HEADER VIRAL PROTEIN/IMMUNE SYSTEM 24-DEC-24 9L6C TITLE CRYO-EM STRUCTURE OF DELTA RBD COMPLEXED WITH COND-852, P2C-1F11 AND TITLE 2 S304 FABS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF FAB COND-852; 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 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LIGHT CHAIN OF FAB COND-852; COMPND 11 CHAIN: B; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HEAVY CHAIN OF FAB S304; COMPND 15 CHAIN: H; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: LIGHT CHAIN OF FAB S304; COMPND 19 CHAIN: L; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: HEAVY CHAIN OF FAB P2C-1F11; COMPND 23 CHAIN: D; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 7; COMPND 26 MOLECULE: LIGHT CHAIN OF FAC P2C-1F11; COMPND 27 CHAIN: F; COMPND 28 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 9 2; SOURCE 10 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2; SOURCE 11 ORGANISM_TAXID: 2697049; SOURCE 12 GENE: S, 2; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 33 MOL_ID: 6; SOURCE 34 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 35 ORGANISM_COMMON: HUMAN; SOURCE 36 ORGANISM_TAXID: 9606; SOURCE 37 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 38 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 39 MOL_ID: 7; SOURCE 40 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 41 ORGANISM_COMMON: HUMAN; SOURCE 42 ORGANISM_TAXID: 9606; SOURCE 43 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 44 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS DELTA RBD, COND-852, P2C-1F11, S304 FABS, VIRAL PROTEIN/IMMUNE KEYWDS 2 SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Z.ZHENG,J.BING,L.CONGCONG,Z.BING REVDAT 1 19-MAR-25 9L6C 0 JRNL AUTH Z.ZHENG,J.BING,L.CONGCONG,Z.BING JRNL TITL CRYO-EM STRUCTURE OF DELTA RBD COMPLEXED WITH COND-852, JRNL TITL 2 P2C-1F11 AND S304 FABS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.33 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, SERIALEM, GCTF, UCSF REMARK 3 CHIMERA, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7CDI REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT 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) : 3.330 REMARK 3 NUMBER OF PARTICLES : 116698 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 9L6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 27-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1300055017. 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 : STRUCTURE OF DELTA RBD, COND REMARK 245 -852, S304 AND P2C-1F11 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 : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 3523 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) : 1500.00 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) : 156.25 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: HEPTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, B, H, L, D, F, C 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 GLU B 0 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 PHE A 29 50.47 -90.85 REMARK 500 VAL A 48 -59.15 -120.96 REMARK 500 ASN A 57 43.14 163.13 REMARK 500 ALA A 92 -177.12 -172.29 REMARK 500 LEU A 103 -7.26 72.85 REMARK 500 LEU A 109 130.57 -33.18 REMARK 500 PRO E 337 13.34 -68.37 REMARK 500 PHE E 338 49.88 -77.99 REMARK 500 ALA E 352 58.88 -96.59 REMARK 500 ALA E 372 9.64 59.74 REMARK 500 LEU E 441 -22.96 -141.05 REMARK 500 GLU B 16 -146.37 43.14 REMARK 500 SER B 31 20.08 -146.11 REMARK 500 ALA B 51 -9.33 72.37 REMARK 500 SER B 53 -175.36 -174.15 REMARK 500 SER B 76 -163.33 -79.32 REMARK 500 PRO B 80 46.62 -73.00 REMARK 500 ASP B 82 50.20 -92.11 REMARK 500 SER B 94 170.69 66.16 REMARK 500 ALA L 51 -1.55 65.55 REMARK 500 ASP L 82 53.06 -92.41 REMARK 500 VAL D 100 -75.07 59.91 REMARK 500 SER F 53 13.42 -143.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62852 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF DELTA RBD COMPLEXED WITH COND-852, P2C-1F11 REMARK 900 AND S304 FABS DBREF 9L6C A 1 123 PDB 9L6C 9L6C 1 123 DBREF 9L6C E 333 526 UNP P0DTC2 SPIKE_SARS2 333 526 DBREF 9L6C B 0 108 PDB 9L6C 9L6C 0 108 DBREF 9L6C H 1 119 PDB 9L6C 9L6C 1 119 DBREF 9L6C L 1 108 PDB 9L6C 9L6C 1 108 DBREF 9L6C D 2 116 PDB 9L6C 9L6C 2 116 DBREF 9L6C F 1 107 PDB 9L6C 9L6C 1 107 SEQADV 9L6C ARG E 452 UNP P0DTC2 LEU 452 VARIANT SEQADV 9L6C LYS E 478 UNP P0DTC2 THR 478 VARIANT SEQRES 1 A 123 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 A 123 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 123 PHE THR PHE SER SER TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 A 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE TRP SEQRES 5 A 123 PHE ASP GLY SER ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 123 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 123 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 123 ALA VAL TYR TYR CYS ALA ARG ASP GLY LEU ASP LEU GLU SEQRES 9 A 123 TRP LEU PHE GLY LEU PHE ASP TYR TRP GLY GLN GLY THR SEQRES 10 A 123 LEU VAL THR VAL SER SER SEQRES 1 E 194 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 2 E 194 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SEQRES 3 E 194 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 4 E 194 ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO SEQRES 5 E 194 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 6 E 194 ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE SEQRES 7 E 194 ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR SEQRES 8 E 194 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 9 E 194 ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR SEQRES 10 E 194 ASN TYR ARG TYR ARG LEU PHE ARG LYS SER ASN LEU LYS SEQRES 11 E 194 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 12 E 194 GLY SER LYS PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS SEQRES 13 E 194 TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN SEQRES 14 E 194 GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER SEQRES 15 E 194 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 1 B 109 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 B 109 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 B 109 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 B 109 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 B 109 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 B 109 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 B 109 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 B 109 TYR GLY SER SER PRO GLU LEU THR PHE GLY GLY GLY THR SEQRES 9 B 109 LYS VAL GLU ILE LYS SEQRES 1 H 119 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 119 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 119 PHE THR PHE SER SER TYR ASP MET HIS TRP VAL ARG GLN SEQRES 4 H 119 THR THR GLY LYS GLY LEU GLU TRP VAL SER THR ILE GLY SEQRES 5 H 119 THR ALA GLY ASP THR TYR TYR PRO ASP SER VAL LYS GLY SEQRES 6 H 119 ARG PHE THR ILE SER ARG GLU ASP ALA LYS ASN SER LEU SEQRES 7 H 119 TYR LEU GLN MET ASN SER LEU ARG ALA GLY ASP THR ALA SEQRES 8 H 119 VAL TYR TYR CYS ALA ARG GLY ASP SER SER GLY TYR TYR SEQRES 9 H 119 TYR TYR PHE ASP TYR TRP GLY GLN GLY THR LEU LEU THR SEQRES 10 H 119 VAL SER SEQRES 1 L 108 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 108 ALA VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 108 GLN SER ILE GLY SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 108 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 108 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 108 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 108 GLN PRO GLU ASP PHE ALA ILE TYR TYR CYS GLN GLN SER SEQRES 8 L 108 TYR VAL SER PRO THR TYR THR PHE GLY PRO GLY THR LYS SEQRES 9 L 108 VAL ASP ILE LYS SEQRES 1 D 115 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 D 115 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY ILE SEQRES 3 D 115 THR VAL SER SER ASN TYR MET ASN TRP VAL ARG GLN ALA SEQRES 4 D 115 PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE TYR SER SEQRES 5 D 115 GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY ARG SEQRES 6 D 115 PHE THR ILE SER ARG ASP ASN SER LYS ASN THR LEU TYR SEQRES 7 D 115 LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA VAL SEQRES 8 D 115 TYR HIS CYS ALA ARG ASP LEU VAL VAL TYR GLY MET ASP SEQRES 9 D 115 VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SEQRES 1 F 107 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 F 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 F 107 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 F 107 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 F 107 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 F 107 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 F 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 F 107 TYR GLY SER SER PRO THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 F 107 GLU ILE LYS HET NAG C 1 14 HET NAG C 2 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 8 NAG 2(C8 H15 N O6) HELIX 1 AA1 ASP E 364 LEU E 368 5 5 HELIX 2 AA2 SER E 383 LEU E 390 5 8 HELIX 3 AA3 ASP E 405 ILE E 410 5 6 HELIX 4 AA4 GLY E 416 ASN E 422 1 7 HELIX 5 AA5 THR D 28 ASN D 32 5 5 HELIX 6 AA6 ASP D 61 LYS D 64 5 4 HELIX 7 AA7 ARG D 86 THR D 90 5 5 HELIX 8 AA8 SER F 30 TYR F 33 5 4 SHEET 1 AA1 4 GLN A 3 LEU A 4 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82 SHEET 1 AA2 5 GLY A 10 VAL A 11 0 SHEET 2 AA2 5 LEU A 118 THR A 120 1 O THR A 120 N GLY A 10 SHEET 3 AA2 5 ALA A 92 TYR A 95 -1 N ALA A 92 O VAL A 119 SHEET 4 AA2 5 GLY A 33 ALA A 40 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 5 GLY A 44 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 1 AA3 6 GLY A 10 VAL A 11 0 SHEET 2 AA3 6 LEU A 118 THR A 120 1 O THR A 120 N GLY A 10 SHEET 3 AA3 6 ALA A 92 TYR A 95 -1 N ALA A 92 O VAL A 119 SHEET 4 AA3 6 GLY A 33 ALA A 40 -1 N VAL A 37 O TYR A 95 SHEET 5 AA3 6 ALA A 97 ASP A 99 -1 O ASP A 99 N GLY A 33 SHEET 6 AA3 6 PHE A 110 TRP A 113 -1 O ASP A 111 N ARG A 98 SHEET 1 AA4 6 ASN E 354 ILE E 358 0 SHEET 2 AA4 6 VAL E 395 ARG E 403 -1 O ALA E 397 N LYS E 356 SHEET 3 AA4 6 PRO E 507 SER E 514 -1 O VAL E 512 N ASP E 398 SHEET 4 AA4 6 GLY E 431 ASN E 437 -1 N ILE E 434 O VAL E 511 SHEET 5 AA4 6 PHE E 377 TYR E 380 -1 N TYR E 380 O GLY E 431 SHEET 6 AA4 6 VAL L 93 SER L 94 -1 O SER L 94 N CYS E 379 SHEET 1 AA5 2 ARG 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 2 LEU B 10 SER B 11 0 SHEET 2 AA7 2 VAL B 105 GLU B 106 1 O GLU B 106 N LEU B 10 SHEET 1 AA8 3 ALA B 18 SER B 21 0 SHEET 2 AA8 3 ASP B 70 ILE B 75 -1 O ILE B 75 N ALA B 18 SHEET 3 AA8 3 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AA9 4 ARG B 45 ILE B 48 0 SHEET 2 AA9 4 LEU B 33 GLN B 38 -1 N GLN B 37 O ARG B 45 SHEET 3 AA9 4 VAL B 85 GLN B 90 -1 O GLN B 89 N ALA B 34 SHEET 4 AA9 4 THR B 98 PHE B 99 -1 O THR B 98 N GLN B 90 SHEET 1 AB1 4 VAL H 5 SER H 7 0 SHEET 2 AB1 4 SER H 17 ALA H 23 -1 O SER H 21 N SER H 7 SHEET 3 AB1 4 SER H 77 ASN H 83 -1 O MET H 82 N LEU H 18 SHEET 4 AB1 4 PHE H 67 GLU H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AB2 6 LEU H 11 VAL H 12 0 SHEET 2 AB2 6 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AB2 6 ALA H 91 SER H 101 -1 N ALA H 91 O LEU H 116 SHEET 4 AB2 6 ASP H 33 THR H 40 -1 N VAL H 37 O TYR H 94 SHEET 5 AB2 6 GLY H 44 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AB2 6 THR H 57 TYR H 58 -1 O TYR H 58 N THR H 50 SHEET 1 AB3 4 LEU H 11 VAL H 12 0 SHEET 2 AB3 4 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AB3 4 ALA H 91 SER H 101 -1 N ALA H 91 O LEU H 116 SHEET 4 AB3 4 TYR H 104 TRP H 110 -1 O TYR H 106 N ASP H 99 SHEET 1 AB4 4 MET L 4 SER L 7 0 SHEET 2 AB4 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB4 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AB4 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AB5 6 SER L 10 ALA L 13 0 SHEET 2 AB5 6 THR L 103 ILE L 107 1 O ASP L 106 N ALA L 13 SHEET 3 AB5 6 ILE L 85 GLN L 90 -1 N TYR L 86 O THR L 103 SHEET 4 AB5 6 LEU L 33 GLN L 38 -1 N ASN L 34 O GLN L 89 SHEET 5 AB5 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AB5 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AB6 4 GLN D 3 SER D 7 0 SHEET 2 AB6 4 LEU D 18 SER D 25 -1 O SER D 21 N SER D 7 SHEET 3 AB6 4 THR D 77 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AB6 4 PHE D 67 THR D 68 -1 N THR D 68 O GLN D 81 SHEET 1 AB7 4 GLN D 3 SER D 7 0 SHEET 2 AB7 4 LEU D 18 SER D 25 -1 O SER D 21 N SER D 7 SHEET 3 AB7 4 THR D 77 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AB7 4 ARG D 71 ASP D 72 -1 N ASP D 72 O THR D 77 SHEET 1 AB8 6 GLY D 10 VAL D 12 0 SHEET 2 AB8 6 THR D 111 VAL D 115 1 O THR D 114 N VAL D 12 SHEET 3 AB8 6 ALA D 91 ASP D 98 -1 N TYR D 93 O THR D 111 SHEET 4 AB8 6 TYR D 33 GLN D 39 -1 N TYR D 33 O ASP D 98 SHEET 5 AB8 6 LEU D 45 ILE D 51 -1 O VAL D 48 N TRP D 36 SHEET 6 AB8 6 THR D 57 TYR D 59 -1 O TYR D 58 N LEU D 50 SHEET 1 AB9 4 GLY D 10 VAL D 12 0 SHEET 2 AB9 4 THR D 111 VAL D 115 1 O THR D 114 N VAL D 12 SHEET 3 AB9 4 ALA D 91 ASP D 98 -1 N TYR D 93 O THR D 111 SHEET 4 AB9 4 MET D 104 TRP D 107 -1 O VAL D 106 N ARG D 97 SHEET 1 AC1 2 LEU F 4 THR F 5 0 SHEET 2 AC1 2 ARG F 24 ALA F 25 -1 O ARG F 24 N THR F 5 SHEET 1 AC2 6 THR F 10 LEU F 13 0 SHEET 2 AC2 6 THR F 102 ILE F 106 1 O GLU F 105 N LEU F 13 SHEET 3 AC2 6 VAL F 86 TYR F 92 -1 N TYR F 87 O THR F 102 SHEET 4 AC2 6 ALA F 35 GLN F 39 -1 N TYR F 37 O TYR F 88 SHEET 5 AC2 6 ARG F 46 TYR F 50 -1 O ARG F 46 N GLN F 38 SHEET 6 AC2 6 SER F 54 ARG F 55 -1 O SER F 54 N TYR F 50 SHEET 1 AC3 4 THR F 10 LEU F 13 0 SHEET 2 AC3 4 THR F 102 ILE F 106 1 O GLU F 105 N LEU F 13 SHEET 3 AC3 4 VAL F 86 TYR F 92 -1 N TYR F 87 O THR F 102 SHEET 4 AC3 4 PRO F 96 PHE F 98 -1 O THR F 97 N GLN F 91 SHEET 1 AC4 3 LEU F 21 SER F 22 0 SHEET 2 AC4 3 ASP F 71 ILE F 76 -1 O LEU F 74 N LEU F 21 SHEET 3 AC4 3 PHE F 63 SER F 68 -1 N SER F 64 O THR F 75 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS E 336 CYS E 361 1555 1555 2.03 SSBOND 3 CYS E 379 CYS E 432 1555 1555 2.03 SSBOND 4 CYS E 391 CYS E 525 1555 1555 2.03 SSBOND 5 CYS E 480 CYS E 488 1555 1555 2.03 SSBOND 6 CYS B 22 CYS B 88 1555 1555 2.03 SSBOND 7 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 8 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 9 CYS D 22 CYS D 95 1555 1555 2.03 SSBOND 10 CYS F 23 CYS F 89 1555 1555 2.04 LINK ND2 ASN E 343 C1 NAG C 1 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45 CISPEP 1 SER B 6 PRO B 7 0 -2.52 CISPEP 2 SER L 7 PRO L 8 0 -0.68 CISPEP 3 SER L 94 PRO L 95 0 3.12 CISPEP 4 SER F 7 PRO F 8 0 -1.22 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