HEADER VIRAL PROTEIN/IMMUNE SYSTEM 05-MAY-24 9BOP TITLE A BROADLY-NEUTRALIZING ANTIBODY AGAINST EBOLAVIRUS GLYCOPROTEIN THAT TITLE 2 CAN POTENTIATE THE BREADTH AND NEUTRALIZATION POTENCY OF OTHER ANTI- TITLE 3 GLYCOPROTEIN ANTIBODIES COMPND MOL_ID: 1; COMPND 2 MOLECULE: 11883 HEAVY CHAIN; COMPND 3 CHAIN: A, C, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 11883 LIGHT CHAIN; COMPND 7 CHAIN: B, D, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 11886 HEAVY CHAIN; COMPND 11 CHAIN: M, O; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: 11886 LIGHT CHAIN; COMPND 15 CHAIN: N, P; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: VIRION SPIKE GLYCOPROTEIN GP1; COMPND 19 CHAIN: S, T, U; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: VIRION SPIKE GLYCOPROTEIN GP2; COMPND 23 CHAIN: V, W, X; COMPND 24 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 3 ORGANISM_COMMON: RABBIT; SOURCE 4 ORGANISM_TAXID: 9986; SOURCE 5 ORGAN: SPLEEN; SOURCE 6 CELL: SPLENOCYTES; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 13 ORGANISM_COMMON: RABBIT; SOURCE 14 ORGANISM_TAXID: 9986; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO-S; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 21 ORGANISM_COMMON: RABBIT; SOURCE 22 ORGANISM_TAXID: 9986; SOURCE 23 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 24 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 27 MOL_ID: 4; SOURCE 28 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 29 ORGANISM_COMMON: RABBIT; SOURCE 30 ORGANISM_TAXID: 9986; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 34 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO-S; SOURCE 35 MOL_ID: 5; SOURCE 36 ORGANISM_SCIENTIFIC: EBOLAVIRUS; SOURCE 37 ORGANISM_TAXID: 186536; SOURCE 38 VARIANT: MAYINGA; SOURCE 39 GENE: GP; SOURCE 40 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 41 EXPRESSION_SYSTEM_COMMON: FRUIT FLY; SOURCE 42 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 43 MOL_ID: 6; SOURCE 44 ORGANISM_SCIENTIFIC: EBOLAVIRUS; SOURCE 45 ORGANISM_TAXID: 186536; SOURCE 46 VARIANT: MAYINGA; SOURCE 47 GENE: GP; SOURCE 48 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 49 EXPRESSION_SYSTEM_COMMON: FRUIT FLY; SOURCE 50 EXPRESSION_SYSTEM_TAXID: 7227 KEYWDS EBOLA, IGG, NEUTRALIZATION, COMPLEX, GLYCOPROTEIN, VIRAL PROTEIN- KEYWDS 2 IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR F.R.DONNELLAN,V.RAYAPROLU,P.RIJAL,V.O'DOWD,A.PARVATE,H.CALLAWAY, AUTHOR 2 C.HARIHARAN,D.PAREKH,S.HUI,K.SHAFFER,K.HASTIE,L.SHIMANSKI,H.MULLER- AUTHOR 3 KRAUTER,T.STECKER,A.BALARAM,P.HALFMANN,E.O.SAPHIRE,D.J.LIGHTWOOD, AUTHOR 4 A.R.TOWNSEND,S.J.DRAPER REVDAT 1 05-NOV-25 9BOP 0 JRNL AUTH F.R.DONNELLAN,V.RAYAPROLU,P.RIJAL,V.O'DOWD,A.PARVATE, JRNL AUTH 2 H.CALLAWAY,C.HARIHARAN,D.PAREKH,S.HUI,K.SHAFFER,K.HASTIE, JRNL AUTH 3 L.SHIMANSKI,H.MULLER-KRAUTER,T.STECKER,A.BALARAM,P.HALFMANN, JRNL AUTH 4 E.O.SAPHIRE,D.J.LIGHTWOOD,A.R.TOWNSEND,S.J.DRAPER JRNL TITL A BROADLY-NEUTRALIZING ANTIBODY AGAINST EBOLAVIRUS JRNL TITL 2 GLYCOPROTEIN THAT CAN POTENTIATE THE BREADTH AND JRNL TITL 3 NEUTRALIZATION POTENCY OF OTHER ANTI-GLYCOPROTEIN ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, UCSF REMARK 3 CHIMERAX, CRYOSPARC, PHENIX, COOT 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 : AB INITIO MODEL 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 66500 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 9BOP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000283799. 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 : ZAIRE EBOLA GLYCOPROTEIN DTM REMARK 245 (GP1 AND GP2 INCLUDING MLD) REMARK 245 COMPLEXED WITH 11883 AND 11886; REMARK 245 ZAIRE EBOLAVIRUS GLYCOPROTEIN REMARK 245 CONTAINING MLD; 11883 FAB HEAVY REMARK 245 AND LIGHT CHAINS; 11886 FAB REMARK 245 HEAVY AND LIGHT CHAINS REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.90 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 9552 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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 : 75000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : TOTAL DOSE OF 50E/A2 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: HEXADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, M, N, O, P, S, V, C, E, REMARK 350 AND CHAINS: D, F, W, X, T, U, G, H, I 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 SER A -23 REMARK 465 PHE A -22 REMARK 465 GLU A -21 REMARK 465 ALA A -20 REMARK 465 THR A -19 REMARK 465 MET A -18 REMARK 465 GLU A -17 REMARK 465 THR A -16 REMARK 465 GLY A -15 REMARK 465 LEU A -14 REMARK 465 ARG A -13 REMARK 465 TRP A -12 REMARK 465 LEU A -11 REMARK 465 LEU A -10 REMARK 465 LEU A -9 REMARK 465 VAL A -8 REMARK 465 ALA A -7 REMARK 465 VAL A -6 REMARK 465 LEU A -5 REMARK 465 LYS A -4 REMARK 465 GLY A -3 REMARK 465 VAL A -2 REMARK 465 GLN A -1 REMARK 465 CYS A 0 REMARK 465 SER A 124 REMARK 465 SER B -26 REMARK 465 PHE B -25 REMARK 465 GLU B -24 REMARK 465 ALA B -23 REMARK 465 THR B -22 REMARK 465 MET B -21 REMARK 465 ASN B -20 REMARK 465 MET B -19 REMARK 465 ARG B -18 REMARK 465 ALA B -17 REMARK 465 PRO B -16 REMARK 465 THR B -15 REMARK 465 GLN B -14 REMARK 465 LEU B -13 REMARK 465 LEU B -12 REMARK 465 GLY B -11 REMARK 465 LEU B -10 REMARK 465 LEU B -9 REMARK 465 LEU B -8 REMARK 465 LEU B -7 REMARK 465 TRP B -6 REMARK 465 LEU B -5 REMARK 465 PRO B -4 REMARK 465 GLY B -3 REMARK 465 ALA B -2 REMARK 465 ARG B -1 REMARK 465 CYS B 0 REMARK 465 ALA B 1 REMARK 465 LYS B 111 REMARK 465 ARG B 112 REMARK 465 THR B 113 REMARK 465 ARG M -24 REMARK 465 SER M -23 REMARK 465 PHE M -22 REMARK 465 GLU M -21 REMARK 465 ALA M -20 REMARK 465 THR M -19 REMARK 465 MET M -18 REMARK 465 GLU M -17 REMARK 465 THR M -16 REMARK 465 GLY M -15 REMARK 465 LEU M -14 REMARK 465 ARG M -13 REMARK 465 TRP M -12 REMARK 465 LEU M -11 REMARK 465 LEU M -10 REMARK 465 LEU M -9 REMARK 465 VAL M -8 REMARK 465 ALA M -7 REMARK 465 VAL M -6 REMARK 465 LEU M -5 REMARK 465 LYS M -4 REMARK 465 GLY M -3 REMARK 465 VAL M -2 REMARK 465 GLN M -1 REMARK 465 CYS M 0 REMARK 465 SER M 121 REMARK 465 ARG N -27 REMARK 465 SER N -26 REMARK 465 PHE N -25 REMARK 465 GLU N -24 REMARK 465 ALA N -23 REMARK 465 THR N -22 REMARK 465 MET N -21 REMARK 465 ASN N -20 REMARK 465 MET N -19 REMARK 465 ARG N -18 REMARK 465 ALA N -17 REMARK 465 PRO N -16 REMARK 465 THR N -15 REMARK 465 GLN N -14 REMARK 465 LEU N -13 REMARK 465 LEU N -12 REMARK 465 GLY N -11 REMARK 465 LEU N -10 REMARK 465 LEU N -9 REMARK 465 LEU N -8 REMARK 465 LEU N -7 REMARK 465 TRP N -6 REMARK 465 LEU N -5 REMARK 465 PRO N -4 REMARK 465 GLY N -3 REMARK 465 ALA N -2 REMARK 465 ARG N -1 REMARK 465 CYS N 0 REMARK 465 VAL N 110 REMARK 465 LYS N 111 REMARK 465 ARG N 112 REMARK 465 THR N 113 REMARK 465 ARG O -24 REMARK 465 SER O -23 REMARK 465 PHE O -22 REMARK 465 GLU O -21 REMARK 465 ALA O -20 REMARK 465 THR O -19 REMARK 465 MET O -18 REMARK 465 GLU O -17 REMARK 465 THR O -16 REMARK 465 GLY O -15 REMARK 465 LEU O -14 REMARK 465 ARG O -13 REMARK 465 TRP O -12 REMARK 465 LEU O -11 REMARK 465 LEU O -10 REMARK 465 LEU O -9 REMARK 465 VAL O -8 REMARK 465 ALA O -7 REMARK 465 VAL O -6 REMARK 465 LEU O -5 REMARK 465 LYS O -4 REMARK 465 GLY O -3 REMARK 465 VAL O -2 REMARK 465 GLN O -1 REMARK 465 CYS O 0 REMARK 465 PRO O 40 REMARK 465 GLY O 41 REMARK 465 LYS O 42 REMARK 465 GLY O 43 REMARK 465 SER O 121 REMARK 465 ARG P -27 REMARK 465 SER P -26 REMARK 465 PHE P -25 REMARK 465 GLU P -24 REMARK 465 ALA P -23 REMARK 465 THR P -22 REMARK 465 MET P -21 REMARK 465 ASN P -20 REMARK 465 MET P -19 REMARK 465 ARG P -18 REMARK 465 ALA P -17 REMARK 465 PRO P -16 REMARK 465 THR P -15 REMARK 465 GLN P -14 REMARK 465 LEU P -13 REMARK 465 LEU P -12 REMARK 465 GLY P -11 REMARK 465 LEU P -10 REMARK 465 LEU P -9 REMARK 465 LEU P -8 REMARK 465 LEU P -7 REMARK 465 TRP P -6 REMARK 465 LEU P -5 REMARK 465 PRO P -4 REMARK 465 GLY P -3 REMARK 465 ALA P -2 REMARK 465 ARG P -1 REMARK 465 CYS P 0 REMARK 465 GLY P 16 REMARK 465 GLY P 17 REMARK 465 THR P 18 REMARK 465 SER P 56 REMARK 465 GLY P 57 REMARK 465 VAL P 58 REMARK 465 PRO P 59 REMARK 465 SER P 60 REMARK 465 SER P 76 REMARK 465 ASP P 77 REMARK 465 LEU P 78 REMARK 465 GLU P 79 REMARK 465 CYS P 80 REMARK 465 ALA P 81 REMARK 465 VAL P 110 REMARK 465 LYS P 111 REMARK 465 ARG P 112 REMARK 465 THR P 113 REMARK 465 ARG S 31 REMARK 465 LYS S 190 REMARK 465 LYS S 191 REMARK 465 ASP S 192 REMARK 465 PHE S 193 REMARK 465 PHE S 194 REMARK 465 SER S 195 REMARK 465 SER S 196 REMARK 465 HIS S 197 REMARK 465 PRO S 198 REMARK 465 LEU S 199 REMARK 465 ARG S 200 REMARK 465 GLU S 201 REMARK 465 PRO S 202 REMARK 465 VAL S 203 REMARK 465 ASN S 204 REMARK 465 ALA S 205 REMARK 465 THR S 206 REMARK 465 GLU S 207 REMARK 465 ASP S 208 REMARK 465 PRO S 209 REMARK 465 SER S 210 REMARK 465 SER S 211 REMARK 465 TRP S 288 REMARK 465 ALA S 289 REMARK 465 PHE S 290 REMARK 465 TRP S 291 REMARK 465 GLU S 292 REMARK 465 THR S 293 REMARK 465 LYS S 294 REMARK 465 LYS S 295 REMARK 465 ASN S 296 REMARK 465 LEU S 297 REMARK 465 THR S 298 REMARK 465 ARG S 299 REMARK 465 LYS S 300 REMARK 465 ILE S 301 REMARK 465 ARG S 302 REMARK 465 SER S 303 REMARK 465 GLU S 304 REMARK 465 GLU S 305 REMARK 465 LEU S 306 REMARK 465 SER S 307 REMARK 465 PHE S 308 REMARK 465 THR S 309 REMARK 465 GLY V 524 REMARK 465 ALA V 525 REMARK 465 ALA V 526 REMARK 465 ASP V 614 REMARK 465 TRP V 615 REMARK 465 THR V 616 REMARK 465 LYS V 617 REMARK 465 ASN V 618 REMARK 465 ILE V 619 REMARK 465 THR V 620 REMARK 465 ASP V 621 REMARK 465 LYS V 622 REMARK 465 ILE V 623 REMARK 465 ASP V 624 REMARK 465 GLN V 625 REMARK 465 ILE V 626 REMARK 465 ILE V 627 REMARK 465 HIS V 628 REMARK 465 ASP V 629 REMARK 465 PHE V 630 REMARK 465 VAL V 631 REMARK 465 ASP V 632 REMARK 465 LYS V 633 REMARK 465 THR V 634 REMARK 465 LEU V 635 REMARK 465 PRO V 636 REMARK 465 ASP V 637 REMARK 465 SER C -23 REMARK 465 PHE C -22 REMARK 465 GLU C -21 REMARK 465 ALA C -20 REMARK 465 THR C -19 REMARK 465 MET C -18 REMARK 465 GLU C -17 REMARK 465 THR C -16 REMARK 465 GLY C -15 REMARK 465 LEU C -14 REMARK 465 ARG C -13 REMARK 465 TRP C -12 REMARK 465 LEU C -11 REMARK 465 LEU C -10 REMARK 465 LEU C -9 REMARK 465 VAL C -8 REMARK 465 ALA C -7 REMARK 465 VAL C -6 REMARK 465 LEU C -5 REMARK 465 LYS C -4 REMARK 465 GLY C -3 REMARK 465 VAL C -2 REMARK 465 GLN C -1 REMARK 465 CYS C 0 REMARK 465 SER C 124 REMARK 465 SER E -23 REMARK 465 PHE E -22 REMARK 465 GLU E -21 REMARK 465 ALA E -20 REMARK 465 THR E -19 REMARK 465 MET E -18 REMARK 465 GLU E -17 REMARK 465 THR E -16 REMARK 465 GLY E -15 REMARK 465 LEU E -14 REMARK 465 ARG E -13 REMARK 465 TRP E -12 REMARK 465 LEU E -11 REMARK 465 LEU E -10 REMARK 465 LEU E -9 REMARK 465 VAL E -8 REMARK 465 ALA E -7 REMARK 465 VAL E -6 REMARK 465 LEU E -5 REMARK 465 LYS E -4 REMARK 465 GLY E -3 REMARK 465 VAL E -2 REMARK 465 GLN E -1 REMARK 465 CYS E 0 REMARK 465 SER E 124 REMARK 465 SER D -26 REMARK 465 PHE D -25 REMARK 465 GLU D -24 REMARK 465 ALA D -23 REMARK 465 THR D -22 REMARK 465 MET D -21 REMARK 465 ASN D -20 REMARK 465 MET D -19 REMARK 465 ARG D -18 REMARK 465 ALA D -17 REMARK 465 PRO D -16 REMARK 465 THR D -15 REMARK 465 GLN D -14 REMARK 465 LEU D -13 REMARK 465 LEU D -12 REMARK 465 GLY D -11 REMARK 465 LEU D -10 REMARK 465 LEU D -9 REMARK 465 LEU D -8 REMARK 465 LEU D -7 REMARK 465 TRP D -6 REMARK 465 LEU D -5 REMARK 465 PRO D -4 REMARK 465 GLY D -3 REMARK 465 ALA D -2 REMARK 465 ARG D -1 REMARK 465 CYS D 0 REMARK 465 ALA D 1 REMARK 465 LYS D 111 REMARK 465 ARG D 112 REMARK 465 THR D 113 REMARK 465 SER F -26 REMARK 465 PHE F -25 REMARK 465 GLU F -24 REMARK 465 ALA F -23 REMARK 465 THR F -22 REMARK 465 MET F -21 REMARK 465 ASN F -20 REMARK 465 MET F -19 REMARK 465 ARG F -18 REMARK 465 ALA F -17 REMARK 465 PRO F -16 REMARK 465 THR F -15 REMARK 465 GLN F -14 REMARK 465 LEU F -13 REMARK 465 LEU F -12 REMARK 465 GLY F -11 REMARK 465 LEU F -10 REMARK 465 LEU F -9 REMARK 465 LEU F -8 REMARK 465 LEU F -7 REMARK 465 TRP F -6 REMARK 465 LEU F -5 REMARK 465 PRO F -4 REMARK 465 GLY F -3 REMARK 465 ALA F -2 REMARK 465 ARG F -1 REMARK 465 CYS F 0 REMARK 465 ALA F 1 REMARK 465 LYS F 111 REMARK 465 ARG F 112 REMARK 465 THR F 113 REMARK 465 GLY W 524 REMARK 465 ALA W 525 REMARK 465 ALA W 526 REMARK 465 ASP W 614 REMARK 465 TRP W 615 REMARK 465 THR W 616 REMARK 465 LYS W 617 REMARK 465 ASN W 618 REMARK 465 ILE W 619 REMARK 465 THR W 620 REMARK 465 ASP W 621 REMARK 465 LYS W 622 REMARK 465 ILE W 623 REMARK 465 ASP W 624 REMARK 465 GLN W 625 REMARK 465 ILE W 626 REMARK 465 ILE W 627 REMARK 465 HIS W 628 REMARK 465 ASP W 629 REMARK 465 PHE W 630 REMARK 465 VAL W 631 REMARK 465 ASP W 632 REMARK 465 LYS W 633 REMARK 465 THR W 634 REMARK 465 LEU W 635 REMARK 465 PRO W 636 REMARK 465 ASP W 637 REMARK 465 GLY X 524 REMARK 465 ALA X 525 REMARK 465 ALA X 526 REMARK 465 ASP X 614 REMARK 465 TRP X 615 REMARK 465 THR X 616 REMARK 465 LYS X 617 REMARK 465 ASN X 618 REMARK 465 ILE X 619 REMARK 465 THR X 620 REMARK 465 ASP X 621 REMARK 465 LYS X 622 REMARK 465 ILE X 623 REMARK 465 ASP X 624 REMARK 465 GLN X 625 REMARK 465 ILE X 626 REMARK 465 ILE X 627 REMARK 465 HIS X 628 REMARK 465 ASP X 629 REMARK 465 PHE X 630 REMARK 465 VAL X 631 REMARK 465 ASP X 632 REMARK 465 LYS X 633 REMARK 465 THR X 634 REMARK 465 LEU X 635 REMARK 465 PRO X 636 REMARK 465 ASP X 637 REMARK 465 ARG T 31 REMARK 465 LYS T 190 REMARK 465 LYS T 191 REMARK 465 ASP T 192 REMARK 465 PHE T 193 REMARK 465 PHE T 194 REMARK 465 SER T 195 REMARK 465 SER T 196 REMARK 465 HIS T 197 REMARK 465 PRO T 198 REMARK 465 LEU T 199 REMARK 465 ARG T 200 REMARK 465 GLU T 201 REMARK 465 PRO T 202 REMARK 465 VAL T 203 REMARK 465 ASN T 204 REMARK 465 ALA T 205 REMARK 465 THR T 206 REMARK 465 GLU T 207 REMARK 465 ASP T 208 REMARK 465 PRO T 209 REMARK 465 SER T 210 REMARK 465 SER T 211 REMARK 465 TRP T 288 REMARK 465 ALA T 289 REMARK 465 PHE T 290 REMARK 465 TRP T 291 REMARK 465 GLU T 292 REMARK 465 THR T 293 REMARK 465 LYS T 294 REMARK 465 LYS T 295 REMARK 465 ASN T 296 REMARK 465 LEU T 297 REMARK 465 THR T 298 REMARK 465 ARG T 299 REMARK 465 LYS T 300 REMARK 465 ILE T 301 REMARK 465 ARG T 302 REMARK 465 SER T 303 REMARK 465 GLU T 304 REMARK 465 GLU T 305 REMARK 465 LEU T 306 REMARK 465 SER T 307 REMARK 465 PHE T 308 REMARK 465 THR T 309 REMARK 465 ARG U 31 REMARK 465 LYS U 190 REMARK 465 LYS U 191 REMARK 465 ASP U 192 REMARK 465 PHE U 193 REMARK 465 PHE U 194 REMARK 465 SER U 195 REMARK 465 SER U 196 REMARK 465 HIS U 197 REMARK 465 PRO U 198 REMARK 465 LEU U 199 REMARK 465 ARG U 200 REMARK 465 GLU U 201 REMARK 465 PRO U 202 REMARK 465 VAL U 203 REMARK 465 ASN U 204 REMARK 465 ALA U 205 REMARK 465 THR U 206 REMARK 465 GLU U 207 REMARK 465 ASP U 208 REMARK 465 PRO U 209 REMARK 465 SER U 210 REMARK 465 SER U 211 REMARK 465 TRP U 288 REMARK 465 ALA U 289 REMARK 465 PHE U 290 REMARK 465 TRP U 291 REMARK 465 GLU U 292 REMARK 465 THR U 293 REMARK 465 LYS U 294 REMARK 465 LYS U 295 REMARK 465 ASN U 296 REMARK 465 LEU U 297 REMARK 465 THR U 298 REMARK 465 ARG U 299 REMARK 465 LYS U 300 REMARK 465 ILE U 301 REMARK 465 ARG U 302 REMARK 465 SER U 303 REMARK 465 GLU U 304 REMARK 465 GLU U 305 REMARK 465 LEU U 306 REMARK 465 SER U 307 REMARK 465 PHE U 308 REMARK 465 THR U 309 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O VAL S 236 OH TYR S 261 2.13 REMARK 500 OG1 THR O 71 OG1 THR O 75 2.16 REMARK 500 REMARK 500 REMARK: NULL 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 ALA A 94 -168.90 -164.80 REMARK 500 ALA B 51 -8.29 71.71 REMARK 500 ASP B 77 59.53 37.48 REMARK 500 ILE M 47 -61.02 -96.52 REMARK 500 ALA M 72 -154.50 56.97 REMARK 500 ALA N 51 -8.18 71.67 REMARK 500 ILE O 47 -60.98 -94.02 REMARK 500 ALA O 72 -158.86 56.78 REMARK 500 SER O 82 70.21 55.27 REMARK 500 ALA P 51 -5.11 68.40 REMARK 500 TYR S 162 -149.07 58.79 REMARK 500 ARG S 164 19.88 57.14 REMARK 500 ASP V 552 57.39 -96.48 REMARK 500 PRO C 14 171.41 -58.59 REMARK 500 ALA D 51 -7.48 70.99 REMARK 500 PRO F 10 76.17 -69.85 REMARK 500 ALA F 51 -8.84 71.37 REMARK 500 TYR T 162 -158.74 55.03 REMARK 500 ASN U 40 49.50 39.75 REMARK 500 ASP U 163 99.37 -68.35 REMARK 500 SER U 246 30.64 -99.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44747 RELATED DB: EMDB REMARK 900 A BROADLY-NEUTRALIZING ANTIBODY AGAINST EBOLAVIRUS GLYCOPROTEIN REMARK 900 THAT CAN POTENTIATE THE BREADTH AND NEUTRALIZATION POTENCY OF OTHER REMARK 900 ANTI-GLYCOPROTEIN ANTIBODIES DBREF 9BOP A -23 124 PDB 9BOP 9BOP -23 124 DBREF 9BOP B -26 113 PDB 9BOP 9BOP -26 113 DBREF 9BOP M -24 121 PDB 9BOP 9BOP -24 121 DBREF 9BOP N -27 113 PDB 9BOP 9BOP -27 113 DBREF 9BOP O -24 121 PDB 9BOP 9BOP -24 121 DBREF 9BOP P -27 113 PDB 9BOP 9BOP -27 113 DBREF1 9BOP S 32 309 UNP A0A8G0KJC2_9MONO DBREF2 9BOP S A0A8G0KJC2 32 309 DBREF1 9BOP V 503 637 UNP A0A8G0KMX8_9MONO DBREF2 9BOP V A0A8G0KMX8 503 637 DBREF 9BOP C -23 124 PDB 9BOP 9BOP -23 124 DBREF 9BOP E -23 124 PDB 9BOP 9BOP -23 124 DBREF 9BOP D -26 113 PDB 9BOP 9BOP -26 113 DBREF 9BOP F -26 113 PDB 9BOP 9BOP -26 113 DBREF1 9BOP W 503 637 UNP A0A8G0KMX8_9MONO DBREF2 9BOP W A0A8G0KMX8 503 637 DBREF1 9BOP X 503 637 UNP A0A8G0KMX8_9MONO DBREF2 9BOP X A0A8G0KMX8 503 637 DBREF1 9BOP T 32 309 UNP A0A8G0KJC2_9MONO DBREF2 9BOP T A0A8G0KJC2 32 309 DBREF1 9BOP U 32 309 UNP A0A8G0KJC2_9MONO DBREF2 9BOP U A0A8G0KJC2 32 309 SEQADV 9BOP ARG S 31 UNP A0A8G0KJC EXPRESSION TAG SEQADV 9BOP ARG T 31 UNP A0A8G0KJC EXPRESSION TAG SEQADV 9BOP ARG U 31 UNP A0A8G0KJC EXPRESSION TAG SEQRES 1 A 148 SER PHE GLU ALA THR MET GLU THR GLY LEU ARG TRP LEU SEQRES 2 A 148 LEU LEU VAL ALA VAL LEU LYS GLY VAL GLN CYS GLN GLU SEQRES 3 A 148 GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLU SEQRES 4 A 148 GLY SER LEU THR LEU THR CYS THR ALA SER GLY PHE SER SEQRES 5 A 148 PHE SER SER ASN CYS TRP ARG CYS TRP VAL ARG GLN ALA SEQRES 6 A 148 PRO GLY LYS GLY LEU GLU TRP ILE ALA CYS VAL CYS ALA SEQRES 7 A 148 GLY ARG SER GLY GLY THR THR TYR TYR ALA SER TRP ALA SEQRES 8 A 148 LYS GLY ARG PHE THR ILE SER LYS THR SER SER PRO THR SEQRES 9 A 148 VAL THR LEU GLN MET THR SER LEU THR ALA ALA ASP THR SEQRES 10 A 148 ALA THR TYR PHE CYS ALA ARG ALA GLY TYR ASP ASP TYR SEQRES 11 A 148 GLY ASP ALA SER PHE PHE ASN LEU TRP GLY PRO GLY THR SEQRES 12 A 148 LEU VAL THR VAL SER SEQRES 1 B 140 SER PHE GLU ALA THR MET ASN MET ARG ALA PRO THR GLN SEQRES 2 B 140 LEU LEU GLY LEU LEU LEU LEU TRP LEU PRO GLY ALA ARG SEQRES 3 B 140 CYS ALA VAL VAL LEU THR GLN THR ALA SER PRO VAL SER SEQRES 4 B 140 THR PRO VAL GLY GLY THR VAL THR ILE LYS CYS GLN ALA SEQRES 5 B 140 SER GLN ASN ILE TYR SER ASN LEU ALA TRP TYR GLN GLN SEQRES 6 B 140 LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR SER ALA SEQRES 7 B 140 SER THR LEU ALA SER GLY VAL PRO SER ARG PHE LYS GLY SEQRES 8 B 140 SER GLY SER GLY THR GLU TYR THR LEU THR ILE SER ASP SEQRES 9 B 140 LEU GLU CYS ALA ASP ALA ALA THR TYR TYR CYS GLN ARG SEQRES 10 B 140 TYR TYR TYR LEU SER GLY SER ALA ASP ASN THR PHE GLY SEQRES 11 B 140 GLY GLY THR GLU VAL VAL VAL LYS ARG THR SEQRES 1 M 146 ARG SER PHE GLU ALA THR MET GLU THR GLY LEU ARG TRP SEQRES 2 M 146 LEU LEU LEU VAL ALA VAL LEU LYS GLY VAL GLN CYS GLN SEQRES 3 M 146 SER VAL GLU GLU SER GLY GLY ARG LEU VAL THR PRO GLY SEQRES 4 M 146 THR PRO LEU THR LEU THR CYS ILE VAL SER GLY PHE SER SEQRES 5 M 146 LEU SER ASN TYR TYR MET SER TRP VAL ARG GLN VAL PRO SEQRES 6 M 146 GLY LYS GLY LEU GLU TRP ILE GLY VAL ILE GLY TRP SER SEQRES 7 M 146 GLY THR SER SER TYR ALA SER TRP ALA LYS GLY ARG PHE SEQRES 8 M 146 THR ILE SER LYS THR ALA SER THR THR VAL ASP LEU LYS SEQRES 9 M 146 ILE THR SER PRO THR THR GLU ASP THR ALA THR TYR PHE SEQRES 10 M 146 CYS ALA ARG VAL LEU TYR ILE GLY GLY GLY PHE ASN TYR SEQRES 11 M 146 TYR ASP ALA PHE ASP PRO TRP GLY PRO GLY THR LEU VAL SEQRES 12 M 146 THR VAL SER SEQRES 1 N 141 ARG SER PHE GLU ALA THR MET ASN MET ARG ALA PRO THR SEQRES 2 N 141 GLN LEU LEU GLY LEU LEU LEU LEU TRP LEU PRO GLY ALA SEQRES 3 N 141 ARG CYS ASP VAL VAL MET THR GLN THR PRO ALA SER VAL SEQRES 4 N 141 SER GLU PRO VAL GLY GLY THR VAL THR ILE LYS CYS GLN SEQRES 5 N 141 ALA SER GLN SER ILE GLY SER ASN LEU ALA TRP TYR GLN SEQRES 6 N 141 GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ALA SEQRES 7 N 141 ALA SER THR LEU ALA SER GLY VAL PRO SER ARG PHE LYS SEQRES 8 N 141 GLY SER GLY SER GLY THR GLU PHE THR LEU THR ILE SER SEQRES 9 N 141 ASP LEU GLU CYS ALA ASP ALA ALA THR TYR TYR CYS GLN SEQRES 10 N 141 CYS THR TYR TYR ASP SER SER TYR VAL TYR ASN ASN PHE SEQRES 11 N 141 GLY GLY GLY THR GLU VAL VAL VAL LYS ARG THR SEQRES 1 O 146 ARG SER PHE GLU ALA THR MET GLU THR GLY LEU ARG TRP SEQRES 2 O 146 LEU LEU LEU VAL ALA VAL LEU LYS GLY VAL GLN CYS GLN SEQRES 3 O 146 SER VAL GLU GLU SER GLY GLY ARG LEU VAL THR PRO GLY SEQRES 4 O 146 THR PRO LEU THR LEU THR CYS ILE VAL SER GLY PHE SER SEQRES 5 O 146 LEU SER ASN TYR TYR MET SER TRP VAL ARG GLN VAL PRO SEQRES 6 O 146 GLY LYS GLY LEU GLU TRP ILE GLY VAL ILE GLY TRP SER SEQRES 7 O 146 GLY THR SER SER TYR ALA SER TRP ALA LYS GLY ARG PHE SEQRES 8 O 146 THR ILE SER LYS THR ALA SER THR THR VAL ASP LEU LYS SEQRES 9 O 146 ILE THR SER PRO THR THR GLU ASP THR ALA THR TYR PHE SEQRES 10 O 146 CYS ALA ARG VAL LEU TYR ILE GLY GLY GLY PHE ASN TYR SEQRES 11 O 146 TYR ASP ALA PHE ASP PRO TRP GLY PRO GLY THR LEU VAL SEQRES 12 O 146 THR VAL SER SEQRES 1 P 141 ARG SER PHE GLU ALA THR MET ASN MET ARG ALA PRO THR SEQRES 2 P 141 GLN LEU LEU GLY LEU LEU LEU LEU TRP LEU PRO GLY ALA SEQRES 3 P 141 ARG CYS ASP VAL VAL MET THR GLN THR PRO ALA SER VAL SEQRES 4 P 141 SER GLU PRO VAL GLY GLY THR VAL THR ILE LYS CYS GLN SEQRES 5 P 141 ALA SER GLN SER ILE GLY SER ASN LEU ALA TRP TYR GLN SEQRES 6 P 141 GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ALA SEQRES 7 P 141 ALA SER THR LEU ALA SER GLY VAL PRO SER ARG PHE LYS SEQRES 8 P 141 GLY SER GLY SER GLY THR GLU PHE THR LEU THR ILE SER SEQRES 9 P 141 ASP LEU GLU CYS ALA ASP ALA ALA THR TYR TYR CYS GLN SEQRES 10 P 141 CYS THR TYR TYR ASP SER SER TYR VAL TYR ASN ASN PHE SEQRES 11 P 141 GLY GLY GLY THR GLU VAL VAL VAL LYS ARG THR SEQRES 1 S 279 ARG SER ILE PRO LEU GLY VAL ILE HIS ASN SER THR LEU SEQRES 2 S 279 GLN VAL SER ASP VAL ASP LYS LEU VAL CYS ARG ASP LYS SEQRES 3 S 279 LEU SER SER THR ASN GLN LEU ARG SER VAL GLY LEU ASN SEQRES 4 S 279 LEU GLU GLY ASN GLY VAL ALA THR ASP VAL PRO SER ALA SEQRES 5 S 279 THR LYS ARG TRP GLY PHE ARG SER GLY VAL PRO PRO LYS SEQRES 6 S 279 VAL VAL ASN TYR GLU ALA GLY GLU TRP ALA GLU ASN CYS SEQRES 7 S 279 TYR ASN LEU GLU ILE LYS LYS PRO ASP GLY SER GLU CYS SEQRES 8 S 279 LEU PRO ALA ALA PRO ASP GLY ILE ARG GLY PHE PRO ARG SEQRES 9 S 279 CYS ARG TYR VAL HIS LYS VAL SER GLY THR GLY PRO CYS SEQRES 10 S 279 ALA GLY ASP PHE ALA PHE HIS LYS GLU GLY ALA PHE PHE SEQRES 11 S 279 LEU TYR ASP ARG LEU ALA SER THR VAL ILE TYR ARG GLY SEQRES 12 S 279 THR THR PHE ALA GLU GLY VAL VAL ALA PHE LEU ILE LEU SEQRES 13 S 279 PRO GLN ALA LYS LYS ASP PHE PHE SER SER HIS PRO LEU SEQRES 14 S 279 ARG GLU PRO VAL ASN ALA THR GLU ASP PRO SER SER GLY SEQRES 15 S 279 TYR TYR SER THR THR ILE ARG TYR GLN ALA THR GLY PHE SEQRES 16 S 279 GLY THR ASN GLU THR GLU TYR LEU PHE GLU VAL ASP ASN SEQRES 17 S 279 LEU THR TYR VAL GLN LEU GLU SER ARG PHE THR PRO GLN SEQRES 18 S 279 PHE LEU LEU GLN LEU ASN GLU THR ILE TYR THR SER GLY SEQRES 19 S 279 LYS ARG SER ASN THR THR GLY LYS LEU ILE TRP LYS VAL SEQRES 20 S 279 ASN PRO GLU ILE ASP THR THR ILE GLY GLU TRP ALA PHE SEQRES 21 S 279 TRP GLU THR LYS LYS ASN LEU THR ARG LYS ILE ARG SER SEQRES 22 S 279 GLU GLU LEU SER PHE THR SEQRES 1 V 135 ALA ILE VAL ASN ALA GLN PRO LYS CYS ASN PRO ASN LEU SEQRES 2 V 135 HIS TYR TRP THR THR GLN ASP GLU GLY ALA ALA ILE GLY SEQRES 3 V 135 LEU ALA TRP ILE PRO TYR PHE GLY PRO ALA ALA GLU GLY SEQRES 4 V 135 ILE TYR THR GLU GLY LEU MET HIS ASN GLN ASP GLY LEU SEQRES 5 V 135 ILE CYS GLY LEU ARG GLN LEU ALA ASN GLU THR THR GLN SEQRES 6 V 135 ALA LEU GLN LEU PHE LEU ARG ALA THR THR GLU LEU ARG SEQRES 7 V 135 THR PHE SER ILE LEU ASN ARG LYS ALA ILE ASP PHE LEU SEQRES 8 V 135 LEU GLN ARG TRP GLY GLY THR CYS HIS ILE LEU GLY PRO SEQRES 9 V 135 ASP CYS CYS ILE GLU PRO HIS ASP TRP THR LYS ASN ILE SEQRES 10 V 135 THR ASP LYS ILE ASP GLN ILE ILE HIS ASP PHE VAL ASP SEQRES 11 V 135 LYS THR LEU PRO ASP SEQRES 1 C 148 SER PHE GLU ALA THR MET GLU THR GLY LEU ARG TRP LEU SEQRES 2 C 148 LEU LEU VAL ALA VAL LEU LYS GLY VAL GLN CYS GLN GLU SEQRES 3 C 148 GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLU SEQRES 4 C 148 GLY SER LEU THR LEU THR CYS THR ALA SER GLY PHE SER SEQRES 5 C 148 PHE SER SER ASN CYS TRP ARG CYS TRP VAL ARG GLN ALA SEQRES 6 C 148 PRO GLY LYS GLY LEU GLU TRP ILE ALA CYS VAL CYS ALA SEQRES 7 C 148 GLY ARG SER GLY GLY THR THR TYR TYR ALA SER TRP ALA SEQRES 8 C 148 LYS GLY ARG PHE THR ILE SER LYS THR SER SER PRO THR SEQRES 9 C 148 VAL THR LEU GLN MET THR SER LEU THR ALA ALA ASP THR SEQRES 10 C 148 ALA THR TYR PHE CYS ALA ARG ALA GLY TYR ASP ASP TYR SEQRES 11 C 148 GLY ASP ALA SER PHE PHE ASN LEU TRP GLY PRO GLY THR SEQRES 12 C 148 LEU VAL THR VAL SER SEQRES 1 E 148 SER PHE GLU ALA THR MET GLU THR GLY LEU ARG TRP LEU SEQRES 2 E 148 LEU LEU VAL ALA VAL LEU LYS GLY VAL GLN CYS GLN GLU SEQRES 3 E 148 GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLU SEQRES 4 E 148 GLY SER LEU THR LEU THR CYS THR ALA SER GLY PHE SER SEQRES 5 E 148 PHE SER SER ASN CYS TRP ARG CYS TRP VAL ARG GLN ALA SEQRES 6 E 148 PRO GLY LYS GLY LEU GLU TRP ILE ALA CYS VAL CYS ALA SEQRES 7 E 148 GLY ARG SER GLY GLY THR THR TYR TYR ALA SER TRP ALA SEQRES 8 E 148 LYS GLY ARG PHE THR ILE SER LYS THR SER SER PRO THR SEQRES 9 E 148 VAL THR LEU GLN MET THR SER LEU THR ALA ALA ASP THR SEQRES 10 E 148 ALA THR TYR PHE CYS ALA ARG ALA GLY TYR ASP ASP TYR SEQRES 11 E 148 GLY ASP ALA SER PHE PHE ASN LEU TRP GLY PRO GLY THR SEQRES 12 E 148 LEU VAL THR VAL SER SEQRES 1 D 140 SER PHE GLU ALA THR MET ASN MET ARG ALA PRO THR GLN SEQRES 2 D 140 LEU LEU GLY LEU LEU LEU LEU TRP LEU PRO GLY ALA ARG SEQRES 3 D 140 CYS ALA VAL VAL LEU THR GLN THR ALA SER PRO VAL SER SEQRES 4 D 140 THR PRO VAL GLY GLY THR VAL THR ILE LYS CYS GLN ALA SEQRES 5 D 140 SER GLN ASN ILE TYR SER ASN LEU ALA TRP TYR GLN GLN SEQRES 6 D 140 LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR SER ALA SEQRES 7 D 140 SER THR LEU ALA SER GLY VAL PRO SER ARG PHE LYS GLY SEQRES 8 D 140 SER GLY SER GLY THR GLU TYR THR LEU THR ILE SER ASP SEQRES 9 D 140 LEU GLU CYS ALA ASP ALA ALA THR TYR TYR CYS GLN ARG SEQRES 10 D 140 TYR TYR TYR LEU SER GLY SER ALA ASP ASN THR PHE GLY SEQRES 11 D 140 GLY GLY THR GLU VAL VAL VAL LYS ARG THR SEQRES 1 F 140 SER PHE GLU ALA THR MET ASN MET ARG ALA PRO THR GLN SEQRES 2 F 140 LEU LEU GLY LEU LEU LEU LEU TRP LEU PRO GLY ALA ARG SEQRES 3 F 140 CYS ALA VAL VAL LEU THR GLN THR ALA SER PRO VAL SER SEQRES 4 F 140 THR PRO VAL GLY GLY THR VAL THR ILE LYS CYS GLN ALA SEQRES 5 F 140 SER GLN ASN ILE TYR SER ASN LEU ALA TRP TYR GLN GLN SEQRES 6 F 140 LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR SER ALA SEQRES 7 F 140 SER THR LEU ALA SER GLY VAL PRO SER ARG PHE LYS GLY SEQRES 8 F 140 SER GLY SER GLY THR GLU TYR THR LEU THR ILE SER ASP SEQRES 9 F 140 LEU GLU CYS ALA ASP ALA ALA THR TYR TYR CYS GLN ARG SEQRES 10 F 140 TYR TYR TYR LEU SER GLY SER ALA ASP ASN THR PHE GLY SEQRES 11 F 140 GLY GLY THR GLU VAL VAL VAL LYS ARG THR SEQRES 1 W 135 ALA ILE VAL ASN ALA GLN PRO LYS CYS ASN PRO ASN LEU SEQRES 2 W 135 HIS TYR TRP THR THR GLN ASP GLU GLY ALA ALA ILE GLY SEQRES 3 W 135 LEU ALA TRP ILE PRO TYR PHE GLY PRO ALA ALA GLU GLY SEQRES 4 W 135 ILE TYR THR GLU GLY LEU MET HIS ASN GLN ASP GLY LEU SEQRES 5 W 135 ILE CYS GLY LEU ARG GLN LEU ALA ASN GLU THR THR GLN SEQRES 6 W 135 ALA LEU GLN LEU PHE LEU ARG ALA THR THR GLU LEU ARG SEQRES 7 W 135 THR PHE SER ILE LEU ASN ARG LYS ALA ILE ASP PHE LEU SEQRES 8 W 135 LEU GLN ARG TRP GLY GLY THR CYS HIS ILE LEU GLY PRO SEQRES 9 W 135 ASP CYS CYS ILE GLU PRO HIS ASP TRP THR LYS ASN ILE SEQRES 10 W 135 THR ASP LYS ILE ASP GLN ILE ILE HIS ASP PHE VAL ASP SEQRES 11 W 135 LYS THR LEU PRO ASP SEQRES 1 X 135 ALA ILE VAL ASN ALA GLN PRO LYS CYS ASN PRO ASN LEU SEQRES 2 X 135 HIS TYR TRP THR THR GLN ASP GLU GLY ALA ALA ILE GLY SEQRES 3 X 135 LEU ALA TRP ILE PRO TYR PHE GLY PRO ALA ALA GLU GLY SEQRES 4 X 135 ILE TYR THR GLU GLY LEU MET HIS ASN GLN ASP GLY LEU SEQRES 5 X 135 ILE CYS GLY LEU ARG GLN LEU ALA ASN GLU THR THR GLN SEQRES 6 X 135 ALA LEU GLN LEU PHE LEU ARG ALA THR THR GLU LEU ARG SEQRES 7 X 135 THR PHE SER ILE LEU ASN ARG LYS ALA ILE ASP PHE LEU SEQRES 8 X 135 LEU GLN ARG TRP GLY GLY THR CYS HIS ILE LEU GLY PRO SEQRES 9 X 135 ASP CYS CYS ILE GLU PRO HIS ASP TRP THR LYS ASN ILE SEQRES 10 X 135 THR ASP LYS ILE ASP GLN ILE ILE HIS ASP PHE VAL ASP SEQRES 11 X 135 LYS THR LEU PRO ASP SEQRES 1 T 279 ARG SER ILE PRO LEU GLY VAL ILE HIS ASN SER THR LEU SEQRES 2 T 279 GLN VAL SER ASP VAL ASP LYS LEU VAL CYS ARG ASP LYS SEQRES 3 T 279 LEU SER SER THR ASN GLN LEU ARG SER VAL GLY LEU ASN SEQRES 4 T 279 LEU GLU GLY ASN GLY VAL ALA THR ASP VAL PRO SER ALA SEQRES 5 T 279 THR LYS ARG TRP GLY PHE ARG SER GLY VAL PRO PRO LYS SEQRES 6 T 279 VAL VAL ASN TYR GLU ALA GLY GLU TRP ALA GLU ASN CYS SEQRES 7 T 279 TYR ASN LEU GLU ILE LYS LYS PRO ASP GLY SER GLU CYS SEQRES 8 T 279 LEU PRO ALA ALA PRO ASP GLY ILE ARG GLY PHE PRO ARG SEQRES 9 T 279 CYS ARG TYR VAL HIS LYS VAL SER GLY THR GLY PRO CYS SEQRES 10 T 279 ALA GLY ASP PHE ALA PHE HIS LYS GLU GLY ALA PHE PHE SEQRES 11 T 279 LEU TYR ASP ARG LEU ALA SER THR VAL ILE TYR ARG GLY SEQRES 12 T 279 THR THR PHE ALA GLU GLY VAL VAL ALA PHE LEU ILE LEU SEQRES 13 T 279 PRO GLN ALA LYS LYS ASP PHE PHE SER SER HIS PRO LEU SEQRES 14 T 279 ARG GLU PRO VAL ASN ALA THR GLU ASP PRO SER SER GLY SEQRES 15 T 279 TYR TYR SER THR THR ILE ARG TYR GLN ALA THR GLY PHE SEQRES 16 T 279 GLY THR ASN GLU THR GLU TYR LEU PHE GLU VAL ASP ASN SEQRES 17 T 279 LEU THR TYR VAL GLN LEU GLU SER ARG PHE THR PRO GLN SEQRES 18 T 279 PHE LEU LEU GLN LEU ASN GLU THR ILE TYR THR SER GLY SEQRES 19 T 279 LYS ARG SER ASN THR THR GLY LYS LEU ILE TRP LYS VAL SEQRES 20 T 279 ASN PRO GLU ILE ASP THR THR ILE GLY GLU TRP ALA PHE SEQRES 21 T 279 TRP GLU THR LYS LYS ASN LEU THR ARG LYS ILE ARG SER SEQRES 22 T 279 GLU GLU LEU SER PHE THR SEQRES 1 U 279 ARG SER ILE PRO LEU GLY VAL ILE HIS ASN SER THR LEU SEQRES 2 U 279 GLN VAL SER ASP VAL ASP LYS LEU VAL CYS ARG ASP LYS SEQRES 3 U 279 LEU SER SER THR ASN GLN LEU ARG SER VAL GLY LEU ASN SEQRES 4 U 279 LEU GLU GLY ASN GLY VAL ALA THR ASP VAL PRO SER ALA SEQRES 5 U 279 THR LYS ARG TRP GLY PHE ARG SER GLY VAL PRO PRO LYS SEQRES 6 U 279 VAL VAL ASN TYR GLU ALA GLY GLU TRP ALA GLU ASN CYS SEQRES 7 U 279 TYR ASN LEU GLU ILE LYS LYS PRO ASP GLY SER GLU CYS SEQRES 8 U 279 LEU PRO ALA ALA PRO ASP GLY ILE ARG GLY PHE PRO ARG SEQRES 9 U 279 CYS ARG TYR VAL HIS LYS VAL SER GLY THR GLY PRO CYS SEQRES 10 U 279 ALA GLY ASP PHE ALA PHE HIS LYS GLU GLY ALA PHE PHE SEQRES 11 U 279 LEU TYR ASP ARG LEU ALA SER THR VAL ILE TYR ARG GLY SEQRES 12 U 279 THR THR PHE ALA GLU GLY VAL VAL ALA PHE LEU ILE LEU SEQRES 13 U 279 PRO GLN ALA LYS LYS ASP PHE PHE SER SER HIS PRO LEU SEQRES 14 U 279 ARG GLU PRO VAL ASN ALA THR GLU ASP PRO SER SER GLY SEQRES 15 U 279 TYR TYR SER THR THR ILE ARG TYR GLN ALA THR GLY PHE SEQRES 16 U 279 GLY THR ASN GLU THR GLU TYR LEU PHE GLU VAL ASP ASN SEQRES 17 U 279 LEU THR TYR VAL GLN LEU GLU SER ARG PHE THR PRO GLN SEQRES 18 U 279 PHE LEU LEU GLN LEU ASN GLU THR ILE TYR THR SER GLY SEQRES 19 U 279 LYS ARG SER ASN THR THR GLY LYS LEU ILE TRP LYS VAL SEQRES 20 U 279 ASN PRO GLU ILE ASP THR THR ILE GLY GLU TRP ALA PHE SEQRES 21 U 279 TRP GLU THR LYS LYS ASN LEU THR ARG LYS ILE ARG SER SEQRES 22 U 279 GLU GLU LEU SER PHE THR HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET MAN G 4 11 HET MAN G 5 11 HET NAG H 1 14 HET NAG H 2 14 HET BMA H 3 11 HET MAN H 4 11 HET MAN H 5 11 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET MAN I 4 11 HET MAN I 5 11 HET NAG S 401 14 HET NAG S 402 14 HET NAG S 403 14 HET NAG T 401 14 HET NAG T 402 14 HET NAG T 403 14 HET NAG U 401 14 HET NAG U 402 14 HET NAG U 403 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 17 NAG 15(C8 H15 N O6) FORMUL 17 BMA 3(C6 H12 O6) FORMUL 17 MAN 6(C6 H12 O6) HELIX 1 AA1 THR A 89 THR A 93 5 5 HELIX 2 AA2 SER M 27 TYR M 31 5 5 HELIX 3 AA3 SER M 60 LYS M 63 5 4 HELIX 4 AA4 THR M 84 THR M 88 5 5 HELIX 5 AA5 GLU N 79 ALA N 83 5 5 HELIX 6 AA6 GLU S 71 GLY S 74 5 4 HELIX 7 AA7 ASP S 78 THR S 83 1 6 HELIX 8 AA8 THR S 249 GLY S 264 1 16 HELIX 9 AA9 GLY V 553 THR V 576 1 24 HELIX 10 AB1 SER V 583 TRP V 597 1 15 HELIX 11 AB2 THR C 89 THR C 93 5 5 HELIX 12 AB3 THR E 89 THR E 93 5 5 HELIX 13 AB4 GLY W 553 THR W 576 1 24 HELIX 14 AB5 SER W 583 TRP W 597 1 15 HELIX 15 AB6 GLY X 553 THR X 576 1 24 HELIX 16 AB7 SER X 583 TRP X 597 1 15 HELIX 17 AB8 GLU T 71 GLY T 74 5 4 HELIX 18 AB9 ASP T 78 THR T 83 1 6 HELIX 19 AC1 THR T 249 GLY T 264 1 16 HELIX 20 AC2 GLU U 71 GLY U 74 5 4 HELIX 21 AC3 ASP U 78 THR U 83 1 6 HELIX 22 AC4 THR U 249 GLY U 264 1 16 SHEET 1 AA1 4 GLU A 6 SER A 7 0 SHEET 2 AA1 4 SER A 17 CYS A 22 -1 O THR A 21 N SER A 7 SHEET 3 AA1 4 VAL A 81 THR A 86 -1 O LEU A 83 N LEU A 20 SHEET 4 AA1 4 PHE A 71 SER A 74 -1 N THR A 72 O GLN A 84 SHEET 1 AA2 5 THR A 61 TYR A 63 0 SHEET 2 AA2 5 LEU A 46 CYS A 53 -1 N CYS A 51 O TYR A 62 SHEET 3 AA2 5 TRP A 34 GLN A 40 -1 N ARG A 39 O GLU A 47 SHEET 4 AA2 5 ALA A 94 ASP A 104 -1 O THR A 95 N GLN A 40 SHEET 5 AA2 5 GLY A 107 LEU A 114 -1 O GLY A 107 N ASP A 104 SHEET 1 AA3 5 THR A 61 TYR A 63 0 SHEET 2 AA3 5 LEU A 46 CYS A 53 -1 N CYS A 51 O TYR A 62 SHEET 3 AA3 5 TRP A 34 GLN A 40 -1 N ARG A 39 O GLU A 47 SHEET 4 AA3 5 ALA A 94 ASP A 104 -1 O THR A 95 N GLN A 40 SHEET 5 AA3 5 THR A 119 VAL A 121 -1 O VAL A 121 N ALA A 94 SHEET 1 AA4 6 VAL B 11 SER B 12 0 SHEET 2 AA4 6 THR B 106 VAL B 109 1 O VAL B 109 N VAL B 11 SHEET 3 AA4 6 THR B 85 ARG B 90 -1 N TYR B 86 O THR B 106 SHEET 4 AA4 6 LEU B 33 GLN B 38 -1 N GLN B 38 O THR B 85 SHEET 5 AA4 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA4 6 THR B 53 LEU B 54 -1 O THR B 53 N TYR B 49 SHEET 1 AA5 4 VAL B 11 SER B 12 0 SHEET 2 AA5 4 THR B 106 VAL B 109 1 O VAL B 109 N VAL B 11 SHEET 3 AA5 4 THR B 85 ARG B 90 -1 N TYR B 86 O THR B 106 SHEET 4 AA5 4 THR B 101 PHE B 102 -1 O THR B 101 N ARG B 90 SHEET 1 AA6 3 VAL B 19 GLN B 24 0 SHEET 2 AA6 3 GLU B 70 ILE B 75 -1 O TYR B 71 N CYS B 23 SHEET 3 AA6 3 PHE B 62 SER B 67 -1 N LYS B 63 O THR B 74 SHEET 1 AA7 4 SER M 2 SER M 6 0 SHEET 2 AA7 4 LEU M 17 SER M 24 -1 O THR M 20 N SER M 6 SHEET 3 AA7 4 THR M 75 ILE M 80 -1 O VAL M 76 N CYS M 21 SHEET 4 AA7 4 PHE M 66 THR M 71 -1 N THR M 67 O LYS M 79 SHEET 1 AA8 5 SER M 56 TYR M 58 0 SHEET 2 AA8 5 LEU M 44 ILE M 50 -1 N VAL M 49 O SER M 57 SHEET 3 AA8 5 MET M 33 GLN M 38 -1 N TRP M 35 O ILE M 47 SHEET 4 AA8 5 ALA M 89 TYR M 91 -1 O THR M 90 N GLN M 38 SHEET 5 AA8 5 THR M 116 VAL M 118 -1 O VAL M 118 N ALA M 89 SHEET 1 AA9 2 VAL M 96 LEU M 97 0 SHEET 2 AA9 2 ALA M 108 PHE M 109 -1 O ALA M 108 N LEU M 97 SHEET 1 AB1 4 MET N 4 GLN N 6 0 SHEET 2 AB1 4 THR N 18 ALA N 25 -1 O GLN N 24 N THR N 5 SHEET 3 AB1 4 GLU N 70 SER N 76 -1 O PHE N 71 N CYS N 23 SHEET 4 AB1 4 PHE N 62 SER N 67 -1 N LYS N 63 O THR N 74 SHEET 1 AB2 6 SER N 10 VAL N 11 0 SHEET 2 AB2 6 THR N 106 VAL N 108 1 O GLU N 107 N VAL N 11 SHEET 3 AB2 6 THR N 85 CYS N 90 -1 N TYR N 86 O THR N 106 SHEET 4 AB2 6 LEU N 33 GLN N 38 -1 N GLN N 38 O THR N 85 SHEET 5 AB2 6 LYS N 45 TYR N 49 -1 O LEU N 47 N TRP N 35 SHEET 6 AB2 6 THR N 53 LEU N 54 -1 O THR N 53 N TYR N 49 SHEET 1 AB3 4 SER O 2 SER O 6 0 SHEET 2 AB3 4 THR O 20 SER O 24 -1 O ILE O 22 N GLU O 4 SHEET 3 AB3 4 THR O 75 ILE O 80 -1 O VAL O 76 N CYS O 21 SHEET 4 AB3 4 LEU O 17 THR O 18 -1 N LEU O 17 O ILE O 80 SHEET 1 AB4 4 SER O 2 SER O 6 0 SHEET 2 AB4 4 THR O 20 SER O 24 -1 O ILE O 22 N GLU O 4 SHEET 3 AB4 4 THR O 75 ILE O 80 -1 O VAL O 76 N CYS O 21 SHEET 4 AB4 4 PHE O 66 THR O 71 -1 N SER O 69 O ASP O 77 SHEET 1 AB5 5 SER O 56 TYR O 58 0 SHEET 2 AB5 5 GLU O 45 ILE O 50 -1 N VAL O 49 O SER O 57 SHEET 3 AB5 5 MET O 33 GLN O 38 -1 N TRP O 35 O ILE O 47 SHEET 4 AB5 5 ALA O 94 LEU O 97 -1 O ALA O 94 N SER O 34 SHEET 5 AB5 5 ALA O 108 TRP O 112 -1 O ALA O 108 N LEU O 97 SHEET 1 AB6 5 SER O 56 TYR O 58 0 SHEET 2 AB6 5 GLU O 45 ILE O 50 -1 N VAL O 49 O SER O 57 SHEET 3 AB6 5 MET O 33 GLN O 38 -1 N TRP O 35 O ILE O 47 SHEET 4 AB6 5 ALA O 89 TYR O 91 -1 O THR O 90 N GLN O 38 SHEET 5 AB6 5 THR O 116 VAL O 118 -1 O VAL O 118 N ALA O 89 SHEET 1 AB7 4 MET P 4 GLN P 6 0 SHEET 2 AB7 4 THR P 20 ALA P 25 -1 O GLN P 24 N THR P 5 SHEET 3 AB7 4 GLU P 70 THR P 74 -1 O PHE P 71 N CYS P 23 SHEET 4 AB7 4 LYS P 63 SER P 67 -1 N LYS P 63 O THR P 74 SHEET 1 AB8 6 SER P 10 VAL P 11 0 SHEET 2 AB8 6 THR P 106 VAL P 108 1 O GLU P 107 N VAL P 11 SHEET 3 AB8 6 THR P 85 CYS P 90 -1 N TYR P 86 O THR P 106 SHEET 4 AB8 6 LEU P 33 GLN P 38 -1 N ALA P 34 O GLN P 89 SHEET 5 AB8 6 LYS P 45 TYR P 49 -1 O LYS P 45 N GLN P 37 SHEET 6 AB8 6 THR P 53 LEU P 54 -1 O THR P 53 N TYR P 49 SHEET 1 AB9 4 THR S 42 VAL S 45 0 SHEET 2 AB9 4 GLY S 36 HIS S 39 -1 N VAL S 37 O GLN S 44 SHEET 3 AB9 4 GLU S 178 ILE S 185 1 O PHE S 183 N GLY S 36 SHEET 4 AB9 4 LEU S 63 ASN S 69 -1 N ARG S 64 O LEU S 184 SHEET 1 AC1 4 THR S 42 VAL S 45 0 SHEET 2 AC1 4 GLY S 36 HIS S 39 -1 N VAL S 37 O GLN S 44 SHEET 3 AC1 4 GLU S 178 ILE S 185 1 O PHE S 183 N GLY S 36 SHEET 4 AC1 4 PHE S 159 PHE S 160 -1 N PHE S 159 O GLY S 179 SHEET 1 AC2 2 TRP S 86 ARG S 89 0 SHEET 2 AC2 2 PHE S 151 HIS S 154 -1 O PHE S 151 N ARG S 89 SHEET 1 AC3 3 LEU S 165 SER S 167 0 SHEET 2 AC3 3 VAL S 96 ASN S 98 -1 N VAL S 97 O ALA S 166 SHEET 3 AC3 3 ARG V 580 THR V 581 1 O THR V 581 N VAL S 96 SHEET 1 AC4 3 ALA S 101 GLU S 103 0 SHEET 2 AC4 3 HIS V 516 THR V 519 -1 O TRP V 518 N GLY S 102 SHEET 3 AC4 3 GLY V 546 LEU V 547 -1 O GLY V 546 N TYR V 517 SHEET 1 AC5 7 ALA S 105 LYS S 114 0 SHEET 2 AC5 7 CYS S 135 THR S 144 1 O HIS S 139 N CYS S 108 SHEET 3 AC5 7 THR S 216 THR S 223 1 O THR S 216 N VAL S 138 SHEET 4 AC5 7 GLU S 231 GLU S 235 -1 O GLU S 235 N ARG S 219 SHEET 5 AC5 7 THR S 240 GLN S 243 -1 O VAL S 242 N PHE S 234 SHEET 6 AC5 7 LEU S 273 VAL S 277 1 O LEU S 273 N TYR S 241 SHEET 7 AC5 7 ILE S 285 GLY S 286 -1 O GLY S 286 N LYS S 276 SHEET 1 AC6 2 CYS V 601 HIS V 602 0 SHEET 2 AC6 2 ILE W 610 GLU W 611 1 O GLU W 611 N CYS V 601 SHEET 1 AC7 2 ILE V 610 GLU V 611 0 SHEET 2 AC7 2 CYS X 601 HIS X 602 1 O CYS X 601 N GLU V 611 SHEET 1 AC8 4 GLU C 6 SER C 7 0 SHEET 2 AC8 4 SER C 17 CYS C 22 -1 O THR C 21 N SER C 7 SHEET 3 AC8 4 VAL C 81 THR C 86 -1 O LEU C 83 N LEU C 20 SHEET 4 AC8 4 PHE C 71 ILE C 73 -1 N THR C 72 O GLN C 84 SHEET 1 AC9 5 TYR C 62 TYR C 63 0 SHEET 2 AC9 5 LEU C 46 CYS C 53 -1 N CYS C 51 O TYR C 62 SHEET 3 AC9 5 TRP C 34 GLN C 40 -1 N ARG C 39 O GLU C 47 SHEET 4 AC9 5 ALA C 94 ASP C 104 -1 O THR C 95 N GLN C 40 SHEET 5 AC9 5 GLY C 107 LEU C 114 -1 O PHE C 111 N GLY C 102 SHEET 1 AD1 5 TYR C 62 TYR C 63 0 SHEET 2 AD1 5 LEU C 46 CYS C 53 -1 N CYS C 51 O TYR C 62 SHEET 3 AD1 5 TRP C 34 GLN C 40 -1 N ARG C 39 O GLU C 47 SHEET 4 AD1 5 ALA C 94 ASP C 104 -1 O THR C 95 N GLN C 40 SHEET 5 AD1 5 THR C 119 VAL C 121 -1 O THR C 119 N TYR C 96 SHEET 1 AD2 4 GLU E 6 SER E 7 0 SHEET 2 AD2 4 SER E 17 CYS E 22 -1 O THR E 21 N SER E 7 SHEET 3 AD2 4 VAL E 81 THR E 86 -1 O LEU E 83 N LEU E 20 SHEET 4 AD2 4 THR E 72 SER E 74 -1 N THR E 72 O GLN E 84 SHEET 1 AD3 5 TYR E 62 TYR E 63 0 SHEET 2 AD3 5 LEU E 46 CYS E 53 -1 N CYS E 51 O TYR E 62 SHEET 3 AD3 5 TRP E 34 GLN E 40 -1 N ARG E 39 O GLU E 47 SHEET 4 AD3 5 ALA E 94 ASP E 104 -1 O THR E 95 N GLN E 40 SHEET 5 AD3 5 GLY E 107 LEU E 114 -1 O GLY E 107 N ASP E 104 SHEET 1 AD4 5 TYR E 62 TYR E 63 0 SHEET 2 AD4 5 LEU E 46 CYS E 53 -1 N CYS E 51 O TYR E 62 SHEET 3 AD4 5 TRP E 34 GLN E 40 -1 N ARG E 39 O GLU E 47 SHEET 4 AD4 5 ALA E 94 ASP E 104 -1 O THR E 95 N GLN E 40 SHEET 5 AD4 5 THR E 119 VAL E 121 -1 O VAL E 121 N ALA E 94 SHEET 1 AD5 2 LEU D 4 THR D 5 0 SHEET 2 AD5 2 GLN D 24 ALA D 25 -1 O GLN D 24 N THR D 5 SHEET 1 AD6 6 VAL D 11 SER D 12 0 SHEET 2 AD6 6 THR D 106 VAL D 109 1 O VAL D 109 N VAL D 11 SHEET 3 AD6 6 THR D 85 TYR D 91 -1 N TYR D 86 O THR D 106 SHEET 4 AD6 6 LEU D 33 GLN D 38 -1 N GLN D 38 O THR D 85 SHEET 5 AD6 6 LYS D 45 TYR D 49 -1 O LYS D 45 N GLN D 37 SHEET 6 AD6 6 THR D 53 LEU D 54 -1 O THR D 53 N TYR D 49 SHEET 1 AD7 4 VAL D 11 SER D 12 0 SHEET 2 AD7 4 THR D 106 VAL D 109 1 O VAL D 109 N VAL D 11 SHEET 3 AD7 4 THR D 85 TYR D 91 -1 N TYR D 86 O THR D 106 SHEET 4 AD7 4 ASN D 100 PHE D 102 -1 O THR D 101 N ARG D 90 SHEET 1 AD8 3 VAL D 19 LYS D 22 0 SHEET 2 AD8 3 GLU D 70 ILE D 75 -1 O ILE D 75 N VAL D 19 SHEET 3 AD8 3 PHE D 62 SER D 67 -1 N LYS D 63 O THR D 74 SHEET 1 AD9 4 LEU F 4 THR F 5 0 SHEET 2 AD9 4 VAL F 19 ALA F 25 -1 O GLN F 24 N THR F 5 SHEET 3 AD9 4 GLU F 70 ILE F 75 -1 O TYR F 71 N CYS F 23 SHEET 4 AD9 4 PHE F 62 SER F 67 -1 N LYS F 63 O THR F 74 SHEET 1 AE1 6 VAL F 11 SER F 12 0 SHEET 2 AE1 6 THR F 106 VAL F 109 1 O VAL F 109 N VAL F 11 SHEET 3 AE1 6 THR F 85 ARG F 90 -1 N TYR F 86 O THR F 106 SHEET 4 AE1 6 LEU F 33 GLN F 38 -1 N GLN F 38 O THR F 85 SHEET 5 AE1 6 LYS F 45 TYR F 49 -1 O LEU F 47 N TRP F 35 SHEET 6 AE1 6 THR F 53 LEU F 54 -1 O THR F 53 N TYR F 49 SHEET 1 AE2 3 GLY W 546 LEU W 547 0 SHEET 2 AE2 3 HIS W 516 THR W 519 -1 N TYR W 517 O GLY W 546 SHEET 3 AE2 3 ALA T 101 GLU T 103 -1 O GLY T 102 N TRP W 518 SHEET 1 AE3 3 ARG W 580 THR W 581 0 SHEET 2 AE3 3 VAL T 96 ASN T 98 1 O VAL T 96 N THR W 581 SHEET 3 AE3 3 LEU T 165 SER T 167 -1 O ALA T 166 N VAL T 97 SHEET 1 AE4 3 GLY X 546 LEU X 547 0 SHEET 2 AE4 3 HIS X 516 THR X 519 -1 N TYR X 517 O GLY X 546 SHEET 3 AE4 3 ALA U 101 GLU U 103 -1 O GLY U 102 N TRP X 518 SHEET 1 AE5 7 ARG X 580 THR X 581 0 SHEET 2 AE5 7 VAL U 96 ASN U 98 1 O VAL U 96 N THR X 581 SHEET 3 AE5 7 LEU U 165 SER U 167 -1 O ALA U 166 N VAL U 97 SHEET 4 AE5 7 PHE U 159 TYR U 162 -1 N TYR U 162 O LEU U 165 SHEET 5 AE5 7 ALA U 177 ILE U 185 -1 O ALA U 177 N LEU U 161 SHEET 6 AE5 7 GLY U 36 HIS U 39 1 N GLY U 36 O PHE U 183 SHEET 7 AE5 7 THR U 42 VAL U 45 -1 O GLN U 44 N VAL U 37 SHEET 1 AE6 6 ARG X 580 THR X 581 0 SHEET 2 AE6 6 VAL U 96 ASN U 98 1 O VAL U 96 N THR X 581 SHEET 3 AE6 6 LEU U 165 SER U 167 -1 O ALA U 166 N VAL U 97 SHEET 4 AE6 6 PHE U 159 TYR U 162 -1 N TYR U 162 O LEU U 165 SHEET 5 AE6 6 ALA U 177 ILE U 185 -1 O ALA U 177 N LEU U 161 SHEET 6 AE6 6 LEU U 63 ASN U 69 -1 N VAL U 66 O ALA U 182 SHEET 1 AE7 4 THR T 42 VAL T 45 0 SHEET 2 AE7 4 GLY T 36 HIS T 39 -1 N VAL T 37 O GLN T 44 SHEET 3 AE7 4 GLU T 178 ILE T 185 1 O PHE T 183 N GLY T 36 SHEET 4 AE7 4 LEU T 63 ASN T 69 -1 N ARG T 64 O LEU T 184 SHEET 1 AE8 4 THR T 42 VAL T 45 0 SHEET 2 AE8 4 GLY T 36 HIS T 39 -1 N VAL T 37 O GLN T 44 SHEET 3 AE8 4 GLU T 178 ILE T 185 1 O PHE T 183 N GLY T 36 SHEET 4 AE8 4 PHE T 159 PHE T 160 -1 N PHE T 159 O GLY T 179 SHEET 1 AE9 2 TRP T 86 ARG T 89 0 SHEET 2 AE9 2 PHE T 151 HIS T 154 -1 N PHE T 151 O ARG T 89 SHEET 1 AF1 7 ALA T 105 LYS T 114 0 SHEET 2 AF1 7 CYS T 135 THR T 144 1 O HIS T 139 N CYS T 108 SHEET 3 AF1 7 THR T 216 THR T 223 1 O TYR T 220 N LYS T 140 SHEET 4 AF1 7 GLU T 231 GLU T 235 -1 O GLU T 231 N THR T 223 SHEET 5 AF1 7 THR T 240 GLN T 243 -1 O VAL T 242 N PHE T 234 SHEET 6 AF1 7 LEU T 273 VAL T 277 1 O TRP T 275 N GLN T 243 SHEET 7 AF1 7 ILE T 285 GLY T 286 -1 O GLY T 286 N LYS T 276 SHEET 1 AF2 2 TRP U 86 ARG U 89 0 SHEET 2 AF2 2 PHE U 151 HIS U 154 -1 N PHE U 151 O ARG U 89 SHEET 1 AF3 3 ALA U 105 LYS U 114 0 SHEET 2 AF3 3 CYS U 135 THR U 144 1 O HIS U 139 N CYS U 108 SHEET 3 AF3 3 THR U 216 ARG U 219 1 O ILE U 218 N VAL U 138 SHEET 1 AF4 7 ALA U 105 LYS U 114 0 SHEET 2 AF4 7 CYS U 135 THR U 144 1 O HIS U 139 N CYS U 108 SHEET 3 AF4 7 ALA U 222 THR U 223 1 O ALA U 222 N THR U 144 SHEET 4 AF4 7 GLU U 231 GLU U 235 -1 O GLU U 231 N THR U 223 SHEET 5 AF4 7 THR U 240 GLN U 243 -1 O VAL U 242 N PHE U 234 SHEET 6 AF4 7 LEU U 273 VAL U 277 1 O TRP U 275 N TYR U 241 SHEET 7 AF4 7 ILE U 285 GLY U 286 -1 O GLY U 286 N LYS U 276 SSBOND 1 CYS A 22 CYS A 98 1555 1555 2.03 SSBOND 2 CYS A 36 CYS A 51 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.03 SSBOND 4 CYS M 21 CYS M 93 1555 1555 2.03 SSBOND 5 CYS N 23 CYS N 88 1555 1555 2.04 SSBOND 6 CYS O 21 CYS O 93 1555 1555 2.03 SSBOND 7 CYS P 23 CYS P 88 1555 1555 2.04 SSBOND 8 CYS S 108 CYS S 135 1555 1555 2.03 SSBOND 9 CYS S 121 CYS S 147 1555 1555 2.03 SSBOND 10 CYS V 511 CYS V 556 1555 1555 2.03 SSBOND 11 CYS V 601 CYS V 608 1555 1555 2.03 SSBOND 12 CYS C 22 CYS C 98 1555 1555 2.03 SSBOND 13 CYS C 36 CYS C 51 1555 1555 2.03 SSBOND 14 CYS E 22 CYS E 98 1555 1555 2.03 SSBOND 15 CYS E 36 CYS E 51 1555 1555 2.03 SSBOND 16 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 17 CYS F 23 CYS F 88 1555 1555 2.03 SSBOND 18 CYS W 511 CYS W 556 1555 1555 2.03 SSBOND 19 CYS W 601 CYS W 608 1555 1555 2.03 SSBOND 20 CYS X 511 CYS X 556 1555 1555 2.03 SSBOND 21 CYS X 601 CYS X 608 1555 1555 2.03 SSBOND 22 CYS T 108 CYS T 135 1555 1555 2.03 SSBOND 23 CYS T 121 CYS T 147 1555 1555 2.03 SSBOND 24 CYS U 108 CYS U 135 1555 1555 2.03 SSBOND 25 CYS U 121 CYS U 147 1555 1555 2.03 LINK ND2 ASN S 228 C1 NAG S 403 1555 1555 1.44 LINK ND2 ASN S 257 C1 NAG S 401 1555 1555 1.44 LINK O4 NAG S 401 C1 NAG S 402 1555 1555 1.44 LINK ND2 ASN V 563 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN W 563 C1 NAG H 1 1555 1555 1.44 LINK ND2 ASN X 563 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN T 228 C1 NAG T 403 1555 1555 1.44 LINK ND2 ASN T 257 C1 NAG T 401 1555 1555 1.44 LINK O4 NAG T 401 C1 NAG T 402 1555 1555 1.45 LINK ND2 ASN U 228 C1 NAG U 403 1555 1555 1.44 LINK ND2 ASN U 257 C1 NAG U 401 1555 1555 1.44 LINK O4 NAG U 401 C1 NAG U 402 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.44 LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.44 LINK O6 BMA G 3 C1 MAN G 5 1555 1555 1.44 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45 LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.44 LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.45 LINK O6 BMA H 3 C1 MAN H 5 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.44 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.45 LINK O6 BMA I 3 C1 MAN I 5 1555 1555 1.44 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