HEADER VIRAL PROTEIN/IMMUNE SYSTEM 23-DEC-25 9ZT7 TITLE SARS-COV-2 S2 IN COMPLEX WITH COV2-2509 COMPND MOL_ID: 1; COMPND 2 MOLECULE: COV2-2509 FAB-HEAVY CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: COV2-2509 FAB-LIGHT CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SPIKE PROTEIN S2; COMPND 11 CHAIN: C, D, E; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: S, 2; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SARS-COV-2, CORONAVIRUS, IMMUNE SYSTEM, ANTIBODY, VIRAL PROTEIN, KEYWDS 2 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR S.PARK,A.B.WARD REVDAT 1 11-MAR-26 9ZT7 0 JRNL AUTH S.PARK,J.MISCHKA,N.OKBA,A.ABBAD,M.YUAN,K.SRIVASTAVA, JRNL AUTH 2 C.GLEASON,L.C.F.MULDER,J.COPPS,K.SAAM,S.BANGARU,F.KRAMMER, JRNL AUTH 3 I.A.WILSON,V.SIMON,A.B.WARD JRNL TITL THE BURIED S2 APEX OF SARS-COV-2 SPIKE ELICITS AN JRNL TITL 2 IMMUNODOMINANT GERMLINE-RESTRICTED PUBLIC ANTIBODY RESPONSE. JRNL REF BIORXIV 2026 JRNL REFN ISSN 2692-8205 JRNL PMID 41756886 JRNL DOI 10.64898/2026.02.18.706653 REMARK 2 REMARK 2 RESOLUTION. 3.11 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6XR8 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) : 3.110 REMARK 3 NUMBER OF PARTICLES : 139283 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 9ZT7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-26. REMARK 100 THE DEPOSITION ID IS D_1000302437. 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 : SARS-COV-2 S2 IN COMPLEX WITH REMARK 245 COV2-2509 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.50 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : TFS FALCON 4I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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) : 4500.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 190000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC 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 REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER C 698 REMARK 465 LEU C 699 REMARK 465 GLY C 700 REMARK 465 ALA C 701 REMARK 465 GLU C 702 REMARK 465 ASN C 703 REMARK 465 CYS C 704 REMARK 465 ASP C 843 REMARK 465 ILE C 844 REMARK 465 ALA C 845 REMARK 465 ALA C 846 REMARK 465 SER C 940 REMARK 465 THR C 941 REMARK 465 PRO C 942 REMARK 465 SER C 943 REMARK 465 GLY C 971 REMARK 465 ALA C 972 REMARK 465 ILE C 973 REMARK 465 SER C 974 REMARK 465 SER C 975 REMARK 465 VAL C 976 REMARK 465 LEU C 977 REMARK 465 ASN C 978 REMARK 465 ASP C 979 REMARK 465 ILE C 980 REMARK 465 LEU C 981 REMARK 465 SER C 982 REMARK 465 ARG C 983 REMARK 465 LEU C 984 REMARK 465 ASP C 985 REMARK 465 PRO C 986 REMARK 465 PRO C 987 REMARK 465 LEU C 1145 REMARK 465 ASP C 1146 REMARK 465 SER C 1147 REMARK 465 PHE C 1148 REMARK 465 LYS C 1149 REMARK 465 GLU C 1150 REMARK 465 GLU C 1151 REMARK 465 LEU C 1152 REMARK 465 ASP C 1153 REMARK 465 LYS C 1154 REMARK 465 TYR C 1155 REMARK 465 PHE C 1156 REMARK 465 LYS C 1157 REMARK 465 ASN C 1158 REMARK 465 HIS C 1159 REMARK 465 THR C 1160 REMARK 465 SER C 1161 REMARK 465 GLY C 1162 REMARK 465 SER C 1163 REMARK 465 HIS C 1164 REMARK 465 HIS C 1165 REMARK 465 HIS C 1166 REMARK 465 HIS C 1167 REMARK 465 HIS C 1168 REMARK 465 HIS C 1169 REMARK 465 HIS C 1170 REMARK 465 HIS C 1171 REMARK 465 SER D 698 REMARK 465 LEU D 699 REMARK 465 GLY D 700 REMARK 465 ALA D 701 REMARK 465 GLU D 702 REMARK 465 ASN D 703 REMARK 465 CYS D 704 REMARK 465 VAL D 705 REMARK 465 ALA D 706 REMARK 465 ASP D 808 REMARK 465 PRO D 809 REMARK 465 SER D 810 REMARK 465 LYS D 811 REMARK 465 PRO D 812 REMARK 465 SER D 813 REMARK 465 GLY D 842 REMARK 465 ASP D 843 REMARK 465 ILE D 844 REMARK 465 ALA D 845 REMARK 465 ALA D 846 REMARK 465 ARG D 847 REMARK 465 LEU D 938 REMARK 465 SER D 939 REMARK 465 SER D 940 REMARK 465 THR D 941 REMARK 465 PRO D 942 REMARK 465 SER D 943 REMARK 465 SER D 967 REMARK 465 SER D 968 REMARK 465 ASN D 969 REMARK 465 PHE D 970 REMARK 465 GLY D 971 REMARK 465 ALA D 972 REMARK 465 ILE D 973 REMARK 465 SER D 974 REMARK 465 SER D 975 REMARK 465 VAL D 976 REMARK 465 LEU D 977 REMARK 465 ASN D 978 REMARK 465 ASP D 979 REMARK 465 ILE D 980 REMARK 465 LEU D 981 REMARK 465 SER D 982 REMARK 465 ARG D 983 REMARK 465 LEU D 984 REMARK 465 ASP D 985 REMARK 465 PRO D 986 REMARK 465 PRO D 987 REMARK 465 GLU D 988 REMARK 465 ALA D 989 REMARK 465 LEU D 1145 REMARK 465 ASP D 1146 REMARK 465 SER D 1147 REMARK 465 PHE D 1148 REMARK 465 LYS D 1149 REMARK 465 GLU D 1150 REMARK 465 GLU D 1151 REMARK 465 LEU D 1152 REMARK 465 ASP D 1153 REMARK 465 LYS D 1154 REMARK 465 TYR D 1155 REMARK 465 PHE D 1156 REMARK 465 LYS D 1157 REMARK 465 ASN D 1158 REMARK 465 HIS D 1159 REMARK 465 THR D 1160 REMARK 465 SER D 1161 REMARK 465 GLY D 1162 REMARK 465 SER D 1163 REMARK 465 HIS D 1164 REMARK 465 HIS D 1165 REMARK 465 HIS D 1166 REMARK 465 HIS D 1167 REMARK 465 HIS D 1168 REMARK 465 HIS D 1169 REMARK 465 HIS D 1170 REMARK 465 HIS D 1171 REMARK 465 SER E 698 REMARK 465 LEU E 699 REMARK 465 GLY E 700 REMARK 465 ALA E 701 REMARK 465 GLU E 702 REMARK 465 ASN E 703 REMARK 465 CYS E 704 REMARK 465 VAL E 705 REMARK 465 LYS E 786 REMARK 465 GLN E 787 REMARK 465 LYS E 811 REMARK 465 PRO E 812 REMARK 465 SER E 813 REMARK 465 ASP E 843 REMARK 465 ILE E 844 REMARK 465 ALA E 845 REMARK 465 ALA E 846 REMARK 465 SER E 940 REMARK 465 THR E 941 REMARK 465 PRO E 942 REMARK 465 SER E 943 REMARK 465 GLY E 971 REMARK 465 ALA E 972 REMARK 465 ILE E 973 REMARK 465 LEU E 1145 REMARK 465 ASP E 1146 REMARK 465 SER E 1147 REMARK 465 PHE E 1148 REMARK 465 LYS E 1149 REMARK 465 GLU E 1150 REMARK 465 GLU E 1151 REMARK 465 LEU E 1152 REMARK 465 ASP E 1153 REMARK 465 LYS E 1154 REMARK 465 TYR E 1155 REMARK 465 PHE E 1156 REMARK 465 LYS E 1157 REMARK 465 ASN E 1158 REMARK 465 HIS E 1159 REMARK 465 THR E 1160 REMARK 465 SER E 1161 REMARK 465 GLY E 1162 REMARK 465 SER E 1163 REMARK 465 HIS E 1164 REMARK 465 HIS E 1165 REMARK 465 HIS E 1166 REMARK 465 HIS E 1167 REMARK 465 HIS E 1168 REMARK 465 HIS E 1169 REMARK 465 HIS E 1170 REMARK 465 HIS E 1171 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 ASP A 144 61.73 62.10 REMARK 500 SER B 30 -135.03 58.32 REMARK 500 ALA B 51 -3.20 71.54 REMARK 500 SER B 52 -14.32 -142.52 REMARK 500 GLU C 748 40.75 -107.39 REMARK 500 TYR C 789 -124.04 52.81 REMARK 500 LYS C 811 70.11 58.29 REMARK 500 THR C 827 -141.44 53.71 REMARK 500 ALA C 831 -130.74 57.14 REMARK 500 SER C 937 -60.44 -98.30 REMARK 500 LEU C 945 58.21 -93.58 REMARK 500 ILE D 742 -63.66 -108.15 REMARK 500 THR D 791 70.79 51.48 REMARK 500 ILE D 794 -71.62 -71.80 REMARK 500 LYS D 795 44.49 -140.29 REMARK 500 GLU E 748 37.03 -99.66 REMARK 500 HIS E1083 -62.31 -92.57 REMARK 500 ASP E1084 44.93 -140.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-74739 RELATED DB: EMDB REMARK 900 SARS-COV-2 S2 IN COMPLEX WITH COV2-2509 DBREF 9ZT7 A 1 216 PDB 9ZT7 9ZT7 1 216 DBREF 9ZT7 B 1 214 PDB 9ZT7 9ZT7 1 214 DBREF 9ZT7 C 698 1161 UNP P0DTC2 SPIKE_SARS2 698 1161 DBREF 9ZT7 D 698 1161 UNP P0DTC2 SPIKE_SARS2 698 1161 DBREF 9ZT7 E 698 1161 UNP P0DTC2 SPIKE_SARS2 698 1161 SEQADV 9ZT7 CYS C 704 UNP P0DTC2 SER 704 ENGINEERED MUTATION SEQADV 9ZT7 CYS C 790 UNP P0DTC2 LYS 790 ENGINEERED MUTATION SEQADV 9ZT7 CYS C 880 UNP P0DTC2 GLY 880 ENGINEERED MUTATION SEQADV 9ZT7 CYS C 888 UNP P0DTC2 PHE 888 ENGINEERED MUTATION SEQADV 9ZT7 PRO C 892 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 9ZT7 PRO C 899 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 9ZT7 PRO C 942 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 9ZT7 PHE C 961 UNP P0DTC2 THR 961 ENGINEERED MUTATION SEQADV 9ZT7 PRO C 986 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 9ZT7 PRO C 987 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 9ZT7 TRP C 991 UNP P0DTC2 VAL 991 ENGINEERED MUTATION SEQADV 9ZT7 TRP C 998 UNP P0DTC2 THR 998 ENGINEERED MUTATION SEQADV 9ZT7 GLY C 1162 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 SER C 1163 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS C 1164 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS C 1165 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS C 1166 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS C 1167 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS C 1168 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS C 1169 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS C 1170 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS C 1171 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 CYS D 704 UNP P0DTC2 SER 704 ENGINEERED MUTATION SEQADV 9ZT7 CYS D 790 UNP P0DTC2 LYS 790 ENGINEERED MUTATION SEQADV 9ZT7 CYS D 880 UNP P0DTC2 GLY 880 ENGINEERED MUTATION SEQADV 9ZT7 CYS D 888 UNP P0DTC2 PHE 888 ENGINEERED MUTATION SEQADV 9ZT7 PRO D 892 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 9ZT7 PRO D 899 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 9ZT7 PRO D 942 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 9ZT7 PHE D 961 UNP P0DTC2 THR 961 ENGINEERED MUTATION SEQADV 9ZT7 PRO D 986 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 9ZT7 PRO D 987 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 9ZT7 TRP D 991 UNP P0DTC2 VAL 991 ENGINEERED MUTATION SEQADV 9ZT7 TRP D 998 UNP P0DTC2 THR 998 ENGINEERED MUTATION SEQADV 9ZT7 GLY D 1162 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 SER D 1163 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS D 1164 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS D 1165 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS D 1166 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS D 1167 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS D 1168 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS D 1169 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS D 1170 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS D 1171 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 CYS E 704 UNP P0DTC2 SER 704 ENGINEERED MUTATION SEQADV 9ZT7 CYS E 790 UNP P0DTC2 LYS 790 ENGINEERED MUTATION SEQADV 9ZT7 CYS E 880 UNP P0DTC2 GLY 880 ENGINEERED MUTATION SEQADV 9ZT7 CYS E 888 UNP P0DTC2 PHE 888 ENGINEERED MUTATION SEQADV 9ZT7 PRO E 892 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 9ZT7 PRO E 899 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 9ZT7 PRO E 942 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 9ZT7 PHE E 961 UNP P0DTC2 THR 961 ENGINEERED MUTATION SEQADV 9ZT7 PRO E 986 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 9ZT7 PRO E 987 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 9ZT7 TRP E 991 UNP P0DTC2 VAL 991 ENGINEERED MUTATION SEQADV 9ZT7 TRP E 998 UNP P0DTC2 THR 998 ENGINEERED MUTATION SEQADV 9ZT7 GLY E 1162 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 SER E 1163 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS E 1164 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS E 1165 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS E 1166 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS E 1167 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS E 1168 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS E 1169 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS E 1170 UNP P0DTC2 EXPRESSION TAG SEQADV 9ZT7 HIS E 1171 UNP P0DTC2 EXPRESSION TAG SEQRES 1 A 224 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 A 224 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 224 PHE ILE PHE SER THR TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 A 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE SER SEQRES 5 A 224 TYR ASP GLY ASP ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 224 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 224 LEU TYR LEU GLU MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 224 ALA VAL TYR TYR CYS ALA ARG PRO ARG GLY GLY SER TYR SEQRES 9 A 224 GLN THR CYS PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 A 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 A 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 A 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 A 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 A 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 A 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 A 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 A 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 A 224 LYS SER CYS SEQRES 1 B 214 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 B 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 B 214 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 B 214 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 214 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 B 214 ASN ASN TRP PRO GLY THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS SEQRES 1 C 474 SER LEU GLY ALA GLU ASN CYS VAL ALA TYR SER ASN ASN SEQRES 2 C 474 SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL THR SEQRES 3 C 474 THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER VAL SEQRES 4 C 474 ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU CYS SEQRES 5 C 474 SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR GLN SEQRES 6 C 474 LEU ASN ARG ALA LEU THR GLY ILE ALA VAL GLU GLN ASP SEQRES 7 C 474 LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN ILE SEQRES 8 C 474 TYR CYS THR PRO PRO ILE LYS ASP PHE GLY GLY PHE ASN SEQRES 9 C 474 PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER LYS SEQRES 10 C 474 ARG SER PHE ILE GLU ASP LEU LEU PHE ASN LYS VAL THR SEQRES 11 C 474 LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP CYS SEQRES 12 C 474 LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA GLN SEQRES 13 C 474 LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU THR SEQRES 14 C 474 ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU ALA SEQRES 15 C 474 CYS THR ILE THR SER GLY TRP THR CYS GLY ALA GLY PRO SEQRES 16 C 474 ALA LEU GLN ILE PRO PHE PRO MET GLN MET ALA TYR ARG SEQRES 17 C 474 PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR GLU SEQRES 18 C 474 ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA ILE SEQRES 19 C 474 GLY LYS ILE GLN ASP SER LEU SER SER THR PRO SER ALA SEQRES 20 C 474 LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN ASN ALA GLN SEQRES 21 C 474 ALA LEU ASN PHE LEU VAL LYS GLN LEU SER SER ASN PHE SEQRES 22 C 474 GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER ARG SEQRES 23 C 474 LEU ASP PRO PRO GLU ALA GLU TRP GLN ILE ASP ARG LEU SEQRES 24 C 474 ILE TRP GLY ARG LEU GLN SER LEU GLN THR TYR VAL THR SEQRES 25 C 474 GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER ALA SEQRES 26 C 474 ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU GLY SEQRES 27 C 474 GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR HIS SEQRES 28 C 474 LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL VAL SEQRES 29 C 474 PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS ASN SEQRES 30 C 474 PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS ALA SEQRES 31 C 474 HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY THR SEQRES 32 C 474 HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO GLN SEQRES 33 C 474 ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN CYS SEQRES 34 C 474 ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR ASP SEQRES 35 C 474 PRO LEU GLN PRO GLU LEU ASP SER PHE LYS GLU GLU LEU SEQRES 36 C 474 ASP LYS TYR PHE LYS ASN HIS THR SER GLY SER HIS HIS SEQRES 37 C 474 HIS HIS HIS HIS HIS HIS SEQRES 1 D 474 SER LEU GLY ALA GLU ASN CYS VAL ALA TYR SER ASN ASN SEQRES 2 D 474 SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL THR SEQRES 3 D 474 THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER VAL SEQRES 4 D 474 ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU CYS SEQRES 5 D 474 SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR GLN SEQRES 6 D 474 LEU ASN ARG ALA LEU THR GLY ILE ALA VAL GLU GLN ASP SEQRES 7 D 474 LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN ILE SEQRES 8 D 474 TYR CYS THR PRO PRO ILE LYS ASP PHE GLY GLY PHE ASN SEQRES 9 D 474 PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER LYS SEQRES 10 D 474 ARG SER PHE ILE GLU ASP LEU LEU PHE ASN LYS VAL THR SEQRES 11 D 474 LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP CYS SEQRES 12 D 474 LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA GLN SEQRES 13 D 474 LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU THR SEQRES 14 D 474 ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU ALA SEQRES 15 D 474 CYS THR ILE THR SER GLY TRP THR CYS GLY ALA GLY PRO SEQRES 16 D 474 ALA LEU GLN ILE PRO PHE PRO MET GLN MET ALA TYR ARG SEQRES 17 D 474 PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR GLU SEQRES 18 D 474 ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA ILE SEQRES 19 D 474 GLY LYS ILE GLN ASP SER LEU SER SER THR PRO SER ALA SEQRES 20 D 474 LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN ASN ALA GLN SEQRES 21 D 474 ALA LEU ASN PHE LEU VAL LYS GLN LEU SER SER ASN PHE SEQRES 22 D 474 GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER ARG SEQRES 23 D 474 LEU ASP PRO PRO GLU ALA GLU TRP GLN ILE ASP ARG LEU SEQRES 24 D 474 ILE TRP GLY ARG LEU GLN SER LEU GLN THR TYR VAL THR SEQRES 25 D 474 GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER ALA SEQRES 26 D 474 ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU GLY SEQRES 27 D 474 GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR HIS SEQRES 28 D 474 LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL VAL SEQRES 29 D 474 PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS ASN SEQRES 30 D 474 PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS ALA SEQRES 31 D 474 HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY THR SEQRES 32 D 474 HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO GLN SEQRES 33 D 474 ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN CYS SEQRES 34 D 474 ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR ASP SEQRES 35 D 474 PRO LEU GLN PRO GLU LEU ASP SER PHE LYS GLU GLU LEU SEQRES 36 D 474 ASP LYS TYR PHE LYS ASN HIS THR SER GLY SER HIS HIS SEQRES 37 D 474 HIS HIS HIS HIS HIS HIS SEQRES 1 E 474 SER LEU GLY ALA GLU ASN CYS VAL ALA TYR SER ASN ASN SEQRES 2 E 474 SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL THR SEQRES 3 E 474 THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER VAL SEQRES 4 E 474 ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU CYS SEQRES 5 E 474 SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR GLN SEQRES 6 E 474 LEU ASN ARG ALA LEU THR GLY ILE ALA VAL GLU GLN ASP SEQRES 7 E 474 LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN ILE SEQRES 8 E 474 TYR CYS THR PRO PRO ILE LYS ASP PHE GLY GLY PHE ASN SEQRES 9 E 474 PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER LYS SEQRES 10 E 474 ARG SER PHE ILE GLU ASP LEU LEU PHE ASN LYS VAL THR SEQRES 11 E 474 LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP CYS SEQRES 12 E 474 LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA GLN SEQRES 13 E 474 LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU THR SEQRES 14 E 474 ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU ALA SEQRES 15 E 474 CYS THR ILE THR SER GLY TRP THR CYS GLY ALA GLY PRO SEQRES 16 E 474 ALA LEU GLN ILE PRO PHE PRO MET GLN MET ALA TYR ARG SEQRES 17 E 474 PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR GLU SEQRES 18 E 474 ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA ILE SEQRES 19 E 474 GLY LYS ILE GLN ASP SER LEU SER SER THR PRO SER ALA SEQRES 20 E 474 LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN ASN ALA GLN SEQRES 21 E 474 ALA LEU ASN PHE LEU VAL LYS GLN LEU SER SER ASN PHE SEQRES 22 E 474 GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER ARG SEQRES 23 E 474 LEU ASP PRO PRO GLU ALA GLU TRP GLN ILE ASP ARG LEU SEQRES 24 E 474 ILE TRP GLY ARG LEU GLN SER LEU GLN THR TYR VAL THR SEQRES 25 E 474 GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER ALA SEQRES 26 E 474 ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU GLY SEQRES 27 E 474 GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR HIS SEQRES 28 E 474 LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL VAL SEQRES 29 E 474 PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS ASN SEQRES 30 E 474 PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS ALA SEQRES 31 E 474 HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY THR SEQRES 32 E 474 HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO GLN SEQRES 33 E 474 ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN CYS SEQRES 34 E 474 ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR ASP SEQRES 35 E 474 PRO LEU GLN PRO GLU LEU ASP SER PHE LYS GLU GLU LEU SEQRES 36 E 474 ASP LYS TYR PHE LYS ASN HIS THR SER GLY SER HIS HIS SEQRES 37 E 474 HIS HIS HIS HIS HIS HIS HET NAG F 1 14 HET NAG F 2 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG H 1 14 HET NAG H 2 14 HET NAG I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 HET NAG K 1 14 HET NAG K 2 14 HET NAG L 1 14 HET NAG L 2 14 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 HET NAG C2000 14 HET NAG D1201 14 HET NAG E1201 14 HET NAG E1202 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 6 NAG 24(C8 H15 N O6) HELIX 1 AA1 ILE A 28 TYR A 32 5 5 HELIX 2 AA2 ARG A 83 THR A 87 5 5 HELIX 3 AA3 SER A 156 ALA A 158 5 3 HELIX 4 AA4 SER A 187 LEU A 189 5 3 HELIX 5 AA5 GLN B 79 PHE B 83 5 5 HELIX 6 AA6 SER B 121 GLY B 128 1 8 HELIX 7 AA7 LYS B 183 LYS B 188 1 6 HELIX 8 AA8 ASP C 737 ILE C 742 1 6 HELIX 9 AA9 GLU C 748 ALA C 783 1 36 HELIX 10 AB1 PRO C 793 GLY C 798 5 6 HELIX 11 AB2 SER C 816 THR C 827 1 12 HELIX 12 AB3 PHE C 833 GLY C 842 1 10 HELIX 13 AB4 ASP C 848 PHE C 855 1 8 HELIX 14 AB5 THR C 866 ILE C 882 1 17 HELIX 15 AB6 PRO C 897 GLY C 908 1 12 HELIX 16 AB7 GLN C 913 GLU C 918 1 6 HELIX 17 AB8 ASN C 919 SER C 937 1 19 HELIX 18 AB9 LEU C 945 SER C 967 1 23 HELIX 19 AC1 ALA C 989 CYS C 1032 1 44 HELIX 20 AC2 ASP D 737 CYS D 743 1 7 HELIX 21 AC3 GLU D 748 ALA D 783 1 36 HELIX 22 AC4 SER D 816 VAL D 826 1 11 HELIX 23 AC5 GLY D 832 LEU D 841 1 10 HELIX 24 AC6 LEU D 849 PHE D 855 1 7 HELIX 25 AC7 THR D 866 SER D 884 1 19 HELIX 26 AC8 PRO D 897 GLY D 910 1 14 HELIX 27 AC9 GLN D 913 ASN D 919 1 7 HELIX 28 AD1 ASN D 919 SER D 937 1 19 HELIX 29 AD2 LEU D 945 LEU D 966 1 22 HELIX 30 AD3 TRP D 991 CYS D 1032 1 42 HELIX 31 AD4 ASP E 737 GLY E 744 1 8 HELIX 32 AD5 GLU E 748 VAL E 781 1 34 HELIX 33 AD6 PRO E 793 GLY E 798 5 6 HELIX 34 AD7 SER E 816 VAL E 826 1 11 HELIX 35 AD8 GLY E 832 GLY E 842 1 11 HELIX 36 AD9 ASP E 848 PHE E 855 1 8 HELIX 37 AE1 THR E 866 ILE E 882 1 17 HELIX 38 AE2 PRO E 897 GLY E 910 1 14 HELIX 39 AE3 GLN E 913 GLU E 918 1 6 HELIX 40 AE4 ASN E 919 LEU E 938 1 20 HELIX 41 AE5 LEU E 945 SER E 967 1 23 HELIX 42 AE6 VAL E 976 LEU E 984 1 9 HELIX 43 AE7 ASP E 985 CYS E 1032 1 48 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA1 4 THR A 77 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AA1 4 PHE A 67 ASP A 72 -1 N SER A 70 O TYR A 79 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 110 N GLY A 10 SHEET 3 AA2 6 ALA A 88 PRO A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N HIS A 35 O ALA A 93 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 LYS A 57 TYR A 59 -1 O TYR A 58 N VAL A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O THR A 110 N GLY A 10 SHEET 3 AA3 4 ALA A 88 PRO A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AA3 4 PHE A 100D TRP A 103 -1 O TYR A 102 N ARG A 94 SHEET 1 AA4 4 SER A 120 LEU A 124 0 SHEET 2 AA4 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA4 4 TYR A 176 PRO A 185 -1 O VAL A 184 N ALA A 136 SHEET 4 AA4 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AA5 4 SER A 120 LEU A 124 0 SHEET 2 AA5 4 THR A 135 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA5 4 TYR A 176 PRO A 185 -1 O VAL A 184 N ALA A 136 SHEET 4 AA5 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AA6 3 THR A 151 TRP A 154 0 SHEET 2 AA6 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AA6 3 THR A 205 LYS A 210 -1 O LYS A 209 N CYS A 196 SHEET 1 AA7 4 MET B 4 GLN B 6 0 SHEET 2 AA7 4 ALA B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA7 4 GLU B 70 ILE B 75 -1 O ILE B 75 N ALA B 19 SHEET 4 AA7 4 PHE B 62 SER B 67 -1 N SER B 65 O THR B 72 SHEET 1 AA8 6 THR B 10 SER B 12 0 SHEET 2 AA8 6 THR B 102 GLU B 105 1 O GLU B 105 N LEU B 11 SHEET 3 AA8 6 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA8 6 LEU B 33 GLN B 38 -1 N GLN B 38 O VAL B 85 SHEET 5 AA8 6 ARG B 45 TYR B 49 -1 O ARG B 45 N GLN B 37 SHEET 6 AA8 6 THR B 53 ARG B 54 -1 O THR B 53 N TYR B 49 SHEET 1 AA9 4 SER B 114 PHE B 118 0 SHEET 2 AA9 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AA9 4 TYR B 173 SER B 182 -1 O SER B 177 N CYS B 134 SHEET 4 AA9 4 SER B 159 VAL B 163 -1 N SER B 162 O SER B 176 SHEET 1 AB1 3 ALA B 144 VAL B 150 0 SHEET 2 AB1 3 VAL B 191 HIS B 198 -1 O THR B 197 N LYS B 145 SHEET 3 AB1 3 VAL B 205 ASN B 210 -1 O PHE B 209 N TYR B 192 SHEET 1 AB2 3 SER C 711 PRO C 728 0 SHEET 2 AB2 3 GLY C1059 THR C1077 -1 O VAL C1068 N THR C 719 SHEET 3 AB2 3 TYR C1047 ALA C1056 -1 N GLN C1054 O VAL C1061 SHEET 1 AB3 5 SER C 711 PRO C 728 0 SHEET 2 AB3 5 GLY C1059 THR C1077 -1 O VAL C1068 N THR C 719 SHEET 3 AB3 5 VAL C1094 SER C1097 -1 O SER C1097 N THR C1076 SHEET 4 AB3 5 TRP C1102 THR C1105 -1 O PHE C1103 N VAL C1096 SHEET 5 AB3 5 GLN C1113 ILE C1114 -1 O GLN C1113 N VAL C1104 SHEET 1 AB4 2 LYS C 733 VAL C 736 0 SHEET 2 AB4 2 LEU C 858 LEU C 861 -1 O THR C 859 N SER C 735 SHEET 1 AB5 4 THR C1120 ASN C1125 0 SHEET 2 AB5 4 LYS C1086 PRO C1090 -1 N PHE C1089 O PHE C1121 SHEET 3 AB5 4 ILE C1081 HIS C1083 -1 N HIS C1083 O LYS C1086 SHEET 4 AB5 4 VAL C1133 ASN C1134 1 O VAL C1133 N CYS C1082 SHEET 1 AB6 3 SER D 711 PRO D 728 0 SHEET 2 AB6 3 GLY D1059 THR D1076 -1 O THR D1066 N SER D 721 SHEET 3 AB6 3 TYR D1047 ALA D1056 -1 N TYR D1047 O TYR D1067 SHEET 1 AB7 2 LYS D 733 VAL D 736 0 SHEET 2 AB7 2 LEU D 858 LEU D 861 -1 O THR D 859 N SER D 735 SHEET 1 AB8 4 THR D1120 ASN D1125 0 SHEET 2 AB8 4 LYS D1086 PRO D1090 -1 N PHE D1089 O PHE D1121 SHEET 3 AB8 4 ILE D1081 HIS D1083 -1 N ILE D1081 O HIS D1088 SHEET 4 AB8 4 VAL D1133 ASN D1134 1 O VAL D1133 N CYS D1082 SHEET 1 AB9 3 VAL D1094 SER D1097 0 SHEET 2 AB9 3 TRP D1102 THR D1105 -1 O PHE D1103 N VAL D1096 SHEET 3 AB9 3 GLN D1113 ILE D1114 -1 O GLN D1113 N VAL D1104 SHEET 1 AC1 3 SER E 711 PRO E 728 0 SHEET 2 AC1 3 GLY E1059 THR E1076 -1 O PHE E1062 N GLU E 725 SHEET 3 AC1 3 TYR E1047 ALA E1056 -1 N MET E1050 O VAL E1065 SHEET 1 AC2 2 LYS E 733 VAL E 736 0 SHEET 2 AC2 2 LEU E 858 LEU E 861 -1 O LEU E 861 N LYS E 733 SHEET 1 AC3 4 THR E1120 ASN E1125 0 SHEET 2 AC3 4 LYS E1086 PRO E1090 -1 N PHE E1089 O PHE E1121 SHEET 3 AC3 4 ILE E1081 CYS E1082 -1 N ILE E1081 O HIS E1088 SHEET 4 AC3 4 VAL E1133 ASN E1134 1 O VAL E1133 N CYS E1082 SHEET 1 AC4 3 VAL E1094 SER E1097 0 SHEET 2 AC4 3 TRP E1102 THR E1105 -1 O PHE E1103 N VAL E1096 SHEET 3 AC4 3 GLN E1113 ILE E1114 -1 O GLN E1113 N VAL E1104 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.03 SSBOND 2 CYS A 140 CYS A 196 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.03 SSBOND 5 CYS C 738 CYS C 760 1555 1555 2.03 SSBOND 6 CYS C 743 CYS C 749 1555 1555 2.03 SSBOND 7 CYS C 840 CYS C 851 1555 1555 2.04 SSBOND 8 CYS C 880 CYS C 888 1555 1555 2.03 SSBOND 9 CYS C 1032 CYS C 1043 1555 1555 2.03 SSBOND 10 CYS C 1082 CYS C 1126 1555 1555 2.03 SSBOND 11 CYS D 738 CYS D 760 1555 1555 2.03 SSBOND 12 CYS D 743 CYS D 749 1555 1555 2.03 SSBOND 13 CYS D 840 CYS D 851 1555 1555 2.03 SSBOND 14 CYS D 880 CYS D 888 1555 1555 2.03 SSBOND 15 CYS D 1032 CYS D 1043 1555 1555 2.03 SSBOND 16 CYS D 1082 CYS D 1126 1555 1555 2.03 SSBOND 17 CYS E 738 CYS E 760 1555 1555 2.03 SSBOND 18 CYS E 743 CYS E 749 1555 1555 2.03 SSBOND 19 CYS E 840 CYS E 851 1555 1555 2.03 SSBOND 20 CYS E 880 CYS E 888 1555 1555 2.03 SSBOND 21 CYS E 1032 CYS E 1043 1555 1555 2.03 SSBOND 22 CYS E 1082 CYS E 1126 1555 1555 2.03 LINK ND2 ASN C 709 C1 NAG C2000 1555 1555 1.44 LINK ND2 ASN C 717 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN C 801 C1 NAG G 1 1555 1555 1.44 LINK OG1 THR C1100 C1 NAG H 1 1555 1555 1.44 LINK ND2 ASN D 709 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN D 717 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN D 801 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN D1098 C1 NAG L 1 1555 1555 1.44 LINK ND2 ASN D1134 C1 NAG D1201 1555 1555 1.44 LINK ND2 ASN E 709 C1 NAG E1201 1555 1555 1.44 LINK ND2 ASN E 717 C1 NAG M 1 1555 1555 1.44 LINK OG SER E 803 C1 NAG N 1 1555 1555 1.45 LINK ND2 ASN E1098 C1 NAG O 1 1555 1555 1.45 LINK ND2 ASN E1134 C1 NAG E1202 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 CISPEP 1 PHE A 146 PRO A 147 0 -6.74 CISPEP 2 GLU A 148 PRO A 149 0 -5.56 CISPEP 3 TRP B 94 PRO B 95 0 -5.30 CISPEP 4 TYR B 140 PRO B 141 0 2.41 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