HEADER IMMUNE SYSTEM 20-SEP-24 9DPC TITLE STRUCTURE OF FAB 297 IN COMPLEX WITH INFLUENZA H1N1 TITLE 2 A/VICTORIA/4897/2022 NEURAMINIDASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A, B, C, D; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: VARIABLE DOMAIN OF THE HEAVY CHAIN OF FAB 297; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: VARIABLE DOMAIN OF THE LIGHT CHAIN OF FAB 297; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 STRAIN: A/VICTORIA/4897/2022; SOURCE 5 GENE: NA; 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 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS INFLUENZA, NEURAMINIDASE, ANTIBODY, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR T.PHOLCHAREE,N.C.WU REVDAT 1 19-MAR-25 9DPC 0 JRNL AUTH A.MADSEN,N.OKBA JRNL TITL IDENTIFICATION OF A BROADLY PROTECTIVE SEASONAL INFLUENZA JRNL TITL 2 VACCINATION-INDUCED NEURAMINIDASE ANTIBODY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 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) : 2.650 REMARK 3 NUMBER OF PARTICLES : 288521 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9DPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000287827. 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 COMPLEX OF NEURAMINIDASE FROM REMARK 245 INFLUENZA A A/VICTORIA/4897/ REMARK 245 2022 WITH HUMAN FAB 297 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NEURAMINIDASE WAS EXPRESSED REMARK 245 RECOMBINANTLY IN SF9 CELLS. FAB 297 WAS EXPRESSED RECOMBINANTLY REMARK 245 IN EXPI293F CELLS. 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 : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 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) : 5735.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, H, L 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 MET A 1 REMARK 465 ASN A 2 REMARK 465 PRO A 3 REMARK 465 ASN A 4 REMARK 465 GLN A 5 REMARK 465 LYS A 6 REMARK 465 ILE A 7 REMARK 465 ILE A 8 REMARK 465 THR A 9 REMARK 465 ILE A 10 REMARK 465 GLY A 11 REMARK 465 SER A 12 REMARK 465 ILE A 13 REMARK 465 CYS A 14 REMARK 465 MET A 15 REMARK 465 THR A 16 REMARK 465 ILE A 17 REMARK 465 GLY A 18 REMARK 465 THR A 19 REMARK 465 ALA A 20 REMARK 465 ASN A 21 REMARK 465 LEU A 22 REMARK 465 ILE A 23 REMARK 465 LEU A 24 REMARK 465 GLN A 25 REMARK 465 ILE A 26 REMARK 465 GLY A 27 REMARK 465 ASN A 28 REMARK 465 ILE A 29 REMARK 465 ILE A 30 REMARK 465 SER A 31 REMARK 465 ILE A 32 REMARK 465 TRP A 33 REMARK 465 VAL A 34 REMARK 465 SER A 35 REMARK 465 HIS A 36 REMARK 465 SER A 37 REMARK 465 ILE A 38 REMARK 465 GLN A 39 REMARK 465 ILE A 40 REMARK 465 GLY A 41 REMARK 465 ASN A 42 REMARK 465 GLN A 43 REMARK 465 SER A 44 REMARK 465 GLN A 45 REMARK 465 ILE A 46 REMARK 465 GLU A 47 REMARK 465 THR A 48 REMARK 465 CYS A 49 REMARK 465 ASP A 50 REMARK 465 LYS A 51 REMARK 465 SER A 52 REMARK 465 VAL A 53 REMARK 465 ILE A 54 REMARK 465 THR A 55 REMARK 465 TYR A 56 REMARK 465 GLU A 57 REMARK 465 ASN A 58 REMARK 465 ASN A 59 REMARK 465 THR A 60 REMARK 465 TRP A 61 REMARK 465 VAL A 62 REMARK 465 ASN A 63 REMARK 465 GLN A 64 REMARK 465 THR A 65 REMARK 465 PHE A 66 REMARK 465 VAL A 67 REMARK 465 ASN A 68 REMARK 465 ILE A 69 REMARK 465 SER A 70 REMARK 465 ASN A 71 REMARK 465 THR A 72 REMARK 465 ASN A 73 REMARK 465 SER A 74 REMARK 465 ALA A 75 REMARK 465 ALA A 76 REMARK 465 ARG A 77 REMARK 465 GLN A 78 REMARK 465 SER A 79 REMARK 465 VAL A 80 REMARK 465 ALA A 81 REMARK 465 SER A 82 REMARK 465 MET B 1 REMARK 465 ASN B 2 REMARK 465 PRO B 3 REMARK 465 ASN B 4 REMARK 465 GLN B 5 REMARK 465 LYS B 6 REMARK 465 ILE B 7 REMARK 465 ILE B 8 REMARK 465 THR B 9 REMARK 465 ILE B 10 REMARK 465 GLY B 11 REMARK 465 SER B 12 REMARK 465 ILE B 13 REMARK 465 CYS B 14 REMARK 465 MET B 15 REMARK 465 THR B 16 REMARK 465 ILE B 17 REMARK 465 GLY B 18 REMARK 465 THR B 19 REMARK 465 ALA B 20 REMARK 465 ASN B 21 REMARK 465 LEU B 22 REMARK 465 ILE B 23 REMARK 465 LEU B 24 REMARK 465 GLN B 25 REMARK 465 ILE B 26 REMARK 465 GLY B 27 REMARK 465 ASN B 28 REMARK 465 ILE B 29 REMARK 465 ILE B 30 REMARK 465 SER B 31 REMARK 465 ILE B 32 REMARK 465 TRP B 33 REMARK 465 VAL B 34 REMARK 465 SER B 35 REMARK 465 HIS B 36 REMARK 465 SER B 37 REMARK 465 ILE B 38 REMARK 465 GLN B 39 REMARK 465 ILE B 40 REMARK 465 GLY B 41 REMARK 465 ASN B 42 REMARK 465 GLN B 43 REMARK 465 SER B 44 REMARK 465 GLN B 45 REMARK 465 ILE B 46 REMARK 465 GLU B 47 REMARK 465 THR B 48 REMARK 465 CYS B 49 REMARK 465 ASP B 50 REMARK 465 LYS B 51 REMARK 465 SER B 52 REMARK 465 VAL B 53 REMARK 465 ILE B 54 REMARK 465 THR B 55 REMARK 465 TYR B 56 REMARK 465 GLU B 57 REMARK 465 ASN B 58 REMARK 465 ASN B 59 REMARK 465 THR B 60 REMARK 465 TRP B 61 REMARK 465 VAL B 62 REMARK 465 ASN B 63 REMARK 465 GLN B 64 REMARK 465 THR B 65 REMARK 465 PHE B 66 REMARK 465 VAL B 67 REMARK 465 ASN B 68 REMARK 465 ILE B 69 REMARK 465 SER B 70 REMARK 465 ASN B 71 REMARK 465 THR B 72 REMARK 465 ASN B 73 REMARK 465 SER B 74 REMARK 465 ALA B 75 REMARK 465 ALA B 76 REMARK 465 ARG B 77 REMARK 465 GLN B 78 REMARK 465 SER B 79 REMARK 465 VAL B 80 REMARK 465 ALA B 81 REMARK 465 SER B 82 REMARK 465 ASN B 469 REMARK 465 MET C 1 REMARK 465 ASN C 2 REMARK 465 PRO C 3 REMARK 465 ASN C 4 REMARK 465 GLN C 5 REMARK 465 LYS C 6 REMARK 465 ILE C 7 REMARK 465 ILE C 8 REMARK 465 THR C 9 REMARK 465 ILE C 10 REMARK 465 GLY C 11 REMARK 465 SER C 12 REMARK 465 ILE C 13 REMARK 465 CYS C 14 REMARK 465 MET C 15 REMARK 465 THR C 16 REMARK 465 ILE C 17 REMARK 465 GLY C 18 REMARK 465 THR C 19 REMARK 465 ALA C 20 REMARK 465 ASN C 21 REMARK 465 LEU C 22 REMARK 465 ILE C 23 REMARK 465 LEU C 24 REMARK 465 GLN C 25 REMARK 465 ILE C 26 REMARK 465 GLY C 27 REMARK 465 ASN C 28 REMARK 465 ILE C 29 REMARK 465 ILE C 30 REMARK 465 SER C 31 REMARK 465 ILE C 32 REMARK 465 TRP C 33 REMARK 465 VAL C 34 REMARK 465 SER C 35 REMARK 465 HIS C 36 REMARK 465 SER C 37 REMARK 465 ILE C 38 REMARK 465 GLN C 39 REMARK 465 ILE C 40 REMARK 465 GLY C 41 REMARK 465 ASN C 42 REMARK 465 GLN C 43 REMARK 465 SER C 44 REMARK 465 GLN C 45 REMARK 465 ILE C 46 REMARK 465 GLU C 47 REMARK 465 THR C 48 REMARK 465 CYS C 49 REMARK 465 ASP C 50 REMARK 465 LYS C 51 REMARK 465 SER C 52 REMARK 465 VAL C 53 REMARK 465 ILE C 54 REMARK 465 THR C 55 REMARK 465 TYR C 56 REMARK 465 GLU C 57 REMARK 465 ASN C 58 REMARK 465 ASN C 59 REMARK 465 THR C 60 REMARK 465 TRP C 61 REMARK 465 VAL C 62 REMARK 465 ASN C 63 REMARK 465 GLN C 64 REMARK 465 THR C 65 REMARK 465 PHE C 66 REMARK 465 VAL C 67 REMARK 465 ASN C 68 REMARK 465 ILE C 69 REMARK 465 SER C 70 REMARK 465 ASN C 71 REMARK 465 THR C 72 REMARK 465 ASN C 73 REMARK 465 SER C 74 REMARK 465 ALA C 75 REMARK 465 ALA C 76 REMARK 465 ARG C 77 REMARK 465 GLN C 78 REMARK 465 SER C 79 REMARK 465 VAL C 80 REMARK 465 ALA C 81 REMARK 465 SER C 82 REMARK 465 ASN C 469 REMARK 465 MET D 1 REMARK 465 ASN D 2 REMARK 465 PRO D 3 REMARK 465 ASN D 4 REMARK 465 GLN D 5 REMARK 465 LYS D 6 REMARK 465 ILE D 7 REMARK 465 ILE D 8 REMARK 465 THR D 9 REMARK 465 ILE D 10 REMARK 465 GLY D 11 REMARK 465 SER D 12 REMARK 465 ILE D 13 REMARK 465 CYS D 14 REMARK 465 MET D 15 REMARK 465 THR D 16 REMARK 465 ILE D 17 REMARK 465 GLY D 18 REMARK 465 THR D 19 REMARK 465 ALA D 20 REMARK 465 ASN D 21 REMARK 465 LEU D 22 REMARK 465 ILE D 23 REMARK 465 LEU D 24 REMARK 465 GLN D 25 REMARK 465 ILE D 26 REMARK 465 GLY D 27 REMARK 465 ASN D 28 REMARK 465 ILE D 29 REMARK 465 ILE D 30 REMARK 465 SER D 31 REMARK 465 ILE D 32 REMARK 465 TRP D 33 REMARK 465 VAL D 34 REMARK 465 SER D 35 REMARK 465 HIS D 36 REMARK 465 SER D 37 REMARK 465 ILE D 38 REMARK 465 GLN D 39 REMARK 465 ILE D 40 REMARK 465 GLY D 41 REMARK 465 ASN D 42 REMARK 465 GLN D 43 REMARK 465 SER D 44 REMARK 465 GLN D 45 REMARK 465 ILE D 46 REMARK 465 GLU D 47 REMARK 465 THR D 48 REMARK 465 CYS D 49 REMARK 465 ASP D 50 REMARK 465 LYS D 51 REMARK 465 SER D 52 REMARK 465 VAL D 53 REMARK 465 ILE D 54 REMARK 465 THR D 55 REMARK 465 TYR D 56 REMARK 465 GLU D 57 REMARK 465 ASN D 58 REMARK 465 ASN D 59 REMARK 465 THR D 60 REMARK 465 TRP D 61 REMARK 465 VAL D 62 REMARK 465 ASN D 63 REMARK 465 GLN D 64 REMARK 465 THR D 65 REMARK 465 PHE D 66 REMARK 465 VAL D 67 REMARK 465 ASN D 68 REMARK 465 ILE D 69 REMARK 465 SER D 70 REMARK 465 ASN D 71 REMARK 465 THR D 72 REMARK 465 ASN D 73 REMARK 465 SER D 74 REMARK 465 ALA D 75 REMARK 465 ALA D 76 REMARK 465 ARG D 77 REMARK 465 GLN D 78 REMARK 465 SER D 79 REMARK 465 VAL D 80 REMARK 465 ALA D 81 REMARK 465 SER D 82 REMARK 465 GLN H 1 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 LYS A 84 CG CD CE NZ REMARK 470 ASP A 103 CG OD1 OD2 REMARK 470 ASP A 113 CG OD1 OD2 REMARK 470 GLU A 119 CG CD OE1 OE2 REMARK 470 GLU A 128 CG CD OE1 OE2 REMARK 470 ASP A 142 CG OD1 OD2 REMARK 470 ASP A 151 CG OD1 OD2 REMARK 470 LYS A 217 CG CD CE NZ REMARK 470 GLU A 228 CG CD OE1 OE2 REMARK 470 GLU A 230 CG CD OE1 OE2 REMARK 470 ASP A 248 CG OD1 OD2 REMARK 470 GLU A 259 CG CD OE1 OE2 REMARK 470 LYS A 260 CD CE NZ REMARK 470 LYS A 270 CG CD CE NZ REMARK 470 GLU A 278 CG CD OE1 OE2 REMARK 470 ASP A 284 CG OD1 OD2 REMARK 470 ASP A 324 CG OD1 OD2 REMARK 470 GLU A 382 CG CD OE1 OE2 REMARK 470 ASP A 384 CG OD1 OD2 REMARK 470 ASN A 385 CG OD1 ND2 REMARK 470 LYS A 386 CE NZ REMARK 470 GLU A 398 CG CD OE1 OE2 REMARK 470 ASP A 459 CG OD1 OD2 REMARK 470 ASP A 468 CG OD1 OD2 REMARK 470 ASN A 469 CG OD1 ND2 REMARK 470 LYS B 84 CG CD CE NZ REMARK 470 ASP B 103 CG OD1 OD2 REMARK 470 ASP B 113 CG OD1 OD2 REMARK 470 GLU B 119 CG CD OE1 OE2 REMARK 470 GLU B 128 CG CD OE1 OE2 REMARK 470 ASP B 142 CG OD1 OD2 REMARK 470 ASP B 151 CG OD1 OD2 REMARK 470 LYS B 217 CG CD CE NZ REMARK 470 GLU B 228 CG CD OE1 OE2 REMARK 470 GLU B 230 CG CD OE1 OE2 REMARK 470 ASP B 248 CG OD1 OD2 REMARK 470 GLU B 259 CG CD OE1 OE2 REMARK 470 LYS B 270 CG CD CE NZ REMARK 470 GLU B 278 CG CD OE1 OE2 REMARK 470 ASP B 284 CG OD1 OD2 REMARK 470 ASP B 324 CG OD1 OD2 REMARK 470 GLU B 382 CG CD OE1 OE2 REMARK 470 ASP B 384 CG OD1 OD2 REMARK 470 ASN B 385 CG OD1 ND2 REMARK 470 GLU B 398 CG CD OE1 OE2 REMARK 470 MET B 453 CG SD CE REMARK 470 ASP B 459 CG OD1 OD2 REMARK 470 ASP B 468 CG OD1 OD2 REMARK 470 LYS C 84 CG CD CE NZ REMARK 470 ASP C 103 CG OD1 OD2 REMARK 470 ASP C 113 CG OD1 OD2 REMARK 470 GLU C 119 CG CD OE1 OE2 REMARK 470 GLU C 128 CG CD OE1 OE2 REMARK 470 ASP C 142 CG OD1 OD2 REMARK 470 LYS C 150 CE NZ REMARK 470 ASP C 151 CG OD1 OD2 REMARK 470 LYS C 217 CG CD CE NZ REMARK 470 GLU C 228 CG CD OE1 OE2 REMARK 470 GLU C 230 CG CD OE1 OE2 REMARK 470 ASP C 248 CG OD1 OD2 REMARK 470 GLU C 259 CG CD OE1 OE2 REMARK 470 LYS C 270 CG CD CE NZ REMARK 470 GLU C 278 CG CD OE1 OE2 REMARK 470 ASP C 284 CG OD1 OD2 REMARK 470 ASP C 324 CG OD1 OD2 REMARK 470 GLU C 382 CG CD OE1 OE2 REMARK 470 ASP C 384 CG OD1 OD2 REMARK 470 ASN C 385 CG OD1 ND2 REMARK 470 GLU C 398 CG CD OE1 OE2 REMARK 470 ASP C 459 CG OD1 OD2 REMARK 470 ASP C 468 CG OD1 OD2 REMARK 470 LYS D 84 CG CD CE NZ REMARK 470 ASP D 103 CG OD1 OD2 REMARK 470 ASP D 113 CG OD1 OD2 REMARK 470 GLU D 128 CG CD OE1 OE2 REMARK 470 ASP D 142 CG OD1 OD2 REMARK 470 LYS D 150 CD CE NZ REMARK 470 ASP D 151 CG OD1 OD2 REMARK 470 LYS D 217 CG CD CE NZ REMARK 470 GLU D 228 CG CD OE1 OE2 REMARK 470 GLU D 230 CG CD OE1 OE2 REMARK 470 ASP D 248 CG OD1 OD2 REMARK 470 GLU D 259 CG CD OE1 OE2 REMARK 470 LYS D 260 CE NZ REMARK 470 LYS D 262 CE NZ REMARK 470 LYS D 270 CG CD CE NZ REMARK 470 GLU D 278 CG CD OE1 OE2 REMARK 470 ASP D 284 CG OD1 OD2 REMARK 470 ASP D 324 CG OD1 OD2 REMARK 470 GLU D 382 CG CD OE1 OE2 REMARK 470 ASP D 384 CG OD1 OD2 REMARK 470 ASN D 385 CG OD1 ND2 REMARK 470 GLU D 398 CG CD OE1 OE2 REMARK 470 ASP D 459 CG OD1 OD2 REMARK 470 GLU D 462 CG CD OE1 OE2 REMARK 470 ASP D 468 CG OD1 OD2 REMARK 470 ASN D 469 CG OD1 ND2 REMARK 470 LYS H 13 CD CE NZ REMARK 470 GLN H 61 CG CD OE1 NE2 REMARK 470 ASP H 72 CG OD1 OD2 REMARK 470 GLU H 73 CG CD OE1 OE2 REMARK 470 GLU H 81 CG CD OE1 OE2 REMARK 470 ARG H 83 CG CD NE CZ NH1 NH2 REMARK 470 ASP L 1 CG OD1 OD2 REMARK 470 GLN L 3 CG CD OE1 NE2 REMARK 470 ARG L 16 CD NE CZ NH1 NH2 REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 42 CD CE NZ REMARK 470 GLU L 81 CG CD OE1 OE2 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 LEU A 127 14.65 53.88 REMARK 500 ASN A 171 12.81 -140.15 REMARK 500 HIS A 297 30.29 -145.28 REMARK 500 GLU A 311 -169.18 -118.28 REMARK 500 ASN A 344 -168.03 59.95 REMARK 500 LEU A 415 -168.82 -79.78 REMARK 500 ASP A 468 53.53 -92.13 REMARK 500 ASN B 88 51.90 -91.65 REMARK 500 CYS B 292 -155.08 -120.98 REMARK 500 HIS B 297 31.28 -143.89 REMARK 500 LEU B 310 82.32 -69.69 REMARK 500 ASN B 344 -158.38 60.39 REMARK 500 ASN C 88 51.48 -90.51 REMARK 500 ARG C 118 16.21 -141.12 REMARK 500 GLU C 119 72.90 -161.23 REMARK 500 PRO C 126 -7.69 -57.70 REMARK 500 ASN C 209 31.71 -140.24 REMARK 500 ASN C 235 -139.13 66.92 REMARK 500 SER C 286 10.99 58.84 REMARK 500 HIS C 297 20.90 -144.74 REMARK 500 LYS D 222 -65.28 -99.97 REMARK 500 ASP D 248 77.44 -100.49 REMARK 500 ASN D 273 55.88 -100.22 REMARK 500 SER D 286 -4.19 68.97 REMARK 500 HIS D 297 31.80 -157.06 REMARK 500 ASN D 344 -177.70 65.16 REMARK 500 GLU D 462 109.64 -59.10 REMARK 500 ASP H 100 -97.06 58.33 REMARK 500 SER L 9 -5.43 66.47 REMARK 500 PHE L 30 -132.37 56.87 REMARK 500 ALA L 50 19.62 57.21 REMARK 500 ALA L 51 -8.32 72.21 REMARK 500 SER L 52 -15.51 -140.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-47102 RELATED DB: EMDB REMARK 900 STRUCTURE OF FAB 297 IN COMPLEX WITH INFLUENZA H1N1 A/VICTORIA/4897/ REMARK 900 2022 NEURAMINIDASE DBREF1 9DPC A 1 468 UNP A0A6H1QYJ4_9INFA DBREF2 9DPC A A0A6H1QYJ4 1 468 DBREF1 9DPC B 1 468 UNP A0A6H1QYJ4_9INFA DBREF2 9DPC B A0A6H1QYJ4 1 468 DBREF1 9DPC C 1 468 UNP A0A6H1QYJ4_9INFA DBREF2 9DPC C A0A6H1QYJ4 1 468 DBREF1 9DPC D 1 468 UNP A0A6H1QYJ4_9INFA DBREF2 9DPC D A0A6H1QYJ4 1 468 DBREF 9DPC H 1 113 PDB 9DPC 9DPC 1 113 DBREF 9DPC L 1 106 PDB 9DPC 9DPC 1 106 SEQADV 9DPC ASP A 50 UNP A0A6H1QYJ ASN 50 CONFLICT SEQADV 9DPC MET A 453 UNP A0A6H1QYJ VAL 453 CONFLICT SEQADV 9DPC ASN A 469 UNP A0A6H1QYJ EXPRESSION TAG SEQADV 9DPC ASP B 50 UNP A0A6H1QYJ ASN 50 CONFLICT SEQADV 9DPC MET B 453 UNP A0A6H1QYJ VAL 453 CONFLICT SEQADV 9DPC ASN B 469 UNP A0A6H1QYJ EXPRESSION TAG SEQADV 9DPC ASP C 50 UNP A0A6H1QYJ ASN 50 CONFLICT SEQADV 9DPC MET C 453 UNP A0A6H1QYJ VAL 453 CONFLICT SEQADV 9DPC ASN C 469 UNP A0A6H1QYJ EXPRESSION TAG SEQADV 9DPC ASP D 50 UNP A0A6H1QYJ ASN 50 CONFLICT SEQADV 9DPC MET D 453 UNP A0A6H1QYJ VAL 453 CONFLICT SEQADV 9DPC ASN D 469 UNP A0A6H1QYJ EXPRESSION TAG SEQRES 1 A 469 MET ASN PRO ASN GLN LYS ILE ILE THR ILE GLY SER ILE SEQRES 2 A 469 CYS MET THR ILE GLY THR ALA ASN LEU ILE LEU GLN ILE SEQRES 3 A 469 GLY ASN ILE ILE SER ILE TRP VAL SER HIS SER ILE GLN SEQRES 4 A 469 ILE GLY ASN GLN SER GLN ILE GLU THR CYS ASP LYS SER SEQRES 5 A 469 VAL ILE THR TYR GLU ASN ASN THR TRP VAL ASN GLN THR SEQRES 6 A 469 PHE VAL ASN ILE SER ASN THR ASN SER ALA ALA ARG GLN SEQRES 7 A 469 SER VAL ALA SER VAL LYS LEU ALA GLY ASN SER SER LEU SEQRES 8 A 469 CYS PRO VAL SER GLY TRP ALA ILE TYR SER LYS ASP ASN SEQRES 9 A 469 SER VAL ARG ILE GLY SER LYS GLY ASP VAL PHE VAL ILE SEQRES 10 A 469 ARG GLU PRO PHE ILE SER CYS SER PRO LEU GLU CYS ARG SEQRES 11 A 469 THR PHE PHE LEU THR GLN GLY ALA LEU LEU ASN ASP LYS SEQRES 12 A 469 HIS SER ASN GLY THR ILE LYS ASP ARG SER PRO TYR ARG SEQRES 13 A 469 THR LEU MET SER CYS PRO ILE GLY GLU VAL PRO SER PRO SEQRES 14 A 469 TYR ASN SER ARG PHE GLU SER VAL ALA TRP SER ALA SER SEQRES 15 A 469 ALA CYS HIS ASP GLY THR ASN TRP LEU THR ILE GLY ILE SEQRES 16 A 469 SER GLY PRO ASP SER GLY ALA VAL ALA VAL LEU LYS TYR SEQRES 17 A 469 ASN GLY ILE ILE THR ASP THR ILE LYS SER TRP ARG ASN SEQRES 18 A 469 LYS ILE LEU ARG THR GLN GLU SER GLU CYS ALA CYS VAL SEQRES 19 A 469 ASN GLY SER CYS PHE THR ILE MET THR ASP GLY PRO SER SEQRES 20 A 469 ASP GLY GLN ALA SER TYR LYS ILE PHE ARG ILE GLU LYS SEQRES 21 A 469 GLY LYS ILE ILE LYS SER VAL GLU MET LYS ALA PRO ASN SEQRES 22 A 469 TYR HIS TYR GLU GLU CYS SER CYS TYR PRO ASP SER SER SEQRES 23 A 469 GLU ILE THR CYS VAL CYS ARG ASP ASN TRP HIS GLY SER SEQRES 24 A 469 ASN ARG PRO TRP VAL SER PHE ASN GLN ASN LEU GLU TYR SEQRES 25 A 469 GLN MET GLY TYR ILE CYS SER GLY VAL PHE GLY ASP ASN SEQRES 26 A 469 PRO ARG PRO ASN ASP LYS THR GLY SER CYS GLY PRO VAL SEQRES 27 A 469 SER SER ASN GLY ALA ASN GLY VAL LYS GLY PHE SER PHE SEQRES 28 A 469 LYS TYR GLY ASN GLY VAL TRP ILE GLY ARG THR LYS SER SEQRES 29 A 469 ILE SER SER ARG LYS GLY PHE GLU MET ILE TRP ASP PRO SEQRES 30 A 469 ASN GLY TRP THR GLU THR ASP ASN LYS PHE SER LYS LYS SEQRES 31 A 469 GLN ASP ILE VAL GLY ILE ASN GLU TRP SER GLY TYR SER SEQRES 32 A 469 GLY SER PHE VAL GLN HIS PRO GLU LEU THR GLY LEU ASN SEQRES 33 A 469 CYS ILE ARG PRO CYS PHE TRP VAL GLU LEU ILE ARG GLY SEQRES 34 A 469 ARG PRO GLU GLU ASN THR ILE TRP THR SER GLY SER SER SEQRES 35 A 469 ILE SER PHE CYS GLY VAL ASP SER ASP ILE MET GLY TRP SEQRES 36 A 469 SER TRP PRO ASP GLY ALA GLU LEU PRO PHE THR ILE ASP SEQRES 37 A 469 ASN SEQRES 1 B 469 MET ASN PRO ASN GLN LYS ILE ILE THR ILE GLY SER ILE SEQRES 2 B 469 CYS MET THR ILE GLY THR ALA ASN LEU ILE LEU GLN ILE SEQRES 3 B 469 GLY ASN ILE ILE SER ILE TRP VAL SER HIS SER ILE GLN SEQRES 4 B 469 ILE GLY ASN GLN SER GLN ILE GLU THR CYS ASP LYS SER SEQRES 5 B 469 VAL ILE THR TYR GLU ASN ASN THR TRP VAL ASN GLN THR SEQRES 6 B 469 PHE VAL ASN ILE SER ASN THR ASN SER ALA ALA ARG GLN SEQRES 7 B 469 SER VAL ALA SER VAL LYS LEU ALA GLY ASN SER SER LEU SEQRES 8 B 469 CYS PRO VAL SER GLY TRP ALA ILE TYR SER LYS ASP ASN SEQRES 9 B 469 SER VAL ARG ILE GLY SER LYS GLY ASP VAL PHE VAL ILE SEQRES 10 B 469 ARG GLU PRO PHE ILE SER CYS SER PRO LEU GLU CYS ARG SEQRES 11 B 469 THR PHE PHE LEU THR GLN GLY ALA LEU LEU ASN ASP LYS SEQRES 12 B 469 HIS SER ASN GLY THR ILE LYS ASP ARG SER PRO TYR ARG SEQRES 13 B 469 THR LEU MET SER CYS PRO ILE GLY GLU VAL PRO SER PRO SEQRES 14 B 469 TYR ASN SER ARG PHE GLU SER VAL ALA TRP SER ALA SER SEQRES 15 B 469 ALA CYS HIS ASP GLY THR ASN TRP LEU THR ILE GLY ILE SEQRES 16 B 469 SER GLY PRO ASP SER GLY ALA VAL ALA VAL LEU LYS TYR SEQRES 17 B 469 ASN GLY ILE ILE THR ASP THR ILE LYS SER TRP ARG ASN SEQRES 18 B 469 LYS ILE LEU ARG THR GLN GLU SER GLU CYS ALA CYS VAL SEQRES 19 B 469 ASN GLY SER CYS PHE THR ILE MET THR ASP GLY PRO SER SEQRES 20 B 469 ASP GLY GLN ALA SER TYR LYS ILE PHE ARG ILE GLU LYS SEQRES 21 B 469 GLY LYS ILE ILE LYS SER VAL GLU MET LYS ALA PRO ASN SEQRES 22 B 469 TYR HIS TYR GLU GLU CYS SER CYS TYR PRO ASP SER SER SEQRES 23 B 469 GLU ILE THR CYS VAL CYS ARG ASP ASN TRP HIS GLY SER SEQRES 24 B 469 ASN ARG PRO TRP VAL SER PHE ASN GLN ASN LEU GLU TYR SEQRES 25 B 469 GLN MET GLY TYR ILE CYS SER GLY VAL PHE GLY ASP ASN SEQRES 26 B 469 PRO ARG PRO ASN ASP LYS THR GLY SER CYS GLY PRO VAL SEQRES 27 B 469 SER SER ASN GLY ALA ASN GLY VAL LYS GLY PHE SER PHE SEQRES 28 B 469 LYS TYR GLY ASN GLY VAL TRP ILE GLY ARG THR LYS SER SEQRES 29 B 469 ILE SER SER ARG LYS GLY PHE GLU MET ILE TRP ASP PRO SEQRES 30 B 469 ASN GLY TRP THR GLU THR ASP ASN LYS PHE SER LYS LYS SEQRES 31 B 469 GLN ASP ILE VAL GLY ILE ASN GLU TRP SER GLY TYR SER SEQRES 32 B 469 GLY SER PHE VAL GLN HIS PRO GLU LEU THR GLY LEU ASN SEQRES 33 B 469 CYS ILE ARG PRO CYS PHE TRP VAL GLU LEU ILE ARG GLY SEQRES 34 B 469 ARG PRO GLU GLU ASN THR ILE TRP THR SER GLY SER SER SEQRES 35 B 469 ILE SER PHE CYS GLY VAL ASP SER ASP ILE MET GLY TRP SEQRES 36 B 469 SER TRP PRO ASP GLY ALA GLU LEU PRO PHE THR ILE ASP SEQRES 37 B 469 ASN SEQRES 1 C 469 MET ASN PRO ASN GLN LYS ILE ILE THR ILE GLY SER ILE SEQRES 2 C 469 CYS MET THR ILE GLY THR ALA ASN LEU ILE LEU GLN ILE SEQRES 3 C 469 GLY ASN ILE ILE SER ILE TRP VAL SER HIS SER ILE GLN SEQRES 4 C 469 ILE GLY ASN GLN SER GLN ILE GLU THR CYS ASP LYS SER SEQRES 5 C 469 VAL ILE THR TYR GLU ASN ASN THR TRP VAL ASN GLN THR SEQRES 6 C 469 PHE VAL ASN ILE SER ASN THR ASN SER ALA ALA ARG GLN SEQRES 7 C 469 SER VAL ALA SER VAL LYS LEU ALA GLY ASN SER SER LEU SEQRES 8 C 469 CYS PRO VAL SER GLY TRP ALA ILE TYR SER LYS ASP ASN SEQRES 9 C 469 SER VAL ARG ILE GLY SER LYS GLY ASP VAL PHE VAL ILE SEQRES 10 C 469 ARG GLU PRO PHE ILE SER CYS SER PRO LEU GLU CYS ARG SEQRES 11 C 469 THR PHE PHE LEU THR GLN GLY ALA LEU LEU ASN ASP LYS SEQRES 12 C 469 HIS SER ASN GLY THR ILE LYS ASP ARG SER PRO TYR ARG SEQRES 13 C 469 THR LEU MET SER CYS PRO ILE GLY GLU VAL PRO SER PRO SEQRES 14 C 469 TYR ASN SER ARG PHE GLU SER VAL ALA TRP SER ALA SER SEQRES 15 C 469 ALA CYS HIS ASP GLY THR ASN TRP LEU THR ILE GLY ILE SEQRES 16 C 469 SER GLY PRO ASP SER GLY ALA VAL ALA VAL LEU LYS TYR SEQRES 17 C 469 ASN GLY ILE ILE THR ASP THR ILE LYS SER TRP ARG ASN SEQRES 18 C 469 LYS ILE LEU ARG THR GLN GLU SER GLU CYS ALA CYS VAL SEQRES 19 C 469 ASN GLY SER CYS PHE THR ILE MET THR ASP GLY PRO SER SEQRES 20 C 469 ASP GLY GLN ALA SER TYR LYS ILE PHE ARG ILE GLU LYS SEQRES 21 C 469 GLY LYS ILE ILE LYS SER VAL GLU MET LYS ALA PRO ASN SEQRES 22 C 469 TYR HIS TYR GLU GLU CYS SER CYS TYR PRO ASP SER SER SEQRES 23 C 469 GLU ILE THR CYS VAL CYS ARG ASP ASN TRP HIS GLY SER SEQRES 24 C 469 ASN ARG PRO TRP VAL SER PHE ASN GLN ASN LEU GLU TYR SEQRES 25 C 469 GLN MET GLY TYR ILE CYS SER GLY VAL PHE GLY ASP ASN SEQRES 26 C 469 PRO ARG PRO ASN ASP LYS THR GLY SER CYS GLY PRO VAL SEQRES 27 C 469 SER SER ASN GLY ALA ASN GLY VAL LYS GLY PHE SER PHE SEQRES 28 C 469 LYS TYR GLY ASN GLY VAL TRP ILE GLY ARG THR LYS SER SEQRES 29 C 469 ILE SER SER ARG LYS GLY PHE GLU MET ILE TRP ASP PRO SEQRES 30 C 469 ASN GLY TRP THR GLU THR ASP ASN LYS PHE SER LYS LYS SEQRES 31 C 469 GLN ASP ILE VAL GLY ILE ASN GLU TRP SER GLY TYR SER SEQRES 32 C 469 GLY SER PHE VAL GLN HIS PRO GLU LEU THR GLY LEU ASN SEQRES 33 C 469 CYS ILE ARG PRO CYS PHE TRP VAL GLU LEU ILE ARG GLY SEQRES 34 C 469 ARG PRO GLU GLU ASN THR ILE TRP THR SER GLY SER SER SEQRES 35 C 469 ILE SER PHE CYS GLY VAL ASP SER ASP ILE MET GLY TRP SEQRES 36 C 469 SER TRP PRO ASP GLY ALA GLU LEU PRO PHE THR ILE ASP SEQRES 37 C 469 ASN SEQRES 1 D 469 MET ASN PRO ASN GLN LYS ILE ILE THR ILE GLY SER ILE SEQRES 2 D 469 CYS MET THR ILE GLY THR ALA ASN LEU ILE LEU GLN ILE SEQRES 3 D 469 GLY ASN ILE ILE SER ILE TRP VAL SER HIS SER ILE GLN SEQRES 4 D 469 ILE GLY ASN GLN SER GLN ILE GLU THR CYS ASP LYS SER SEQRES 5 D 469 VAL ILE THR TYR GLU ASN ASN THR TRP VAL ASN GLN THR SEQRES 6 D 469 PHE VAL ASN ILE SER ASN THR ASN SER ALA ALA ARG GLN SEQRES 7 D 469 SER VAL ALA SER VAL LYS LEU ALA GLY ASN SER SER LEU SEQRES 8 D 469 CYS PRO VAL SER GLY TRP ALA ILE TYR SER LYS ASP ASN SEQRES 9 D 469 SER VAL ARG ILE GLY SER LYS GLY ASP VAL PHE VAL ILE SEQRES 10 D 469 ARG GLU PRO PHE ILE SER CYS SER PRO LEU GLU CYS ARG SEQRES 11 D 469 THR PHE PHE LEU THR GLN GLY ALA LEU LEU ASN ASP LYS SEQRES 12 D 469 HIS SER ASN GLY THR ILE LYS ASP ARG SER PRO TYR ARG SEQRES 13 D 469 THR LEU MET SER CYS PRO ILE GLY GLU VAL PRO SER PRO SEQRES 14 D 469 TYR ASN SER ARG PHE GLU SER VAL ALA TRP SER ALA SER SEQRES 15 D 469 ALA CYS HIS ASP GLY THR ASN TRP LEU THR ILE GLY ILE SEQRES 16 D 469 SER GLY PRO ASP SER GLY ALA VAL ALA VAL LEU LYS TYR SEQRES 17 D 469 ASN GLY ILE ILE THR ASP THR ILE LYS SER TRP ARG ASN SEQRES 18 D 469 LYS ILE LEU ARG THR GLN GLU SER GLU CYS ALA CYS VAL SEQRES 19 D 469 ASN GLY SER CYS PHE THR ILE MET THR ASP GLY PRO SER SEQRES 20 D 469 ASP GLY GLN ALA SER TYR LYS ILE PHE ARG ILE GLU LYS SEQRES 21 D 469 GLY LYS ILE ILE LYS SER VAL GLU MET LYS ALA PRO ASN SEQRES 22 D 469 TYR HIS TYR GLU GLU CYS SER CYS TYR PRO ASP SER SER SEQRES 23 D 469 GLU ILE THR CYS VAL CYS ARG ASP ASN TRP HIS GLY SER SEQRES 24 D 469 ASN ARG PRO TRP VAL SER PHE ASN GLN ASN LEU GLU TYR SEQRES 25 D 469 GLN MET GLY TYR ILE CYS SER GLY VAL PHE GLY ASP ASN SEQRES 26 D 469 PRO ARG PRO ASN ASP LYS THR GLY SER CYS GLY PRO VAL SEQRES 27 D 469 SER SER ASN GLY ALA ASN GLY VAL LYS GLY PHE SER PHE SEQRES 28 D 469 LYS TYR GLY ASN GLY VAL TRP ILE GLY ARG THR LYS SER SEQRES 29 D 469 ILE SER SER ARG LYS GLY PHE GLU MET ILE TRP ASP PRO SEQRES 30 D 469 ASN GLY TRP THR GLU THR ASP ASN LYS PHE SER LYS LYS SEQRES 31 D 469 GLN ASP ILE VAL GLY ILE ASN GLU TRP SER GLY TYR SER SEQRES 32 D 469 GLY SER PHE VAL GLN HIS PRO GLU LEU THR GLY LEU ASN SEQRES 33 D 469 CYS ILE ARG PRO CYS PHE TRP VAL GLU LEU ILE ARG GLY SEQRES 34 D 469 ARG PRO GLU GLU ASN THR ILE TRP THR SER GLY SER SER SEQRES 35 D 469 ILE SER PHE CYS GLY VAL ASP SER ASP ILE MET GLY TRP SEQRES 36 D 469 SER TRP PRO ASP GLY ALA GLU LEU PRO PHE THR ILE ASP SEQRES 37 D 469 ASN SEQRES 1 H 126 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 126 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 126 ASP THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 126 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 H 126 PRO PHE LEU GLY THR THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 126 GLY ARG VAL THR ILE THR THR ASP GLU SER SER THR THR SEQRES 7 H 126 ALA ASP MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 126 ALA VAL TYR TYR CYS ALA THR SER TYR SER GLY TYR ASP SEQRES 9 H 126 ARG ILE GLN TYR TYR TYR SER GLY MET ASP VAL TRP GLY SEQRES 10 H 126 GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 L 106 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 106 SER VAL ARG ASP ARG VAL THR ILE THR CYS ARG SER SER SEQRES 3 L 106 GLN SER VAL PHE THR TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 106 PRO GLY LYS ALA PRO LYS LEU LEU ILE SER ALA ALA SER SEQRES 5 L 106 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 106 GLY SER GLY THR ASP PHE THR LEU THR ILE ASN SER LEU SEQRES 7 L 106 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 106 PHE SER THR PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 L 106 ASP ILE HELIX 1 AA1 ASN A 104 SER A 110 1 7 HELIX 2 AA2 ASP A 142 ASN A 146 5 5 HELIX 3 AA3 HIS A 409 GLY A 414 1 6 HELIX 4 AA4 ASN B 104 SER B 110 1 7 HELIX 5 AA5 ASP B 142 ASN B 146 5 5 HELIX 6 AA6 HIS B 409 GLY B 414 1 6 HELIX 7 AA7 ASN C 104 GLY C 109 1 6 HELIX 8 AA8 ASP C 142 ASN C 146 5 5 HELIX 9 AA9 HIS C 409 GLY C 414 1 6 HELIX 10 AB1 ASN D 104 GLY D 109 1 6 HELIX 11 AB2 ASP D 142 ASN D 146 5 5 HELIX 12 AB3 HIS D 409 GLY D 414 1 6 HELIX 13 AB4 GLN H 61 GLN H 64 5 4 HELIX 14 AB5 ARG H 83 THR H 87 5 5 HELIX 15 AB6 GLN L 79 PHE L 83 5 5 SHEET 1 AA1 4 GLY A 96 ASP A 103 0 SHEET 2 AA1 4 THR A 438 VAL A 448 -1 O SER A 444 N TYR A 100 SHEET 3 AA1 4 ARG A 419 GLY A 429 -1 N PHE A 422 O PHE A 445 SHEET 4 AA1 4 SER A 403 GLN A 408 -1 N GLN A 408 O ARG A 419 SHEET 1 AA2 4 PHE A 115 SER A 125 0 SHEET 2 AA2 4 GLU A 128 LEU A 139 -1 O PHE A 132 N PHE A 121 SHEET 3 AA2 4 THR A 157 PRO A 162 -1 O CYS A 161 N THR A 131 SHEET 4 AA2 4 ARG A 173 SER A 176 -1 O ARG A 173 N SER A 160 SHEET 1 AA3 4 SER A 180 HIS A 185 0 SHEET 2 AA3 4 TRP A 190 SER A 196 -1 O ILE A 193 N SER A 182 SHEET 3 AA3 4 VAL A 203 TYR A 208 -1 O VAL A 205 N GLY A 194 SHEET 4 AA3 4 ILE A 211 LYS A 217 -1 O THR A 213 N LEU A 206 SHEET 1 AA4 3 ARG A 225 THR A 226 0 SHEET 2 AA4 3 SER A 237 ASP A 244 -1 O THR A 243 N ARG A 225 SHEET 3 AA4 3 ALA A 232 VAL A 234 -1 N ALA A 232 O PHE A 239 SHEET 1 AA5 4 ARG A 225 THR A 226 0 SHEET 2 AA5 4 SER A 237 ASP A 244 -1 O THR A 243 N ARG A 225 SHEET 3 AA5 4 SER A 252 GLU A 259 -1 O ILE A 258 N CYS A 238 SHEET 4 AA5 4 LYS A 262 GLU A 268 -1 O LYS A 265 N ARG A 257 SHEET 1 AA6 4 GLU A 277 ASP A 284 0 SHEET 2 AA6 4 GLU A 287 ARG A 293 -1 O THR A 289 N TYR A 282 SHEET 3 AA6 4 PRO A 302 PHE A 306 -1 O PRO A 302 N CYS A 292 SHEET 4 AA6 4 GLN A 313 TYR A 316 -1 O GLY A 315 N TRP A 303 SHEET 1 AA7 4 SER A 350 TYR A 353 0 SHEET 2 AA7 4 GLY A 356 ARG A 361 -1 O TRP A 358 N PHE A 351 SHEET 3 AA7 4 LYS A 369 ASP A 376 -1 O ILE A 374 N ILE A 359 SHEET 4 AA7 4 LYS A 389 TRP A 399 -1 O GLN A 391 N MET A 373 SHEET 1 AA8 4 GLY B 96 ASP B 103 0 SHEET 2 AA8 4 THR B 438 VAL B 448 -1 O VAL B 448 N GLY B 96 SHEET 3 AA8 4 ARG B 419 GLY B 429 -1 N VAL B 424 O ILE B 443 SHEET 4 AA8 4 SER B 403 GLN B 408 -1 N GLN B 408 O ARG B 419 SHEET 1 AA9 4 PHE B 115 CYS B 124 0 SHEET 2 AA9 4 CYS B 129 LEU B 139 -1 O ALA B 138 N VAL B 116 SHEET 3 AA9 4 THR B 157 PRO B 162 -1 O CYS B 161 N THR B 131 SHEET 4 AA9 4 ARG B 173 SER B 176 -1 O ARG B 173 N SER B 160 SHEET 1 AB1 4 SER B 180 HIS B 185 0 SHEET 2 AB1 4 TRP B 190 SER B 196 -1 O LEU B 191 N CYS B 184 SHEET 3 AB1 4 VAL B 203 TYR B 208 -1 O VAL B 203 N SER B 196 SHEET 4 AB1 4 ILE B 211 LYS B 217 -1 O THR B 213 N LEU B 206 SHEET 1 AB2 3 LEU B 224 THR B 226 0 SHEET 2 AB2 3 SER B 237 ASP B 244 -1 O THR B 243 N ARG B 225 SHEET 3 AB2 3 ALA B 232 VAL B 234 -1 N ALA B 232 O PHE B 239 SHEET 1 AB3 4 LEU B 224 THR B 226 0 SHEET 2 AB3 4 SER B 237 ASP B 244 -1 O THR B 243 N ARG B 225 SHEET 3 AB3 4 SER B 252 GLU B 259 -1 O SER B 252 N ASP B 244 SHEET 4 AB3 4 LYS B 262 GLU B 268 -1 O VAL B 267 N ILE B 255 SHEET 1 AB4 4 GLU B 277 ASP B 284 0 SHEET 2 AB4 4 GLU B 287 ARG B 293 -1 O GLU B 287 N ASP B 284 SHEET 3 AB4 4 PRO B 302 PHE B 306 -1 O PRO B 302 N CYS B 292 SHEET 4 AB4 4 TYR B 312 TYR B 316 -1 O GLY B 315 N TRP B 303 SHEET 1 AB5 4 SER B 350 TYR B 353 0 SHEET 2 AB5 4 GLY B 356 ARG B 361 -1 O GLY B 356 N TYR B 353 SHEET 3 AB5 4 LYS B 369 ASP B 376 -1 O ASP B 376 N VAL B 357 SHEET 4 AB5 4 LYS B 389 TRP B 399 -1 O GLN B 391 N MET B 373 SHEET 1 AB6 4 GLY C 96 ASP C 103 0 SHEET 2 AB6 4 THR C 438 VAL C 448 -1 O SER C 444 N TYR C 100 SHEET 3 AB6 4 ARG C 419 GLY C 429 -1 N ARG C 428 O SER C 439 SHEET 4 AB6 4 SER C 403 GLN C 408 -1 N GLN C 408 O ARG C 419 SHEET 1 AB7 3 PHE C 115 ILE C 117 0 SHEET 2 AB7 3 CYS C 129 LEU C 139 -1 O GLN C 136 N VAL C 116 SHEET 3 AB7 3 PHE C 121 CYS C 124 -1 N SER C 123 O ARG C 130 SHEET 1 AB8 4 PHE C 115 ILE C 117 0 SHEET 2 AB8 4 CYS C 129 LEU C 139 -1 O GLN C 136 N VAL C 116 SHEET 3 AB8 4 THR C 157 PRO C 162 -1 O CYS C 161 N THR C 131 SHEET 4 AB8 4 ARG C 173 VAL C 177 -1 O ARG C 173 N SER C 160 SHEET 1 AB9 4 SER C 180 HIS C 185 0 SHEET 2 AB9 4 TRP C 190 SER C 196 -1 O LEU C 191 N CYS C 184 SHEET 3 AB9 4 VAL C 203 LYS C 207 -1 O VAL C 203 N SER C 196 SHEET 4 AB9 4 ILE C 212 LYS C 217 -1 O THR C 213 N LEU C 206 SHEET 1 AC1 3 LEU C 224 THR C 226 0 SHEET 2 AC1 3 SER C 237 ASP C 244 -1 O THR C 243 N ARG C 225 SHEET 3 AC1 3 CYS C 233 VAL C 234 -1 N VAL C 234 O SER C 237 SHEET 1 AC2 4 LEU C 224 THR C 226 0 SHEET 2 AC2 4 SER C 237 ASP C 244 -1 O THR C 243 N ARG C 225 SHEET 3 AC2 4 SER C 252 GLU C 259 -1 O PHE C 256 N THR C 240 SHEET 4 AC2 4 LYS C 262 GLU C 268 -1 O LYS C 265 N ARG C 257 SHEET 1 AC3 4 SER C 280 ASP C 284 0 SHEET 2 AC3 4 GLU C 287 VAL C 291 -1 O THR C 289 N TYR C 282 SHEET 3 AC3 4 PRO C 302 PHE C 306 -1 O VAL C 304 N CYS C 290 SHEET 4 AC3 4 GLN C 313 TYR C 316 -1 O GLY C 315 N TRP C 303 SHEET 1 AC4 4 SER C 350 TYR C 353 0 SHEET 2 AC4 4 GLY C 356 ARG C 361 -1 O GLY C 356 N TYR C 353 SHEET 3 AC4 4 LYS C 369 ASP C 376 -1 O ILE C 374 N ILE C 359 SHEET 4 AC4 4 LYS C 389 TRP C 399 -1 O GLN C 391 N MET C 373 SHEET 1 AC5 4 GLY D 96 ASP D 103 0 SHEET 2 AC5 4 THR D 438 VAL D 448 -1 O SER D 444 N TYR D 100 SHEET 3 AC5 4 ARG D 419 GLY D 429 -1 N PHE D 422 O PHE D 445 SHEET 4 AC5 4 SER D 403 GLN D 408 -1 N PHE D 406 O CYS D 421 SHEET 1 AC6 3 PHE D 115 ILE D 117 0 SHEET 2 AC6 3 CYS D 129 LEU D 139 -1 O ALA D 138 N VAL D 116 SHEET 3 AC6 3 PHE D 121 CYS D 124 -1 N SER D 123 O ARG D 130 SHEET 1 AC7 4 PHE D 115 ILE D 117 0 SHEET 2 AC7 4 CYS D 129 LEU D 139 -1 O ALA D 138 N VAL D 116 SHEET 3 AC7 4 THR D 157 PRO D 162 -1 O THR D 157 N THR D 135 SHEET 4 AC7 4 ARG D 173 VAL D 177 -1 O ARG D 173 N SER D 160 SHEET 1 AC8 4 SER D 180 HIS D 185 0 SHEET 2 AC8 4 TRP D 190 SER D 196 -1 O LEU D 191 N CYS D 184 SHEET 3 AC8 4 VAL D 203 TYR D 208 -1 O VAL D 203 N SER D 196 SHEET 4 AC8 4 ILE D 211 LYS D 217 -1 O ASP D 214 N LEU D 206 SHEET 1 AC9 3 LEU D 224 THR D 226 0 SHEET 2 AC9 3 SER D 237 ASP D 244 -1 O THR D 243 N ARG D 225 SHEET 3 AC9 3 ALA D 232 VAL D 234 -1 N VAL D 234 O SER D 237 SHEET 1 AD1 4 LEU D 224 THR D 226 0 SHEET 2 AD1 4 SER D 237 ASP D 244 -1 O THR D 243 N ARG D 225 SHEET 3 AD1 4 SER D 252 GLU D 259 -1 O PHE D 256 N THR D 240 SHEET 4 AD1 4 LYS D 262 MET D 269 -1 O VAL D 267 N ILE D 255 SHEET 1 AD2 4 SER D 280 ASP D 284 0 SHEET 2 AD2 4 GLU D 287 VAL D 291 -1 O GLU D 287 N ASP D 284 SHEET 3 AD2 4 PRO D 302 PHE D 306 -1 O PHE D 306 N ILE D 288 SHEET 4 AD2 4 TYR D 312 TYR D 316 -1 O GLY D 315 N TRP D 303 SHEET 1 AD3 4 SER D 350 TYR D 353 0 SHEET 2 AD3 4 GLY D 356 ARG D 361 -1 O GLY D 356 N TYR D 353 SHEET 3 AD3 4 LYS D 369 ASP D 376 -1 O ASP D 376 N VAL D 357 SHEET 4 AD3 4 LYS D 389 TRP D 399 -1 O VAL D 394 N PHE D 371 SHEET 1 AD4 4 GLN H 3 GLN H 6 0 SHEET 2 AD4 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AD4 4 THR H 77 LEU H 82 -1 O MET H 80 N VAL H 20 SHEET 4 AD4 4 VAL H 67 THR H 71 -1 N THR H 70 O ASP H 79 SHEET 1 AD5 6 GLU H 10 LYS H 12 0 SHEET 2 AD5 6 THR H 107 VAL H 111 1 O THR H 108 N GLU H 10 SHEET 3 AD5 6 ALA H 88 TYR H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AD5 6 TYR H 32 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AD5 6 LEU H 45 ILE H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AD5 6 THR H 56 TYR H 59 -1 O THR H 56 N ILE H 52 SHEET 1 AD6 4 MET L 4 GLN L 6 0 SHEET 2 AD6 4 VAL L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AD6 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AD6 4 PHE L 62 SER L 65 -1 N SER L 65 O THR L 72 SHEET 1 AD7 6 SER L 10 SER L 12 0 SHEET 2 AD7 6 THR L 102 ASP L 105 1 O ASP L 105 N LEU L 11 SHEET 3 AD7 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AD7 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AD7 6 LYS L 45 SER L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AD7 6 THR L 53 LEU L 54 -1 O THR L 53 N SER L 49 SSBOND 1 CYS A 124 CYS A 129 1555 1555 2.03 SSBOND 2 CYS A 184 CYS A 231 1555 1555 2.03 SSBOND 3 CYS A 233 CYS A 238 1555 1555 2.03 SSBOND 4 CYS A 279 CYS A 292 1555 1555 2.03 SSBOND 5 CYS A 281 CYS A 290 1555 1555 2.03 SSBOND 6 CYS A 318 CYS A 335 1555 1555 2.03 SSBOND 7 CYS B 124 CYS B 129 1555 1555 2.03 SSBOND 8 CYS B 184 CYS B 231 1555 1555 2.03 SSBOND 9 CYS B 233 CYS B 238 1555 1555 2.03 SSBOND 10 CYS B 279 CYS B 292 1555 1555 2.04 SSBOND 11 CYS B 281 CYS B 290 1555 1555 2.03 SSBOND 12 CYS B 318 CYS B 335 1555 1555 2.03 SSBOND 13 CYS B 421 CYS B 446 1555 1555 2.03 SSBOND 14 CYS C 92 CYS C 417 1555 1555 2.03 SSBOND 15 CYS C 124 CYS C 129 1555 1555 2.03 SSBOND 16 CYS C 184 CYS C 231 1555 1555 2.04 SSBOND 17 CYS C 233 CYS C 238 1555 1555 2.04 SSBOND 18 CYS C 279 CYS C 292 1555 1555 2.03 SSBOND 19 CYS C 281 CYS C 290 1555 1555 2.03 SSBOND 20 CYS C 318 CYS C 335 1555 1555 2.03 SSBOND 21 CYS C 421 CYS C 446 1555 1555 2.03 SSBOND 22 CYS D 92 CYS D 417 1555 1555 2.03 SSBOND 23 CYS D 124 CYS D 129 1555 1555 2.03 SSBOND 24 CYS D 184 CYS D 231 1555 1555 2.03 SSBOND 25 CYS D 233 CYS D 238 1555 1555 2.03 SSBOND 26 CYS D 279 CYS D 292 1555 1555 2.03 SSBOND 27 CYS D 281 CYS D 290 1555 1555 2.03 SSBOND 28 CYS D 318 CYS D 335 1555 1555 2.03 SSBOND 29 CYS D 421 CYS D 446 1555 1555 2.03 SSBOND 30 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 31 CYS L 23 CYS L 88 1555 1555 2.04 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