HEADER VIRAL PROTEIN 24-JAN-25 9N0D TITLE JUNV GP1, GP2, SSP COMPLEX WITH NEUTRALIZING ANTIBODY IN A PSEUDOTYPED TITLE 2 VIRUS MEMBRANE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PRE-GLYCOPROTEIN POLYPROTEIN GP COMPLEX; COMPND 3 CHAIN: A, F, K; COMPND 4 SYNONYM: PRE-GP-C; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: PRE-GLYCOPROTEIN POLYPROTEIN GP COMPLEX; COMPND 8 CHAIN: B, G, L; COMPND 9 SYNONYM: PRE-GP-C; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: PRE-GLYCOPROTEIN POLYPROTEIN GP COMPLEX; COMPND 13 CHAIN: C, H, M; COMPND 14 SYNONYM: PRE-GP-C; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: NEUTRALIZING ANTIBODY LIGHT CHAIN; COMPND 18 CHAIN: D, I, N; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: NEUTRALIZING ANTIBODY HEAVY CHAIN; COMPND 22 CHAIN: E, J, O; COMPND 23 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MAMMARENAVIRUS JUNINENSE; SOURCE 3 ORGANISM_TAXID: 2169991; SOURCE 4 GENE: GPC, GP-C; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293TT; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MAMMARENAVIRUS JUNINENSE; SOURCE 10 ORGANISM_TAXID: 2169991; SOURCE 11 GENE: GPC, GP-C; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HEK293TT; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MAMMARENAVIRUS JUNINENSE; SOURCE 17 ORGANISM_TAXID: 2169991; SOURCE 18 GENE: GPC, GP-C; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: HEK293TT; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 24 ORGANISM_TAXID: 10090; SOURCE 25 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: MOUSE HYBRIDOMA CELLS; SOURCE 28 MOL_ID: 5; SOURCE 29 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 30 ORGANISM_TAXID: 10090; SOURCE 31 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 33 EXPRESSION_SYSTEM_CELL_LINE: MOUSE HYBRIDOMA CELLS KEYWDS VIRAL PROTEIN, GLYCOPROTEIN, GPC, JUNV, JUNIN MAMMARENAVIRUS, GP1, KEYWDS 2 GP2, SIGNAL PEPTIDE, VIRUS MEMBRANE, ANTIBODY EXPDTA ELECTRON MICROSCOPY AUTHOR L.J.TAYLOR,M.R.SAWAYA,R.CASTELLS-GRAELLS,J.A.RODRIGUEZ REVDAT 1 23-JUL-25 9N0D 0 JRNL AUTH L.J.TAYLOR,M.R.SAWAYA,J.B.WESTOVER,C.WANG,F.JIMENEZ, JRNL AUTH 2 A.J.MUNOZ,J.WHITELEGGE,B.B.GOWEN,G.F.HELGUERA, JRNL AUTH 3 R.CASTELLS-GRAELLS,J.A.RODRIGUEZ JRNL TITL IN SITU INSIGHTS INTO ANTIBODY-MEDIATED NEUTRALIZATION OF A JRNL TITL 2 PRE-FUSION JUNIN VIRUS GLYCOPROTEIN COMPLEX. JRNL REF CELL REP V. 44 15971 2025 JRNL REFN ESSN 2211-1247 JRNL PMID 40632652 JRNL DOI 10.1016/J.CELREP.2025.115971 REMARK 2 REMARK 2 RESOLUTION. 3.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 3.800 REMARK 3 NUMBER OF PARTICLES : 279624 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 9N0D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000292182. 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 : JUNV GP1, GP2, SSP COMPLEX WITH REMARK 245 NEUTRALIZING ANTIBODY IN A REMARK 245 PSEUDOTYPED VIRUS MEMBRANE 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 : 8.00 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 : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 600.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL 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: PENTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, M, N, O, Y, h, n, R, REMARK 350 AND CHAINS: W, b 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 THR C 259 REMARK 465 ASP C 260 REMARK 465 SER C 261 REMARK 465 SER C 262 REMARK 465 GLY C 263 REMARK 465 LYS C 264 REMARK 465 ASP C 265 REMARK 465 THR C 266 REMARK 465 PRO C 267 REMARK 465 GLY C 268 REMARK 465 THR H 259 REMARK 465 ASP H 260 REMARK 465 SER H 261 REMARK 465 SER H 262 REMARK 465 GLY H 263 REMARK 465 LYS H 264 REMARK 465 ASP H 265 REMARK 465 THR H 266 REMARK 465 PRO H 267 REMARK 465 GLY H 268 REMARK 465 THR M 259 REMARK 465 ASP M 260 REMARK 465 SER M 261 REMARK 465 SER M 262 REMARK 465 GLY M 263 REMARK 465 LYS M 264 REMARK 465 ASP M 265 REMARK 465 THR M 266 REMARK 465 PRO M 267 REMARK 465 GLY M 268 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 SER D 51 OG REMARK 470 SER I 51 OG REMARK 470 SER N 51 OG 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 I 29 OH TYR I 70 2.19 REMARK 500 O VAL D 29 OH TYR D 70 2.19 REMARK 500 O VAL N 29 OH TYR N 70 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ALA B 106 CB - CA - C ANGL. DEV. = -22.6 DEGREES REMARK 500 ALA B 106 N - CA - C ANGL. DEV. = -20.0 DEGREES REMARK 500 SER B 107 N - CA - CB ANGL. DEV. = -11.5 DEGREES REMARK 500 SER B 107 N - CA - C ANGL. DEV. = -17.5 DEGREES REMARK 500 ASP E 42 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 ALA G 106 CB - CA - C ANGL. DEV. = -22.7 DEGREES REMARK 500 ALA G 106 N - CA - C ANGL. DEV. = -20.0 DEGREES REMARK 500 SER G 107 N - CA - CB ANGL. DEV. = -11.5 DEGREES REMARK 500 SER G 107 N - CA - C ANGL. DEV. = -17.5 DEGREES REMARK 500 ASP J 42 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 ALA L 106 CB - CA - C ANGL. DEV. = -22.6 DEGREES REMARK 500 ALA L 106 N - CA - C ANGL. DEV. = -20.0 DEGREES REMARK 500 SER L 107 N - CA - CB ANGL. DEV. = -11.5 DEGREES REMARK 500 SER L 107 N - CA - C ANGL. DEV. = -17.5 DEGREES REMARK 500 ASP O 42 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES 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 PRO A 12 41.93 -83.93 REMARK 500 ASN B 95 -130.40 53.29 REMARK 500 ASN B 105 33.26 -140.36 REMARK 500 ASP B 114 44.15 -92.79 REMARK 500 ASP B 123 -173.55 -173.45 REMARK 500 HIS B 154 49.36 -143.46 REMARK 500 THR B 170 58.77 -94.56 REMARK 500 CYS B 213 117.13 -161.41 REMARK 500 LEU B 224 50.79 -91.87 REMARK 500 CYS C 293 52.77 -95.17 REMARK 500 ASN C 357 48.99 -96.29 REMARK 500 PRO D 15 76.47 -65.99 REMARK 500 THR D 50 -4.13 62.98 REMARK 500 PHE E 29 -12.24 62.09 REMARK 500 ASP E 90 49.88 -91.33 REMARK 500 ALA E 92 -176.59 -170.90 REMARK 500 PRO F 12 41.97 -83.97 REMARK 500 ASN G 95 -130.38 53.30 REMARK 500 ASN G 105 33.24 -140.36 REMARK 500 ASP G 114 44.20 -92.82 REMARK 500 ASP G 123 -173.57 -173.46 REMARK 500 HIS G 154 49.30 -143.42 REMARK 500 THR G 170 58.74 -94.57 REMARK 500 CYS G 213 117.10 -161.39 REMARK 500 LEU G 224 50.76 -91.86 REMARK 500 CYS H 293 52.72 -95.16 REMARK 500 ASN H 357 48.99 -96.32 REMARK 500 PRO I 15 76.51 -66.00 REMARK 500 THR I 50 -4.11 63.00 REMARK 500 PHE J 29 -12.24 62.04 REMARK 500 ASP J 90 49.85 -91.29 REMARK 500 ALA J 92 -176.58 -170.93 REMARK 500 PRO K 12 41.91 -83.92 REMARK 500 ASN L 95 -130.40 53.29 REMARK 500 ASN L 105 33.25 -140.36 REMARK 500 ASP L 114 44.20 -92.77 REMARK 500 ASP L 123 -173.54 -173.43 REMARK 500 HIS L 154 49.32 -143.49 REMARK 500 THR L 170 58.80 -94.62 REMARK 500 CYS L 213 117.13 -161.38 REMARK 500 LEU L 224 50.71 -91.85 REMARK 500 CYS M 293 52.78 -95.15 REMARK 500 ASN M 357 48.96 -96.27 REMARK 500 PRO N 15 76.48 -65.96 REMARK 500 THR N 50 -4.07 62.92 REMARK 500 PHE O 29 -12.25 62.11 REMARK 500 ASP O 90 49.84 -91.33 REMARK 500 ALA O 92 -176.56 -170.91 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48781 RELATED DB: EMDB REMARK 900 JUNV GP1, GP2, SSP AND CR1-28 FAB COMPLEX IN A PSEUDOTYPED VIRUS REMARK 900 MEMBRANE DBREF 9N0D A 2 58 UNP P26313 GLYC_JUNIN 2 58 DBREF 9N0D B 61 247 UNP P26313 GLYC_JUNIN 61 247 DBREF 9N0D C 252 485 UNP P26313 GLYC_JUNIN 252 485 DBREF 9N0D D 1 106 PDB 9N0D 9N0D 1 106 DBREF 9N0D E 2 121 PDB 9N0D 9N0D 2 121 DBREF 9N0D F 2 58 UNP P26313 GLYC_JUNIN 2 58 DBREF 9N0D G 61 247 UNP P26313 GLYC_JUNIN 61 247 DBREF 9N0D H 252 485 UNP P26313 GLYC_JUNIN 252 485 DBREF 9N0D I 1 106 PDB 9N0D 9N0D 1 106 DBREF 9N0D J 2 121 PDB 9N0D 9N0D 2 121 DBREF 9N0D K 2 58 UNP P26313 GLYC_JUNIN 2 58 DBREF 9N0D L 61 247 UNP P26313 GLYC_JUNIN 61 247 DBREF 9N0D M 252 485 UNP P26313 GLYC_JUNIN 252 485 DBREF 9N0D N 1 106 PDB 9N0D 9N0D 1 106 DBREF 9N0D O 2 121 PDB 9N0D 9N0D 2 121 SEQRES 1 A 57 GLY GLN PHE ILE SER PHE MET GLN GLU ILE PRO THR PHE SEQRES 2 A 57 LEU GLN GLU ALA LEU ASN ILE ALA LEU VAL ALA VAL SER SEQRES 3 A 57 LEU ILE ALA ILE ILE LYS GLY VAL VAL ASN LEU TYR LYS SEQRES 4 A 57 SER GLY LEU PHE GLN PHE PHE VAL PHE LEU ALA LEU ALA SEQRES 5 A 57 GLY ARG SER CYS THR SEQRES 1 B 187 ALA PHE LYS ILE GLY LEU HIS THR GLU PHE GLN THR VAL SEQRES 2 B 187 SER PHE SER MET VAL GLY LEU PHE SER ASN ASN PRO HIS SEQRES 3 B 187 ASP LEU PRO LEU LEU CYS THR LEU ASN LYS SER HIS LEU SEQRES 4 B 187 TYR ILE LYS GLY GLY ASN ALA SER PHE LYS ILE SER PHE SEQRES 5 B 187 ASP ASP ILE ALA VAL LEU LEU PRO GLU TYR ASP VAL ILE SEQRES 6 B 187 ILE GLN HIS PRO ALA ASP MET SER TRP CYS SER LYS SER SEQRES 7 B 187 ASP ASP GLN ILE TRP LEU SER GLN TRP PHE MET ASN ALA SEQRES 8 B 187 VAL GLY HIS ASP TRP TYR LEU ASP PRO PRO PHE LEU CYS SEQRES 9 B 187 ARG ASN ARG THR LYS THR GLU GLY PHE ILE PHE GLN VAL SEQRES 10 B 187 ASN THR SER LYS THR GLY ILE ASN GLU ASN TYR ALA LYS SEQRES 11 B 187 LYS PHE LYS THR GLY MET HIS HIS LEU TYR ARG GLU TYR SEQRES 12 B 187 PRO ASP SER CYS LEU ASP GLY LYS LEU CYS LEU MET LYS SEQRES 13 B 187 ALA GLN PRO THR SER TRP PRO LEU GLN CYS PRO LEU ASP SEQRES 14 B 187 HIS VAL ASN THR LEU HIS PHE LEU THR ARG GLY LYS ASN SEQRES 15 B 187 ILE GLN LEU PRO ARG SEQRES 1 C 234 ALA PHE PHE SER TRP SER LEU THR ASP SER SER GLY LYS SEQRES 2 C 234 ASP THR PRO GLY GLY TYR CYS LEU GLU GLU TRP MET LEU SEQRES 3 C 234 VAL ALA ALA LYS MET LYS CYS PHE GLY ASN THR ALA VAL SEQRES 4 C 234 ALA LYS CYS ASN LEU ASN HIS ASP SER GLU PHE CYS ASP SEQRES 5 C 234 MET LEU ARG LEU PHE ASP TYR ASN LYS ASN ALA ILE LYS SEQRES 6 C 234 THR LEU ASN ASP GLU THR LYS LYS GLN VAL ASN LEU MET SEQRES 7 C 234 GLY GLN THR ILE ASN ALA LEU ILE SER ASP ASN LEU LEU SEQRES 8 C 234 MET LYS ASN LYS ILE ARG GLU LEU MET SER VAL PRO TYR SEQRES 9 C 234 CYS ASN TYR THR LYS PHE TRP TYR VAL ASN HIS THR LEU SEQRES 10 C 234 SER GLY GLN HIS SER LEU PRO ARG CYS TRP LEU ILE LYS SEQRES 11 C 234 ASN ASN SER TYR LEU ASN ILE SER ASP PHE ARG ASN ASP SEQRES 12 C 234 TRP ILE LEU GLU SER ASP PHE LEU ILE SER GLU MET LEU SEQRES 13 C 234 SER LYS GLU TYR SER ASP ARG GLN GLY LYS THR PRO LEU SEQRES 14 C 234 THR LEU VAL ASP ILE CYS PHE TRP SER THR VAL PHE PHE SEQRES 15 C 234 THR ALA SER LEU PHE LEU HIS LEU VAL GLY ILE PRO THR SEQRES 16 C 234 HIS ARG HIS ILE ARG GLY GLU ALA CYS PRO LEU PRO HIS SEQRES 17 C 234 ARG LEU ASN SER LEU GLY GLY CYS ARG CYS GLY LYS TYR SEQRES 18 C 234 PRO ASN LEU LYS LYS PRO THR VAL TRP ARG ARG GLY HIS SEQRES 1 D 106 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA SEQRES 2 D 106 SER PRO GLY GLU LYS VAL THR ILE THR CYS SER ALA SER SEQRES 3 D 106 SER ILE VAL SER TYR MET HIS TRP PHE GLN GLN LYS PRO SEQRES 4 D 106 GLY THR SER PRO LYS LEU TRP ILE TYR GLY THR SER ASN SEQRES 5 D 106 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 D 106 SER GLY THR SER TYR SER LEU THR ILE SER ARG MET GLU SEQRES 7 D 106 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN ARG ASN SEQRES 8 D 106 SER TYR PRO PRO THR PHE GLY GLY GLY THR LYS LEU GLU SEQRES 9 D 106 ILE LYS SEQRES 1 E 119 VAL ALA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 E 119 GLY GLY SER LEU LYS LEU SER CYS ALA SER GLY ALA SER SEQRES 3 E 119 PHE SER ASN ALA GLY MET SER TRP VAL ARG GLN THR PRO SEQRES 4 E 119 ASP ARG ARG LEU GLU LEU VAL ALA ALA ILE ASN ARG ASP SEQRES 5 E 119 GLY ASP ILE THR TYR HIS PRO ASP SER VAL LYS GLY ARG SEQRES 6 E 119 PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR SEQRES 7 E 119 LEU GLN MET SER SER LEU LYS SER GLU ASP THR ALA MET SEQRES 8 E 119 TYR TYR CYS ALA ARG GLU ASP TYR TYR GLY LEU TYR PHE SEQRES 9 E 119 TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 E 119 VAL ALA SEQRES 1 F 57 GLY GLN PHE ILE SER PHE MET GLN GLU ILE PRO THR PHE SEQRES 2 F 57 LEU GLN GLU ALA LEU ASN ILE ALA LEU VAL ALA VAL SER SEQRES 3 F 57 LEU ILE ALA ILE ILE LYS GLY VAL VAL ASN LEU TYR LYS SEQRES 4 F 57 SER GLY LEU PHE GLN PHE PHE VAL PHE LEU ALA LEU ALA SEQRES 5 F 57 GLY ARG SER CYS THR SEQRES 1 G 187 ALA PHE LYS ILE GLY LEU HIS THR GLU PHE GLN THR VAL SEQRES 2 G 187 SER PHE SER MET VAL GLY LEU PHE SER ASN ASN PRO HIS SEQRES 3 G 187 ASP LEU PRO LEU LEU CYS THR LEU ASN LYS SER HIS LEU SEQRES 4 G 187 TYR ILE LYS GLY GLY ASN ALA SER PHE LYS ILE SER PHE SEQRES 5 G 187 ASP ASP ILE ALA VAL LEU LEU PRO GLU TYR ASP VAL ILE SEQRES 6 G 187 ILE GLN HIS PRO ALA ASP MET SER TRP CYS SER LYS SER SEQRES 7 G 187 ASP ASP GLN ILE TRP LEU SER GLN TRP PHE MET ASN ALA SEQRES 8 G 187 VAL GLY HIS ASP TRP TYR LEU ASP PRO PRO PHE LEU CYS SEQRES 9 G 187 ARG ASN ARG THR LYS THR GLU GLY PHE ILE PHE GLN VAL SEQRES 10 G 187 ASN THR SER LYS THR GLY ILE ASN GLU ASN TYR ALA LYS SEQRES 11 G 187 LYS PHE LYS THR GLY MET HIS HIS LEU TYR ARG GLU TYR SEQRES 12 G 187 PRO ASP SER CYS LEU ASP GLY LYS LEU CYS LEU MET LYS SEQRES 13 G 187 ALA GLN PRO THR SER TRP PRO LEU GLN CYS PRO LEU ASP SEQRES 14 G 187 HIS VAL ASN THR LEU HIS PHE LEU THR ARG GLY LYS ASN SEQRES 15 G 187 ILE GLN LEU PRO ARG SEQRES 1 H 234 ALA PHE PHE SER TRP SER LEU THR ASP SER SER GLY LYS SEQRES 2 H 234 ASP THR PRO GLY GLY TYR CYS LEU GLU GLU TRP MET LEU SEQRES 3 H 234 VAL ALA ALA LYS MET LYS CYS PHE GLY ASN THR ALA VAL SEQRES 4 H 234 ALA LYS CYS ASN LEU ASN HIS ASP SER GLU PHE CYS ASP SEQRES 5 H 234 MET LEU ARG LEU PHE ASP TYR ASN LYS ASN ALA ILE LYS SEQRES 6 H 234 THR LEU ASN ASP GLU THR LYS LYS GLN VAL ASN LEU MET SEQRES 7 H 234 GLY GLN THR ILE ASN ALA LEU ILE SER ASP ASN LEU LEU SEQRES 8 H 234 MET LYS ASN LYS ILE ARG GLU LEU MET SER VAL PRO TYR SEQRES 9 H 234 CYS ASN TYR THR LYS PHE TRP TYR VAL ASN HIS THR LEU SEQRES 10 H 234 SER GLY GLN HIS SER LEU PRO ARG CYS TRP LEU ILE LYS SEQRES 11 H 234 ASN ASN SER TYR LEU ASN ILE SER ASP PHE ARG ASN ASP SEQRES 12 H 234 TRP ILE LEU GLU SER ASP PHE LEU ILE SER GLU MET LEU SEQRES 13 H 234 SER LYS GLU TYR SER ASP ARG GLN GLY LYS THR PRO LEU SEQRES 14 H 234 THR LEU VAL ASP ILE CYS PHE TRP SER THR VAL PHE PHE SEQRES 15 H 234 THR ALA SER LEU PHE LEU HIS LEU VAL GLY ILE PRO THR SEQRES 16 H 234 HIS ARG HIS ILE ARG GLY GLU ALA CYS PRO LEU PRO HIS SEQRES 17 H 234 ARG LEU ASN SER LEU GLY GLY CYS ARG CYS GLY LYS TYR SEQRES 18 H 234 PRO ASN LEU LYS LYS PRO THR VAL TRP ARG ARG GLY HIS SEQRES 1 I 106 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA SEQRES 2 I 106 SER PRO GLY GLU LYS VAL THR ILE THR CYS SER ALA SER SEQRES 3 I 106 SER ILE VAL SER TYR MET HIS TRP PHE GLN GLN LYS PRO SEQRES 4 I 106 GLY THR SER PRO LYS LEU TRP ILE TYR GLY THR SER ASN SEQRES 5 I 106 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 I 106 SER GLY THR SER TYR SER LEU THR ILE SER ARG MET GLU SEQRES 7 I 106 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN ARG ASN SEQRES 8 I 106 SER TYR PRO PRO THR PHE GLY GLY GLY THR LYS LEU GLU SEQRES 9 I 106 ILE LYS SEQRES 1 J 119 VAL ALA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 J 119 GLY GLY SER LEU LYS LEU SER CYS ALA SER GLY ALA SER SEQRES 3 J 119 PHE SER ASN ALA GLY MET SER TRP VAL ARG GLN THR PRO SEQRES 4 J 119 ASP ARG ARG LEU GLU LEU VAL ALA ALA ILE ASN ARG ASP SEQRES 5 J 119 GLY ASP ILE THR TYR HIS PRO ASP SER VAL LYS GLY ARG SEQRES 6 J 119 PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR SEQRES 7 J 119 LEU GLN MET SER SER LEU LYS SER GLU ASP THR ALA MET SEQRES 8 J 119 TYR TYR CYS ALA ARG GLU ASP TYR TYR GLY LEU TYR PHE SEQRES 9 J 119 TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 J 119 VAL ALA SEQRES 1 K 57 GLY GLN PHE ILE SER PHE MET GLN GLU ILE PRO THR PHE SEQRES 2 K 57 LEU GLN GLU ALA LEU ASN ILE ALA LEU VAL ALA VAL SER SEQRES 3 K 57 LEU ILE ALA ILE ILE LYS GLY VAL VAL ASN LEU TYR LYS SEQRES 4 K 57 SER GLY LEU PHE GLN PHE PHE VAL PHE LEU ALA LEU ALA SEQRES 5 K 57 GLY ARG SER CYS THR SEQRES 1 L 187 ALA PHE LYS ILE GLY LEU HIS THR GLU PHE GLN THR VAL SEQRES 2 L 187 SER PHE SER MET VAL GLY LEU PHE SER ASN ASN PRO HIS SEQRES 3 L 187 ASP LEU PRO LEU LEU CYS THR LEU ASN LYS SER HIS LEU SEQRES 4 L 187 TYR ILE LYS GLY GLY ASN ALA SER PHE LYS ILE SER PHE SEQRES 5 L 187 ASP ASP ILE ALA VAL LEU LEU PRO GLU TYR ASP VAL ILE SEQRES 6 L 187 ILE GLN HIS PRO ALA ASP MET SER TRP CYS SER LYS SER SEQRES 7 L 187 ASP ASP GLN ILE TRP LEU SER GLN TRP PHE MET ASN ALA SEQRES 8 L 187 VAL GLY HIS ASP TRP TYR LEU ASP PRO PRO PHE LEU CYS SEQRES 9 L 187 ARG ASN ARG THR LYS THR GLU GLY PHE ILE PHE GLN VAL SEQRES 10 L 187 ASN THR SER LYS THR GLY ILE ASN GLU ASN TYR ALA LYS SEQRES 11 L 187 LYS PHE LYS THR GLY MET HIS HIS LEU TYR ARG GLU TYR SEQRES 12 L 187 PRO ASP SER CYS LEU ASP GLY LYS LEU CYS LEU MET LYS SEQRES 13 L 187 ALA GLN PRO THR SER TRP PRO LEU GLN CYS PRO LEU ASP SEQRES 14 L 187 HIS VAL ASN THR LEU HIS PHE LEU THR ARG GLY LYS ASN SEQRES 15 L 187 ILE GLN LEU PRO ARG SEQRES 1 M 234 ALA PHE PHE SER TRP SER LEU THR ASP SER SER GLY LYS SEQRES 2 M 234 ASP THR PRO GLY GLY TYR CYS LEU GLU GLU TRP MET LEU SEQRES 3 M 234 VAL ALA ALA LYS MET LYS CYS PHE GLY ASN THR ALA VAL SEQRES 4 M 234 ALA LYS CYS ASN LEU ASN HIS ASP SER GLU PHE CYS ASP SEQRES 5 M 234 MET LEU ARG LEU PHE ASP TYR ASN LYS ASN ALA ILE LYS SEQRES 6 M 234 THR LEU ASN ASP GLU THR LYS LYS GLN VAL ASN LEU MET SEQRES 7 M 234 GLY GLN THR ILE ASN ALA LEU ILE SER ASP ASN LEU LEU SEQRES 8 M 234 MET LYS ASN LYS ILE ARG GLU LEU MET SER VAL PRO TYR SEQRES 9 M 234 CYS ASN TYR THR LYS PHE TRP TYR VAL ASN HIS THR LEU SEQRES 10 M 234 SER GLY GLN HIS SER LEU PRO ARG CYS TRP LEU ILE LYS SEQRES 11 M 234 ASN ASN SER TYR LEU ASN ILE SER ASP PHE ARG ASN ASP SEQRES 12 M 234 TRP ILE LEU GLU SER ASP PHE LEU ILE SER GLU MET LEU SEQRES 13 M 234 SER LYS GLU TYR SER ASP ARG GLN GLY LYS THR PRO LEU SEQRES 14 M 234 THR LEU VAL ASP ILE CYS PHE TRP SER THR VAL PHE PHE SEQRES 15 M 234 THR ALA SER LEU PHE LEU HIS LEU VAL GLY ILE PRO THR SEQRES 16 M 234 HIS ARG HIS ILE ARG GLY GLU ALA CYS PRO LEU PRO HIS SEQRES 17 M 234 ARG LEU ASN SER LEU GLY GLY CYS ARG CYS GLY LYS TYR SEQRES 18 M 234 PRO ASN LEU LYS LYS PRO THR VAL TRP ARG ARG GLY HIS SEQRES 1 N 106 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA SEQRES 2 N 106 SER PRO GLY GLU LYS VAL THR ILE THR CYS SER ALA SER SEQRES 3 N 106 SER ILE VAL SER TYR MET HIS TRP PHE GLN GLN LYS PRO SEQRES 4 N 106 GLY THR SER PRO LYS LEU TRP ILE TYR GLY THR SER ASN SEQRES 5 N 106 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 N 106 SER GLY THR SER TYR SER LEU THR ILE SER ARG MET GLU SEQRES 7 N 106 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN ARG ASN SEQRES 8 N 106 SER TYR PRO PRO THR PHE GLY GLY GLY THR LYS LEU GLU SEQRES 9 N 106 ILE LYS SEQRES 1 O 119 VAL ALA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 O 119 GLY GLY SER LEU LYS LEU SER CYS ALA SER GLY ALA SER SEQRES 3 O 119 PHE SER ASN ALA GLY MET SER TRP VAL ARG GLN THR PRO SEQRES 4 O 119 ASP ARG ARG LEU GLU LEU VAL ALA ALA ILE ASN ARG ASP SEQRES 5 O 119 GLY ASP ILE THR TYR HIS PRO ASP SER VAL LYS GLY ARG SEQRES 6 O 119 PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR SEQRES 7 O 119 LEU GLN MET SER SER LEU LYS SER GLU ASP THR ALA MET SEQRES 8 O 119 TYR TYR CYS ALA ARG GLU ASP TYR TYR GLY LEU TYR PHE SEQRES 9 O 119 TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 O 119 VAL ALA HET NAG Y 1 14 HET NAG Y 2 14 HET BMA Y 3 11 HET NAG h 1 14 HET NAG h 2 14 HET BMA h 3 11 HET NAG n 1 14 HET NAG n 2 14 HET BMA n 3 11 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET NAG W 1 14 HET NAG W 2 14 HET BMA W 3 11 HET NAG b 1 14 HET NAG b 2 14 HET BMA b 3 11 HET MYR A 101 15 HET NAG B 301 14 HET NAG B 302 14 HET NAG C 501 14 HET NAG C 502 14 HET NAG C 503 14 HET MYR F 101 15 HET NAG G 301 14 HET NAG G 302 14 HET NAG H 501 14 HET NAG H 502 14 HET NAG H 503 14 HET MYR K 101 15 HET NAG L 301 14 HET NAG L 302 14 HET NAG M 501 14 HET NAG M 502 14 HET NAG M 503 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MYR MYRISTIC ACID 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 FORMUL 16 NAG 27(C8 H15 N O6) FORMUL 16 BMA 6(C6 H12 O6) FORMUL 22 MYR 3(C14 H28 O2) HELIX 1 AA1 GLY A 2 LEU A 15 1 14 HELIX 2 AA2 GLU A 17 GLY A 42 1 26 HELIX 3 AA3 GLY A 42 ALA A 53 1 12 HELIX 4 AA4 MET B 77 ASN B 84 1 8 HELIX 5 AA5 ALA B 130 CYS B 135 5 6 HELIX 6 AA6 SER B 138 GLY B 153 1 16 HELIX 7 AA7 ASN B 185 TYR B 200 1 16 HELIX 8 AA8 HIS B 230 GLY B 240 1 11 HELIX 9 AA9 GLU C 273 LEU C 277 5 5 HELIX 10 AB1 GLY C 286 ALA C 291 1 6 HELIX 11 AB2 LYS C 292 LEU C 295 5 4 HELIX 12 AB3 SER C 299 GLU C 321 1 23 HELIX 13 AB4 MET C 329 ILE C 337 1 9 HELIX 14 AB5 SER C 338 MET C 351 1 14 HELIX 15 AB6 ASN C 387 ASP C 390 5 4 HELIX 16 AB7 PHE C 391 GLY C 416 1 26 HELIX 17 AB8 PRO C 419 GLY C 443 1 25 HELIX 18 AB9 PRO E 61 LYS E 65 5 5 HELIX 19 AC1 LYS E 87 THR E 91 5 5 HELIX 20 AC2 GLN F 3 LEU F 15 1 13 HELIX 21 AC3 GLU F 17 GLY F 42 1 26 HELIX 22 AC4 GLY F 42 ALA F 53 1 12 HELIX 23 AC5 MET G 77 ASN G 84 1 8 HELIX 24 AC6 ALA G 130 CYS G 135 5 6 HELIX 25 AC7 SER G 138 GLY G 153 1 16 HELIX 26 AC8 ASN G 185 TYR G 200 1 16 HELIX 27 AC9 HIS G 230 GLY G 240 1 11 HELIX 28 AD1 GLU H 273 LEU H 277 5 5 HELIX 29 AD2 GLY H 286 ALA H 291 1 6 HELIX 30 AD3 LYS H 292 LEU H 295 5 4 HELIX 31 AD4 SER H 299 GLU H 321 1 23 HELIX 32 AD5 MET H 329 ILE H 337 1 9 HELIX 33 AD6 SER H 338 MET H 351 1 14 HELIX 34 AD7 ASN H 387 ASP H 390 5 4 HELIX 35 AD8 PHE H 391 GLY H 416 1 26 HELIX 36 AD9 PRO H 419 GLY H 443 1 25 HELIX 37 AE1 PRO J 61 LYS J 65 5 5 HELIX 38 AE2 LYS J 87 THR J 91 5 5 HELIX 39 AE3 GLN K 3 LEU K 15 1 13 HELIX 40 AE4 GLU K 17 GLY K 42 1 26 HELIX 41 AE5 GLY K 42 ALA K 53 1 12 HELIX 42 AE6 MET L 77 ASN L 84 1 8 HELIX 43 AE7 ALA L 130 CYS L 135 5 6 HELIX 44 AE8 SER L 138 GLY L 153 1 16 HELIX 45 AE9 ASN L 185 TYR L 200 1 16 HELIX 46 AF1 HIS L 230 GLY L 240 1 11 HELIX 47 AF2 GLU M 273 LEU M 277 5 5 HELIX 48 AF3 GLY M 286 ALA M 291 1 6 HELIX 49 AF4 LYS M 292 LEU M 295 5 4 HELIX 50 AF5 SER M 299 GLU M 321 1 23 HELIX 51 AF6 MET M 329 ILE M 337 1 9 HELIX 52 AF7 SER M 338 MET M 351 1 14 HELIX 53 AF8 ASN M 387 ASP M 390 5 4 HELIX 54 AF9 PHE M 391 GLY M 416 1 26 HELIX 55 AG1 PRO M 419 GLY M 443 1 25 HELIX 56 AG2 PRO O 61 LYS O 65 5 5 HELIX 57 AG3 LYS O 87 THR O 91 5 5 SHEET 1 AA1 4 PHE B 62 ILE B 64 0 SHEET 2 AA1 4 THR B 68 SER B 74 -1 O PHE B 70 N PHE B 62 SHEET 3 AA1 4 LYS C 360 HIS C 366 -1 O ASN C 365 N GLU B 69 SHEET 4 AA1 4 ARG C 376 CYS C 377 -1 O ARG C 376 N TRP C 362 SHEET 1 AA2 7 LEU B 90 LEU B 94 0 SHEET 2 AA2 7 HIS B 98 LYS B 102 -1 O LYS B 102 N LEU B 90 SHEET 3 AA2 7 SER B 107 ASP B 113 -1 O ILE B 110 N LEU B 99 SHEET 4 AA2 7 LEU B 214 PRO B 219 -1 O GLN B 218 N LYS B 109 SHEET 5 AA2 7 PHE B 175 ASN B 178 -1 N PHE B 175 O ALA B 217 SHEET 6 AA2 7 PHE B 162 CYS B 164 -1 N LEU B 163 O GLN B 176 SHEET 7 AA2 7 VAL B 124 ILE B 126 -1 N VAL B 124 O CYS B 164 SHEET 1 AA3 2 CYS C 271 LEU C 272 0 SHEET 2 AA3 2 LYS C 283 CYS C 284 -1 O LYS C 283 N LEU C 272 SHEET 1 AA4 2 ILE C 380 LYS C 381 0 SHEET 2 AA4 2 SER C 384 TYR C 385 -1 O SER C 384 N LYS C 381 SHEET 1 AA5 2 HIS C 447 ILE C 450 0 SHEET 2 AA5 2 THR C 479 ARG C 482 -1 O ARG C 482 N HIS C 447 SHEET 1 AA6 4 LEU D 4 SER D 7 0 SHEET 2 AA6 4 VAL D 19 ALA D 25 -1 O SER D 24 N THR D 5 SHEET 3 AA6 4 SER D 69 ILE D 74 -1 O TYR D 70 N CYS D 23 SHEET 4 AA6 4 PHE D 61 SER D 66 -1 N SER D 62 O THR D 73 SHEET 1 AA7 6 ILE D 10 ALA D 13 0 SHEET 2 AA7 6 THR D 101 ILE D 105 1 O GLU D 104 N MET D 11 SHEET 3 AA7 6 THR D 84 GLN D 89 -1 N TYR D 85 O THR D 101 SHEET 4 AA7 6 HIS D 33 GLN D 37 -1 N GLN D 37 O THR D 84 SHEET 5 AA7 6 LYS D 44 TYR D 48 -1 O LYS D 44 N GLN D 36 SHEET 6 AA7 6 ASN D 52 LEU D 53 -1 O ASN D 52 N TYR D 48 SHEET 1 AA8 4 ILE D 10 ALA D 13 0 SHEET 2 AA8 4 THR D 101 ILE D 105 1 O GLU D 104 N MET D 11 SHEET 3 AA8 4 THR D 84 GLN D 89 -1 N TYR D 85 O THR D 101 SHEET 4 AA8 4 THR D 96 PHE D 97 -1 O THR D 96 N GLN D 89 SHEET 1 AA9 6 GLY E 10 VAL E 12 0 SHEET 2 AA9 6 THR E 116 VAL E 120 1 O THR E 119 N GLY E 10 SHEET 3 AA9 6 ALA E 92 TYR E 101 -1 N ALA E 92 O VAL E 118 SHEET 4 AA9 6 MET E 34 THR E 40 -1 N SER E 35 O ALA E 97 SHEET 5 AA9 6 ARG E 44 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AA9 6 THR E 58 TYR E 59 -1 O TYR E 59 N ALA E 50 SHEET 1 AB1 4 GLY E 10 VAL E 12 0 SHEET 2 AB1 4 THR E 116 VAL E 120 1 O THR E 119 N GLY E 10 SHEET 3 AB1 4 ALA E 92 TYR E 101 -1 N ALA E 92 O VAL E 118 SHEET 4 AB1 4 TYR E 107 TRP E 112 -1 O ASP E 110 N ARG E 98 SHEET 1 AB2 3 SER E 17 CYS E 22 0 SHEET 2 AB2 3 THR E 78 SER E 84 -1 O MET E 83 N LEU E 18 SHEET 3 AB2 3 PHE E 68 ASP E 73 -1 N SER E 71 O TYR E 80 SHEET 1 AB3 4 PHE G 62 ILE G 64 0 SHEET 2 AB3 4 THR G 68 SER G 74 -1 O PHE G 70 N PHE G 62 SHEET 3 AB3 4 LYS H 360 HIS H 366 -1 O ASN H 365 N GLU G 69 SHEET 4 AB3 4 ARG H 376 CYS H 377 -1 O ARG H 376 N TRP H 362 SHEET 1 AB4 7 LEU G 90 LEU G 94 0 SHEET 2 AB4 7 HIS G 98 LYS G 102 -1 O LYS G 102 N LEU G 90 SHEET 3 AB4 7 SER G 107 ASP G 113 -1 O ILE G 110 N LEU G 99 SHEET 4 AB4 7 LEU G 214 PRO G 219 -1 O GLN G 218 N LYS G 109 SHEET 5 AB4 7 PHE G 175 ASN G 178 -1 N PHE G 175 O ALA G 217 SHEET 6 AB4 7 PHE G 162 CYS G 164 -1 N LEU G 163 O GLN G 176 SHEET 7 AB4 7 VAL G 124 ILE G 126 -1 N VAL G 124 O CYS G 164 SHEET 1 AB5 2 CYS H 271 LEU H 272 0 SHEET 2 AB5 2 LYS H 283 CYS H 284 -1 O LYS H 283 N LEU H 272 SHEET 1 AB6 2 ILE H 380 LYS H 381 0 SHEET 2 AB6 2 SER H 384 TYR H 385 -1 O SER H 384 N LYS H 381 SHEET 1 AB7 2 HIS H 447 ILE H 450 0 SHEET 2 AB7 2 THR H 479 ARG H 482 -1 O ARG H 482 N HIS H 447 SHEET 1 AB8 4 LEU I 4 SER I 7 0 SHEET 2 AB8 4 VAL I 19 ALA I 25 -1 O SER I 24 N THR I 5 SHEET 3 AB8 4 SER I 69 ILE I 74 -1 O TYR I 70 N CYS I 23 SHEET 4 AB8 4 PHE I 61 SER I 66 -1 N SER I 62 O THR I 73 SHEET 1 AB9 6 ILE I 10 ALA I 13 0 SHEET 2 AB9 6 THR I 101 ILE I 105 1 O GLU I 104 N MET I 11 SHEET 3 AB9 6 THR I 84 GLN I 89 -1 N TYR I 85 O THR I 101 SHEET 4 AB9 6 HIS I 33 GLN I 37 -1 N GLN I 37 O THR I 84 SHEET 5 AB9 6 LYS I 44 TYR I 48 -1 O LYS I 44 N GLN I 36 SHEET 6 AB9 6 ASN I 52 LEU I 53 -1 O ASN I 52 N TYR I 48 SHEET 1 AC1 4 ILE I 10 ALA I 13 0 SHEET 2 AC1 4 THR I 101 ILE I 105 1 O GLU I 104 N MET I 11 SHEET 3 AC1 4 THR I 84 GLN I 89 -1 N TYR I 85 O THR I 101 SHEET 4 AC1 4 THR I 96 PHE I 97 -1 O THR I 96 N GLN I 89 SHEET 1 AC2 6 GLY J 10 VAL J 12 0 SHEET 2 AC2 6 THR J 116 VAL J 120 1 O THR J 119 N GLY J 10 SHEET 3 AC2 6 ALA J 92 TYR J 101 -1 N ALA J 92 O VAL J 118 SHEET 4 AC2 6 MET J 34 THR J 40 -1 N SER J 35 O ALA J 97 SHEET 5 AC2 6 ARG J 44 ILE J 51 -1 O GLU J 46 N ARG J 38 SHEET 6 AC2 6 THR J 58 TYR J 59 -1 O TYR J 59 N ALA J 50 SHEET 1 AC3 4 GLY J 10 VAL J 12 0 SHEET 2 AC3 4 THR J 116 VAL J 120 1 O THR J 119 N GLY J 10 SHEET 3 AC3 4 ALA J 92 TYR J 101 -1 N ALA J 92 O VAL J 118 SHEET 4 AC3 4 TYR J 107 TRP J 112 -1 O ASP J 110 N ARG J 98 SHEET 1 AC4 3 SER J 17 CYS J 22 0 SHEET 2 AC4 3 THR J 78 SER J 84 -1 O MET J 83 N LEU J 18 SHEET 3 AC4 3 PHE J 68 ASP J 73 -1 N SER J 71 O TYR J 80 SHEET 1 AC5 4 PHE L 62 ILE L 64 0 SHEET 2 AC5 4 THR L 68 SER L 74 -1 O PHE L 70 N PHE L 62 SHEET 3 AC5 4 LYS M 360 HIS M 366 -1 O ASN M 365 N GLU L 69 SHEET 4 AC5 4 ARG M 376 CYS M 377 -1 O ARG M 376 N TRP M 362 SHEET 1 AC6 7 LEU L 90 LEU L 94 0 SHEET 2 AC6 7 HIS L 98 LYS L 102 -1 O LYS L 102 N LEU L 90 SHEET 3 AC6 7 SER L 107 ASP L 113 -1 O ILE L 110 N LEU L 99 SHEET 4 AC6 7 LEU L 214 PRO L 219 -1 O GLN L 218 N LYS L 109 SHEET 5 AC6 7 PHE L 175 ASN L 178 -1 N PHE L 175 O ALA L 217 SHEET 6 AC6 7 PHE L 162 CYS L 164 -1 N LEU L 163 O GLN L 176 SHEET 7 AC6 7 VAL L 124 ILE L 126 -1 N VAL L 124 O CYS L 164 SHEET 1 AC7 2 CYS M 271 LEU M 272 0 SHEET 2 AC7 2 LYS M 283 CYS M 284 -1 O LYS M 283 N LEU M 272 SHEET 1 AC8 2 ILE M 380 LYS M 381 0 SHEET 2 AC8 2 SER M 384 TYR M 385 -1 O SER M 384 N LYS M 381 SHEET 1 AC9 2 HIS M 447 ILE M 450 0 SHEET 2 AC9 2 THR M 479 ARG M 482 -1 O ARG M 482 N HIS M 447 SHEET 1 AD1 4 LEU N 4 SER N 7 0 SHEET 2 AD1 4 VAL N 19 ALA N 25 -1 O SER N 24 N THR N 5 SHEET 3 AD1 4 SER N 69 ILE N 74 -1 O TYR N 70 N CYS N 23 SHEET 4 AD1 4 PHE N 61 SER N 66 -1 N SER N 62 O THR N 73 SHEET 1 AD2 6 ILE N 10 ALA N 13 0 SHEET 2 AD2 6 THR N 101 ILE N 105 1 O GLU N 104 N MET N 11 SHEET 3 AD2 6 THR N 84 GLN N 89 -1 N TYR N 85 O THR N 101 SHEET 4 AD2 6 HIS N 33 GLN N 37 -1 N GLN N 37 O THR N 84 SHEET 5 AD2 6 LYS N 44 TYR N 48 -1 O LYS N 44 N GLN N 36 SHEET 6 AD2 6 ASN N 52 LEU N 53 -1 O ASN N 52 N TYR N 48 SHEET 1 AD3 4 ILE N 10 ALA N 13 0 SHEET 2 AD3 4 THR N 101 ILE N 105 1 O GLU N 104 N MET N 11 SHEET 3 AD3 4 THR N 84 GLN N 89 -1 N TYR N 85 O THR N 101 SHEET 4 AD3 4 THR N 96 PHE N 97 -1 O THR N 96 N GLN N 89 SHEET 1 AD4 6 GLY O 10 VAL O 12 0 SHEET 2 AD4 6 THR O 116 VAL O 120 1 O THR O 119 N GLY O 10 SHEET 3 AD4 6 ALA O 92 TYR O 101 -1 N ALA O 92 O VAL O 118 SHEET 4 AD4 6 MET O 34 THR O 40 -1 N SER O 35 O ALA O 97 SHEET 5 AD4 6 ARG O 44 ILE O 51 -1 O GLU O 46 N ARG O 38 SHEET 6 AD4 6 THR O 58 TYR O 59 -1 O TYR O 59 N ALA O 50 SHEET 1 AD5 4 GLY O 10 VAL O 12 0 SHEET 2 AD5 4 THR O 116 VAL O 120 1 O THR O 119 N GLY O 10 SHEET 3 AD5 4 ALA O 92 TYR O 101 -1 N ALA O 92 O VAL O 118 SHEET 4 AD5 4 TYR O 107 TRP O 112 -1 O ASP O 110 N ARG O 98 SHEET 1 AD6 3 SER O 17 CYS O 22 0 SHEET 2 AD6 3 THR O 78 SER O 84 -1 O MET O 83 N LEU O 18 SHEET 3 AD6 3 PHE O 68 ASP O 73 -1 N SER O 71 O TYR O 80 SSBOND 1 CYS A 57 CYS C 469 1555 1555 2.03 SSBOND 2 CYS B 92 CYS B 226 1555 1555 2.03 SSBOND 3 CYS B 135 CYS B 164 1555 1555 2.03 SSBOND 4 CYS B 207 CYS B 213 1555 1555 2.03 SSBOND 5 CYS C 271 CYS C 284 1555 1555 2.04 SSBOND 6 CYS C 293 CYS C 302 1555 1555 2.03 SSBOND 7 CYS C 356 CYS C 377 1555 1555 2.03 SSBOND 8 CYS D 23 CYS D 87 1555 1555 2.04 SSBOND 9 CYS E 22 CYS E 96 1555 1555 2.04 SSBOND 10 CYS F 57 CYS H 469 1555 1555 2.03 SSBOND 11 CYS G 92 CYS G 226 1555 1555 2.03 SSBOND 12 CYS G 135 CYS G 164 1555 1555 2.03 SSBOND 13 CYS G 207 CYS G 213 1555 1555 2.03 SSBOND 14 CYS H 271 CYS H 284 1555 1555 2.04 SSBOND 15 CYS H 293 CYS H 302 1555 1555 2.03 SSBOND 16 CYS H 356 CYS H 377 1555 1555 2.03 SSBOND 17 CYS I 23 CYS I 87 1555 1555 2.04 SSBOND 18 CYS J 22 CYS J 96 1555 1555 2.04 SSBOND 19 CYS K 57 CYS M 469 1555 1555 2.03 SSBOND 20 CYS L 92 CYS L 226 1555 1555 2.03 SSBOND 21 CYS L 135 CYS L 164 1555 1555 2.03 SSBOND 22 CYS L 207 CYS L 213 1555 1555 2.03 SSBOND 23 CYS M 271 CYS M 284 1555 1555 2.04 SSBOND 24 CYS M 293 CYS M 302 1555 1555 2.03 SSBOND 25 CYS M 356 CYS M 377 1555 1555 2.03 SSBOND 26 CYS N 23 CYS N 87 1555 1555 2.04 SSBOND 27 CYS O 22 CYS O 96 1555 1555 2.04 LINK N GLY A 2 C1 MYR A 101 1555 1555 1.34 LINK ND2 ASN B 95 C1 NAG B 301 1555 1555 1.44 LINK ND2 ASN B 166 C1 NAG B 302 1555 1555 1.44 LINK ND2 ASN B 178 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN C 357 C1 NAG Y 1 1555 1555 1.45 LINK ND2 ASN C 365 C1 NAG C 501 1555 1555 1.44 LINK ND2 ASN C 382 C1 NAG C 502 1555 1555 1.44 LINK ND2 ASN C 387 C1 NAG C 503 1555 1555 1.44 LINK N GLY F 2 C1 MYR F 101 1555 1555 1.34 LINK ND2 ASN G 95 C1 NAG G 301 1555 1555 1.44 LINK ND2 ASN G 166 C1 NAG G 302 1555 1555 1.44 LINK ND2 ASN G 178 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN H 357 C1 NAG h 1 1555 1555 1.45 LINK ND2 ASN H 365 C1 NAG H 501 1555 1555 1.44 LINK ND2 ASN H 382 C1 NAG H 502 1555 1555 1.44 LINK ND2 ASN H 387 C1 NAG H 503 1555 1555 1.44 LINK N GLY K 2 C1 MYR K 101 1555 1555 1.34 LINK ND2 ASN L 95 C1 NAG L 301 1555 1555 1.44 LINK ND2 ASN L 166 C1 NAG L 302 1555 1555 1.44 LINK ND2 ASN L 178 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN M 357 C1 NAG n 1 1555 1555 1.45 LINK ND2 ASN M 365 C1 NAG M 501 1555 1555 1.44 LINK ND2 ASN M 382 C1 NAG M 502 1555 1555 1.44 LINK ND2 ASN M 387 C1 NAG M 503 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.44 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG h 2 C1 BMA h 3 1555 1555 1.44 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.44 LINK O4 NAG n 2 C1 BMA n 3 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.45 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.45 LINK O4 NAG b 2 C1 BMA b 3 1555 1555 1.45 CISPEP 1 LEU C 457 PRO C 458 0 1.29 CISPEP 2 SER D 7 PRO D 8 0 -8.75 CISPEP 3 TYR D 93 PRO D 94 0 -0.24 CISPEP 4 LEU H 457 PRO H 458 0 1.27 CISPEP 5 SER I 7 PRO I 8 0 -8.71 CISPEP 6 TYR I 93 PRO I 94 0 -0.22 CISPEP 7 LEU M 457 PRO M 458 0 1.24 CISPEP 8 SER N 7 PRO N 8 0 -8.77 CISPEP 9 TYR N 93 PRO N 94 0 -0.31 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