP G 26 REMARK 465 ARG G 27 REMARK 465 ILE G 28 REMARK 465 LYS G 64 REMARK 465 LYS G 65 REMARK 465 PHE G 66 REMARK 465 PHE G 67 REMARK 465 CYS G 68 REMARK 465 ALA G 69 REMARK 465 ILE G 70 REMARK 465 LEU G 71 REMARK 465 ASP H 1 REMARK 465 GLY H 121A REMARK 465 GLY H 121B REMARK 465 GLY H 121C REMARK 465 GLY H 121D REMARK 465 SER H 121E REMARK 465 GLY H 121F REMARK 465 GLY H 121G REMARK 465 GLY H 121H REMARK 465 GLY H 121I REMARK 465 SER H 121J REMARK 465 GLY H 121K REMARK 465 GLY H 121L REMARK 465 GLY H 121M REMARK 465 GLY H 121N REMARK 465 SER H 121O REMARK 465 LYS H 248 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN L 6 CG CD OE1 NE2 REMARK 470 GLN L 14 CG CD OE1 NE2 REMARK 470 ARG L 15 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 16 CG CD CE NZ REMARK 470 LYS L 20 CG CD CE NZ REMARK 470 LYS L 27 CG CD CE NZ REMARK 470 LYS L 45 CG CD CE NZ REMARK 470 ARG L 46 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 56 CG CD CE NZ REMARK 470 LYS L 69 CG CD CE NZ REMARK 470 ASP R 30 CG OD1 OD2 REMARK 470 ASP R 31 CG OD1 OD2 REMARK 470 TYR R 32 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE R 33 CG1 CG2 CD1 REMARK 470 ASP R 35 CG OD1 OD2 REMARK 470 GLU R 45 CG CD OE1 OE2 REMARK 470 ARG R 54 CG CD NE CZ NH1 NH2 REMARK 470 MET R 64 CG SD CE REMARK 470 ASP R 104 CG OD1 OD2 REMARK 470 LYS R 120 CG CD CE NZ REMARK 470 SER R 121 OG REMARK 470 MET R 144 CG SD CE REMARK 470 GLN R 200 CG CD OE1 NE2 REMARK 470 ARG R 201 CG CD NE CZ NH1 NH2 REMARK 470 SER R 202 OG REMARK 470 GLU R 205 CG CD OE1 OE2 REMARK 470 GLN R 206 CG CD OE1 NE2 REMARK 470 GLU R 215 CG CD OE1 OE2 REMARK 470 GLU R 218 CG CD OE1 OE2 REMARK 470 ILE R 221 CG1 CG2 CD1 REMARK 470 ASP R 309 CG OD1 OD2 REMARK 470 ASN R 335 CG OD1 ND2 REMARK 470 LYS R 339 CG CD CE NZ REMARK 470 PHE R 341 CG CD1 CD2 CE1 CE2 CZ REMARK 470 MET A 18 CG SD CE REMARK 470 GLU A 43 CG CD OE1 OE2 REMARK 470 LYS A 51 CG CD CE NZ REMARK 470 LYS A 54 CG CD CE NZ REMARK 470 ARG A 205 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 248 CG CD CE NZ REMARK 470 LYS A 257 CG CD CE NZ REMARK 470 LYS A 277 CG CD CE NZ REMARK 470 LYS A 312 CG CD CE NZ REMARK 470 GLU A 328 CG CD OE1 OE2 REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 44 CG CD OE1 NE2 REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 75 CG CD OE1 NE2 REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 130 CG CD OE1 OE2 REMARK 470 ASP B 153 CG OD1 OD2 REMARK 470 GLU B 172 CG CD OE1 OE2 REMARK 470 ARG B 197 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 215 CG CD OE1 OE2 REMARK 470 THR B 221 OG1 CG2 REMARK 470 THR B 223 OG1 CG2 REMARK 470 GLU B 226 CG CD OE1 OE2 REMARK 470 ASN B 239 CG OD1 ND2 REMARK 470 ARG B 256 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 258 CG OD1 OD2 REMARK 470 GLU B 260 CG CD OE1 OE2 REMARK 470 LEU B 285 CG CD1 CD2 REMARK 470 LYS G 29 CG CD CE NZ REMARK 470 LYS G 32 CG CD CE NZ REMARK 470 SER G 57 OG REMARK 470 GLU G 58 CG CD OE1 OE2 REMARK 470 ARG G 62 CG CD NE CZ NH1 NH2 REMARK 470 GLU G 63 CG CD OE1 OE2 REMARK 470 GLN H 13 CG CD OE1 NE2 REMARK 470 GLU H 42 CG CD OE1 OE2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 LYS H 65 CG CD CE NZ REMARK 470 ASP H 73 CG OD1 OD2 REMARK 470 LYS H 76 CG CD CE NZ REMARK 470 THR H 84 OG1 CG2 REMARK 470 GLU H 89 CG CD OE1 OE2 REMARK 470 GLU H 153 CG CD OE1 OE2 REMARK 470 ARG H 160 CG CD NE CZ NH1 NH2 REMARK 470 SER H 197 OG REMARK 470 ASP H 201 CG OD1 OD2 REMARK 470 SER H 204 OG REMARK 470 SER H 206 OG REMARK 470 ARG H 218 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP L 2 73.48 -62.73 REMARK 500 SER L 72 156.17 68.74 REMARK 500 ASP R 31 -60.85 -94.83 REMARK 500 GLN R 160 41.81 -108.80 REMARK 500 SER R 203 -106.73 43.36 REMARK 500 SER R 295 67.99 60.63 REMARK 500 ALA A 291 20.62 -141.12 REMARK 500 LEU A 310 -163.97 55.45 REMARK 500 ARG B 68 -33.79 -130.93 REMARK 500 THR B 87 33.66 -99.55 REMARK 500 GLU B 215 -3.23 76.80 REMARK 500 ASP B 247 -174.51 -69.95 REMARK 500 ALA B 299 5.47 -68.34 REMARK 500 TRP B 332 2.36 -65.06 REMARK 500 LYS H 65 128.24 -38.35 REMARK 500 LEU H 166 96.83 -69.34 REMARK 500 TYR H 173 57.61 -91.94 REMARK 500 ARG H 191 -142.83 53.86 REMARK 500 SER H 193 60.54 60.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62469 RELATED DB: EMDB REMARK 900 A CRYO_EM STRUCTURE OF CCR7 COMPLEX WITH CCL21 DBREF 9KO4 L 1 78 UNP O00585 CCL21_HUMAN 24 101 DBREF 9KO4 R 25 368 UNP P32248 CCR7_HUMAN 25 368 DBREF 9KO4 A 1 354 UNP P63096 GNAI1_HUMAN 1 354 DBREF 9KO4 B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9KO4 G 2 71 UNP P59768 GBG2_HUMAN 2 71 DBREF 9KO4 H 1 248 PDB 9KO4 9KO4 1 248 SEQADV 9KO4 ALA A 203 UNP P63096 GLY 203 CONFLICT SEQADV 9KO4 SER A 326 UNP P63096 ALA 326 CONFLICT SEQADV 9KO4 GLU A 328 UNP P63096 ASP 328 CONFLICT SEQADV 9KO4 GLY B -3 UNP P62873 EXPRESSION TAG SEQADV 9KO4 SER B -2 UNP P62873 EXPRESSION TAG SEQADV 9KO4 LEU B -1 UNP P62873 EXPRESSION TAG SEQADV 9KO4 LEU B 0 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLN B 1 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 341 UNP P62873 EXPRESSION TAG SEQADV 9KO4 SER B 342 UNP P62873 EXPRESSION TAG SEQADV 9KO4 SER B 343 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 344 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 345 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 346 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 347 UNP P62873 EXPRESSION TAG SEQADV 9KO4 SER B 348 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 349 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 350 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 351 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 352 UNP P62873 EXPRESSION TAG SEQADV 9KO4 SER B 353 UNP P62873 EXPRESSION TAG SEQADV 9KO4 SER B 354 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 355 UNP P62873 EXPRESSION TAG SEQADV 9KO4 VAL B 356 UNP P62873 EXPRESSION TAG SEQADV 9KO4 SER B 357 UNP P62873 EXPRESSION TAG SEQADV 9KO4 GLY B 358 UNP P62873 EXPRESSION TAG SEQADV 9KO4 TRP B 359 UNP P62873 EXPRESSION TAG SEQADV 9KO4 ARG B 360 UNP P62873 EXPRESSION TAG SEQADV 9KO4 LEU B 361 UNP P62873 EXPRESSION TAG SEQADV 9KO4 PHE B 362 UNP P62873 EXPRESSION TAG SEQADV 9KO4 LYS B 363 UNP P62873 EXPRESSION TAG SEQADV 9KO4 LYS B 364 UNP P62873 EXPRESSION TAG SEQADV 9KO4 ILE B 365 UNP P62873 EXPRESSION TAG SEQADV 9KO4 SER B 366 UNP P62873 EXPRESSION TAG SEQRES 1 L 78 SER ASP GLY GLY ALA GLN ASP CYS CYS LEU LYS TYR SER SEQRES 2 L 78 GLN ARG LYS ILE PRO ALA LYS VAL VAL ARG SER TYR ARG SEQRES 3 L 78 LYS GLN GLU PRO SER LEU GLY CYS SER ILE PRO ALA ILE SEQRES 4 L 78 LEU PHE LEU PRO ARG LYS ARG SER GLN ALA GLU LEU CYS SEQRES 5 L 78 ALA ASP PRO LYS GLU LEU TRP VAL GLN GLN LEU MET GLN SEQRES 6 L 78 HIS LEU ASP LYS THR PRO SER PRO GLN LYS PRO ALA GLN SEQRES 1 R 344 GLN ASP GLU VAL THR ASP ASP TYR ILE GLY ASP ASN THR SEQRES 2 R 344 THR VAL ASP TYR THR LEU PHE GLU SER LEU CYS SER LYS SEQRES 3 R 344 LYS ASP VAL ARG ASN PHE LYS ALA TRP PHE LEU PRO ILE SEQRES 4 R 344 MET TYR SER ILE ILE CYS PHE VAL GLY LEU LEU GLY ASN SEQRES 5 R 344 GLY LEU VAL VAL LEU THR TYR ILE TYR PHE LYS ARG LEU SEQRES 6 R 344 LYS THR MET THR ASP THR TYR LEU LEU ASN LEU ALA VAL SEQRES 7 R 344 ALA ASP ILE LEU PHE LEU LEU THR LEU PRO PHE TRP ALA SEQRES 8 R 344 TYR SER ALA ALA LYS SER TRP VAL PHE GLY VAL HIS PHE SEQRES 9 R 344 CYS LYS LEU ILE PHE ALA ILE TYR LYS MET SER PHE PHE SEQRES 10 R 344 SER GLY MET LEU LEU LEU LEU CYS ILE SER ILE ASP ARG SEQRES 11 R 344 TYR VAL ALA ILE VAL GLN ALA VAL SER ALA HIS ARG HIS SEQRES 12 R 344 ARG ALA ARG VAL LEU LEU ILE SER LYS LEU SER CYS VAL SEQRES 13 R 344 GLY ILE TRP ILE LEU ALA THR VAL LEU SER ILE PRO GLU SEQRES 14 R 344 LEU LEU TYR SER ASP LEU GLN ARG SER SER SER GLU GLN SEQRES 15 R 344 ALA MET ARG CYS SER LEU ILE THR GLU HIS VAL GLU ALA SEQRES 16 R 344 PHE ILE THR ILE GLN VAL ALA GLN MET VAL ILE GLY PHE SEQRES 17 R 344 LEU VAL PRO LEU LEU ALA MET SER PHE CYS TYR LEU VAL SEQRES 18 R 344 ILE ILE ARG THR LEU LEU GLN ALA ARG ASN PHE GLU ARG SEQRES 19 R 344 ASN LYS ALA ILE LYS VAL ILE ILE ALA VAL VAL VAL VAL SEQRES 20 R 344 PHE ILE VAL PHE GLN LEU PRO TYR ASN GLY VAL VAL LEU SEQRES 21 R 344 ALA GLN THR VAL ALA ASN PHE ASN ILE THR SER SER THR SEQRES 22 R 344 CYS GLU LEU SER LYS GLN LEU ASN ILE ALA TYR ASP VAL SEQRES 23 R 344 THR TYR SER LEU ALA CYS VAL ARG CYS CYS VAL ASN PRO SEQRES 24 R 344 PHE LEU TYR ALA PHE ILE GLY VAL LYS PHE ARG ASN ASP SEQRES 25 R 344 LEU PHE LYS LEU PHE LYS ASP LEU GLY CYS LEU SER GLN SEQRES 26 R 344 GLU GLN LEU ARG GLN TRP SER SER CYS ARG HIS ILE ARG SEQRES 27 R 344 ARG SER SER MET SER VAL SEQRES 1 A 354 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 354 GLU ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP SEQRES 3 A 354 GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU SEQRES 4 A 354 GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 354 MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU GLU SEQRES 6 A 354 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 354 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 354 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 354 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 354 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 354 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 354 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 354 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 354 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR SEQRES 15 A 354 GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS SEQRES 16 A 354 PHE LYS MET PHE ASP VAL GLY ALA GLN ARG SER GLU ARG SEQRES 17 A 354 LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE SEQRES 18 A 354 ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU SEQRES 19 A 354 ALA GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER MET SEQRES 20 A 354 LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR SEQRES 21 A 354 ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU SEQRES 22 A 354 PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS SEQRES 23 A 354 TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA SEQRES 24 A 354 ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS SEQRES 25 A 354 ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SEQRES 26 A 354 SER THR GLU THR LYS ASN VAL GLN PHE VAL PHE ASP ALA SEQRES 27 A 354 VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS SEQRES 28 A 354 GLY LEU PHE SEQRES 1 B 370 GLY SER LEU LEU GLN SER GLU LEU ASP GLN LEU ARG GLN SEQRES 2 B 370 GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG SEQRES 3 B 370 LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN SEQRES 4 B 370 ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG SEQRES 5 B 370 ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET SEQRES 6 B 370 HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER SEQRES 7 B 370 GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR SEQRES 8 B 370 ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL SEQRES 9 B 370 MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA SEQRES 10 B 370 CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU SEQRES 11 B 370 LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU SEQRES 12 B 370 ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU SEQRES 13 B 370 ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR SEQRES 14 B 370 CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR SEQRES 15 B 370 THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER SEQRES 16 B 370 LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS SEQRES 17 B 370 ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET SEQRES 18 B 370 CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN SEQRES 19 B 370 ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR SEQRES 20 B 370 GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG SEQRES 21 B 370 ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE SEQRES 22 B 370 ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY SEQRES 23 B 370 ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN SEQRES 24 B 370 VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU SEQRES 25 B 370 ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR SEQRES 26 B 370 ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER SEQRES 27 B 370 PHE LEU LYS ILE TRP ASN GLY SER SER GLY GLY GLY GLY SEQRES 28 B 370 SER GLY GLY GLY GLY SER SER GLY VAL SER GLY TRP ARG SEQRES 29 B 370 LEU PHE LYS LYS ILE SER SEQRES 1 G 70 ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG LYS SEQRES 2 G 70 LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP ARG SEQRES 3 G 70 ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA TYR SEQRES 4 G 70 CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR PRO SEQRES 5 G 70 VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS PHE SEQRES 6 G 70 PHE CYS ALA ILE LEU SEQRES 1 H 249 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 249 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 H 249 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 H 249 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 H 249 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 H 249 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 H 249 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 H 249 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 H 249 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 H 249 THR VAL SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 H 249 SER GLY GLY GLY GLY SER ALA ASP ILE VAL MET THR GLN SEQRES 12 H 249 ALA THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SEQRES 13 H 249 SER ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER SEQRES 14 H 249 ASN GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO SEQRES 15 H 249 GLY GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN SEQRES 16 H 249 LEU ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SEQRES 17 H 249 SER GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU SEQRES 18 H 249 ALA GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU SEQRES 19 H 249 GLU TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU SEQRES 20 H 249 LEU LYS HELIX 1 AA1 PRO L 18 LYS L 20 5 3 HELIX 2 AA2 GLU L 57 LEU L 67 1 11 HELIX 3 AA3 ASP R 40 PHE R 44 5 5 HELIX 4 AA4 LYS R 50 LYS R 87 1 38 HELIX 5 AA5 THR R 91 LYS R 120 1 30 HELIX 6 AA6 GLY R 125 VAL R 159 1 35 HELIX 7 AA7 GLN R 160 HIS R 165 1 6 HELIX 8 AA8 HIS R 167 SER R 190 1 24 HELIX 9 AA9 SER R 190 SER R 197 1 8 HELIX 10 AB1 HIS R 216 ILE R 230 1 15 HELIX 11 AB2 PHE R 232 LEU R 251 1 20 HELIX 12 AB3 ARG R 258 ASN R 292 1 35 HELIX 13 AB4 THR R 297 TYR R 326 1 30 HELIX 14 AB5 GLY R 330 ASP R 343 1 14 HELIX 15 AB6 SER A 6 ARG A 32 1 27 HELIX 16 AB7 ALA A 41 MET A 53 1 13 HELIX 17 AB8 GLU A 207 TRP A 211 5 5 HELIX 18 AB9 ILE A 212 GLU A 216 5 5 HELIX 19 AC1 SER A 228 ASP A 231 5 4 HELIX 20 AC2 ARG A 242 ASN A 256 1 15 HELIX 21 AC3 LYS A 257 THR A 260 5 4 HELIX 22 AC4 LYS A 270 SER A 281 1 12 HELIX 23 AC5 PRO A 282 CYS A 286 5 5 HELIX 24 AC6 THR A 295 ASP A 309 1 15 HELIX 25 AC7 THR A 327 CYS A 351 1 25 HELIX 26 AC8 VAL G 30 HIS G 44 1 15 HELIX 27 AC9 ALA H 28 PHE H 32 5 5 HELIX 28 AD1 ARG H 87 THR H 91 5 5 HELIX 29 AD2 GLU H 220 VAL H 224 5 5 SHEET 1 AA1 3 VAL L 22 TYR L 25 0 SHEET 2 AA1 3 ILE L 39 PRO L 43 -1 O LEU L 42 N SER L 24 SHEET 3 AA1 3 LEU L 51 ALA L 53 -1 O ALA L 53 N ILE L 39 SHEET 1 AA2 2 ASP R 198 SER R 202 0 SHEET 2 AA2 2 GLN R 206 SER R 211 -1 O ARG R 209 N GLN R 200 SHEET 1 AA3 6 VAL A 185 PHE A 191 0 SHEET 2 AA3 6 LEU A 194 ASP A 200 -1 O ASP A 200 N VAL A 185 SHEET 3 AA3 6 VAL A 34 GLY A 40 1 N VAL A 34 O LYS A 197 SHEET 4 AA3 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 39 SHEET 5 AA3 6 SER A 263 ASN A 269 1 O PHE A 267 N VAL A 225 SHEET 6 AA3 6 ILE A 319 PHE A 323 1 O TYR A 320 N LEU A 266 SHEET 1 AA4 4 THR B 47 THR B 50 0 SHEET 2 AA4 4 LEU B 336 TRP B 339 -1 O ILE B 338 N ARG B 49 SHEET 3 AA4 4 VAL B 327 GLY B 330 -1 N THR B 329 O LYS B 337 SHEET 4 AA4 4 CYS B 317 VAL B 320 -1 N CYS B 317 O GLY B 330 SHEET 1 AA5 4 ILE B 58 TRP B 63 0 SHEET 2 AA5 4 LEU B 69 SER B 74 -1 O VAL B 71 N HIS B 62 SHEET 3 AA5 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA5 4 ASN B 88 PRO B 94 -1 O ASN B 88 N ASP B 83 SHEET 1 AA6 4 VAL B 100 TYR B 105 0 SHEET 2 AA6 4 TYR B 111 GLY B 116 -1 O ALA B 113 N ALA B 104 SHEET 3 AA6 4 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA6 4 ARG B 134 ALA B 140 -1 O ARG B 134 N ASN B 125 SHEET 1 AA7 4 CYS B 148 ASP B 153 0 SHEET 2 AA7 4 GLN B 156 SER B 160 -1 O VAL B 158 N ARG B 150 SHEET 3 AA7 4 CYS B 166 TRP B 169 -1 O TRP B 169 N ILE B 157 SHEET 4 AA7 4 GLN B 176 PHE B 180 -1 O PHE B 180 N CYS B 166 SHEET 1 AA8 3 SER B 189 LEU B 192 0 SHEET 2 AA8 3 LEU B 198 GLY B 202 -1 O VAL B 200 N SER B 191 SHEET 3 AA8 3 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 1 AA9 4 ILE B 229 PHE B 234 0 SHEET 2 AA9 4 ALA B 240 SER B 245 -1 O GLY B 244 N ALA B 231 SHEET 3 AA9 4 CYS B 250 ASP B 254 -1 O ARG B 251 N THR B 243 SHEET 4 AA9 4 ALA B 257 TYR B 264 -1 O LEU B 261 N LEU B 252 SHEET 1 AB1 4 ILE B 273 PHE B 278 0 SHEET 2 AB1 4 LEU B 285 TYR B 289 -1 O GLY B 288 N SER B 275 SHEET 3 AB1 4 CYS B 294 ASP B 298 -1 O ASN B 295 N ALA B 287 SHEET 4 AB1 4 ASP B 303 VAL B 307 -1 O GLY B 306 N VAL B 296 SHEET 1 AB2 4 GLN H 3 SER H 7 0 SHEET 2 AB2 4 SER H 17 SER H 25 -1 O SER H 23 N VAL H 5 SHEET 3 AB2 4 THR H 78 THR H 84 -1 O MET H 83 N ARG H 18 SHEET 4 AB2 4 PHE H 68 ASP H 73 -1 N SER H 71 O PHE H 80 SHEET 1 AB3 6 GLY H 10 VAL H 12 0 SHEET 2 AB3 6 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AB3 6 ALA H 92 SER H 99 -1 N ALA H 92 O LEU H 117 SHEET 4 AB3 6 GLY H 33 GLN H 39 -1 N GLN H 39 O MET H 93 SHEET 5 AB3 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AB3 6 TYR H 59 TYR H 60 -1 O TYR H 59 N TYR H 50 SHEET 1 AB4 4 GLY H 10 VAL H 12 0 SHEET 2 AB4 4 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AB4 4 ALA H 92 SER H 99 -1 N ALA H 92 O LEU H 117 SHEET 4 AB4 4 PHE H 110 TRP H 111 -1 O PHE H 110 N ARG H 98 SHEET 1 AB5 4 MET H 140 THR H 141 0 SHEET 2 AB5 4 VAL H 155 SER H 161 -1 O ARG H 160 N THR H 141 SHEET 3 AB5 4 ALA H 211 ILE H 216 -1 O ILE H 216 N VAL H 155 SHEET 4 AB5 4 PHE H 203 GLY H 207 -1 N SER H 204 O THR H 215 SHEET 1 AB6 5 SER H 146 PRO H 148 0 SHEET 2 AB6 5 THR H 243 GLU H 246 1 O LYS H 244 N VAL H 147 SHEET 3 AB6 5 GLY H 225 GLN H 231 -1 N GLY H 225 O LEU H 245 SHEET 4 AB6 5 LEU H 174 GLN H 179 -1 N GLN H 179 O VAL H 226 SHEET 5 AB6 5 PRO H 185 ILE H 189 -1 O ILE H 189 N TRP H 176 SSBOND 1 CYS L 8 CYS L 34 1555 1555 2.03 SSBOND 2 CYS L 9 CYS L 52 1555 1555 2.03 SSBOND 3 CYS R 48 CYS R 298 1555 1555 2.03 SSBOND 4 CYS R 129 CYS R 210 1555 1555 2.03 SSBOND 5 CYS B 121 CYS B 149 1555 1555 2.04 SSBOND 6 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 7 CYS H 159 CYS H 229 1555 1555 2.03 CISPEP 1 TYR H 235 PRO H 236 0 1.13 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000