HEADER IMMUNE SYSTEM 21-SEP-24 9DPE TITLE CRYOEM STRUCTURE OF HUMAN BTN2A1 ECTODOMAIN IN COMPLEX WITH TCR- TITLE 2 BLOCKING 2A1.12 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: BUTYROPHILIN SUBFAMILY 2 MEMBER A1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: BTN2A1 ECTODOMAIN WITH N- AND C-TERMINAL LINKERS. N- COMPND 6 TERMINAL (ADLQ) AND C-TERMINAL (VSPCGSGLEVLFQ) RESIDUES ARE COMPND 7 DISORDERED AND NOT MODELED. 3 GLYCANS ARE DENOTED AS NAG.; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: HUMAN IGG1 FRAGMENT ANTIBODY HEAVY CHAIN; COMPND 10 CHAIN: H; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: HEAVY CHAIN OF HERCEPTIN FAB SCAFFOLD WITH CDR LOOPS COMPND 13 MODIFIED THROUGH PHAGE-DISPLAY EVOLUTION. (CDR1: FSSSI) (CDR2: COMPND 14 SIYSSSGYTY) (CDR3: IEYGRGYWDAF). N-TERMINAL (EIS) IS A COMPND 15 LINKER/RESTRICTION ENZYME ARTIFACT AND FIRST RESIDUE OF FAB, AND COMPND 16 DISORDERED AND NOT MODELED.; COMPND 17 MOL_ID: 3; COMPND 18 MOLECULE: HUMAN IGG1 FRAGMENT ANTIBODY LIGHT CHAIN; COMPND 19 CHAIN: L; COMPND 20 ENGINEERED: YES; COMPND 21 OTHER_DETAILS: LIGHT CHAIN OF HERCEPTIN FAB SCAFFOLD WITH CDR LOOPS COMPND 22 MODIFIED THROUGH PHAGE-DISPLAY EVOLUTION. (CDR1: VSSAV) (CDR2: COMPND 23 IYSASSLY) (CDR3: SSSSLI). N-TERMINAL (S) RESIDUE IS A COMPND 24 LINKER/RESTRICTION ENZYME ARTIFACT.; COMPND 25 MOL_ID: 4; COMPND 26 MOLECULE: HUMAN VARIABLE HEAVY-CHAIN DOMAIN NANOBODY; COMPND 27 CHAIN: N; COMPND 28 ENGINEERED: YES; COMPND 29 OTHER_DETAILS: HUMAN VARIABLE HEAVY-CHAIN DOMAIN NANOBODY SPECIFIC COMPND 30 FOR HUMAN FAB KAPPA LIGHT CHAIN WITH A HEXAHISTIDINE TAG AND LINKER COMPND 31 (HHHHHHGENLYFQGS). TAG AND LINKER ARE DISORDERED AND NOT SHOWN. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: BTN2A1, BT2.1, BTF1; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PAC-GP67A; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 17 EXPRESSION_SYSTEM_PLASMID: RH2.2; SOURCE 18 MOL_ID: 3; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_COMMON: HUMAN; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 23 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 25 EXPRESSION_SYSTEM_PLASMID: RH2.2; SOURCE 26 MOL_ID: 4; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 28 ORGANISM_COMMON: HUMAN; SOURCE 29 ORGANISM_TAXID: 9606; SOURCE 30 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 31 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS COMPLEX, ANTIBODY, IMMUNE RECOGNITION, SIGNALING PROTEIN, IMMUNE KEYWDS 2 SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR A.RAMESH,J.R.FULLER,S.ROY,E.ADAMS REVDAT 1 23-APR-25 9DPE 0 JRNL AUTH A.RAMESH,S.ROY,T.SLEZAK,J.FULLER,H.GRAVES,M.R.MAMEDOV, JRNL AUTH 2 A.MARSON,A.A.KOSSIAKOFF,E.J.ADAMS JRNL TITL MAPPING THE EXTRACELLULAR MOLECULAR ARCHITECTURE OF THE JRNL TITL 2 PAG-SIGNALING COMPLEX WITH ALPHA-BUTYROPHILIN ANTIBODIES. JRNL REF SCI REP V. 15 12162 2025 JRNL REFN ESSN 2045-2322 JRNL PMID 40204806 JRNL DOI 10.1038/S41598-025-94347-W REMARK 2 REMARK 2 RESOLUTION. 3.86 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : TOPAZ, EPU, CTFFIND, RELION, PHENIX, REMARK 3 RELION, RELION, RELION, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 8DFW REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT REMARK 3 REFINEMENT TARGET : CROSS-CORRELATION 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) : 3.860 REMARK 3 NUMBER OF PARTICLES : 213773 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 9DPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000286079. 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 DIMERIC HUMAN BTN2A1 REMARK 245 ECTODOMAIN WITH TCR-BLOCKING REMARK 245 2A1.12 FAB AND BULKING NANOBODY; REMARK 245 HUMAN BTN2A1 ECTODOMAIN; ANTI- REMARK 245 BTN2A1 FAB 2A1.12; HEAVY CHAIN REMARK 245 OF 2A1.12 FAB; LIGHT CHAIN OF REMARK 245 2A1.12 FAB; VARIABLE HEAVY REMARK 245 CHAIN DOMAIN NANOBODY REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.85 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 : 5438 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 900.00 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) : 6000.00 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, N 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 ALA A -2 REMARK 465 ASP A -1 REMARK 465 LEU A 0 REMARK 465 GLN A 1 REMARK 465 VAL A 216 REMARK 465 SER A 217 REMARK 465 PRO A 218 REMARK 465 CYS A 219 REMARK 465 GLY A 220 REMARK 465 SER A 221 REMARK 465 GLY A 222 REMARK 465 LEU A 223 REMARK 465 GLU A 224 REMARK 465 VAL A 225 REMARK 465 LEU A 226 REMARK 465 PHE A 227 REMARK 465 GLN A 228 REMARK 465 GLU H -2 REMARK 465 ILE H -1 REMARK 465 SER H 0 REMARK 465 HIS N -5 REMARK 465 HIS N -4 REMARK 465 HIS N -3 REMARK 465 HIS N -2 REMARK 465 HIS N -1 REMARK 465 HIS N 0 REMARK 465 GLY N 1 REMARK 465 GLU N 2 REMARK 465 ASN N 3 REMARK 465 LEU N 4 REMARK 465 TYR N 5 REMARK 465 PHE N 6 REMARK 465 GLN N 7 REMARK 465 GLY N 8 REMARK 465 SER N 9 REMARK 465 GLN N 10 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O GLN L 37 H LYS L 45 1.55 REMARK 500 OD2 ASP N 65 OH TYR N 113 2.12 REMARK 500 ND1 HIS H 209 OG SER H 212 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 ARG A 40 -63.18 -99.99 REMARK 500 PRO A 144 -159.62 -73.31 REMARK 500 VAL H 48 -61.94 -94.14 REMARK 500 ASP H 153 61.24 60.31 REMARK 500 SER L 30 -142.41 57.25 REMARK 500 ALA L 51 -3.22 73.92 REMARK 500 ALA L 84 -175.47 -172.62 REMARK 500 PRO L 141 -165.98 -77.78 REMARK 500 VAL N 57 -56.80 -123.49 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8VC7 RELATED DB: PDB REMARK 900 8CF7 CONTAINS BTN2A1 COMPLEXED WITH A DIFFERENT FAB REMARK 900 RELATED ID: EMD-47104 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF HUMAN BTN2A1 ECTODOMAIN IN COMPLEX WITH TCR- REMARK 900 BLOCKING 2A1.12 FAB DBREF 9DPE A 1 219 UNP Q7KYR7 BT2A1_HUMAN 29 247 DBREF 9DPE H -2 230 PDB 9DPE 9DPE -2 230 DBREF 9DPE L 0 214 PDB 9DPE 9DPE 0 214 DBREF 9DPE N -5 130 PDB 9DPE 9DPE -5 130 SEQADV 9DPE ALA A -2 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE ASP A -1 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE LEU A 0 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE GLY A 220 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE SER A 221 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE GLY A 222 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE LEU A 223 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE GLU A 224 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE VAL A 225 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE LEU A 226 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE PHE A 227 UNP Q7KYR7 EXPRESSION TAG SEQADV 9DPE GLN A 228 UNP Q7KYR7 EXPRESSION TAG SEQRES 1 A 231 ALA ASP LEU GLN PHE ILE VAL VAL GLY PRO THR ASP PRO SEQRES 2 A 231 ILE LEU ALA THR VAL GLY GLU ASN THR THR LEU ARG CYS SEQRES 3 A 231 HIS LEU SER PRO GLU LYS ASN ALA GLU ASP MET GLU VAL SEQRES 4 A 231 ARG TRP PHE ARG SER GLN PHE SER PRO ALA VAL PHE VAL SEQRES 5 A 231 TYR LYS GLY GLY ARG GLU ARG THR GLU GLU GLN MET GLU SEQRES 6 A 231 GLU TYR ARG GLY ARG THR THR PHE VAL SER LYS ASP ILE SEQRES 7 A 231 SER ARG GLY SER VAL ALA LEU VAL ILE HIS ASN ILE THR SEQRES 8 A 231 ALA GLN GLU ASN GLY THR TYR ARG CYS TYR PHE GLN GLU SEQRES 9 A 231 GLY ARG SER TYR ASP GLU ALA ILE LEU HIS LEU VAL VAL SEQRES 10 A 231 ALA GLY LEU GLY SER LYS PRO LEU ILE SER MET ARG GLY SEQRES 11 A 231 HIS GLU ASP GLY GLY ILE ARG LEU GLU CYS ILE SER ARG SEQRES 12 A 231 GLY TRP TYR PRO LYS PRO LEU THR VAL TRP ARG ASP PRO SEQRES 13 A 231 TYR GLY GLY VAL ALA PRO ALA LEU LYS GLU VAL SER MET SEQRES 14 A 231 PRO ASP ALA ASP GLY LEU PHE MET VAL THR THR ALA VAL SEQRES 15 A 231 ILE ILE ARG ASP LYS SER VAL ARG ASN MET SER CYS SER SEQRES 16 A 231 ILE ASN ASN THR LEU LEU GLY GLN LYS LYS GLU SER VAL SEQRES 17 A 231 ILE PHE ILE PRO GLU SER PHE MET PRO SER VAL SER PRO SEQRES 18 A 231 CYS GLY SER GLY LEU GLU VAL LEU PHE GLN SEQRES 1 H 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 233 ALA SER GLY PHE ASN PHE SER SER SER SER ILE HIS TRP SEQRES 4 H 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 233 SER ILE TYR SER SER SER GLY TYR THR TYR TYR ALA ASP SEQRES 6 H 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG ILE GLU TYR SEQRES 9 H 233 GLY ARG GLY TYR TRP ASP ALA PHE ASP TYR TRP GLY GLN SEQRES 10 H 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 H 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 L 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 215 SER SER SER SER LEU ILE THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 N 136 HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE GLN SEQRES 2 N 136 GLY SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU SEQRES 3 N 136 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 4 N 136 SER GLY ARG THR ILE SER ARG TYR ALA MET SER TRP PHE SEQRES 5 N 136 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL SEQRES 6 N 136 ALA ARG ARG SER GLY ASP GLY ALA PHE TYR ALA ASP SER SEQRES 7 N 136 VAL GLN GLY ARG PHE THR VAL SER ARG ASP ASP ALA LYS SEQRES 8 N 136 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 9 N 136 ASP THR ALA VAL TYR TYR CYS ALA ILE ASP SER ASP THR SEQRES 10 N 136 PHE TYR SER GLY SER TYR ASP TYR TRP GLY GLN GLY THR SEQRES 11 N 136 GLN VAL THR VAL SER SER HET NAG A 301 28 HET NAG A 302 28 HET NAG A 303 28 HET NAG A 304 28 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 5 NAG 4(C8 H15 N O6) HELIX 1 AA1 MET A 61 ARG A 65 5 5 HELIX 2 AA2 THR A 88 ASN A 92 5 5 HELIX 3 AA3 PRO A 209 MET A 213 5 5 HELIX 4 AA4 ARG H 87 THR H 91 5 5 HELIX 5 AA5 SER H 137 GLY H 142 5 6 HELIX 6 AA6 SER H 165 ALA H 167 5 3 HELIX 7 AA7 SER H 196 THR H 200 5 5 HELIX 8 AA8 SER L 121 LYS L 126 1 6 HELIX 9 AA9 LYS L 183 HIS L 189 1 7 HELIX 10 AB1 THR N 37 TYR N 41 5 5 HELIX 11 AB2 LYS N 96 THR N 100 5 5 SHEET 1 AA1 4 ILE A 3 VAL A 5 0 SHEET 2 AA1 4 THR A 19 SER A 26 -1 O HIS A 24 N VAL A 5 SHEET 3 AA1 4 SER A 79 ILE A 84 -1 O ILE A 84 N THR A 19 SHEET 4 AA1 4 THR A 68 VAL A 71 -1 N THR A 69 O VAL A 83 SHEET 1 AA2 6 ILE A 11 THR A 14 0 SHEET 2 AA2 6 TYR A 105 ALA A 115 1 O VAL A 113 N ILE A 11 SHEET 3 AA2 6 GLY A 93 GLN A 100 -1 N GLY A 93 O LEU A 112 SHEET 4 AA2 6 GLU A 35 PHE A 39 -1 N GLU A 35 O GLN A 100 SHEET 5 AA2 6 PHE A 48 LYS A 51 -1 O TYR A 50 N VAL A 36 SHEET 6 AA2 6 ARG A 54 GLU A 55 -1 O ARG A 54 N LYS A 51 SHEET 1 AA3 4 LEU A 122 GLU A 129 0 SHEET 2 AA3 4 GLY A 132 TRP A 142 -1 O ARG A 134 N ARG A 126 SHEET 3 AA3 4 PHE A 173 ILE A 181 -1 O VAL A 179 N LEU A 135 SHEET 4 AA3 4 GLU A 163 PRO A 167 -1 N VAL A 164 O THR A 176 SHEET 1 AA4 3 LEU A 147 ARG A 151 0 SHEET 2 AA4 3 ASN A 188 ASN A 195 -1 O SER A 192 N VAL A 149 SHEET 3 AA4 3 GLN A 200 PHE A 207 -1 O ILE A 206 N MET A 189 SHEET 1 AA5 4 GLN H 3 SER H 7 0 SHEET 2 AA5 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA5 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA5 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AA6 6 GLY H 10 VAL H 12 0 SHEET 2 AA6 6 THR H 116 VAL H 120 1 O LEU H 117 N GLY H 10 SHEET 3 AA6 6 ALA H 92 GLU H 100 -1 N TYR H 94 O THR H 116 SHEET 4 AA6 6 SER H 32 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA6 6 GLU H 46 TYR H 52 -1 O VAL H 48 N TRP H 36 SHEET 6 AA6 6 THR H 58 TYR H 60 -1 O TYR H 59 N SER H 50 SHEET 1 AA7 4 GLY H 10 VAL H 12 0 SHEET 2 AA7 4 THR H 116 VAL H 120 1 O LEU H 117 N GLY H 10 SHEET 3 AA7 4 ALA H 92 GLU H 100 -1 N TYR H 94 O THR H 116 SHEET 4 AA7 4 TYR H 111 TRP H 112 -1 O TYR H 111 N ARG H 98 SHEET 1 AA8 4 SER H 129 LEU H 133 0 SHEET 2 AA8 4 THR H 144 TYR H 154 -1 O LEU H 150 N PHE H 131 SHEET 3 AA8 4 TYR H 185 PRO H 194 -1 O VAL H 193 N ALA H 145 SHEET 4 AA8 4 VAL H 172 THR H 174 -1 N HIS H 173 O VAL H 190 SHEET 1 AA9 4 SER H 129 LEU H 133 0 SHEET 2 AA9 4 THR H 144 TYR H 154 -1 O LEU H 150 N PHE H 131 SHEET 3 AA9 4 TYR H 185 PRO H 194 -1 O VAL H 193 N ALA H 145 SHEET 4 AA9 4 VAL H 178 LEU H 179 -1 N VAL H 178 O SER H 186 SHEET 1 AB1 3 VAL H 159 TRP H 163 0 SHEET 2 AB1 3 TYR H 203 HIS H 209 -1 O ASN H 208 N THR H 160 SHEET 3 AB1 3 THR H 214 VAL H 220 -1 O LYS H 218 N CYS H 205 SHEET 1 AB2 4 THR L 5 SER L 7 0 SHEET 2 AB2 4 VAL L 19 ARG L 24 -1 O THR L 22 N SER L 7 SHEET 3 AB2 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AB2 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB3 6 SER L 10 ALA L 13 0 SHEET 2 AB3 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AB3 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB3 6 VAL L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AB3 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB3 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AB4 4 SER L 10 ALA L 13 0 SHEET 2 AB4 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AB4 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB4 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB5 4 SER L 114 PHE L 118 0 SHEET 2 AB5 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB5 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AB5 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB6 4 ALA L 153 LEU L 154 0 SHEET 2 AB6 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB6 4 VAL L 191 HIS L 198 -1 O THR L 197 N LYS L 145 SHEET 4 AB6 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SHEET 1 AB7 4 GLN N 12 SER N 16 0 SHEET 2 AB7 4 LEU N 27 SER N 34 -1 O SER N 30 N SER N 16 SHEET 3 AB7 4 THR N 87 MET N 92 -1 O VAL N 88 N CYS N 31 SHEET 4 AB7 4 THR N 78 ASP N 82 -1 N SER N 80 O TYR N 89 SHEET 1 AB8 6 GLY N 19 VAL N 21 0 SHEET 2 AB8 6 THR N 124 VAL N 128 1 O THR N 127 N GLY N 19 SHEET 3 AB8 6 ALA N 101 ASP N 108 -1 N TYR N 103 O THR N 124 SHEET 4 AB8 6 ALA N 42 GLN N 48 -1 N ALA N 42 O ASP N 108 SHEET 5 AB8 6 GLU N 55 ALA N 60 -1 O GLU N 55 N ARG N 47 SHEET 6 AB8 6 ALA N 67 TYR N 69 -1 O PHE N 68 N VAL N 59 SHEET 1 AB9 4 GLY N 19 VAL N 21 0 SHEET 2 AB9 4 THR N 124 VAL N 128 1 O THR N 127 N GLY N 19 SHEET 3 AB9 4 ALA N 101 ASP N 108 -1 N TYR N 103 O THR N 124 SHEET 4 AB9 4 TYR N 119 TRP N 120 -1 O TYR N 119 N ILE N 107 SSBOND 1 CYS A 23 CYS A 97 1555 1555 2.04 SSBOND 2 CYS A 137 CYS A 191 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 4 CYS H 149 CYS H 205 1555 1555 2.03 SSBOND 5 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 6 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 7 CYS N 31 CYS N 105 1555 1555 2.03 LINK ND2 ASN A 18 C1 NAG A 302 1555 1555 1.44 LINK ND2 ASN A 86 C1 NAG A 301 1555 1555 1.44 LINK ND2 ASN A 92 C1 NAG A 304 1555 1555 1.44 LINK ND2 ASN A 188 C1 NAG A 303 1555 1555 1.44 CISPEP 1 SER A 26 PRO A 27 0 1.15 CISPEP 2 SER A 44 PRO A 45 0 0.69 CISPEP 3 TYR A 143 PRO A 144 0 -4.98 CISPEP 4 PHE H 155 PRO H 156 0 -4.02 CISPEP 5 GLU H 157 PRO H 158 0 -2.33 CISPEP 6 SER L 7 PRO L 8 0 -6.84 CISPEP 7 TYR L 140 PRO L 141 0 1.01 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