HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-JUN-23 8JQN TITLE CRYOEM STRUCTURE OF SNS1 COMPLEXED WITH FAB 2E11 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 2E11 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, h; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 2E11 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, l; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NON-STRUCTURAL PROTEIN 1; COMPND 11 CHAIN: a, A; COMPND 12 ENGINEERED: 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: ZIKA VIRUS; SOURCE 13 ORGANISM_TAXID: 64320; SOURCE 14 GENE: POLY; SOURCE 15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS ZIKV VIRUS, NON-STRUCTURAL PROTEIN 1, ANTIBODY, IMMUNE SYSTEM, VIRAL KEYWDS 2 PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Q.CHEN,P.QI REVDAT 1 11-DEC-24 8JQN 0 JRNL AUTH Q.PAN,X.XING,J.YU,Q.CHEN,H.JIAO,W.ZHANG,Y.WEN,M.GAO,W.ZHAO, JRNL AUTH 2 L.YU,H.HU JRNL TITL STRUCTURAL INSIGHTS INTO THE DISTINCT PROTECTIVE MECHANISMS JRNL TITL 2 OF HUMAN ANTIBODIES TARGETING ZIKV NS1 JRNL REF HLIFE V. 2 527 2024 JRNL REFN ESSN 2949-9283 JRNL DOI 10.1016/J.HLIFE.2024.05.003 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 2.800 REMARK 3 NUMBER OF PARTICLES : 460530 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 8JQN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JUN-23. REMARK 100 THE DEPOSITION ID IS D_1300038580. 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 : THE COMPLEX OF ZIKV NS1 WITH REMARK 245 ANTIBODY 2E11; ANTIBODY 2E11; REMARK 245 ZIKV NS1 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 : 8.50 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 KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 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 : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 100.00 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, h, l, a, A 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 H 1 REMARK 465 LEU L 1 REMARK 465 PRO L 2 REMARK 465 VAL L 3 REMARK 465 SER h 1 REMARK 465 SER h 118 REMARK 465 LEU l 1 REMARK 465 PRO l 2 REMARK 465 VAL l 3 REMARK 465 HIS a -3 REMARK 465 HIS a -2 REMARK 465 HIS a -1 REMARK 465 HIS a 0 REMARK 465 GLY a 353 REMARK 465 SER a 354 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 GLY A 353 REMARK 465 SER A 354 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 ARG H 16 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 16 CG CD OE1 NE2 REMARK 470 ARG L 19 CG CD NE CZ NH1 NH2 REMARK 470 GLU L 59 CG CD OE1 OE2 REMARK 470 ARG h 16 CG CD NE CZ NH1 NH2 REMARK 470 LYS h 76 CG CD CE NZ REMARK 470 ARG h 87 CG CD NE CZ NH1 NH2 REMARK 470 GLN l 16 CG CD OE1 NE2 REMARK 470 GLU l 59 CG CD OE1 OE2 REMARK 470 GLU l 80 CG CD OE1 OE2 REMARK 470 ARG a 29 CG CD NE CZ NH1 NH2 REMARK 470 LYS a 33 CG CD CE NZ REMARK 470 LYS a 116 CG CD CE NZ REMARK 470 LYS a 120 CG CD CE NZ REMARK 470 LYS a 141 CG CD CE NZ REMARK 470 GLU a 258 CG CD OE1 OE2 REMARK 470 LYS a 284 CG CD CE NZ REMARK 470 GLU a 310 CG CD OE1 OE2 REMARK 470 LYS A 11 CG CD CE NZ REMARK 470 GLU A 26 CG CD OE1 OE2 REMARK 470 TRP A 28 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 28 CZ3 CH2 REMARK 470 ARG A 31 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 33 CG CD CE NZ REMARK 470 LYS A 116 CG CD CE NZ REMARK 470 LYS A 120 CG CD CE NZ REMARK 470 TYR A 122 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 125 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 141 CG CD CE NZ REMARK 470 GLU A 289 CG CD OE1 OE2 REMARK 470 GLU A 315 CG CD OE1 OE2 REMARK 470 LYS A 326 CG CD CE NZ 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 VAL H 48 -59.99 -124.10 REMARK 500 TYR H 103 9.11 53.47 REMARK 500 ASP L 50 -13.98 74.23 REMARK 500 SER L 51 -4.47 -144.71 REMARK 500 THR L 68 17.98 -143.71 REMARK 500 VAL h 48 -61.22 -121.67 REMARK 500 ALA l 26 -5.18 68.51 REMARK 500 ASP l 50 -12.42 75.10 REMARK 500 SER l 51 -3.25 -143.94 REMARK 500 GLU l 80 21.97 -77.99 REMARK 500 GLU l 82 109.99 -49.72 REMARK 500 VAL a 25 -62.22 -94.43 REMARK 500 SER a 38 145.14 -170.43 REMARK 500 TRP a 118 54.74 -91.53 REMARK 500 ASP a 157 -90.85 -45.22 REMARK 500 HIS a 158 45.40 -88.63 REMARK 500 ASN a 207 -63.36 -95.36 REMARK 500 ASN a 255 34.97 -99.59 REMARK 500 GLU A 26 -55.82 -121.60 REMARK 500 ALA A 27 -61.00 -104.19 REMARK 500 PRO A 36 -176.04 -64.42 REMARK 500 PRO A 112 43.93 -85.63 REMARK 500 LYS A 120 -166.01 -161.28 REMARK 500 SER A 121 -7.14 77.59 REMARK 500 LEU A 140 48.58 -90.91 REMARK 500 ASN A 207 -81.82 -101.83 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-36576 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF SNS1 COMPLEXED WITH FAB 2E11 DBREF 8JQN H 1 118 PDB 8JQN 8JQN 1 118 DBREF 8JQN L 1 108 PDB 8JQN 8JQN 1 108 DBREF 8JQN h 1 118 PDB 8JQN 8JQN 1 118 DBREF 8JQN l 1 108 PDB 8JQN 8JQN 1 108 DBREF1 8JQN a 3 354 UNP A0A7U3RUT3_ZIKV DBREF2 8JQN a A0A7U3RUT3 797 1148 DBREF1 8JQN A 3 354 UNP A0A7U3RUT3_ZIKV DBREF2 8JQN A A0A7U3RUT3 797 1148 SEQADV 8JQN HIS a -3 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS a -2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS a -1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS a 0 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS a 1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS a 2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS A -3 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS A -2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS A -1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS A 0 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS A 1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQN HIS A 2 UNP A0A7U3RUT EXPRESSION TAG SEQRES 1 H 118 SER VAL GLU LEU ILE GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 118 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 118 PHE THR PHE SER ASN TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 H 118 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA PHE ILE SER SEQRES 5 H 118 TYR ASP GLY SER ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 118 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 118 LEU SER LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 118 ALA LEU TYR TYR CYS ALA ARG VAL PHE ASN GLY TYR GLU SEQRES 9 H 118 GLY ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 H 118 SER SEQRES 1 L 108 LEU PRO VAL LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 L 108 PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY ASP ALA SEQRES 3 L 108 LEU PRO LYS LYS TYR ALA TYR TRP TYR GLN GLN LYS SER SEQRES 4 L 108 GLY GLN ALA PRO VAL LEU VAL ILE TYR GLU ASP SER LYS SEQRES 5 L 108 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER SER SEQRES 6 L 108 SER GLY THR MET ALA THR LEU THR ILE SER GLY ALA GLN SEQRES 7 L 108 VAL GLU ASP GLU ALA ASP TYR TYR CYS TYR SER THR ASP SEQRES 8 L 108 SER SER GLY ASN LEU TYR VAL PHE GLY THR GLY THR LYS SEQRES 9 L 108 VAL THR VAL LEU SEQRES 1 h 118 SER VAL GLU LEU ILE GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 h 118 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 h 118 PHE THR PHE SER ASN TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 h 118 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA PHE ILE SER SEQRES 5 h 118 TYR ASP GLY SER ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 h 118 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 h 118 LEU SER LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 h 118 ALA LEU TYR TYR CYS ALA ARG VAL PHE ASN GLY TYR GLU SEQRES 9 h 118 GLY ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 h 118 SER SEQRES 1 l 108 LEU PRO VAL LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 l 108 PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY ASP ALA SEQRES 3 l 108 LEU PRO LYS LYS TYR ALA TYR TRP TYR GLN GLN LYS SER SEQRES 4 l 108 GLY GLN ALA PRO VAL LEU VAL ILE TYR GLU ASP SER LYS SEQRES 5 l 108 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER SER SEQRES 6 l 108 SER GLY THR MET ALA THR LEU THR ILE SER GLY ALA GLN SEQRES 7 l 108 VAL GLU ASP GLU ALA ASP TYR TYR CYS TYR SER THR ASP SEQRES 8 l 108 SER SER GLY ASN LEU TYR VAL PHE GLY THR GLY THR LYS SEQRES 9 l 108 VAL THR VAL LEU SEQRES 1 a 358 HIS HIS HIS HIS HIS HIS GLY CYS SER VAL ASP PHE SER SEQRES 2 a 358 LYS LYS GLU THR ARG CYS GLY THR GLY VAL PHE VAL TYR SEQRES 3 a 358 ASN ASP VAL GLU ALA TRP ARG ASP ARG TYR LYS TYR HIS SEQRES 4 a 358 PRO ASP SER PRO ARG ARG LEU ALA ALA ALA VAL LYS GLN SEQRES 5 a 358 ALA TRP GLU ASP GLY ILE CYS GLY ILE SER SER VAL SER SEQRES 6 a 358 ARG MET GLU ASN ILE MET TRP ARG SER VAL GLU GLY GLU SEQRES 7 a 358 LEU ASN ALA ILE LEU GLU GLU ASN GLY VAL GLN LEU THR SEQRES 8 a 358 VAL VAL VAL GLY SER VAL LYS ASN PRO MET TRP ARG GLY SEQRES 9 a 358 PRO GLN ARG LEU PRO VAL PRO VAL ASN GLU LEU PRO HIS SEQRES 10 a 358 GLY TRP LYS ALA TRP GLY LYS SER TYR PHE VAL ARG ALA SEQRES 11 a 358 ALA LYS THR ASN ASN SER PHE VAL VAL ASP GLY ASP THR SEQRES 12 a 358 LEU LYS GLU CYS PRO LEU LYS HIS ARG ALA TRP ASN SER SEQRES 13 a 358 PHE LEU VAL GLU ASP HIS GLY PHE GLY VAL PHE HIS THR SEQRES 14 a 358 SER VAL TRP LEU LYS VAL ARG GLU ASP TYR SER LEU GLU SEQRES 15 a 358 CYS ASP PRO ALA VAL ILE GLY THR ALA VAL LYS GLY LYS SEQRES 16 a 358 GLU ALA VAL HIS SER ASP LEU GLY TYR TRP ILE GLU SER SEQRES 17 a 358 GLU LYS ASN ASP THR TRP ARG LEU LYS ARG ALA HIS LEU SEQRES 18 a 358 ILE GLU MET LYS THR CYS GLU TRP PRO LYS SER HIS THR SEQRES 19 a 358 LEU TRP THR ASP GLY ILE GLU GLU SER ASP LEU ILE ILE SEQRES 20 a 358 PRO LYS SER LEU ALA GLY PRO LEU SER HIS HIS ASN THR SEQRES 21 a 358 ARG GLU GLY TYR ARG THR GLN MET LYS GLY PRO TRP HIS SEQRES 22 a 358 SER GLU GLU LEU GLU ILE ARG PHE GLU GLU CYS PRO GLY SEQRES 23 a 358 THR LYS VAL HIS VAL GLU GLU THR CYS GLY THR ARG GLY SEQRES 24 a 358 PRO SER LEU ARG SER THR THR ALA SER GLY ARG VAL ILE SEQRES 25 a 358 GLU GLU TRP CYS CYS ARG GLU CYS THR MET PRO PRO LEU SEQRES 26 a 358 SER PHE ARG ALA LYS ASP GLY CYS TRP TYR GLY MET GLU SEQRES 27 a 358 ILE ARG PRO ARG LYS GLU PRO GLU SER ASN LEU VAL ARG SEQRES 28 a 358 SER MET VAL THR ALA GLY SER SEQRES 1 A 358 HIS HIS HIS HIS HIS HIS GLY CYS SER VAL ASP PHE SER SEQRES 2 A 358 LYS LYS GLU THR ARG CYS GLY THR GLY VAL PHE VAL TYR SEQRES 3 A 358 ASN ASP VAL GLU ALA TRP ARG ASP ARG TYR LYS TYR HIS SEQRES 4 A 358 PRO ASP SER PRO ARG ARG LEU ALA ALA ALA VAL LYS GLN SEQRES 5 A 358 ALA TRP GLU ASP GLY ILE CYS GLY ILE SER SER VAL SER SEQRES 6 A 358 ARG MET GLU ASN ILE MET TRP ARG SER VAL GLU GLY GLU SEQRES 7 A 358 LEU ASN ALA ILE LEU GLU GLU ASN GLY VAL GLN LEU THR SEQRES 8 A 358 VAL VAL VAL GLY SER VAL LYS ASN PRO MET TRP ARG GLY SEQRES 9 A 358 PRO GLN ARG LEU PRO VAL PRO VAL ASN GLU LEU PRO HIS SEQRES 10 A 358 GLY TRP LYS ALA TRP GLY LYS SER TYR PHE VAL ARG ALA SEQRES 11 A 358 ALA LYS THR ASN ASN SER PHE VAL VAL ASP GLY ASP THR SEQRES 12 A 358 LEU LYS GLU CYS PRO LEU LYS HIS ARG ALA TRP ASN SER SEQRES 13 A 358 PHE LEU VAL GLU ASP HIS GLY PHE GLY VAL PHE HIS THR SEQRES 14 A 358 SER VAL TRP LEU LYS VAL ARG GLU ASP TYR SER LEU GLU SEQRES 15 A 358 CYS ASP PRO ALA VAL ILE GLY THR ALA VAL LYS GLY LYS SEQRES 16 A 358 GLU ALA VAL HIS SER ASP LEU GLY TYR TRP ILE GLU SER SEQRES 17 A 358 GLU LYS ASN ASP THR TRP ARG LEU LYS ARG ALA HIS LEU SEQRES 18 A 358 ILE GLU MET LYS THR CYS GLU TRP PRO LYS SER HIS THR SEQRES 19 A 358 LEU TRP THR ASP GLY ILE GLU GLU SER ASP LEU ILE ILE SEQRES 20 A 358 PRO LYS SER LEU ALA GLY PRO LEU SER HIS HIS ASN THR SEQRES 21 A 358 ARG GLU GLY TYR ARG THR GLN MET LYS GLY PRO TRP HIS SEQRES 22 A 358 SER GLU GLU LEU GLU ILE ARG PHE GLU GLU CYS PRO GLY SEQRES 23 A 358 THR LYS VAL HIS VAL GLU GLU THR CYS GLY THR ARG GLY SEQRES 24 A 358 PRO SER LEU ARG SER THR THR ALA SER GLY ARG VAL ILE SEQRES 25 A 358 GLU GLU TRP CYS CYS ARG GLU CYS THR MET PRO PRO LEU SEQRES 26 A 358 SER PHE ARG ALA LYS ASP GLY CYS TRP TYR GLY MET GLU SEQRES 27 A 358 ILE ARG PRO ARG LYS GLU PRO GLU SER ASN LEU VAL ARG SEQRES 28 A 358 SER MET VAL THR ALA GLY SER HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 ASP H 62 LYS H 65 5 4 HELIX 3 AA3 ARG H 87 THR H 91 5 5 HELIX 4 AA4 ALA L 26 LYS L 30 5 5 HELIX 5 AA5 GLN L 78 GLU L 82 5 5 HELIX 6 AA6 THR h 28 TYR h 32 5 5 HELIX 7 AA7 ASP h 62 LYS h 65 5 4 HELIX 8 AA8 ARG h 87 THR h 91 5 5 HELIX 9 AA9 ASN h 101 GLY h 105 5 5 HELIX 10 AB1 GLN l 78 GLU l 82 5 5 HELIX 11 AB2 SER a 38 ASP a 52 1 15 HELIX 12 AB3 SER a 61 ASN a 82 1 22 HELIX 13 AB4 PRO a 144 LYS a 146 5 3 HELIX 14 AB5 ASP a 157 PHE a 160 5 4 HELIX 15 AB6 ASP a 180 VAL a 183 5 4 HELIX 16 AB7 PRO a 226 THR a 230 5 5 HELIX 17 AB8 PRO a 244 ALA a 248 5 5 HELIX 18 AB9 SER a 252 THR a 256 5 5 HELIX 19 AC1 PRO a 341 LEU a 345 5 5 HELIX 20 AC2 SER A 38 ASP A 52 1 15 HELIX 21 AC3 SER A 61 ASN A 82 1 22 HELIX 22 AC4 PRO A 144 LYS A 146 5 3 HELIX 23 AC5 ASP A 180 VAL A 183 5 4 HELIX 24 AC6 PRO A 226 THR A 230 5 5 HELIX 25 AC7 GLU A 237 LEU A 241 5 5 HELIX 26 AC8 PRO A 244 ALA A 248 5 5 HELIX 27 AC9 SER A 252 THR A 256 5 5 HELIX 28 AD1 PRO A 341 LEU A 345 5 5 SHEET 1 AA1 4 GLU H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O ALA H 23 N ILE H 5 SHEET 3 AA1 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA1 4 THR H 69 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA2 6 VAL H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 112 VAL H 116 1 O THR H 115 N VAL H 12 SHEET 3 AA2 6 ALA H 92 ALA H 97 -1 N ALA H 92 O VAL H 114 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 LYS H 58 TYR H 60 -1 O TYR H 59 N PHE H 50 SHEET 1 AA3 5 SER L 9 VAL L 12 0 SHEET 2 AA3 5 THR L 103 VAL L 107 1 O LYS L 104 N VAL L 10 SHEET 3 AA3 5 ALA L 83 THR L 90 -1 N ALA L 83 O VAL L 105 SHEET 4 AA3 5 TYR L 33 GLN L 37 -1 N TYR L 33 O TYR L 88 SHEET 5 AA3 5 VAL L 44 ILE L 47 -1 O VAL L 44 N GLN L 36 SHEET 1 AA4 4 SER L 9 VAL L 12 0 SHEET 2 AA4 4 THR L 103 VAL L 107 1 O LYS L 104 N VAL L 10 SHEET 3 AA4 4 ALA L 83 THR L 90 -1 N ALA L 83 O VAL L 105 SHEET 4 AA4 4 TYR L 97 PHE L 99 -1 O VAL L 98 N SER L 89 SHEET 1 AA5 3 THR L 17 SER L 23 0 SHEET 2 AA5 3 MET L 69 SER L 75 -1 O LEU L 72 N ILE L 20 SHEET 3 AA5 3 PHE L 61 SER L 66 -1 N SER L 62 O THR L 73 SHEET 1 AA6 4 GLU h 3 SER h 7 0 SHEET 2 AA6 4 SER h 17 SER h 25 -1 O ALA h 23 N ILE h 5 SHEET 3 AA6 4 THR h 78 ASN h 84 -1 O MET h 83 N LEU h 18 SHEET 4 AA6 4 PHE h 68 ASP h 73 -1 N ASP h 73 O THR h 78 SHEET 1 AA7 6 VAL h 11 VAL h 12 0 SHEET 2 AA7 6 THR h 112 VAL h 116 1 O THR h 115 N VAL h 12 SHEET 3 AA7 6 ALA h 92 ALA h 97 -1 N ALA h 92 O VAL h 114 SHEET 4 AA7 6 MET h 34 GLN h 39 -1 N VAL h 37 O TYR h 95 SHEET 5 AA7 6 LEU h 45 ILE h 51 -1 O GLU h 46 N ARG h 38 SHEET 6 AA7 6 LYS h 58 TYR h 60 -1 O TYR h 59 N PHE h 50 SHEET 1 AA8 5 SER l 9 VAL l 12 0 SHEET 2 AA8 5 THR l 103 VAL l 107 1 O THR l 106 N VAL l 12 SHEET 3 AA8 5 ASP l 84 THR l 90 -1 N TYR l 85 O THR l 103 SHEET 4 AA8 5 TYR l 33 GLN l 37 -1 N TYR l 33 O TYR l 88 SHEET 5 AA8 5 VAL l 44 ILE l 47 -1 O VAL l 44 N GLN l 36 SHEET 1 AA9 4 SER l 9 VAL l 12 0 SHEET 2 AA9 4 THR l 103 VAL l 107 1 O THR l 106 N VAL l 12 SHEET 3 AA9 4 ASP l 84 THR l 90 -1 N TYR l 85 O THR l 103 SHEET 4 AA9 4 TYR l 97 PHE l 99 -1 O VAL l 98 N SER l 89 SHEET 1 AB1 3 ALA l 18 SER l 23 0 SHEET 2 AB1 3 MET l 69 ILE l 74 -1 O ALA l 70 N CYS l 22 SHEET 3 AB1 3 PHE l 61 SER l 66 -1 N SER l 62 O THR l 73 SHEET 1 AB2 5 HIS a 2 ASP a 7 0 SHEET 2 AB2 5 GLU a 12 TYR a 22 -1 O GLU a 12 N ASP a 7 SHEET 3 AB2 5 GLU A 12 TYR A 22 -1 O VAL A 19 N VAL a 21 SHEET 4 AB2 5 HIS A 1 ASP A 7 -1 N SER A 5 O ARG A 14 SHEET 5 AB2 5 HIS a 2 ASP a 7 -1 N VAL a 6 O HIS A 2 SHEET 1 AB3 4 THR a 87 VAL a 90 0 SHEET 2 AB3 4 SER a 132 VAL a 135 1 O VAL a 135 N VAL a 89 SHEET 3 AB3 4 GLY a 56 ILE a 57 1 N ILE a 57 O VAL a 134 SHEET 4 AB3 4 ARG a 148 ALA a 149 1 O ALA a 149 N GLY a 56 SHEET 1 AB4 2 PHE a 153 VAL a 155 0 SHEET 2 AB4 2 LEU a 169 VAL a 171 -1 O LYS a 170 N LEU a 154 SHEET 1 AB514 CYS a 329 TYR a 331 0 SHEET 2 AB514 LEU a 321 ARG a 324 -1 N PHE a 323 O TRP a 330 SHEET 3 AB514 LEU a 273 PHE a 277 -1 N GLU a 274 O ARG a 324 SHEET 4 AB514 TRP a 210 LEU a 217 -1 N LEU a 217 O LEU a 273 SHEET 5 AB514 TYR a 200 LYS a 206 -1 N GLU a 203 O ARG a 214 SHEET 6 AB514 GLU a 192 SER a 196 -1 N HIS a 195 O ILE a 202 SHEET 7 AB514 GLY a 185 LYS a 189 -1 N LYS a 189 O GLU a 192 SHEET 8 AB514 GLY A 185 LYS A 189 -1 O THR A 186 N VAL a 188 SHEET 9 AB514 GLU A 192 SER A 196 -1 O GLU A 192 N LYS A 189 SHEET 10 AB514 TYR A 200 LYS A 206 -1 O ILE A 202 N HIS A 195 SHEET 11 AB514 TRP A 210 LEU A 217 -1 O ARG A 214 N GLU A 203 SHEET 12 AB514 LEU A 273 PHE A 277 -1 O LEU A 273 N LEU A 217 SHEET 13 AB514 LEU A 321 ARG A 324 -1 O SER A 322 N ARG A 276 SHEET 14 AB514 CYS A 329 TYR A 331 -1 O TRP A 330 N PHE A 323 SHEET 1 AB6 3 LYS a 284 VAL a 287 0 SHEET 2 AB6 3 GLU a 310 CYS a 313 1 O TRP a 311 N LYS a 284 SHEET 3 AB6 3 ARG a 336 PRO a 337 -1 O ARG a 336 N CYS a 312 SHEET 1 AB7 3 TYR A 32 HIS A 35 0 SHEET 2 AB7 3 THR A 165 TRP A 168 1 O VAL A 167 N HIS A 35 SHEET 3 AB7 3 ASP A 157 HIS A 158 -1 N ASP A 157 O TRP A 168 SHEET 1 AB8 4 THR A 87 VAL A 90 0 SHEET 2 AB8 4 SER A 132 VAL A 135 1 O PHE A 133 N THR A 87 SHEET 3 AB8 4 GLY A 56 ILE A 57 1 N ILE A 57 O VAL A 134 SHEET 4 AB8 4 ARG A 148 ALA A 149 1 O ALA A 149 N GLY A 56 SHEET 1 AB9 3 VAL A 285 VAL A 287 0 SHEET 2 AB9 3 TRP A 311 CYS A 313 1 O TRP A 311 N HIS A 286 SHEET 3 AB9 3 ILE A 335 PRO A 337 -1 O ARG A 336 N CYS A 312 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS L 22 CYS L 87 1555 1555 2.03 SSBOND 3 CYS h 22 CYS h 96 1555 1555 2.04 SSBOND 4 CYS l 22 CYS l 87 1555 1555 2.03 SSBOND 5 CYS a 4 CYS a 15 1555 1555 2.03 SSBOND 6 CYS a 55 CYS a 143 1555 1555 2.03 SSBOND 7 CYS a 179 CYS a 223 1555 1555 2.03 SSBOND 8 CYS a 280 CYS a 329 1555 1555 2.03 SSBOND 9 CYS a 291 CYS a 312 1555 1555 2.03 SSBOND 10 CYS a 313 CYS a 316 1555 1555 2.03 SSBOND 11 CYS A 4 CYS A 15 1555 1555 2.03 SSBOND 12 CYS A 55 CYS A 143 1555 1555 2.03 SSBOND 13 CYS A 179 CYS A 223 1555 1555 2.03 SSBOND 14 CYS A 280 CYS A 329 1555 1555 2.03 SSBOND 15 CYS A 291 CYS A 312 1555 1555 2.04 SSBOND 16 CYS A 313 CYS A 316 1555 1555 2.03 CISPEP 1 ASN a 95 PRO a 96 0 -7.56 CISPEP 2 MET a 318 PRO a 319 0 -4.06 CISPEP 3 ASN A 95 PRO A 96 0 -9.90 CISPEP 4 MET A 318 PRO A 319 0 -4.45 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