HEADER VIRAL PROTEIN/IMMUNE SYSTEM 04-JUL-22 7YDI TITLE SARS-COV-2 SPIKE (6P) IN COMPLEX WITH 3 R1-32 FABS AND 3 ACE2, FOCUSED TITLE 2 REFINEMENT OF RBD REGION COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROCESSED ANGIOTENSIN-CONVERTING ENZYME 2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SPIKE PROTEIN S1; COMPND 7 CHAIN: E; COMPND 8 FRAGMENT: SPIKE PROTOMER RBD DOMAIN; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: HEAVY CHAIN OF R1-32; COMPND 12 CHAIN: H; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: LIGHT CHAIN OF R1-32; COMPND 16 CHAIN: L; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ACE2, UNQ868/PRO1885; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 11 2; SOURCE 12 ORGANISM_TAXID: 2697049; SOURCE 13 GENE: S, 2; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS ANTIBODIES, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR B.LIU,X.GAO,Z.LI,X.CHEN,J.HE,L.CHEN,X.XIONG REVDAT 1 24-AUG-22 7YDI 0 JRNL AUTH X.XIONG,L.CHEN,J.HE,X.CHEN,X.GAO JRNL TITL SPIKE_GSAS_6P AND R1-32 FAB WITH 3TO1 RATIO JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.98 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : WARP, SERIALEM, WARP, RELION, REMARK 3 CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.980 REMARK 3 NUMBER OF PARTICLES : 150762 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 7YDI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-22. REMARK 100 THE DEPOSITION ID IS D_1300030061. 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 S-GSAS/6P SPIKE REMARK 245 TRIMER BOUND TO R1-32 FAB WITH REMARK 245 3:1 RATIO; ACE2; SARS-COV-2 S- REMARK 245 GSAS/6P SPIKE TRIMER; R1-32 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 : 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 : 6989 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 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 : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6300.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 45000 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, H, 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 SER A 19 REMARK 465 PRO A 616 REMARK 465 LEU A 617 REMARK 465 VAL A 618 REMARK 465 PRO A 619 REMARK 465 ARG A 620 REMARK 465 GLU H 1 REMARK 465 GLN L 1 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS H 217 CG CD CE NZ REMARK 470 LYS L 115 CG CD CE NZ REMARK 470 GLU L 188 CG CD OE1 OE2 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 OE1 GLU H 6 N GLY H 117 2.09 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 258 43.46 -83.52 REMARK 500 ASP A 292 115.51 -160.36 REMARK 500 TYR A 385 55.08 -94.64 REMARK 500 ARG A 393 -160.76 -78.81 REMARK 500 GLU A 398 30.07 -94.35 REMARK 500 ASP A 509 63.90 60.49 REMARK 500 VAL A 573 -56.45 -120.32 REMARK 500 ASN A 599 54.47 -92.12 REMARK 500 THR E 393 -60.76 -93.55 REMARK 500 ARG E 403 -166.64 -79.86 REMARK 500 SER H 16 -162.00 57.51 REMARK 500 PHE H 29 51.40 -94.10 REMARK 500 SER H 31 14.97 54.98 REMARK 500 SER H 85 70.24 58.21 REMARK 500 ARG H 87 -153.02 -112.26 REMARK 500 ASN L 53 -11.01 72.24 REMARK 500 GLN L 113 72.60 -161.78 REMARK 500 ASP L 156 -0.49 66.26 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 901 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 374 NE2 REMARK 620 2 HIS A 378 NE2 67.2 REMARK 620 3 GLU A 402 OE1 84.1 89.2 REMARK 620 N 1 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-33748 RELATED DB: EMDB REMARK 900 SPIKE_GSAS_6P PROTOMER RBD DOMAIN BOUND WITH R1-32 FAB AND ACE2 REMARK 900 WITH 3:3:3 RATIO DBREF 7YDI A 19 615 UNP Q9BYF1 ACE2_HUMAN 19 615 DBREF 7YDI E 334 526 UNP P0DTC2 SPIKE_SARS2 334 526 DBREF 7YDI H 1 228 PDB 7YDI 7YDI 1 228 DBREF 7YDI L 1 214 PDB 7YDI 7YDI 1 214 SEQADV 7YDI PRO A 616 UNP Q9BYF1 EXPRESSION TAG SEQADV 7YDI LEU A 617 UNP Q9BYF1 EXPRESSION TAG SEQADV 7YDI VAL A 618 UNP Q9BYF1 EXPRESSION TAG SEQADV 7YDI PRO A 619 UNP Q9BYF1 EXPRESSION TAG SEQADV 7YDI ARG A 620 UNP Q9BYF1 EXPRESSION TAG SEQRES 1 A 602 SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS SEQRES 2 A 602 PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER SEQRES 3 A 602 LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU SEQRES 4 A 602 ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER SEQRES 5 A 602 ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR SEQRES 6 A 602 PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN SEQRES 7 A 602 LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER SEQRES 8 A 602 GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR SEQRES 9 A 602 MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO SEQRES 10 A 602 ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU SEQRES 11 A 602 ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG SEQRES 12 A 602 LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS SEQRES 13 A 602 GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS SEQRES 14 A 602 ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY SEQRES 15 A 602 ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP SEQRES 16 A 602 GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL SEQRES 17 A 602 GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS SEQRES 18 A 602 LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR SEQRES 19 A 602 PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS SEQRES 20 A 602 LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU SEQRES 21 A 602 TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE SEQRES 22 A 602 ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA SEQRES 23 A 602 GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER SEQRES 24 A 602 VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN SEQRES 25 A 602 SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL SEQRES 26 A 602 CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE SEQRES 27 A 602 ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE SEQRES 28 A 602 LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP SEQRES 29 A 602 MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY SEQRES 30 A 602 ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET SEQRES 31 A 602 SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE SEQRES 32 A 602 GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR SEQRES 33 A 602 GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL SEQRES 34 A 602 GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG SEQRES 35 A 602 TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP SEQRES 36 A 602 MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY SEQRES 37 A 602 VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP SEQRES 38 A 602 PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE SEQRES 39 A 602 ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE SEQRES 40 A 602 GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO SEQRES 41 A 602 LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY SEQRES 42 A 602 GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU SEQRES 43 A 602 PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS SEQRES 44 A 602 ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO SEQRES 45 A 602 LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE SEQRES 46 A 602 VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA ASP PRO SEQRES 47 A 602 LEU VAL PRO ARG SEQRES 1 E 193 ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR ARG SEQRES 2 E 193 PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SER SEQRES 3 E 193 ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER ALA SEQRES 4 E 193 SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO THR SEQRES 5 E 193 LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA ASP SEQRES 6 E 193 SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE ALA SEQRES 7 E 193 PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR LYS SEQRES 8 E 193 LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP ASN SEQRES 9 E 193 SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR ASN SEQRES 10 E 193 TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS PRO SEQRES 11 E 193 PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA GLY SEQRES 12 E 193 SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS TYR SEQRES 13 E 193 PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN GLY SEQRES 14 E 193 VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 15 E 193 GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 1 H 228 GLU VAL GLN LEU VAL GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 228 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 228 GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 228 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE SEQRES 5 H 228 PRO ILE LEU GLY ILE ALA ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 228 GLY ARG VAL THR ILE THR ALA ASP LYS SER THR SER THR SEQRES 7 H 228 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 228 ALA VAL TYR TYR CYS ALA ARG GLU ASN GLY TYR SER GLY SEQRES 9 H 228 TYR GLY ALA ALA ALA ASN PHE ASP LEU TRP GLY ARG GLY SEQRES 10 H 228 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 228 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 228 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 228 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 228 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 228 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 228 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 228 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 H 228 VAL GLU PRO LYS SER CYS ASP SEQRES 1 L 214 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 214 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3 L 214 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4 L 214 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5 L 214 ASN SER ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 214 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 L 214 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 L 214 SER TYR ASP SER SER LEU SER GLY SER VAL PHE GLY GLY SEQRES 9 L 214 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 L 214 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 214 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 L 214 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 L 214 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 L 214 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 L 214 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 L 214 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 L 214 LYS THR VAL ALA PRO THR HET ZN A 901 1 HET NAG A 902 14 HET NAG A 903 14 HET NAG A 904 14 HET NAG A 905 14 HETNAM ZN ZINC ION 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 ZN ZN 2+ FORMUL 6 NAG 4(C8 H15 N O6) HELIX 1 AA1 THR A 20 ASN A 53 1 34 HELIX 2 AA2 THR A 55 TYR A 83 1 29 HELIX 3 AA3 ASN A 90 GLN A 101 1 12 HELIX 4 AA4 ASN A 103 LEU A 108 5 6 HELIX 5 AA5 SER A 109 THR A 129 1 21 HELIX 6 AA6 GLY A 147 ASN A 154 1 8 HELIX 7 AA7 ASP A 157 SER A 170 1 14 HELIX 8 AA8 VAL A 172 ALA A 193 1 22 HELIX 9 AA9 ASP A 198 GLY A 205 1 8 HELIX 10 AB1 ASP A 206 GLU A 208 5 3 HELIX 11 AB2 SER A 218 TYR A 252 1 35 HELIX 12 AB3 TRP A 275 TYR A 279 5 5 HELIX 13 AB4 VAL A 293 ASP A 299 1 7 HELIX 14 AB5 ASP A 303 VAL A 318 1 16 HELIX 15 AB6 THR A 324 SER A 331 1 8 HELIX 16 AB7 MET A 366 TYR A 385 1 20 HELIX 17 AB8 PRO A 389 ARG A 393 5 5 HELIX 18 AB9 GLY A 399 ALA A 413 1 15 HELIX 19 AC1 THR A 414 ILE A 421 1 8 HELIX 20 AC2 GLU A 433 ILE A 446 1 14 HELIX 21 AC3 THR A 449 GLY A 466 1 18 HELIX 22 AC4 GLN A 472 ILE A 484 1 13 HELIX 23 AC5 ASP A 499 LEU A 503 5 5 HELIX 24 AC6 PHE A 512 ALA A 533 1 22 HELIX 25 AC7 SER A 547 ARG A 559 1 13 HELIX 26 AC8 PRO A 565 GLY A 575 1 11 HELIX 27 AC9 VAL A 581 PHE A 588 1 8 HELIX 28 AD1 PHE A 588 ASN A 599 1 12 HELIX 29 AD2 SER A 611 ASP A 615 5 5 HELIX 30 AD3 PHE E 338 ASN E 343 1 6 HELIX 31 AD4 TYR E 365 ALA E 372 1 8 HELIX 32 AD5 SER H 198 LEU H 200 5 3 HELIX 33 AD6 GLN L 81 GLU L 85 5 5 HELIX 34 AD7 SER L 127 ASN L 133 5 7 HELIX 35 AD8 THR L 186 LYS L 191 1 6 SHEET 1 AA1 2 LYS A 131 CYS A 133 0 SHEET 2 AA1 2 CYS A 141 LEU A 143 -1 O LEU A 142 N VAL A 132 SHEET 1 AA2 2 THR A 347 GLY A 352 0 SHEET 2 AA2 2 ASP A 355 LEU A 359 -1 O LEU A 359 N THR A 347 SHEET 1 AA3 4 ASN E 354 ILE E 358 0 SHEET 2 AA3 4 ASN E 394 ILE E 402 -1 O VAL E 395 N ILE E 358 SHEET 3 AA3 4 TYR E 508 GLU E 516 -1 O TYR E 508 N ILE E 402 SHEET 4 AA3 4 GLY E 431 ASN E 437 -1 N CYS E 432 O LEU E 513 SHEET 1 AA4 2 CYS E 361 VAL E 362 0 SHEET 2 AA4 2 VAL E 524 CYS E 525 1 O CYS E 525 N CYS E 361 SHEET 1 AA5 2 LEU E 452 ARG E 454 0 SHEET 2 AA5 2 LEU E 492 SER E 494 -1 O GLN E 493 N TYR E 453 SHEET 1 AA6 2 TYR E 473 GLN E 474 0 SHEET 2 AA6 2 CYS E 488 TYR E 489 -1 O TYR E 489 N TYR E 473 SHEET 1 AA7 4 LEU H 4 GLU H 6 0 SHEET 2 AA7 4 LYS H 19 ALA H 24 -1 O LYS H 23 N VAL H 5 SHEET 3 AA7 4 THR H 78 LEU H 83 -1 O MET H 81 N VAL H 20 SHEET 4 AA7 4 VAL H 68 ASP H 73 -1 N THR H 69 O GLU H 82 SHEET 1 AA8 6 GLU H 10 LYS H 12 0 SHEET 2 AA8 6 THR H 118 VAL H 122 1 O THR H 121 N LYS H 12 SHEET 3 AA8 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 118 SHEET 4 AA8 6 ILE H 34 ALA H 40 -1 N GLN H 39 O VAL H 93 SHEET 5 AA8 6 GLY H 44 ILE H 52 -1 O ILE H 51 N ILE H 34 SHEET 6 AA8 6 ILE H 57 TYR H 60 -1 O ASN H 59 N GLY H 50 SHEET 1 AA9 4 SER H 131 LEU H 135 0 SHEET 2 AA9 4 THR H 146 LYS H 154 -1 O LYS H 154 N SER H 131 SHEET 3 AA9 4 SER H 191 PRO H 196 -1 O VAL H 195 N ALA H 147 SHEET 4 AA9 4 HIS H 175 THR H 176 -1 N HIS H 175 O VAL H 192 SHEET 1 AB1 3 THR H 162 TRP H 165 0 SHEET 2 AB1 3 TYR H 205 HIS H 211 -1 O ASN H 208 N SER H 164 SHEET 3 AB1 3 THR H 216 VAL H 222 -1 O THR H 216 N HIS H 211 SHEET 1 AB2 5 SER L 9 GLY L 12 0 SHEET 2 AB2 5 LYS L 107 VAL L 110 1 O LYS L 107 N VAL L 10 SHEET 3 AB2 5 ALA L 86 ASP L 94 -1 N ALA L 86 O LEU L 108 SHEET 4 AB2 5 HIS L 36 GLN L 40 -1 N TYR L 38 O TYR L 89 SHEET 5 AB2 5 LYS L 47 ILE L 50 -1 O ILE L 50 N TRP L 37 SHEET 1 AB3 4 SER L 9 GLY L 12 0 SHEET 2 AB3 4 LYS L 107 VAL L 110 1 O LYS L 107 N VAL L 10 SHEET 3 AB3 4 ALA L 86 ASP L 94 -1 N ALA L 86 O LEU L 108 SHEET 4 AB3 4 GLY L 99 VAL L 101 -1 O VAL L 101 N SER L 92 SHEET 1 AB4 3 ILE L 20 THR L 23 0 SHEET 2 AB4 3 SER L 72 ILE L 77 -1 O LEU L 75 N ILE L 20 SHEET 3 AB4 3 PHE L 64 SER L 69 -1 N SER L 65 O ALA L 76 SHEET 1 AB5 4 SER L 119 PHE L 123 0 SHEET 2 AB5 4 ALA L 135 PHE L 144 -1 O LEU L 140 N THR L 121 SHEET 3 AB5 4 TYR L 177 LEU L 185 -1 O LEU L 185 N ALA L 135 SHEET 4 AB5 4 SER L 170 LYS L 171 -1 N SER L 170 O ALA L 178 SHEET 1 AB6 4 PRO L 159 VAL L 160 0 SHEET 2 AB6 4 THR L 150 LYS L 154 -1 N TRP L 153 O VAL L 160 SHEET 3 AB6 4 TYR L 196 HIS L 202 -1 O GLN L 199 N ALA L 152 SHEET 4 AB6 4 SER L 205 VAL L 211 -1 O SER L 205 N HIS L 202 SSBOND 1 CYS A 133 CYS A 141 1555 1555 2.03 SSBOND 2 CYS A 344 CYS A 361 1555 1555 2.03 SSBOND 3 CYS A 530 CYS A 542 1555 1555 2.03 SSBOND 4 CYS E 336 CYS E 361 1555 1555 2.03 SSBOND 5 CYS E 379 CYS E 432 1555 1555 2.03 SSBOND 6 CYS E 391 CYS E 525 1555 1555 2.03 SSBOND 7 CYS E 480 CYS E 488 1555 1555 2.03 SSBOND 8 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 9 CYS H 151 CYS H 207 1555 1555 2.03 SSBOND 10 CYS L 22 CYS L 90 1555 1555 2.03 SSBOND 11 CYS L 139 CYS L 198 1555 1555 2.03 LINK ND2 ASN A 53 C1 NAG A 903 1555 1555 1.44 LINK ND2 ASN A 90 C1 NAG A 902 1555 1555 1.44 LINK ND2 ASN A 322 C1 NAG A 904 1555 1555 1.44 LINK ND2 ASN A 546 C1 NAG A 905 1555 1555 1.44 LINK NE2 HIS A 374 ZN ZN A 901 1555 1555 2.30 LINK NE2 HIS A 378 ZN ZN A 901 1555 1555 2.30 LINK OE1 GLU A 402 ZN ZN A 901 1555 1555 1.94 CISPEP 1 PHE H 157 PRO H 158 0 0.98 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