HEADER VIRAL PROTEIN/IMMUNE SYSTEM 09-DEC-24 9MEW TITLE JUNV GP1, GP2, SSP AND CR1-28 FAB COMPLEX IN A PSEUDOTYPED VIRUS TITLE 2 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: JUNV GP1; COMPND 8 CHAIN: B, G, L; COMPND 9 SYNONYM: PRE-GP-C; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: JUNV GP2; COMPND 13 CHAIN: C, H, M; COMPND 14 SYNONYM: PRE-GP-C; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: CR1-28 FAB LIGHT CHAIN; COMPND 18 CHAIN: D, I, N; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: CR1-28 FAB 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: HOMO SAPIENS; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: HEK293TT; SOURCE 28 MOL_ID: 5; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 33 EXPRESSION_SYSTEM_CELL_LINE: HEK293TT KEYWDS VIRAL PROTEIN, GLYCOPROTEIN, GPC, JUNV, JUNIN MAMMARENAVIRUS, GP1, KEYWDS 2 GP2, SIGNAL PEPTIDE, VIRUS MEMBRANE, CR1-28 FAB, VIRAL PROTEIN- KEYWDS 3 IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR L.J.TAYLOR,M.R.SAWAYA,R.CASTELLS-GRAELLS,J.A.RODRIGUEZ REVDAT 1 23-JUL-25 9MEW 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 : REAL 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 : 397489 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 9MEW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290831. 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 AND CR1-28 REMARK 245 FAB COMPLEX IN A 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) : 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) : 4000.00 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: 15-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 15-MERIC REMARK 350 SOFTWARE USED: PISA 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, P, Q, R, S, REMARK 350 AND CHAINS: T, U 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 GLU B 59 REMARK 465 GLU B 60 REMARK 465 ARG B 248 REMARK 465 SER B 249 REMARK 465 LEU B 250 REMARK 465 LYS B 251 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 MET F 1 REMARK 465 GLU G 59 REMARK 465 GLU G 60 REMARK 465 ARG G 248 REMARK 465 SER G 249 REMARK 465 LEU G 250 REMARK 465 LYS G 251 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 MET K 1 REMARK 465 GLU L 59 REMARK 465 GLU L 60 REMARK 465 ARG L 248 REMARK 465 SER L 249 REMARK 465 LEU L 250 REMARK 465 LYS L 251 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 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 HIS B 67 -3.86 67.82 REMARK 500 ASN B 95 -125.78 54.17 REMARK 500 ARG B 201 -4.06 66.86 REMARK 500 ASP B 209 9.72 -67.94 REMARK 500 LEU B 224 49.41 -93.86 REMARK 500 GLN B 225 -1.79 -141.97 REMARK 500 SER C 257 52.93 -93.10 REMARK 500 GLU C 273 -169.42 -102.19 REMARK 500 ASP C 298 32.77 -140.02 REMARK 500 PRO D 8 -159.83 -85.05 REMARK 500 ASP D 30 -109.85 57.79 REMARK 500 ALA D 51 -4.86 66.08 REMARK 500 SER D 67 -179.68 -170.86 REMARK 500 ALA D 84 -167.09 -166.80 REMARK 500 ALA E 92 -178.63 -171.93 REMARK 500 SER E 108 -166.14 -163.79 REMARK 500 ASP E 157 63.15 60.15 REMARK 500 HIS G 67 -3.86 67.82 REMARK 500 ASN G 95 -125.78 54.17 REMARK 500 ARG G 201 -4.06 66.86 REMARK 500 ASP G 209 9.72 -67.94 REMARK 500 LEU G 224 49.41 -93.86 REMARK 500 GLN G 225 -1.79 -141.97 REMARK 500 SER H 257 52.93 -93.10 REMARK 500 GLU H 273 -169.42 -102.19 REMARK 500 ASP H 298 32.77 -140.02 REMARK 500 PRO I 8 -159.83 -85.05 REMARK 500 ASP I 30 -109.85 57.79 REMARK 500 ALA I 51 -4.86 66.08 REMARK 500 SER I 67 -179.68 -170.86 REMARK 500 ALA I 84 -167.09 -166.80 REMARK 500 ALA J 92 -178.63 -171.93 REMARK 500 SER J 108 -166.14 -163.79 REMARK 500 ASP J 157 63.15 60.15 REMARK 500 HIS L 67 -3.86 67.82 REMARK 500 ASN L 95 -125.78 54.17 REMARK 500 ARG L 201 -4.06 66.86 REMARK 500 ASP L 209 9.72 -67.94 REMARK 500 LEU L 224 49.41 -93.86 REMARK 500 GLN L 225 -1.79 -141.97 REMARK 500 SER M 257 52.93 -93.10 REMARK 500 GLU M 273 -169.42 -102.19 REMARK 500 ASP M 298 32.77 -140.02 REMARK 500 PRO N 8 -159.83 -85.05 REMARK 500 ASP N 30 -109.85 57.78 REMARK 500 ALA N 51 -4.86 66.08 REMARK 500 SER N 67 -179.68 -170.86 REMARK 500 ALA N 84 -167.09 -166.80 REMARK 500 ALA O 92 -178.63 -171.93 REMARK 500 SER O 108 -166.14 -163.79 REMARK 500 REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48221 RELATED DB: EMDB REMARK 900 JUNV GP1, GP2, SSP AND CR1-28 FAB COMPLEX IN A PSEUDOTYPED VIRUS REMARK 900 MEMBRANE DBREF 9MEW A 1 58 UNP P26313 GLYC_JUNIN 1 58 DBREF 9MEW B 59 251 UNP P26313 GLYC_JUNIN 59 251 DBREF 9MEW C 252 485 UNP P26313 GLYC_JUNIN 252 485 DBREF 9MEW D 2 207 PDB 9MEW 9MEW 2 207 DBREF 9MEW E 1 226 PDB 9MEW 9MEW 1 226 DBREF 9MEW F 1 58 UNP P26313 GLYC_JUNIN 1 58 DBREF 9MEW G 59 251 UNP P26313 GLYC_JUNIN 59 251 DBREF 9MEW H 252 485 UNP P26313 GLYC_JUNIN 252 485 DBREF 9MEW I 2 207 PDB 9MEW 9MEW 2 207 DBREF 9MEW J 1 226 PDB 9MEW 9MEW 1 226 DBREF 9MEW K 1 58 UNP P26313 GLYC_JUNIN 1 58 DBREF 9MEW L 59 251 UNP P26313 GLYC_JUNIN 59 251 DBREF 9MEW M 252 485 UNP P26313 GLYC_JUNIN 252 485 DBREF 9MEW N 2 207 PDB 9MEW 9MEW 2 207 DBREF 9MEW O 1 226 PDB 9MEW 9MEW 1 226 SEQRES 1 A 58 MET GLY GLN PHE ILE SER PHE MET GLN GLU ILE PRO THR SEQRES 2 A 58 PHE LEU GLN GLU ALA LEU ASN ILE ALA LEU VAL ALA VAL SEQRES 3 A 58 SER LEU ILE ALA ILE ILE LYS GLY VAL VAL ASN LEU TYR SEQRES 4 A 58 LYS SER GLY LEU PHE GLN PHE PHE VAL PHE LEU ALA LEU SEQRES 5 A 58 ALA GLY ARG SER CYS THR SEQRES 1 B 193 GLU GLU ALA PHE LYS ILE GLY LEU HIS THR GLU PHE GLN SEQRES 2 B 193 THR VAL SER PHE SER MET VAL GLY LEU PHE SER ASN ASN SEQRES 3 B 193 PRO HIS ASP LEU PRO LEU LEU CYS THR LEU ASN LYS SER SEQRES 4 B 193 HIS LEU TYR ILE LYS GLY GLY ASN ALA SER PHE LYS ILE SEQRES 5 B 193 SER PHE ASP ASP ILE ALA VAL LEU LEU PRO GLU TYR ASP SEQRES 6 B 193 VAL ILE ILE GLN HIS PRO ALA ASP MET SER TRP CYS SER SEQRES 7 B 193 LYS SER ASP ASP GLN ILE TRP LEU SER GLN TRP PHE MET SEQRES 8 B 193 ASN ALA VAL GLY HIS ASP TRP TYR LEU ASP PRO PRO PHE SEQRES 9 B 193 LEU CYS ARG ASN ARG THR LYS THR GLU GLY PHE ILE PHE SEQRES 10 B 193 GLN VAL ASN THR SER LYS THR GLY ILE ASN GLU ASN TYR SEQRES 11 B 193 ALA LYS LYS PHE LYS THR GLY MET HIS HIS LEU TYR ARG SEQRES 12 B 193 GLU TYR PRO ASP SER CYS LEU ASP GLY LYS LEU CYS LEU SEQRES 13 B 193 MET LYS ALA GLN PRO THR SER TRP PRO LEU GLN CYS PRO SEQRES 14 B 193 LEU ASP HIS VAL ASN THR LEU HIS PHE LEU THR ARG GLY SEQRES 15 B 193 LYS ASN ILE GLN LEU PRO ARG ARG SER LEU LYS 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 206 ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SER SEQRES 2 D 206 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 D 206 SER ILE ASP ASN TRP LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 4 D 206 GLY LYS ALA PRO LYS LEU LEU ILE TYR THR ALA SER ARG SEQRES 5 D 206 LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 D 206 SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU GLN SEQRES 7 D 206 PRO ASP ASP PHE ALA THR TYR TYR CYS GLN HIS ARG THR SEQRES 8 D 206 PHE GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL SEQRES 9 D 206 ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU SEQRES 10 D 206 GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU SEQRES 11 D 206 ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS SEQRES 12 D 206 VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER SEQRES 13 D 206 VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SEQRES 14 D 206 SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS SEQRES 15 D 206 HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SEQRES 16 D 206 SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 1 E 226 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 E 226 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 226 PHE THR PHE SER SER SER ALA MET HIS TRP VAL ARG GLN SEQRES 4 E 226 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE TRP SEQRES 5 E 226 SER ASP GLY SER ASN GLU ASN TYR ALA ASP SER VAL LYS SEQRES 6 E 226 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 E 226 LEU TYR LEU GLN MET SER SER LEU ARG ALA GLU ASP THR SEQRES 8 E 226 ALA VAL TYR TYR CYS ALA THR ASP LYS THR TYR VAL SER SEQRES 9 E 226 GLY TYR THR SER THR TRP TYR TYR PHE ASN TYR TRP GLY SEQRES 10 E 226 GLN GLY THR LEU VAL THR VAL SER GLY ALA SER THR LYS SEQRES 11 E 226 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 E 226 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 E 226 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 E 226 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 E 226 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 E 226 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 E 226 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 E 226 LYS ARG VAL GLU PRO SEQRES 1 F 58 MET GLY GLN PHE ILE SER PHE MET GLN GLU ILE PRO THR SEQRES 2 F 58 PHE LEU GLN GLU ALA LEU ASN ILE ALA LEU VAL ALA VAL SEQRES 3 F 58 SER LEU ILE ALA ILE ILE LYS GLY VAL VAL ASN LEU TYR SEQRES 4 F 58 LYS SER GLY LEU PHE GLN PHE PHE VAL PHE LEU ALA LEU SEQRES 5 F 58 ALA GLY ARG SER CYS THR SEQRES 1 G 193 GLU GLU ALA PHE LYS ILE GLY LEU HIS THR GLU PHE GLN SEQRES 2 G 193 THR VAL SER PHE SER MET VAL GLY LEU PHE SER ASN ASN SEQRES 3 G 193 PRO HIS ASP LEU PRO LEU LEU CYS THR LEU ASN LYS SER SEQRES 4 G 193 HIS LEU TYR ILE LYS GLY GLY ASN ALA SER PHE LYS ILE SEQRES 5 G 193 SER PHE ASP ASP ILE ALA VAL LEU LEU PRO GLU TYR ASP SEQRES 6 G 193 VAL ILE ILE GLN HIS PRO ALA ASP MET SER TRP CYS SER SEQRES 7 G 193 LYS SER ASP ASP GLN ILE TRP LEU SER GLN TRP PHE MET SEQRES 8 G 193 ASN ALA VAL GLY HIS ASP TRP TYR LEU ASP PRO PRO PHE SEQRES 9 G 193 LEU CYS ARG ASN ARG THR LYS THR GLU GLY PHE ILE PHE SEQRES 10 G 193 GLN VAL ASN THR SER LYS THR GLY ILE ASN GLU ASN TYR SEQRES 11 G 193 ALA LYS LYS PHE LYS THR GLY MET HIS HIS LEU TYR ARG SEQRES 12 G 193 GLU TYR PRO ASP SER CYS LEU ASP GLY LYS LEU CYS LEU SEQRES 13 G 193 MET LYS ALA GLN PRO THR SER TRP PRO LEU GLN CYS PRO SEQRES 14 G 193 LEU ASP HIS VAL ASN THR LEU HIS PHE LEU THR ARG GLY SEQRES 15 G 193 LYS ASN ILE GLN LEU PRO ARG ARG SER LEU LYS 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 206 ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SER SEQRES 2 I 206 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 I 206 SER ILE ASP ASN TRP LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 4 I 206 GLY LYS ALA PRO LYS LEU LEU ILE TYR THR ALA SER ARG SEQRES 5 I 206 LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 I 206 SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU GLN SEQRES 7 I 206 PRO ASP ASP PHE ALA THR TYR TYR CYS GLN HIS ARG THR SEQRES 8 I 206 PHE GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL SEQRES 9 I 206 ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU SEQRES 10 I 206 GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU SEQRES 11 I 206 ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS SEQRES 12 I 206 VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER SEQRES 13 I 206 VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SEQRES 14 I 206 SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS SEQRES 15 I 206 HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SEQRES 16 I 206 SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 1 J 226 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 J 226 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 J 226 PHE THR PHE SER SER SER ALA MET HIS TRP VAL ARG GLN SEQRES 4 J 226 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE TRP SEQRES 5 J 226 SER ASP GLY SER ASN GLU ASN TYR ALA ASP SER VAL LYS SEQRES 6 J 226 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 J 226 LEU TYR LEU GLN MET SER SER LEU ARG ALA GLU ASP THR SEQRES 8 J 226 ALA VAL TYR TYR CYS ALA THR ASP LYS THR TYR VAL SER SEQRES 9 J 226 GLY TYR THR SER THR TRP TYR TYR PHE ASN TYR TRP GLY SEQRES 10 J 226 GLN GLY THR LEU VAL THR VAL SER GLY ALA SER THR LYS SEQRES 11 J 226 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 J 226 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 J 226 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 J 226 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 J 226 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 J 226 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 J 226 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 J 226 LYS ARG VAL GLU PRO SEQRES 1 K 58 MET GLY GLN PHE ILE SER PHE MET GLN GLU ILE PRO THR SEQRES 2 K 58 PHE LEU GLN GLU ALA LEU ASN ILE ALA LEU VAL ALA VAL SEQRES 3 K 58 SER LEU ILE ALA ILE ILE LYS GLY VAL VAL ASN LEU TYR SEQRES 4 K 58 LYS SER GLY LEU PHE GLN PHE PHE VAL PHE LEU ALA LEU SEQRES 5 K 58 ALA GLY ARG SER CYS THR SEQRES 1 L 193 GLU GLU ALA PHE LYS ILE GLY LEU HIS THR GLU PHE GLN SEQRES 2 L 193 THR VAL SER PHE SER MET VAL GLY LEU PHE SER ASN ASN SEQRES 3 L 193 PRO HIS ASP LEU PRO LEU LEU CYS THR LEU ASN LYS SER SEQRES 4 L 193 HIS LEU TYR ILE LYS GLY GLY ASN ALA SER PHE LYS ILE SEQRES 5 L 193 SER PHE ASP ASP ILE ALA VAL LEU LEU PRO GLU TYR ASP SEQRES 6 L 193 VAL ILE ILE GLN HIS PRO ALA ASP MET SER TRP CYS SER SEQRES 7 L 193 LYS SER ASP ASP GLN ILE TRP LEU SER GLN TRP PHE MET SEQRES 8 L 193 ASN ALA VAL GLY HIS ASP TRP TYR LEU ASP PRO PRO PHE SEQRES 9 L 193 LEU CYS ARG ASN ARG THR LYS THR GLU GLY PHE ILE PHE SEQRES 10 L 193 GLN VAL ASN THR SER LYS THR GLY ILE ASN GLU ASN TYR SEQRES 11 L 193 ALA LYS LYS PHE LYS THR GLY MET HIS HIS LEU TYR ARG SEQRES 12 L 193 GLU TYR PRO ASP SER CYS LEU ASP GLY LYS LEU CYS LEU SEQRES 13 L 193 MET LYS ALA GLN PRO THR SER TRP PRO LEU GLN CYS PRO SEQRES 14 L 193 LEU ASP HIS VAL ASN THR LEU HIS PHE LEU THR ARG GLY SEQRES 15 L 193 LYS ASN ILE GLN LEU PRO ARG ARG SER LEU LYS 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 206 ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SER SEQRES 2 N 206 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 N 206 SER ILE ASP ASN TRP LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 4 N 206 GLY LYS ALA PRO LYS LEU LEU ILE TYR THR ALA SER ARG SEQRES 5 N 206 LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 N 206 SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU GLN SEQRES 7 N 206 PRO ASP ASP PHE ALA THR TYR TYR CYS GLN HIS ARG THR SEQRES 8 N 206 PHE GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL SEQRES 9 N 206 ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU SEQRES 10 N 206 GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU SEQRES 11 N 206 ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS SEQRES 12 N 206 VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER SEQRES 13 N 206 VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SEQRES 14 N 206 SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS SEQRES 15 N 206 HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SEQRES 16 N 206 SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 1 O 226 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 O 226 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 O 226 PHE THR PHE SER SER SER ALA MET HIS TRP VAL ARG GLN SEQRES 4 O 226 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE TRP SEQRES 5 O 226 SER ASP GLY SER ASN GLU ASN TYR ALA ASP SER VAL LYS SEQRES 6 O 226 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 O 226 LEU TYR LEU GLN MET SER SER LEU ARG ALA GLU ASP THR SEQRES 8 O 226 ALA VAL TYR TYR CYS ALA THR ASP LYS THR TYR VAL SER SEQRES 9 O 226 GLY TYR THR SER THR TRP TYR TYR PHE ASN TYR TRP GLY SEQRES 10 O 226 GLN GLY THR LEU VAL THR VAL SER GLY ALA SER THR LYS SEQRES 11 O 226 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 O 226 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 O 226 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 O 226 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 O 226 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 O 226 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 O 226 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 O 226 LYS ARG VAL GLU PRO HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 HET NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HET NAG T 1 14 HET NAG T 2 14 HET BMA T 3 11 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 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 SER B 76 ASN B 84 1 9 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 ILE B 184 HIS B 198 1 15 HELIX 8 AA8 HIS B 230 GLY B 240 1 11 HELIX 9 AA9 GLY C 286 ALA C 291 1 6 HELIX 10 AB1 LYS C 292 ASN C 294 5 3 HELIX 11 AB2 SER C 299 GLU C 321 1 23 HELIX 12 AB3 GLY C 330 ALA C 335 1 6 HELIX 13 AB4 SER C 338 MET C 351 1 14 HELIX 14 AB5 ASN C 387 GLY C 416 1 30 HELIX 15 AB6 PRO C 419 GLY C 443 1 25 HELIX 16 AB7 GLN D 79 PHE D 83 5 5 HELIX 17 AB8 SER D 116 GLY D 123 1 8 HELIX 18 AB9 LYS D 178 HIS D 184 1 7 HELIX 19 AC1 THR E 28 SER E 32 5 5 HELIX 20 AC2 ASP E 62 LYS E 65 5 4 HELIX 21 AC3 ARG E 87 THR E 91 5 5 HELIX 22 AC4 SER E 140 THR E 144 5 5 HELIX 23 AC5 SER E 169 ALA E 171 5 3 HELIX 24 AC6 SER E 200 LEU E 202 5 3 HELIX 25 AC7 GLN F 3 LEU F 15 1 13 HELIX 26 AC8 GLU F 17 GLY F 42 1 26 HELIX 27 AC9 GLY F 42 ALA F 53 1 12 HELIX 28 AD1 SER G 76 ASN G 84 1 9 HELIX 29 AD2 ALA G 130 CYS G 135 5 6 HELIX 30 AD3 SER G 138 GLY G 153 1 16 HELIX 31 AD4 ILE G 184 HIS G 198 1 15 HELIX 32 AD5 HIS G 230 GLY G 240 1 11 HELIX 33 AD6 GLY H 286 ALA H 291 1 6 HELIX 34 AD7 LYS H 292 ASN H 294 5 3 HELIX 35 AD8 SER H 299 GLU H 321 1 23 HELIX 36 AD9 GLY H 330 ALA H 335 1 6 HELIX 37 AE1 SER H 338 MET H 351 1 14 HELIX 38 AE2 ASN H 387 GLY H 416 1 30 HELIX 39 AE3 PRO H 419 GLY H 443 1 25 HELIX 40 AE4 GLN I 79 PHE I 83 5 5 HELIX 41 AE5 SER I 116 GLY I 123 1 8 HELIX 42 AE6 LYS I 178 HIS I 184 1 7 HELIX 43 AE7 THR J 28 SER J 32 5 5 HELIX 44 AE8 ASP J 62 LYS J 65 5 4 HELIX 45 AE9 ARG J 87 THR J 91 5 5 HELIX 46 AF1 SER J 140 THR J 144 5 5 HELIX 47 AF2 SER J 169 ALA J 171 5 3 HELIX 48 AF3 SER J 200 LEU J 202 5 3 HELIX 49 AF4 GLN K 3 LEU K 15 1 13 HELIX 50 AF5 GLU K 17 GLY K 42 1 26 HELIX 51 AF6 GLY K 42 ALA K 53 1 12 HELIX 52 AF7 SER L 76 ASN L 84 1 9 HELIX 53 AF8 ALA L 130 CYS L 135 5 6 HELIX 54 AF9 SER L 138 GLY L 153 1 16 HELIX 55 AG1 ILE L 184 HIS L 198 1 15 HELIX 56 AG2 HIS L 230 GLY L 240 1 11 HELIX 57 AG3 GLY M 286 ALA M 291 1 6 HELIX 58 AG4 LYS M 292 ASN M 294 5 3 HELIX 59 AG5 SER M 299 GLU M 321 1 23 HELIX 60 AG6 GLY M 330 ALA M 335 1 6 HELIX 61 AG7 SER M 338 MET M 351 1 14 HELIX 62 AG8 ASN M 387 GLY M 416 1 30 HELIX 63 AG9 PRO M 419 GLY M 443 1 25 HELIX 64 AH1 GLN N 79 PHE N 83 5 5 HELIX 65 AH2 SER N 116 GLY N 123 1 8 HELIX 66 AH3 LYS N 178 HIS N 184 1 7 HELIX 67 AH4 THR O 28 SER O 32 5 5 HELIX 68 AH5 ASP O 62 LYS O 65 5 4 HELIX 69 AH6 ARG O 87 THR O 91 5 5 HELIX 70 AH7 SER O 140 THR O 144 5 5 HELIX 71 AH8 SER O 169 ALA O 171 5 3 HELIX 72 AH9 SER O 200 LEU O 202 5 3 SHEET 1 AA1 3 THR B 68 SER B 74 0 SHEET 2 AA1 3 LYS C 360 HIS C 366 -1 O ASN C 365 N GLU B 69 SHEET 3 AA1 3 GLN C 371 HIS C 372 -1 O GLN C 371 N HIS C 366 SHEET 1 AA2 3 THR B 68 SER B 74 0 SHEET 2 AA2 3 LYS C 360 HIS C 366 -1 O ASN C 365 N GLU B 69 SHEET 3 AA2 3 ARG C 376 CYS C 377 -1 O ARG C 376 N TRP C 362 SHEET 1 AA3 7 LEU B 90 LEU B 94 0 SHEET 2 AA3 7 HIS B 98 GLY B 103 -1 O TYR B 100 N CYS B 92 SHEET 3 AA3 7 ALA B 106 ASP B 113 -1 O ILE B 110 N LEU B 99 SHEET 4 AA3 7 LEU B 214 PRO B 219 -1 O GLN B 218 N LYS B 109 SHEET 5 AA3 7 PHE B 175 ASN B 178 -1 N VAL B 177 O MET B 215 SHEET 6 AA3 7 PHE B 162 CYS B 164 -1 N LEU B 163 O GLN B 176 SHEET 7 AA3 7 VAL B 124 ILE B 126 -1 N VAL B 124 O CYS B 164 SHEET 1 AA4 2 GLN B 244 LEU B 245 0 SHEET 2 AA4 2 LEU C 328 MET C 329 -1 O LEU C 328 N LEU B 245 SHEET 1 AA5 2 CYS C 271 LEU C 272 0 SHEET 2 AA5 2 LYS C 283 CYS C 284 -1 O LYS C 283 N LEU C 272 SHEET 1 AA6 2 ILE C 380 LYS C 381 0 SHEET 2 AA6 2 SER C 384 TYR C 385 -1 O SER C 384 N LYS C 381 SHEET 1 AA7 2 HIS C 447 ILE C 450 0 SHEET 2 AA7 2 THR C 479 ARG C 482 -1 O ARG C 482 N HIS C 447 SHEET 1 AA8 4 MET D 4 SER D 7 0 SHEET 2 AA8 4 VAL D 19 ALA D 25 -1 O THR D 22 N SER D 7 SHEET 3 AA8 4 GLU D 70 ILE D 75 -1 O PHE D 71 N CYS D 23 SHEET 4 AA8 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AA9 6 THR D 10 ALA D 13 0 SHEET 2 AA9 6 THR D 97 ILE D 101 1 O LYS D 98 N LEU D 11 SHEET 3 AA9 6 ALA D 84 GLN D 89 -1 N TYR D 86 O THR D 97 SHEET 4 AA9 6 ALA D 34 GLN D 38 -1 N GLN D 38 O THR D 85 SHEET 5 AA9 6 LYS D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AA9 6 ARG D 53 LEU D 54 -1 O ARG D 53 N TYR D 49 SHEET 1 AB1 4 SER D 109 PHE D 113 0 SHEET 2 AB1 4 THR D 124 PHE D 134 -1 O VAL D 128 N PHE D 113 SHEET 3 AB1 4 TYR D 168 SER D 177 -1 O LEU D 176 N ALA D 125 SHEET 4 AB1 4 SER D 154 THR D 159 -1 N GLN D 155 O THR D 173 SHEET 1 AB2 4 ALA D 148 GLN D 150 0 SHEET 2 AB2 4 ALA D 139 VAL D 145 -1 N VAL D 145 O ALA D 148 SHEET 3 AB2 4 VAL D 186 HIS D 193 -1 O ALA D 188 N LYS D 144 SHEET 4 AB2 4 VAL D 200 ASN D 205 -1 O VAL D 200 N VAL D 191 SHEET 1 AB3 4 GLN E 3 SER E 7 0 SHEET 2 AB3 4 LEU E 18 SER E 25 -1 O SER E 25 N GLN E 3 SHEET 3 AB3 4 THR E 78 MET E 83 -1 O LEU E 81 N LEU E 20 SHEET 4 AB3 4 PHE E 68 ASP E 73 -1 N THR E 69 O GLN E 82 SHEET 1 AB4 6 GLY E 10 VAL E 12 0 SHEET 2 AB4 6 THR E 120 VAL E 124 1 O THR E 123 N VAL E 12 SHEET 3 AB4 6 ALA E 92 ASP E 99 -1 N ALA E 92 O VAL E 122 SHEET 4 AB4 6 MET E 34 GLN E 39 -1 N GLN E 39 O VAL E 93 SHEET 5 AB4 6 LEU E 45 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AB4 6 GLU E 58 TYR E 60 -1 O ASN E 59 N VAL E 50 SHEET 1 AB5 4 GLY E 10 VAL E 12 0 SHEET 2 AB5 4 THR E 120 VAL E 124 1 O THR E 123 N VAL E 12 SHEET 3 AB5 4 ALA E 92 ASP E 99 -1 N ALA E 92 O VAL E 122 SHEET 4 AB5 4 PHE E 113 TYR E 115 -1 O ASN E 114 N THR E 98 SHEET 1 AB6 4 SER E 133 LEU E 137 0 SHEET 2 AB6 4 THR E 148 TYR E 158 -1 O LEU E 154 N PHE E 135 SHEET 3 AB6 4 TYR E 189 PRO E 198 -1 O VAL E 197 N ALA E 149 SHEET 4 AB6 4 VAL E 176 THR E 178 -1 N HIS E 177 O VAL E 194 SHEET 1 AB7 4 SER E 133 LEU E 137 0 SHEET 2 AB7 4 THR E 148 TYR E 158 -1 O LEU E 154 N PHE E 135 SHEET 3 AB7 4 TYR E 189 PRO E 198 -1 O VAL E 197 N ALA E 149 SHEET 4 AB7 4 VAL E 182 LEU E 183 -1 N VAL E 182 O SER E 190 SHEET 1 AB8 3 THR E 164 TRP E 167 0 SHEET 2 AB8 3 TYR E 207 HIS E 213 -1 O ASN E 210 N SER E 166 SHEET 3 AB8 3 THR E 218 VAL E 224 -1 O LYS E 222 N CYS E 209 SHEET 1 AB9 3 THR G 68 SER G 74 0 SHEET 2 AB9 3 LYS H 360 HIS H 366 -1 O ASN H 365 N GLU G 69 SHEET 3 AB9 3 GLN H 371 HIS H 372 -1 O GLN H 371 N HIS H 366 SHEET 1 AC1 3 THR G 68 SER G 74 0 SHEET 2 AC1 3 LYS H 360 HIS H 366 -1 O ASN H 365 N GLU G 69 SHEET 3 AC1 3 ARG H 376 CYS H 377 -1 O ARG H 376 N TRP H 362 SHEET 1 AC2 7 LEU G 90 LEU G 94 0 SHEET 2 AC2 7 HIS G 98 GLY G 103 -1 O TYR G 100 N CYS G 92 SHEET 3 AC2 7 ALA G 106 ASP G 113 -1 O ILE G 110 N LEU G 99 SHEET 4 AC2 7 LEU G 214 PRO G 219 -1 O GLN G 218 N LYS G 109 SHEET 5 AC2 7 PHE G 175 ASN G 178 -1 N VAL G 177 O MET G 215 SHEET 6 AC2 7 PHE G 162 CYS G 164 -1 N LEU G 163 O GLN G 176 SHEET 7 AC2 7 VAL G 124 ILE G 126 -1 N VAL G 124 O CYS G 164 SHEET 1 AC3 2 GLN G 244 LEU G 245 0 SHEET 2 AC3 2 LEU H 328 MET H 329 -1 O LEU H 328 N LEU G 245 SHEET 1 AC4 2 CYS H 271 LEU H 272 0 SHEET 2 AC4 2 LYS H 283 CYS H 284 -1 O LYS H 283 N LEU H 272 SHEET 1 AC5 2 ILE H 380 LYS H 381 0 SHEET 2 AC5 2 SER H 384 TYR H 385 -1 O SER H 384 N LYS H 381 SHEET 1 AC6 2 HIS H 447 ILE H 450 0 SHEET 2 AC6 2 THR H 479 ARG H 482 -1 O ARG H 482 N HIS H 447 SHEET 1 AC7 4 MET I 4 SER I 7 0 SHEET 2 AC7 4 VAL I 19 ALA I 25 -1 O THR I 22 N SER I 7 SHEET 3 AC7 4 GLU I 70 ILE I 75 -1 O PHE I 71 N CYS I 23 SHEET 4 AC7 4 PHE I 62 SER I 67 -1 N SER I 63 O THR I 74 SHEET 1 AC8 6 THR I 10 ALA I 13 0 SHEET 2 AC8 6 THR I 97 ILE I 101 1 O LYS I 98 N LEU I 11 SHEET 3 AC8 6 ALA I 84 GLN I 89 -1 N TYR I 86 O THR I 97 SHEET 4 AC8 6 ALA I 34 GLN I 38 -1 N GLN I 38 O THR I 85 SHEET 5 AC8 6 LYS I 45 TYR I 49 -1 O LEU I 47 N TRP I 35 SHEET 6 AC8 6 ARG I 53 LEU I 54 -1 O ARG I 53 N TYR I 49 SHEET 1 AC9 4 SER I 109 PHE I 113 0 SHEET 2 AC9 4 THR I 124 PHE I 134 -1 O VAL I 128 N PHE I 113 SHEET 3 AC9 4 TYR I 168 SER I 177 -1 O LEU I 176 N ALA I 125 SHEET 4 AC9 4 SER I 154 THR I 159 -1 N GLN I 155 O THR I 173 SHEET 1 AD1 4 ALA I 148 GLN I 150 0 SHEET 2 AD1 4 ALA I 139 VAL I 145 -1 N VAL I 145 O ALA I 148 SHEET 3 AD1 4 VAL I 186 HIS I 193 -1 O ALA I 188 N LYS I 144 SHEET 4 AD1 4 VAL I 200 ASN I 205 -1 O VAL I 200 N VAL I 191 SHEET 1 AD2 4 GLN J 3 SER J 7 0 SHEET 2 AD2 4 LEU J 18 SER J 25 -1 O SER J 25 N GLN J 3 SHEET 3 AD2 4 THR J 78 MET J 83 -1 O LEU J 81 N LEU J 20 SHEET 4 AD2 4 PHE J 68 ASP J 73 -1 N THR J 69 O GLN J 82 SHEET 1 AD3 6 GLY J 10 VAL J 12 0 SHEET 2 AD3 6 THR J 120 VAL J 124 1 O THR J 123 N VAL J 12 SHEET 3 AD3 6 ALA J 92 ASP J 99 -1 N ALA J 92 O VAL J 122 SHEET 4 AD3 6 MET J 34 GLN J 39 -1 N GLN J 39 O VAL J 93 SHEET 5 AD3 6 LEU J 45 ILE J 51 -1 O GLU J 46 N ARG J 38 SHEET 6 AD3 6 GLU J 58 TYR J 60 -1 O ASN J 59 N VAL J 50 SHEET 1 AD4 4 GLY J 10 VAL J 12 0 SHEET 2 AD4 4 THR J 120 VAL J 124 1 O THR J 123 N VAL J 12 SHEET 3 AD4 4 ALA J 92 ASP J 99 -1 N ALA J 92 O VAL J 122 SHEET 4 AD4 4 PHE J 113 TYR J 115 -1 O ASN J 114 N THR J 98 SHEET 1 AD5 4 SER J 133 LEU J 137 0 SHEET 2 AD5 4 THR J 148 TYR J 158 -1 O LEU J 154 N PHE J 135 SHEET 3 AD5 4 TYR J 189 PRO J 198 -1 O VAL J 197 N ALA J 149 SHEET 4 AD5 4 VAL J 176 THR J 178 -1 N HIS J 177 O VAL J 194 SHEET 1 AD6 4 SER J 133 LEU J 137 0 SHEET 2 AD6 4 THR J 148 TYR J 158 -1 O LEU J 154 N PHE J 135 SHEET 3 AD6 4 TYR J 189 PRO J 198 -1 O VAL J 197 N ALA J 149 SHEET 4 AD6 4 VAL J 182 LEU J 183 -1 N VAL J 182 O SER J 190 SHEET 1 AD7 3 THR J 164 TRP J 167 0 SHEET 2 AD7 3 TYR J 207 HIS J 213 -1 O ASN J 210 N SER J 166 SHEET 3 AD7 3 THR J 218 VAL J 224 -1 O LYS J 222 N CYS J 209 SHEET 1 AD8 3 THR L 68 SER L 74 0 SHEET 2 AD8 3 LYS M 360 HIS M 366 -1 O ASN M 365 N GLU L 69 SHEET 3 AD8 3 GLN M 371 HIS M 372 -1 O GLN M 371 N HIS M 366 SHEET 1 AD9 3 THR L 68 SER L 74 0 SHEET 2 AD9 3 LYS M 360 HIS M 366 -1 O ASN M 365 N GLU L 69 SHEET 3 AD9 3 ARG M 376 CYS M 377 -1 O ARG M 376 N TRP M 362 SHEET 1 AE1 7 LEU L 90 LEU L 94 0 SHEET 2 AE1 7 HIS L 98 GLY L 103 -1 O TYR L 100 N CYS L 92 SHEET 3 AE1 7 ALA L 106 ASP L 113 -1 O ILE L 110 N LEU L 99 SHEET 4 AE1 7 LEU L 214 PRO L 219 -1 O GLN L 218 N LYS L 109 SHEET 5 AE1 7 PHE L 175 ASN L 178 -1 N VAL L 177 O MET L 215 SHEET 6 AE1 7 PHE L 162 CYS L 164 -1 N LEU L 163 O GLN L 176 SHEET 7 AE1 7 VAL L 124 ILE L 126 -1 N VAL L 124 O CYS L 164 SHEET 1 AE2 2 GLN L 244 LEU L 245 0 SHEET 2 AE2 2 LEU M 328 MET M 329 -1 O LEU M 328 N LEU L 245 SHEET 1 AE3 2 CYS M 271 LEU M 272 0 SHEET 2 AE3 2 LYS M 283 CYS M 284 -1 O LYS M 283 N LEU M 272 SHEET 1 AE4 2 ILE M 380 LYS M 381 0 SHEET 2 AE4 2 SER M 384 TYR M 385 -1 O SER M 384 N LYS M 381 SHEET 1 AE5 2 HIS M 447 ILE M 450 0 SHEET 2 AE5 2 THR M 479 ARG M 482 -1 O ARG M 482 N HIS M 447 SHEET 1 AE6 4 MET N 4 SER N 7 0 SHEET 2 AE6 4 VAL N 19 ALA N 25 -1 O THR N 22 N SER N 7 SHEET 3 AE6 4 GLU N 70 ILE N 75 -1 O PHE N 71 N CYS N 23 SHEET 4 AE6 4 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74 SHEET 1 AE7 6 THR N 10 ALA N 13 0 SHEET 2 AE7 6 THR N 97 ILE N 101 1 O LYS N 98 N LEU N 11 SHEET 3 AE7 6 ALA N 84 GLN N 89 -1 N TYR N 86 O THR N 97 SHEET 4 AE7 6 ALA N 34 GLN N 38 -1 N GLN N 38 O THR N 85 SHEET 5 AE7 6 LYS N 45 TYR N 49 -1 O LEU N 47 N TRP N 35 SHEET 6 AE7 6 ARG N 53 LEU N 54 -1 O ARG N 53 N TYR N 49 SHEET 1 AE8 4 SER N 109 PHE N 113 0 SHEET 2 AE8 4 THR N 124 PHE N 134 -1 O VAL N 128 N PHE N 113 SHEET 3 AE8 4 TYR N 168 SER N 177 -1 O LEU N 176 N ALA N 125 SHEET 4 AE8 4 SER N 154 THR N 159 -1 N GLN N 155 O THR N 173 SHEET 1 AE9 4 ALA N 148 GLN N 150 0 SHEET 2 AE9 4 ALA N 139 VAL N 145 -1 N VAL N 145 O ALA N 148 SHEET 3 AE9 4 VAL N 186 HIS N 193 -1 O ALA N 188 N LYS N 144 SHEET 4 AE9 4 VAL N 200 ASN N 205 -1 O VAL N 200 N VAL N 191 SHEET 1 AF1 4 GLN O 3 SER O 7 0 SHEET 2 AF1 4 LEU O 18 SER O 25 -1 O SER O 25 N GLN O 3 SHEET 3 AF1 4 THR O 78 MET O 83 -1 O LEU O 81 N LEU O 20 SHEET 4 AF1 4 PHE O 68 ASP O 73 -1 N THR O 69 O GLN O 82 SHEET 1 AF2 6 GLY O 10 VAL O 12 0 SHEET 2 AF2 6 THR O 120 VAL O 124 1 O THR O 123 N VAL O 12 SHEET 3 AF2 6 ALA O 92 ASP O 99 -1 N ALA O 92 O VAL O 122 SHEET 4 AF2 6 MET O 34 GLN O 39 -1 N GLN O 39 O VAL O 93 SHEET 5 AF2 6 LEU O 45 ILE O 51 -1 O GLU O 46 N ARG O 38 SHEET 6 AF2 6 GLU O 58 TYR O 60 -1 O ASN O 59 N VAL O 50 SHEET 1 AF3 4 GLY O 10 VAL O 12 0 SHEET 2 AF3 4 THR O 120 VAL O 124 1 O THR O 123 N VAL O 12 SHEET 3 AF3 4 ALA O 92 ASP O 99 -1 N ALA O 92 O VAL O 122 SHEET 4 AF3 4 PHE O 113 TYR O 115 -1 O ASN O 114 N THR O 98 SHEET 1 AF4 4 SER O 133 LEU O 137 0 SHEET 2 AF4 4 THR O 148 TYR O 158 -1 O LEU O 154 N PHE O 135 SHEET 3 AF4 4 TYR O 189 PRO O 198 -1 O VAL O 197 N ALA O 149 SHEET 4 AF4 4 VAL O 176 THR O 178 -1 N HIS O 177 O VAL O 194 SHEET 1 AF5 4 SER O 133 LEU O 137 0 SHEET 2 AF5 4 THR O 148 TYR O 158 -1 O LEU O 154 N PHE O 135 SHEET 3 AF5 4 TYR O 189 PRO O 198 -1 O VAL O 197 N ALA O 149 SHEET 4 AF5 4 VAL O 182 LEU O 183 -1 N VAL O 182 O SER O 190 SHEET 1 AF6 3 THR O 164 TRP O 167 0 SHEET 2 AF6 3 TYR O 207 HIS O 213 -1 O ASN O 210 N SER O 166 SHEET 3 AF6 3 THR O 218 VAL O 224 -1 O LYS O 222 N CYS O 209 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 2.03 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 88 1555 1555 2.04 SSBOND 9 CYS D 129 CYS D 189 1555 1555 2.04 SSBOND 10 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 11 CYS E 153 CYS E 209 1555 1555 2.03 SSBOND 12 CYS F 57 CYS H 469 1555 1555 2.03 SSBOND 13 CYS G 92 CYS G 226 1555 1555 2.03 SSBOND 14 CYS G 135 CYS G 164 1555 1555 2.03 SSBOND 15 CYS G 207 CYS G 213 1555 1555 2.03 SSBOND 16 CYS H 271 CYS H 284 1555 1555 2.03 SSBOND 17 CYS H 293 CYS H 302 1555 1555 2.03 SSBOND 18 CYS H 356 CYS H 377 1555 1555 2.03 SSBOND 19 CYS I 23 CYS I 88 1555 1555 2.04 SSBOND 20 CYS I 129 CYS I 189 1555 1555 2.04 SSBOND 21 CYS J 22 CYS J 96 1555 1555 2.03 SSBOND 22 CYS J 153 CYS J 209 1555 1555 2.03 SSBOND 23 CYS K 57 CYS M 469 1555 1555 2.03 SSBOND 24 CYS L 92 CYS L 226 1555 1555 2.03 SSBOND 25 CYS L 135 CYS L 164 1555 1555 2.03 SSBOND 26 CYS L 207 CYS L 213 1555 1555 2.03 SSBOND 27 CYS M 271 CYS M 284 1555 1555 2.03 SSBOND 28 CYS M 293 CYS M 302 1555 1555 2.03 SSBOND 29 CYS M 356 CYS M 377 1555 1555 2.03 SSBOND 30 CYS N 23 CYS N 88 1555 1555 2.04 SSBOND 31 CYS N 129 CYS N 189 1555 1555 2.04 SSBOND 32 CYS O 22 CYS O 96 1555 1555 2.03 SSBOND 33 CYS O 153 CYS O 209 1555 1555 2.03 LINK N GLY A 2 C1 MYR A 101 1555 1555 1.34 LINK ND2 ASN B 95 C1 NAG B 301 1555 1555 1.45 LINK ND2 ASN B 166 C1 NAG B 302 1555 1555 1.47 LINK ND2 ASN B 178 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN C 357 C1 NAG Q 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 1.45 LINK N GLY F 2 C1 MYR F 101 1555 1555 1.34 LINK ND2 ASN G 95 C1 NAG G 301 1555 1555 1.45 LINK ND2 ASN G 166 C1 NAG G 302 1555 1555 1.47 LINK ND2 ASN G 178 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN H 357 C1 NAG S 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 1.45 LINK N GLY K 2 C1 MYR K 101 1555 1555 1.34 LINK ND2 ASN L 95 C1 NAG L 301 1555 1555 1.45 LINK ND2 ASN L 166 C1 NAG L 302 1555 1555 1.47 LINK ND2 ASN L 178 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN M 357 C1 NAG U 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 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.45 CISPEP 1 LEU C 457 PRO C 458 0 4.78 CISPEP 2 SER D 7 PRO D 8 0 -2.34 CISPEP 3 TYR D 135 PRO D 136 0 -1.03 CISPEP 4 PHE E 159 PRO E 160 0 -1.75 CISPEP 5 GLU E 161 PRO E 162 0 -4.10 CISPEP 6 LEU H 457 PRO H 458 0 4.78 CISPEP 7 SER I 7 PRO I 8 0 -2.34 CISPEP 8 TYR I 135 PRO I 136 0 -1.03 CISPEP 9 PHE J 159 PRO J 160 0 -1.75 CISPEP 10 GLU J 161 PRO J 162 0 -4.10 CISPEP 11 LEU M 457 PRO M 458 0 4.78 CISPEP 12 SER N 7 PRO N 8 0 -2.34 CISPEP 13 TYR N 135 PRO N 136 0 -1.03 CISPEP 14 PHE O 159 PRO O 160 0 -1.75 CISPEP 15 GLU O 161 PRO O 162 0 -4.10 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 MTRIX1 1 -0.499758 0.866165 0.000001 112.93141 1 MTRIX2 1 -0.866165 -0.499758 0.000002 421.70176 1 MTRIX3 1 0.000002 0.000000 1.000000 -0.00037 1 MTRIX1 2 -0.500122 -0.865955 0.000000 421.72950 1 MTRIX2 2 0.865955 -0.500122 -0.000002 113.03425 1 MTRIX3 2 0.000001 0.000000 1.000000 -0.00019 1 MTRIX1 3 -0.500119 0.865957 0.000000 113.03305 1 MTRIX2 3 -0.865957 -0.500119 0.000000 421.72931 1 MTRIX3 3 0.000000 0.000000 1.000000 -0.00003 1 MTRIX1 4 -0.499761 -0.866163 0.000000 421.70242 1 MTRIX2 4 0.866163 -0.499761 0.000000 112.93251 1 MTRIX3 4 0.000000 -0.000001 1.000000 0.00007 1 MTRIX1 5 -0.500120 -0.865956 0.000000 421.72942 1 MTRIX2 5 0.865956 -0.500120 0.000000 113.03354 1 MTRIX3 5 0.000000 0.000000 1.000000 -0.00003 1 MTRIX1 6 -0.499760 0.866164 0.000001 112.93201 1 MTRIX2 6 -0.866164 -0.499760 0.000000 421.70219 1 MTRIX3 6 0.000001 0.000000 1.000000 -0.00006 1 MTRIX1 7 -0.500119 0.865956 0.000000 113.03318 1 MTRIX2 7 -0.865956 -0.500119 0.000000 421.72934 1 MTRIX3 7 0.000000 0.000000 1.000000 -0.00009 1 MTRIX1 8 -0.499761 -0.866163 0.000001 421.70233 1 MTRIX2 8 0.866163 -0.499761 0.000000 112.93249 1 MTRIX3 8 0.000000 0.000000 1.000000 -0.00014 1 MTRIX1 9 -0.500119 -0.865957 0.000000 421.72936 1 MTRIX2 9 0.865957 -0.500119 0.000000 113.03310 1 MTRIX3 9 0.000000 0.000000 1.000000 0.00002 1 MTRIX1 10 -0.500119 0.865957 -0.000001 113.03328 1 MTRIX2 10 -0.865957 -0.500119 0.000000 421.72941 1 MTRIX3 10 -0.000001 0.000001 1.000000 0.00004 1