HEADER VIRAL PROTEIN/IMMUNE SYSTEM 19-NOV-21 7SWD TITLE STRUCTURE OF EBOV GP LACKING THE MUCIN-LIKE DOMAIN WITH 1C11 SCFV AND TITLE 2 1C3 FAB BOUND COMPND MOL_ID: 1; COMPND 2 MOLECULE: SMALL/SECRETED GLYCOPROTEIN; COMPND 3 CHAIN: A, C, E; COMPND 4 SYNONYM: SGP; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: VIRION SPIKE GLYCOPROTEIN; COMPND 8 CHAIN: B, D, F; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: 1C11 SCFV; COMPND 12 CHAIN: G, H, I; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: 1C3 HEAVY CHAIN; COMPND 16 CHAIN: J; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 5; COMPND 19 MOLECULE: 1C3 LIGHT CHAIN; COMPND 20 CHAIN: K; COMPND 21 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ZAIRE EBOLAVIRUS (STRAIN GABON-94); SOURCE 3 ORGANISM_COMMON: ZEBOV, ZAIRE EBOLA VIRUS; SOURCE 4 ORGANISM_TAXID: 128947; SOURCE 5 STRAIN: GABON-94; SOURCE 6 GENE: GP; SOURCE 7 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: ZAIRE EBOLAVIRUS; SOURCE 11 ORGANISM_TAXID: 186538; SOURCE 12 GENE: GP; SOURCE 13 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 25 MOL_ID: 5; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_TAXID: 9606; SOURCE 28 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS VIRAL PROTEIN, GLYCOPROTEIN, IMMUNE SYSTEM, ANTIBODY, EBOLA VIRUS, KEYWDS 2 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR J.C.MILLIGAN,X.YU,E.O.SAPHIRE REVDAT 1 06-APR-22 7SWD 0 JRNL AUTH J.C.MILLIGAN,C.W.DAVIS,X.YU,P.A.ILINYKH,K.HUANG, JRNL AUTH 2 P.J.HALFMANN,R.W.CROSS,V.BORISEVICH,K.N.AGANS,J.B.GEISBERT, JRNL AUTH 3 C.CHENNAREDDY,A.J.GOFF,A.E.PIPER,S.HUI,K.C.L.SHAFFER,T.BUCK, JRNL AUTH 4 M.L.HEINRICH,L.M.BRANCO,I.CROZIER,M.R.HOLBROOK,J.H.KUHN, JRNL AUTH 5 Y.KAWAOKA,P.J.GLASS,A.BUKREYEV,T.W.GEISBERT,G.WORWA,R.AHMED, JRNL AUTH 6 E.O.SAPHIRE JRNL TITL ASYMMETRIC AND NON-STOICHIOMETRIC GLYCOPROTEIN RECOGNITION JRNL TITL 2 BY TWO DISTINCT ANTIBODIES RESULTS IN BROAD PROTECTION JRNL TITL 3 AGAINST EBOLAVIRUSES. JRNL REF CELL V. 185 995 2022 JRNL REFN ISSN 1097-4172 JRNL PMID 35303429 JRNL DOI 10.1016/J.CELL.2022.02.023 REMARK 2 REMARK 2 RESOLUTION. 3.59 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION, RELION, RELION 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) : 3.590 REMARK 3 NUMBER OF PARTICLES : 75948 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 7SWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-21. REMARK 100 THE DEPOSITION ID IS D_1000261193. 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 : COMPLEX OF EBOV GP LACKING THE REMARK 245 MUCIN-LIKE-DOMAIN WITH 1C11 REMARK 245 SCFV AND 1C3 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 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 : FEI TITAN REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL 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) : 3497.00 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: UNDECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, M, N, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A 47 REMARK 465 VAL A 48 REMARK 465 ASP A 49 REMARK 465 LYS A 50 REMARK 465 LEU A 51 REMARK 465 ASP C 47 REMARK 465 VAL C 48 REMARK 465 ASP C 49 REMARK 465 LYS C 50 REMARK 465 LEU C 51 REMARK 465 HIS E 39 REMARK 465 ASN E 40 REMARK 465 SER E 41 REMARK 465 ASP E 47 REMARK 465 VAL E 48 REMARK 465 ASP E 49 REMARK 465 LYS E 50 REMARK 465 LEU E 51 REMARK 465 GLN E 188 REMARK 465 GLN G 1 REMARK 465 VAL G 119 REMARK 465 SER G 120 REMARK 465 SER G 121 REMARK 465 GLY G 122 REMARK 465 THR G 123 REMARK 465 GLY G 124 REMARK 465 GLY G 125 REMARK 465 SER G 126 REMARK 465 GLY G 127 REMARK 465 GLY G 128 REMARK 465 GLY G 129 REMARK 465 GLY G 130 REMARK 465 SER G 131 REMARK 465 GLY G 132 REMARK 465 GLY G 133 REMARK 465 GLY G 134 REMARK 465 GLY G 135 REMARK 465 SER G 136 REMARK 465 GLY G 137 REMARK 465 GLY G 138 REMARK 465 GLY G 139 REMARK 465 ALA G 140 REMARK 465 SER G 141 REMARK 465 GLU G 251 REMARK 465 ILE G 252 REMARK 465 LYS G 253 REMARK 465 GLN H 1 REMARK 465 VAL H 119 REMARK 465 SER H 120 REMARK 465 SER H 121 REMARK 465 GLY H 122 REMARK 465 THR H 123 REMARK 465 GLY H 124 REMARK 465 GLY H 125 REMARK 465 SER H 126 REMARK 465 GLY H 127 REMARK 465 GLY H 128 REMARK 465 GLY H 129 REMARK 465 GLY H 130 REMARK 465 SER H 131 REMARK 465 GLY H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 GLY H 135 REMARK 465 SER H 136 REMARK 465 GLY H 137 REMARK 465 GLY H 138 REMARK 465 GLY H 139 REMARK 465 ALA H 140 REMARK 465 SER H 141 REMARK 465 GLU H 251 REMARK 465 ILE H 252 REMARK 465 LYS H 253 REMARK 465 GLN I 1 REMARK 465 VAL I 119 REMARK 465 SER I 120 REMARK 465 SER I 121 REMARK 465 GLY I 122 REMARK 465 THR I 123 REMARK 465 GLY I 124 REMARK 465 GLY I 125 REMARK 465 SER I 126 REMARK 465 GLY I 127 REMARK 465 GLY I 128 REMARK 465 GLY I 129 REMARK 465 GLY I 130 REMARK 465 SER I 131 REMARK 465 GLY I 132 REMARK 465 GLY I 133 REMARK 465 GLY I 134 REMARK 465 GLY I 135 REMARK 465 SER I 136 REMARK 465 GLY I 137 REMARK 465 GLY I 138 REMARK 465 GLY I 139 REMARK 465 ALA I 140 REMARK 465 SER I 141 REMARK 465 GLN J 1 REMARK 465 VAL J 2 REMARK 465 SER J 124 REMARK 465 ARG K 114 REMARK 465 THR K 115 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 O6 NAG N 1 O7 NAG N 2 2.12 REMARK 500 OG1 THR G 70 OE2 GLU G 83 2.13 REMARK 500 OE1 GLU E 156 O3 NAG N 1 2.17 REMARK 500 OH TYR I 195 O4 BMA M 3 2.17 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 HIS A 39 -68.46 -94.01 REMARK 500 ASN A 40 -50.61 -126.88 REMARK 500 SER A 41 12.52 -140.42 REMARK 500 TYR A 162 -153.52 56.74 REMARK 500 ARG A 164 16.89 57.08 REMARK 500 LEU B 529 -124.12 53.32 REMARK 500 ASP C 163 -111.40 55.80 REMARK 500 GLU D 523 -7.17 68.04 REMARK 500 ALA D 525 -111.34 45.39 REMARK 500 LEU D 529 -112.23 49.23 REMARK 500 ALA D 538 -167.38 -79.26 REMARK 500 CYS D 556 -2.76 71.67 REMARK 500 TYR E 162 -148.16 56.70 REMARK 500 GLU F 523 -6.40 70.98 REMARK 500 ALA F 526 40.85 -104.82 REMARK 500 LEU F 529 -111.63 52.37 REMARK 500 ASN F 550 -60.59 -95.89 REMARK 500 SER G 7 -178.87 -69.08 REMARK 500 GLU G 10 73.83 -100.25 REMARK 500 ASP G 67 12.67 49.80 REMARK 500 ALA G 93 -167.65 -165.86 REMARK 500 LEU G 150 -8.45 70.10 REMARK 500 SER G 151 138.02 -173.25 REMARK 500 LEU G 193 -62.04 -101.80 REMARK 500 PRO I 53 49.90 -71.95 REMARK 500 ASP I 67 -4.34 71.86 REMARK 500 SER I 115 112.20 -160.56 REMARK 500 PRO I 159 157.27 -49.39 REMARK 500 ASP I 206 2.43 -69.53 REMARK 500 ASN J 103 2.22 59.28 REMARK 500 LYS J 105 24.05 -142.18 REMARK 500 TRP K 56 19.99 57.16 REMARK 500 ALA K 57 -8.61 64.72 REMARK 500 ALA K 90 -175.15 -173.94 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-25471 RELATED DB: EMDB REMARK 900 STRUCTURE OF EBOV GP LACKING THE MUCIN-LIKE DOMAIN WITH 1C11 SCFV REMARK 900 AND 1C3 FAB BOUND DBREF 7SWD A 33 188 UNP O11458 VSGP_EBOG4 33 188 DBREF1 7SWD B 504 599 UNP A0A7S6GAH2_9MONO DBREF2 7SWD B A0A7S6GAH2 504 599 DBREF 7SWD C 33 188 UNP O11458 VSGP_EBOG4 33 188 DBREF1 7SWD D 504 599 UNP A0A7S6GAH2_9MONO DBREF2 7SWD D A0A7S6GAH2 504 599 DBREF 7SWD E 33 188 UNP O11458 VSGP_EBOG4 33 188 DBREF1 7SWD F 504 599 UNP A0A7S6GAH2_9MONO DBREF2 7SWD F A0A7S6GAH2 504 599 DBREF 7SWD G 1 253 PDB 7SWD 7SWD 1 253 DBREF 7SWD H 1 253 PDB 7SWD 7SWD 1 253 DBREF 7SWD I 1 253 PDB 7SWD 7SWD 1 253 DBREF 7SWD J 1 124 PDB 7SWD 7SWD 1 124 DBREF 7SWD K 1 115 PDB 7SWD 7SWD 1 115 SEQRES 1 A 156 ILE PRO LEU GLY VAL ILE HIS ASN SER THR LEU GLN VAL SEQRES 2 A 156 SER ASP VAL ASP LYS LEU VAL CYS ARG ASP LYS LEU SER SEQRES 3 A 156 SER THR ASN GLN LEU ARG SER VAL GLY LEU ASN LEU GLU SEQRES 4 A 156 GLY ASN GLY VAL ALA THR ASP VAL PRO SER ALA THR LYS SEQRES 5 A 156 ARG TRP GLY PHE ARG SER GLY VAL PRO PRO LYS VAL VAL SEQRES 6 A 156 ASN TYR GLU ALA GLY GLU TRP ALA GLU ASN CYS TYR ASN SEQRES 7 A 156 LEU GLU ILE LYS LYS PRO ASP GLY SER GLU CYS LEU PRO SEQRES 8 A 156 ALA ALA PRO ASP GLY ILE ARG GLY PHE PRO ARG CYS ARG SEQRES 9 A 156 TYR VAL HIS LYS VAL SER GLY THR GLY PRO CYS ALA GLY SEQRES 10 A 156 ASP PHE ALA PHE HIS LYS GLU GLY ALA PHE PHE LEU TYR SEQRES 11 A 156 ASP ARG LEU ALA SER THR VAL ILE TYR ARG GLY THR THR SEQRES 12 A 156 PHE ALA GLU GLY VAL VAL ALA PHE LEU ILE LEU PRO GLN SEQRES 1 B 96 ILE VAL ASN ALA GLN PRO LYS CYS ASN PRO ASN LEU HIS SEQRES 2 B 96 TYR TRP THR THR GLN ASP GLU GLY ALA ALA ILE GLY LEU SEQRES 3 B 96 ALA TRP ILE PRO TYR PHE GLY PRO ALA ALA GLU GLY ILE SEQRES 4 B 96 TYR THR GLU GLY LEU MET HIS ASN GLN ASP GLY LEU ILE SEQRES 5 B 96 CYS GLY LEU ARG GLN LEU ALA ASN GLU THR THR GLN ALA SEQRES 6 B 96 LEU GLN LEU PHE LEU ARG ALA THR THR GLU LEU ARG THR SEQRES 7 B 96 PHE SER ILE LEU ASN ARG LYS ALA ILE ASP PHE LEU LEU SEQRES 8 B 96 GLN ARG TRP GLY GLY SEQRES 1 C 156 ILE PRO LEU GLY VAL ILE HIS ASN SER THR LEU GLN VAL SEQRES 2 C 156 SER ASP VAL ASP LYS LEU VAL CYS ARG ASP LYS LEU SER SEQRES 3 C 156 SER THR ASN GLN LEU ARG SER VAL GLY LEU ASN LEU GLU SEQRES 4 C 156 GLY ASN GLY VAL ALA THR ASP VAL PRO SER ALA THR LYS SEQRES 5 C 156 ARG TRP GLY PHE ARG SER GLY VAL PRO PRO LYS VAL VAL SEQRES 6 C 156 ASN TYR GLU ALA GLY GLU TRP ALA GLU ASN CYS TYR ASN SEQRES 7 C 156 LEU GLU ILE LYS LYS PRO ASP GLY SER GLU CYS LEU PRO SEQRES 8 C 156 ALA ALA PRO ASP GLY ILE ARG GLY PHE PRO ARG CYS ARG SEQRES 9 C 156 TYR VAL HIS LYS VAL SER GLY THR GLY PRO CYS ALA GLY SEQRES 10 C 156 ASP PHE ALA PHE HIS LYS GLU GLY ALA PHE PHE LEU TYR SEQRES 11 C 156 ASP ARG LEU ALA SER THR VAL ILE TYR ARG GLY THR THR SEQRES 12 C 156 PHE ALA GLU GLY VAL VAL ALA PHE LEU ILE LEU PRO GLN SEQRES 1 D 96 ILE VAL ASN ALA GLN PRO LYS CYS ASN PRO ASN LEU HIS SEQRES 2 D 96 TYR TRP THR THR GLN ASP GLU GLY ALA ALA ILE GLY LEU SEQRES 3 D 96 ALA TRP ILE PRO TYR PHE GLY PRO ALA ALA GLU GLY ILE SEQRES 4 D 96 TYR THR GLU GLY LEU MET HIS ASN GLN ASP GLY LEU ILE SEQRES 5 D 96 CYS GLY LEU ARG GLN LEU ALA ASN GLU THR THR GLN ALA SEQRES 6 D 96 LEU GLN LEU PHE LEU ARG ALA THR THR GLU LEU ARG THR SEQRES 7 D 96 PHE SER ILE LEU ASN ARG LYS ALA ILE ASP PHE LEU LEU SEQRES 8 D 96 GLN ARG TRP GLY GLY SEQRES 1 E 156 ILE PRO LEU GLY VAL ILE HIS ASN SER THR LEU GLN VAL SEQRES 2 E 156 SER ASP VAL ASP LYS LEU VAL CYS ARG ASP LYS LEU SER SEQRES 3 E 156 SER THR ASN GLN LEU ARG SER VAL GLY LEU ASN LEU GLU SEQRES 4 E 156 GLY ASN GLY VAL ALA THR ASP VAL PRO SER ALA THR LYS SEQRES 5 E 156 ARG TRP GLY PHE ARG SER GLY VAL PRO PRO LYS VAL VAL SEQRES 6 E 156 ASN TYR GLU ALA GLY GLU TRP ALA GLU ASN CYS TYR ASN SEQRES 7 E 156 LEU GLU ILE LYS LYS PRO ASP GLY SER GLU CYS LEU PRO SEQRES 8 E 156 ALA ALA PRO ASP GLY ILE ARG GLY PHE PRO ARG CYS ARG SEQRES 9 E 156 TYR VAL HIS LYS VAL SER GLY THR GLY PRO CYS ALA GLY SEQRES 10 E 156 ASP PHE ALA PHE HIS LYS GLU GLY ALA PHE PHE LEU TYR SEQRES 11 E 156 ASP ARG LEU ALA SER THR VAL ILE TYR ARG GLY THR THR SEQRES 12 E 156 PHE ALA GLU GLY VAL VAL ALA PHE LEU ILE LEU PRO GLN SEQRES 1 F 96 ILE VAL ASN ALA GLN PRO LYS CYS ASN PRO ASN LEU HIS SEQRES 2 F 96 TYR TRP THR THR GLN ASP GLU GLY ALA ALA ILE GLY LEU SEQRES 3 F 96 ALA TRP ILE PRO TYR PHE GLY PRO ALA ALA GLU GLY ILE SEQRES 4 F 96 TYR THR GLU GLY LEU MET HIS ASN GLN ASP GLY LEU ILE SEQRES 5 F 96 CYS GLY LEU ARG GLN LEU ALA ASN GLU THR THR GLN ALA SEQRES 6 F 96 LEU GLN LEU PHE LEU ARG ALA THR THR GLU LEU ARG THR SEQRES 7 F 96 PHE SER ILE LEU ASN ARG LYS ALA ILE ASP PHE LEU LEU SEQRES 8 F 96 GLN ARG TRP GLY GLY SEQRES 1 G 253 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 G 253 PRO GLY ALA SER VAL LYS VAL SER CYS ARG THR SER GLY SEQRES 3 G 253 TYR THR PHE SER SER TYR ASN ILE HIS TRP VAL ARG GLN SEQRES 4 G 253 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY VAL ILE ASN SEQRES 5 G 253 PRO TYR GLY ARG SER THR THR LEU TYR ALA ARG ARG PHE SEQRES 6 G 253 ARG ASP ARG VAL THR MET THR ARG ASP THR SER THR SER SEQRES 7 G 253 THR VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP SEQRES 8 G 253 THR ALA VAL TYR PHE CYS GLY ARG LEU TYR SER GLY ALA SEQRES 9 G 253 PRO TYR GLY LEU ASP VAL TRP GLY GLN GLY SER THR VAL SEQRES 10 G 253 THR VAL SER SER GLY THR GLY GLY SER GLY GLY GLY GLY SEQRES 11 G 253 SER GLY GLY GLY GLY SER GLY GLY GLY ALA SER ASP ILE SEQRES 12 G 253 VAL MET THR GLN SER PRO LEU SER LEU PRO VAL THR PRO SEQRES 13 G 253 GLY GLU PRO ALA SER ILE SER CYS ARG SER SER GLN SER SEQRES 14 G 253 LEU LEU HIS SER ASN GLY TYR ASN TYR VAL ASP TRP TYR SEQRES 15 G 253 LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU ILE TYR SEQRES 16 G 253 LEU GLY SER SER ARG ALA SER GLY VAL PRO ASP ARG PHE SEQRES 17 G 253 SER GLY SER GLY SER GLY THR ASP PHE THR LEU LYS ILE SEQRES 18 G 253 SER ARG VAL GLU THR GLU ASP VAL GLY ILE TYR TYR CYS SEQRES 19 G 253 MET GLN GLY LEU GLN THR PRO LEU THR PHE GLY GLY GLY SEQRES 20 G 253 THR LYS VAL GLU ILE LYS SEQRES 1 H 253 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 253 PRO GLY ALA SER VAL LYS VAL SER CYS ARG THR SER GLY SEQRES 3 H 253 TYR THR PHE SER SER TYR ASN ILE HIS TRP VAL ARG GLN SEQRES 4 H 253 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY VAL ILE ASN SEQRES 5 H 253 PRO TYR GLY ARG SER THR THR LEU TYR ALA ARG ARG PHE SEQRES 6 H 253 ARG ASP ARG VAL THR MET THR ARG ASP THR SER THR SER SEQRES 7 H 253 THR VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP SEQRES 8 H 253 THR ALA VAL TYR PHE CYS GLY ARG LEU TYR SER GLY ALA SEQRES 9 H 253 PRO TYR GLY LEU ASP VAL TRP GLY GLN GLY SER THR VAL SEQRES 10 H 253 THR VAL SER SER GLY THR GLY GLY SER GLY GLY GLY GLY SEQRES 11 H 253 SER GLY GLY GLY GLY SER GLY GLY GLY ALA SER ASP ILE SEQRES 12 H 253 VAL MET THR GLN SER PRO LEU SER LEU PRO VAL THR PRO SEQRES 13 H 253 GLY GLU PRO ALA SER ILE SER CYS ARG SER SER GLN SER SEQRES 14 H 253 LEU LEU HIS SER ASN GLY TYR ASN TYR VAL ASP TRP TYR SEQRES 15 H 253 LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU ILE TYR SEQRES 16 H 253 LEU GLY SER SER ARG ALA SER GLY VAL PRO ASP ARG PHE SEQRES 17 H 253 SER GLY SER GLY SER GLY THR ASP PHE THR LEU LYS ILE SEQRES 18 H 253 SER ARG VAL GLU THR GLU ASP VAL GLY ILE TYR TYR CYS SEQRES 19 H 253 MET GLN GLY LEU GLN THR PRO LEU THR PHE GLY GLY GLY SEQRES 20 H 253 THR LYS VAL GLU ILE LYS SEQRES 1 I 253 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 I 253 PRO GLY ALA SER VAL LYS VAL SER CYS ARG THR SER GLY SEQRES 3 I 253 TYR THR PHE SER SER TYR ASN ILE HIS TRP VAL ARG GLN SEQRES 4 I 253 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY VAL ILE ASN SEQRES 5 I 253 PRO TYR GLY ARG SER THR THR LEU TYR ALA ARG ARG PHE SEQRES 6 I 253 ARG ASP ARG VAL THR MET THR ARG ASP THR SER THR SER SEQRES 7 I 253 THR VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP SEQRES 8 I 253 THR ALA VAL TYR PHE CYS GLY ARG LEU TYR SER GLY ALA SEQRES 9 I 253 PRO TYR GLY LEU ASP VAL TRP GLY GLN GLY SER THR VAL SEQRES 10 I 253 THR VAL SER SER GLY THR GLY GLY SER GLY GLY GLY GLY SEQRES 11 I 253 SER GLY GLY GLY GLY SER GLY GLY GLY ALA SER ASP ILE SEQRES 12 I 253 VAL MET THR GLN SER PRO LEU SER LEU PRO VAL THR PRO SEQRES 13 I 253 GLY GLU PRO ALA SER ILE SER CYS ARG SER SER GLN SER SEQRES 14 I 253 LEU LEU HIS SER ASN GLY TYR ASN TYR VAL ASP TRP TYR SEQRES 15 I 253 LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU ILE TYR SEQRES 16 I 253 LEU GLY SER SER ARG ALA SER GLY VAL PRO ASP ARG PHE SEQRES 17 I 253 SER GLY SER GLY SER GLY THR ASP PHE THR LEU LYS ILE SEQRES 18 I 253 SER ARG VAL GLU THR GLU ASP VAL GLY ILE TYR TYR CYS SEQRES 19 I 253 MET GLN GLY LEU GLN THR PRO LEU THR PHE GLY GLY GLY SEQRES 20 I 253 THR LYS VAL GLU ILE LYS SEQRES 1 J 124 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 J 124 PRO GLY SER SER VAL LYS VAL ALA CYS LYS VAL SER GLY SEQRES 3 J 124 GLY THR PHE SER SER TYR THR ILE SER TRP VAL ARG GLN SEQRES 4 J 124 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 J 124 PRO SER PHE GLY VAL GLY HIS TYR SER GLN LYS PHE ARG SEQRES 6 J 124 ASP ARG VAL THR LEU THR ALA ASP LYS SER THR THR THR SEQRES 7 J 124 ALA PHE LEU GLU LEU SER SER VAL ARG SER GLU ASP THR SEQRES 8 J 124 ALA LEU TYR TYR CYS ALA ILE LEU GLY THR PHE ASN TRP SEQRES 9 J 124 LYS SER GLY GLY ASN TYR PHE GLY PRO TRP GLY GLN GLY SEQRES 10 J 124 THR LEU VAL THR VAL SER SER SEQRES 1 K 115 ASP ILE VAL LEU THR GLN SER PRO ASP SER LEU ALA ALA SEQRES 2 K 115 SER LEU GLY GLU ARG ALA THR ILE SER CYS LYS SER SER SEQRES 3 K 115 HIS SER VAL LEU TYR SER SER ASN ASN LYS ASP PHE PHE SEQRES 4 K 115 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 K 115 LEU ILE SER TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 K 115 VAL ARG PHE ASN GLY GLY GLY SER GLY THR HIS PHE THR SEQRES 7 K 115 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 K 115 TYR TYR CYS GLN GLN TYR PHE SER SER PRO ILE THR PHE SEQRES 9 K 115 GLY GLN GLY THR ARG LEU GLU ILE LYS ARG THR HET NAG M 1 14 HET NAG M 2 14 HET BMA M 3 11 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET NAG L 1 14 HET NAG L 2 14 HET BMA L 3 11 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-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 FORMUL 12 NAG 6(C8 H15 N O6) FORMUL 12 BMA 3(C6 H12 O6) HELIX 1 AA1 SER A 59 ASN A 61 5 3 HELIX 2 AA2 GLU A 71 ASN A 73 5 3 HELIX 3 AA3 ASP A 78 LYS A 84 1 7 HELIX 4 AA4 ASP B 522 ILE B 527 5 6 HELIX 5 AA5 ILE B 532 GLY B 536 5 5 HELIX 6 AA6 GLN B 551 THR B 576 1 26 HELIX 7 AA7 SER B 583 GLY B 598 1 16 HELIX 8 AA8 SER C 59 ASN C 61 5 3 HELIX 9 AA9 GLU C 71 GLY C 74 5 4 HELIX 10 AB1 ASP C 78 LYS C 84 1 7 HELIX 11 AB2 GLY D 557 THR D 576 1 20 HELIX 12 AB3 SER D 583 TRP D 597 1 15 HELIX 13 AB4 SER E 59 ASN E 61 5 3 HELIX 14 AB5 ASP E 78 THR E 83 1 6 HELIX 15 AB6 GLN F 551 THR F 576 1 26 HELIX 16 AB7 ILE F 584 GLY F 598 1 15 HELIX 17 AB8 ARG G 88 THR G 92 5 5 HELIX 18 AB9 ARG H 63 ARG H 66 5 4 HELIX 19 AC1 ARG H 88 THR H 92 5 5 HELIX 20 AC2 GLU H 225 VAL H 229 5 5 HELIX 21 AC3 ARG I 63 ARG I 66 5 4 HELIX 22 AC4 ARG I 88 THR I 92 5 5 HELIX 23 AC5 ARG J 87 THR J 91 5 5 SHEET 1 AA1 2 GLY A 36 ILE A 38 0 SHEET 2 AA1 2 LEU A 43 VAL A 45 -1 O GLN A 44 N VAL A 37 SHEET 1 AA2 6 PHE A 159 PHE A 160 0 SHEET 2 AA2 6 GLU A 178 ILE A 185 -1 O GLY A 179 N PHE A 159 SHEET 3 AA2 6 LEU A 63 ASN A 69 -1 N VAL A 66 O ALA A 182 SHEET 4 AA2 6 ALA A 101 GLU A 103 1 O ALA A 101 N GLY A 67 SHEET 5 AA2 6 HIS B 516 THR B 519 -1 O TRP B 518 N GLY A 102 SHEET 6 AA2 6 THR B 544 LEU B 547 -1 O THR B 544 N THR B 519 SHEET 1 AA3 2 TRP A 86 ARG A 89 0 SHEET 2 AA3 2 PHE A 151 HIS A 154 -1 O PHE A 153 N GLY A 87 SHEET 1 AA4 3 LEU A 165 SER A 167 0 SHEET 2 AA4 3 VAL A 96 ASN A 98 -1 N VAL A 97 O ALA A 166 SHEET 3 AA4 3 ARG B 580 THR B 581 1 O THR B 581 N VAL A 96 SHEET 1 AA5 3 CYS A 135 HIS A 139 0 SHEET 2 AA5 3 ALA A 105 ASN A 110 1 N ASN A 110 O HIS A 139 SHEET 3 AA5 3 THR A 175 PHE A 176 -1 O PHE A 176 N TYR A 109 SHEET 1 AA6 2 GLY C 36 ILE C 38 0 SHEET 2 AA6 2 LEU C 43 VAL C 45 -1 O GLN C 44 N VAL C 37 SHEET 1 AA7 4 LEU C 63 ASN C 69 0 SHEET 2 AA7 4 THR C 175 ILE C 185 -1 O ALA C 182 N VAL C 66 SHEET 3 AA7 4 ALA C 105 ILE C 113 -1 N TYR C 109 O PHE C 176 SHEET 4 AA7 4 CYS C 135 GLY C 143 1 O HIS C 139 N ASN C 110 SHEET 1 AA8 6 LEU C 63 ASN C 69 0 SHEET 2 AA8 6 THR C 175 ILE C 185 -1 O ALA C 182 N VAL C 66 SHEET 3 AA8 6 PHE C 159 TYR C 162 -1 N PHE C 159 O GLY C 179 SHEET 4 AA8 6 LEU C 165 SER C 167 -1 O SER C 167 N PHE C 160 SHEET 5 AA8 6 VAL C 96 ASN C 98 -1 N VAL C 97 O ALA C 166 SHEET 6 AA8 6 ARG D 580 THR D 581 1 O THR D 581 N VAL C 96 SHEET 1 AA9 2 TRP C 86 ARG C 89 0 SHEET 2 AA9 2 PHE C 151 HIS C 154 -1 O PHE C 153 N GLY C 87 SHEET 1 AB1 3 ALA C 101 GLU C 103 0 SHEET 2 AB1 3 LEU D 515 THR D 519 -1 O TRP D 518 N GLY C 102 SHEET 3 AB1 3 THR D 544 MET D 548 -1 O THR D 544 N THR D 519 SHEET 1 AB2 6 PHE E 159 PHE E 160 0 SHEET 2 AB2 6 GLU E 178 ILE E 185 -1 O GLY E 179 N PHE E 159 SHEET 3 AB2 6 LEU E 63 ASN E 69 -1 N ARG E 64 O LEU E 184 SHEET 4 AB2 6 ALA E 101 GLU E 103 1 O ALA E 101 N GLY E 67 SHEET 5 AB2 6 HIS F 516 THR F 519 -1 O TRP F 518 N GLY E 102 SHEET 6 AB2 6 THR F 544 LEU F 547 -1 O THR F 544 N THR F 519 SHEET 1 AB3 2 TRP E 86 ARG E 89 0 SHEET 2 AB3 2 PHE E 151 HIS E 154 -1 O PHE E 151 N ARG E 89 SHEET 1 AB4 3 ALA E 166 SER E 167 0 SHEET 2 AB4 3 VAL E 96 VAL E 97 -1 N VAL E 97 O ALA E 166 SHEET 3 AB4 3 ARG F 580 THR F 581 1 O THR F 581 N VAL E 96 SHEET 1 AB5 2 CYS E 108 LEU E 111 0 SHEET 2 AB5 2 VAL E 138 VAL E 141 1 O HIS E 139 N CYS E 108 SHEET 1 AB6 6 GLU G 10 VAL G 11 0 SHEET 2 AB6 6 GLY G 114 VAL G 117 1 O SER G 115 N GLU G 10 SHEET 3 AB6 6 ALA G 93 LEU G 100 -1 N ALA G 93 O THR G 116 SHEET 4 AB6 6 ASN G 33 GLN G 39 -1 N VAL G 37 O PHE G 96 SHEET 5 AB6 6 LEU G 45 ILE G 51 -1 O GLU G 46 N ARG G 38 SHEET 6 AB6 6 THR G 59 TYR G 61 -1 O LEU G 60 N VAL G 50 SHEET 1 AB7 3 VAL G 18 ARG G 23 0 SHEET 2 AB7 3 THR G 79 LEU G 84 -1 O MET G 82 N VAL G 20 SHEET 3 AB7 3 VAL G 69 ASP G 74 -1 N THR G 72 O TYR G 81 SHEET 1 AB8 4 MET G 145 GLN G 147 0 SHEET 2 AB8 4 GLU G 158 SER G 166 -1 O ARG G 165 N THR G 146 SHEET 3 AB8 4 ASP G 216 VAL G 224 -1 O VAL G 224 N GLU G 158 SHEET 4 AB8 4 PHE G 208 SER G 213 -1 N SER G 211 O THR G 218 SHEET 1 AB9 5 SER G 199 ARG G 200 0 SHEET 2 AB9 5 GLN G 191 TYR G 195 -1 N TYR G 195 O SER G 199 SHEET 3 AB9 5 VAL G 179 GLN G 184 -1 N LEU G 183 O GLN G 191 SHEET 4 AB9 5 GLY G 230 GLN G 236 -1 O TYR G 233 N TYR G 182 SHEET 5 AB9 5 THR G 248 VAL G 250 -1 O VAL G 250 N GLY G 230 SHEET 1 AC1 4 VAL H 5 GLN H 6 0 SHEET 2 AC1 4 SER H 17 ARG H 23 -1 O ARG H 23 N VAL H 5 SHEET 3 AC1 4 THR H 79 SER H 85 -1 O MET H 82 N VAL H 20 SHEET 4 AC1 4 VAL H 69 ASP H 74 -1 N THR H 72 O TYR H 81 SHEET 1 AC2 6 GLU H 10 VAL H 11 0 SHEET 2 AC2 6 GLY H 114 VAL H 117 1 O VAL H 117 N GLU H 10 SHEET 3 AC2 6 VAL H 94 CYS H 97 -1 N TYR H 95 O GLY H 114 SHEET 4 AC2 6 TYR H 32 GLN H 39 -1 N GLN H 39 O VAL H 94 SHEET 5 AC2 6 GLU H 46 ASN H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AC2 6 THR H 58 TYR H 61 -1 O LEU H 60 N VAL H 50 SHEET 1 AC3 5 GLU H 10 VAL H 11 0 SHEET 2 AC3 5 GLY H 114 VAL H 117 1 O VAL H 117 N GLU H 10 SHEET 3 AC3 5 VAL H 94 CYS H 97 -1 N TYR H 95 O GLY H 114 SHEET 4 AC3 5 TYR H 32 GLN H 39 -1 N GLN H 39 O VAL H 94 SHEET 5 AC3 5 LEU H 100 TYR H 101 -1 O LEU H 100 N ASN H 33 SHEET 1 AC4 4 MET H 145 GLN H 147 0 SHEET 2 AC4 4 ALA H 160 SER H 166 -1 O ARG H 165 N THR H 146 SHEET 3 AC4 4 ASP H 216 ILE H 221 -1 O PHE H 217 N CYS H 164 SHEET 4 AC4 4 PHE H 208 GLY H 212 -1 N SER H 211 O THR H 218 SHEET 1 AC5 5 SER H 199 ARG H 200 0 SHEET 2 AC5 5 PRO H 190 TYR H 195 -1 N TYR H 195 O SER H 199 SHEET 3 AC5 5 ASP H 180 GLN H 184 -1 N LEU H 183 O GLN H 191 SHEET 4 AC5 5 GLY H 230 MET H 235 -1 O ILE H 231 N GLN H 184 SHEET 5 AC5 5 THR H 248 VAL H 250 -1 O VAL H 250 N GLY H 230 SHEET 1 AC6 4 GLN I 3 GLN I 6 0 SHEET 2 AC6 4 LYS I 19 SER I 25 -1 O ARG I 23 N VAL I 5 SHEET 3 AC6 4 THR I 79 GLU I 83 -1 O VAL I 80 N CYS I 22 SHEET 4 AC6 4 THR I 70 ASP I 74 -1 N ASP I 74 O THR I 79 SHEET 1 AC7 2 GLU I 10 VAL I 11 0 SHEET 2 AC7 2 THR I 116 VAL I 117 1 O VAL I 117 N GLU I 10 SHEET 1 AC8 5 THR I 59 TYR I 61 0 SHEET 2 AC8 5 LEU I 45 ILE I 51 -1 N VAL I 50 O LEU I 60 SHEET 3 AC8 5 TYR I 32 GLN I 39 -1 N ARG I 38 O GLU I 46 SHEET 4 AC8 5 VAL I 94 TYR I 101 -1 O PHE I 96 N VAL I 37 SHEET 5 AC8 5 VAL I 110 TRP I 111 -1 O VAL I 110 N ARG I 99 SHEET 1 AC9 4 MET I 145 GLN I 147 0 SHEET 2 AC9 4 ALA I 160 SER I 166 -1 O ARG I 165 N THR I 146 SHEET 3 AC9 4 ASP I 216 ILE I 221 -1 O ILE I 221 N ALA I 160 SHEET 4 AC9 4 SER I 209 GLY I 212 -1 N SER I 209 O LYS I 220 SHEET 1 AD1 5 SER I 199 ARG I 200 0 SHEET 2 AD1 5 PRO I 190 TYR I 195 -1 N TYR I 195 O SER I 199 SHEET 3 AD1 5 VAL I 179 GLN I 184 -1 N LEU I 183 O GLN I 191 SHEET 4 AD1 5 GLY I 230 GLN I 236 -1 O ILE I 231 N GLN I 184 SHEET 5 AD1 5 THR I 248 VAL I 250 -1 O VAL I 250 N GLY I 230 SHEET 1 AD2 4 LEU J 4 GLN J 6 0 SHEET 2 AD2 4 LYS J 19 VAL J 24 -1 O LYS J 23 N VAL J 5 SHEET 3 AD2 4 THR J 78 LEU J 83 -1 O ALA J 79 N CYS J 22 SHEET 4 AD2 4 VAL J 68 ASP J 73 -1 N ASP J 73 O THR J 78 SHEET 1 AD3 6 GLU J 10 LYS J 12 0 SHEET 2 AD3 6 THR J 118 VAL J 122 1 O THR J 121 N GLU J 10 SHEET 3 AD3 6 LEU J 93 ILE J 98 -1 N TYR J 94 O THR J 118 SHEET 4 AD3 6 ILE J 34 GLN J 39 -1 N SER J 35 O ALA J 97 SHEET 5 AD3 6 TRP J 47 ILE J 51 -1 O GLY J 49 N TRP J 36 SHEET 6 AD3 6 HIS J 59 TYR J 60 -1 O HIS J 59 N GLY J 50 SHEET 1 AD4 4 LEU K 4 GLN K 6 0 SHEET 2 AD4 4 ALA K 19 SER K 25 -1 O LYS K 24 N THR K 5 SHEET 3 AD4 4 HIS K 76 ILE K 81 -1 O ILE K 81 N ALA K 19 SHEET 4 AD4 4 PHE K 68 SER K 73 -1 N GLY K 71 O THR K 78 SHEET 1 AD5 6 ALA K 12 ALA K 13 0 SHEET 2 AD5 6 THR K 108 ILE K 112 1 O GLU K 111 N ALA K 13 SHEET 3 AD5 6 ALA K 90 GLN K 96 -1 N ALA K 90 O LEU K 110 SHEET 4 AD5 6 PHE K 39 GLN K 44 -1 N GLN K 44 O VAL K 91 SHEET 5 AD5 6 LYS K 51 SER K 55 -1 O LEU K 53 N TRP K 41 SHEET 6 AD5 6 THR K 59 ARG K 60 -1 O THR K 59 N SER K 55 SHEET 1 AD6 4 ALA K 12 ALA K 13 0 SHEET 2 AD6 4 THR K 108 ILE K 112 1 O GLU K 111 N ALA K 13 SHEET 3 AD6 4 ALA K 90 GLN K 96 -1 N ALA K 90 O LEU K 110 SHEET 4 AD6 4 THR K 103 PHE K 104 -1 O THR K 103 N GLN K 96 SSBOND 1 CYS A 108 CYS A 135 1555 1555 2.03 SSBOND 2 CYS A 121 CYS A 147 1555 1555 2.04 SSBOND 3 CYS B 511 CYS B 556 1555 1555 2.04 SSBOND 4 CYS C 108 CYS C 135 1555 1555 2.03 SSBOND 5 CYS C 121 CYS C 147 1555 1555 2.03 SSBOND 6 CYS D 511 CYS D 556 1555 1555 2.04 SSBOND 7 CYS E 108 CYS E 135 1555 1555 2.03 SSBOND 8 CYS E 121 CYS E 147 1555 1555 2.03 SSBOND 9 CYS F 511 CYS F 556 1555 1555 2.03 SSBOND 10 CYS G 22 CYS G 97 1555 1555 2.03 SSBOND 11 CYS G 164 CYS G 234 1555 1555 2.04 SSBOND 12 CYS H 22 CYS H 97 1555 1555 2.03 SSBOND 13 CYS H 164 CYS H 234 1555 1555 2.04 SSBOND 14 CYS I 22 CYS I 97 1555 1555 2.03 SSBOND 15 CYS I 164 CYS I 234 1555 1555 2.04 SSBOND 16 CYS J 22 CYS J 96 1555 1555 2.03 SSBOND 17 CYS K 23 CYS K 94 1555 1555 2.04 LINK ND2 ASN B 563 C1 NAG L 1 1555 1555 1.43 LINK ND2 ASN D 563 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN F 563 C1 NAG N 1 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.45 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.45 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44 LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.44 CISPEP 1 THR G 240 PRO G 241 0 3.47 CISPEP 2 THR H 240 PRO H 241 0 1.26 CISPEP 3 THR I 240 PRO I 241 0 2.34 CISPEP 4 SER K 100 PRO K 101 0 -1.09 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