HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-JUN-23 8JQS TITLE CRYOEM STRUCTURE OF SNS1 COMPLEXED WITH FAB 14G5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NON-STRUCTURAL PROTEIN 1; COMPND 3 CHAIN: a, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 14G5 FAB HEAVY CHAIN; COMPND 7 CHAIN: h, H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 14G5 FAB LIGHT CHAIN; COMPND 11 CHAIN: l, L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ZIKA VIRUS; SOURCE 3 ORGANISM_TAXID: 64320; SOURCE 4 GENE: POLY; SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606 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,Q.PAN REVDAT 1 04-DEC-24 8JQS 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. 2.63 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) : 2.630 REMARK 3 NUMBER OF PARTICLES : 406885 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 8JQS 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_1300038581. 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 14G5; ZIKV NS1; REMARK 245 ANTIBODY 14G5 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 : FEI TITAN 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: a, h, l, H, L, 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 HIS a -3 REMARK 465 HIS a -2 REMARK 465 HIS a -1 REMARK 465 HIS a 0 REMARK 465 GLY a 359 REMARK 465 SER a 360 REMARK 465 GLN h 1 REMARK 465 SER l 1 REMARK 465 TYR l 2 REMARK 465 GLU l 3 REMARK 465 THR l 108 REMARK 465 VAL l 109 REMARK 465 LEU l 110 REMARK 465 GLN H 1 REMARK 465 SER L 1 REMARK 465 TYR L 2 REMARK 465 GLU 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 359 REMARK 465 SER A 360 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 a 15 CG CD CE NZ REMARK 470 GLU a 30 CG CD OE1 OE2 REMARK 470 TRP a 32 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP a 32 CZ3 CH2 REMARK 470 ARG a 33 CG CD NE CZ NH1 NH2 REMARK 470 ASP a 34 CG OD1 OD2 REMARK 470 LYS a 98 CG CD CE NZ REMARK 470 GLU a 114 CG CD OE1 OE2 REMARK 470 LYS a 120 CG CD CE NZ REMARK 470 TYR a 126 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG a 129 CG CD NE CZ NH1 NH2 REMARK 470 LYS a 132 CG CD CE NZ REMARK 470 ASP a 161 CG OD1 OD2 REMARK 470 HIS a 162 CG ND1 CD2 CE1 NE2 REMARK 470 GLU a 177 CG CD OE1 OE2 REMARK 470 GLU a 319 CG CD OE1 OE2 REMARK 470 GLU h 10 CG CD OE1 OE2 REMARK 470 LYS h 13 CG CD CE NZ REMARK 470 GLN h 67 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 GLU l 80 CG CD OE1 OE2 REMARK 470 GLU l 82 CG CD OE1 OE2 REMARK 470 LYS l 106 CG CD CE NZ REMARK 470 LYS H 87 CG CD CE NZ REMARK 470 LYS L 29 CG CD CE NZ REMARK 470 GLU L 59 CG CD OE1 OE2 REMARK 470 LYS A 14 CG CD CE NZ REMARK 470 GLU A 16 CG CD OE1 OE2 REMARK 470 ARG A 35 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 37 CG CD CE NZ REMARK 470 LYS A 120 CG CD CE NZ REMARK 470 TYR A 126 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 132 CG CD CE NZ REMARK 470 GLU A 146 CG CD OE1 OE2 REMARK 470 PHE A 167 CG CD1 CD2 CE1 CE2 CZ REMARK 470 HIS A 168 CG ND1 CD2 CE1 NE2 REMARK 470 GLU A 177 CG CD OE1 OE2 REMARK 470 ASP A 212 CG OD1 OD2 REMARK 470 GLU A 293 CG CD OE1 OE2 REMARK 470 GLU A 319 CG CD OE1 OE2 REMARK 470 LYS A 330 CG CD CE NZ 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 LEU a 235 OG SER a 256 2.14 REMARK 500 O PRO A 40 NE1 TRP A 122 2.16 REMARK 500 OG SER a 301 O TYR a 335 2.17 REMARK 500 OG SER A 301 O TYR A 335 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS A 19 CA - CB - SG ANGL. DEV. = 8.7 DEGREES 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 LEU a 83 -8.50 75.30 REMARK 500 ALA a 121 76.39 61.55 REMARK 500 TRP a 122 135.47 -35.68 REMARK 500 ASP a 140 119.78 -38.92 REMARK 500 THR a 143 39.49 -140.39 REMARK 500 PHE a 167 30.19 -98.15 REMARK 500 ASN a 211 -64.12 -96.38 REMARK 500 TRP a 236 65.67 60.49 REMARK 500 ASN a 259 31.88 -94.85 REMARK 500 SER h 56 74.60 -69.52 REMARK 500 ASP l 50 -14.19 72.84 REMARK 500 SER l 51 -16.16 -143.11 REMARK 500 GLU l 59 4.03 -69.17 REMARK 500 GLU l 80 48.99 -80.41 REMARK 500 SER H 56 65.13 -68.74 REMARK 500 ASP L 50 11.67 52.46 REMARK 500 GLU A 84 41.20 -80.82 REMARK 500 GLU A 85 -9.57 -147.11 REMARK 500 PRO A 111 -176.19 -69.54 REMARK 500 GLU A 114 78.62 60.40 REMARK 500 LEU A 115 136.36 -32.66 REMARK 500 ALA A 121 75.39 61.10 REMARK 500 TRP A 122 134.98 -36.40 REMARK 500 ASP A 140 119.95 -38.86 REMARK 500 THR A 143 28.50 -142.46 REMARK 500 ASP A 201 -159.86 -150.77 REMARK 500 ASN A 211 -63.09 -97.25 REMARK 500 GLN A 267 74.26 -101.03 REMARK 500 GLU A 282 146.71 -171.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-36578 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF SNS1 COMPLEXED WITH FAB 14G5 DBREF1 8JQS a 7 360 UNP A0A7U3RUT3_ZIKV DBREF2 8JQS a A0A7U3RUT3 797 1148 DBREF 8JQS h 1 118 PDB 8JQS 8JQS 1 118 DBREF 8JQS l 1 110 PDB 8JQS 8JQS 1 110 DBREF 8JQS H 1 118 PDB 8JQS 8JQS 1 118 DBREF 8JQS L 1 110 PDB 8JQS 8JQS 1 110 DBREF1 8JQS A 7 360 UNP A0A7U3RUT3_ZIKV DBREF2 8JQS A A0A7U3RUT3 797 1148 SEQADV 8JQS HIS a -3 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS a -2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS a -1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS a 0 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS a 1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS a 2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS A -3 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS A -2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS A -1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS A 0 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS A 1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JQS HIS A 2 UNP A0A7U3RUT EXPRESSION TAG 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 h 118 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 h 118 PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER GLY SEQRES 3 h 118 TYR SER PHE THR SER TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4 h 118 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE TYR SEQRES 5 h 118 PRO GLY ASP SER ASP THR ARG TYR SER PRO SER PHE GLN SEQRES 6 h 118 GLY GLN VAL THR MET SER ALA ASP ARG SER ILE SER THR SEQRES 7 h 118 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 h 118 ALA MET TYR TYR CYS ALA ARG SER ASN VAL ASP GLY SER SEQRES 9 h 118 THR ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 h 118 SER SEQRES 1 l 110 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 l 110 PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY ASP ALA SEQRES 3 l 110 LEU PRO LYS GLN TYR ALA PHE TRP TYR GLN GLN LYS PRO SEQRES 4 l 110 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS ASP SER GLU SEQRES 5 l 110 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER SER SEQRES 6 l 110 SER GLY THR THR VAL THR LEU THR ILE SER GLY VAL GLN SEQRES 7 l 110 ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER ALA ASP SEQRES 8 l 110 SER SER ASP THR TYR VAL PRO TYR VAL PHE GLY THR GLY SEQRES 9 l 110 THR LYS VAL THR VAL LEU SEQRES 1 H 118 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 118 PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER GLY SEQRES 3 H 118 TYR SER PHE THR SER TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4 H 118 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE TYR SEQRES 5 H 118 PRO GLY ASP SER ASP THR ARG TYR SER PRO SER PHE GLN SEQRES 6 H 118 GLY GLN VAL THR MET SER ALA ASP ARG SER ILE SER THR SEQRES 7 H 118 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 H 118 ALA MET TYR TYR CYS ALA ARG SER ASN VAL ASP GLY SER SEQRES 9 H 118 THR ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 H 118 SER SEQRES 1 L 110 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 L 110 PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY ASP ALA SEQRES 3 L 110 LEU PRO LYS GLN TYR ALA PHE TRP TYR GLN GLN LYS PRO SEQRES 4 L 110 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS ASP SER GLU SEQRES 5 L 110 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER SER SEQRES 6 L 110 SER GLY THR THR VAL THR LEU THR ILE SER GLY VAL GLN SEQRES 7 L 110 ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER ALA ASP SEQRES 8 L 110 SER SER ASP THR TYR VAL PRO TYR VAL PHE GLY THR GLY SEQRES 9 L 110 THR LYS 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 HELIX 1 AA1 SER a 42 ASP a 56 1 15 HELIX 2 AA2 SER a 65 ILE a 82 1 18 HELIX 3 AA3 PRO a 148 LYS a 150 5 3 HELIX 4 AA4 ASP a 184 VAL a 187 5 4 HELIX 5 AA5 PRO a 230 THR a 234 5 5 HELIX 6 AA6 PRO a 248 ALA a 252 5 5 HELIX 7 AA7 SER a 256 THR a 260 5 5 HELIX 8 AA8 PRO a 345 LEU a 349 5 5 HELIX 9 AA9 SER h 28 TYR h 32 5 5 HELIX 10 AB1 LYS h 87 THR h 91 5 5 HELIX 11 AB2 ALA l 26 GLN l 30 5 5 HELIX 12 AB3 SER H 28 TYR H 32 5 5 HELIX 13 AB4 LYS H 87 THR H 91 5 5 HELIX 14 AB5 ALA L 26 GLN L 30 5 5 HELIX 15 AB6 SER A 42 ASP A 56 1 15 HELIX 16 AB7 SER A 65 GLU A 84 1 20 HELIX 17 AB8 PRO A 148 LYS A 150 5 3 HELIX 18 AB9 ASP A 184 VAL A 187 5 4 HELIX 19 AC1 PRO A 230 THR A 234 5 5 HELIX 20 AC2 PRO A 248 ALA A 252 5 5 HELIX 21 AC3 SER A 256 THR A 260 5 5 HELIX 22 AC4 PRO A 345 LEU A 349 5 5 SHEET 1 AA1 5 HIS a 2 ASP a 11 0 SHEET 2 AA1 5 GLU a 16 TYR a 26 -1 O GLU a 16 N ASP a 11 SHEET 3 AA1 5 THR A 17 TYR A 26 -1 O VAL A 25 N VAL a 23 SHEET 4 AA1 5 HIS A 2 VAL A 10 -1 N SER A 9 O ARG A 18 SHEET 5 AA1 5 HIS a 2 ASP a 11 -1 N CYS a 8 O CYS A 8 SHEET 1 AA2 3 LYS a 37 HIS a 39 0 SHEET 2 AA2 3 SER a 170 VAL a 175 1 O LEU a 173 N HIS a 39 SHEET 3 AA2 3 PHE a 157 VAL a 159 -1 N LEU a 158 O LYS a 174 SHEET 1 AA3 2 GLY a 60 ILE a 61 0 SHEET 2 AA3 2 ARG a 152 ALA a 153 1 O ALA a 153 N GLY a 60 SHEET 1 AA4 2 THR a 91 VAL a 94 0 SHEET 2 AA4 2 SER a 136 VAL a 139 1 O VAL a 139 N VAL a 93 SHEET 1 AA514 CYS a 333 TYR a 335 0 SHEET 2 AA514 SER a 326 ARG a 328 -1 N PHE a 327 O TRP a 334 SHEET 3 AA514 LEU a 277 ARG a 280 -1 N ARG a 280 O SER a 326 SHEET 4 AA514 TRP a 214 LEU a 221 -1 N LEU a 221 O LEU a 277 SHEET 5 AA514 TYR a 204 LYS a 210 -1 N GLU a 207 O ARG a 218 SHEET 6 AA514 GLU a 196 SER a 200 -1 N HIS a 199 O ILE a 206 SHEET 7 AA514 GLY a 189 LYS a 193 -1 N GLY a 189 O SER a 200 SHEET 8 AA514 GLY A 189 LYS A 193 -1 O THR A 190 N VAL a 192 SHEET 9 AA514 GLU A 196 SER A 200 -1 O GLU A 196 N LYS A 193 SHEET 10 AA514 TYR A 204 LYS A 210 -1 O ILE A 206 N HIS A 199 SHEET 11 AA514 TRP A 214 LEU A 221 -1 O ARG A 218 N GLU A 207 SHEET 12 AA514 LEU A 277 PHE A 281 -1 O LEU A 277 N LEU A 221 SHEET 13 AA514 LEU A 325 ARG A 328 -1 O SER A 326 N ARG A 280 SHEET 14 AA514 CYS A 333 TYR A 335 -1 O TRP A 334 N PHE A 327 SHEET 1 AA6 3 LYS a 288 VAL a 291 0 SHEET 2 AA6 3 GLU a 314 CYS a 317 1 O TRP a 315 N LYS a 288 SHEET 3 AA6 3 ARG a 340 PRO a 341 -1 O ARG a 340 N CYS a 316 SHEET 1 AA7 4 GLN h 3 GLN h 6 0 SHEET 2 AA7 4 LEU h 18 SER h 25 -1 O LYS h 23 N VAL h 5 SHEET 3 AA7 4 THR h 78 TRP h 83 -1 O LEU h 81 N ILE h 20 SHEET 4 AA7 4 THR h 69 ASP h 73 -1 N SER h 71 O TYR h 80 SHEET 1 AA8 6 GLU h 10 LYS h 12 0 SHEET 2 AA8 6 THR h 112 VAL h 116 1 O THR h 115 N LYS h 12 SHEET 3 AA8 6 ALA h 92 SER h 99 -1 N ALA h 92 O VAL h 114 SHEET 4 AA8 6 TRP h 33 GLN h 39 -1 N VAL h 37 O TYR h 95 SHEET 5 AA8 6 LEU h 45 TYR h 52 -1 O MET h 48 N TRP h 36 SHEET 6 AA8 6 ASP h 57 ARG h 59 -1 O ASP h 57 N TYR h 52 SHEET 1 AA9 4 GLU h 10 LYS h 12 0 SHEET 2 AA9 4 THR h 112 VAL h 116 1 O THR h 115 N LYS h 12 SHEET 3 AA9 4 ALA h 92 SER h 99 -1 N ALA h 92 O VAL h 114 SHEET 4 AA9 4 THR h 105 TRP h 108 -1 O ASP h 106 N ARG h 98 SHEET 1 AB1 3 ALA l 18 SER l 23 0 SHEET 2 AB1 3 THR l 69 ILE l 74 -1 O LEU l 72 N ILE l 20 SHEET 3 AB1 3 PHE l 61 SER l 65 -1 N SER l 62 O THR l 73 SHEET 1 AB2 4 VAL l 44 ILE l 47 0 SHEET 2 AB2 4 PHE l 33 GLN l 37 -1 N GLN l 36 O VAL l 44 SHEET 3 AB2 4 ASP l 84 ALA l 90 -1 O TYR l 86 N TYR l 35 SHEET 4 AB2 4 TYR l 99 PHE l 101 -1 O VAL l 100 N SER l 89 SHEET 1 AB3 4 GLN H 3 GLN H 6 0 SHEET 2 AB3 4 LEU H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AB3 4 THR H 78 TRP H 83 -1 O TRP H 83 N LEU H 18 SHEET 4 AB3 4 VAL H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AB4 6 GLU H 10 LYS H 12 0 SHEET 2 AB4 6 THR H 112 VAL H 116 1 O THR H 115 N GLU H 10 SHEET 3 AB4 6 ALA H 92 SER H 99 -1 N ALA H 92 O VAL H 114 SHEET 4 AB4 6 TRP H 33 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB4 6 LEU H 45 TYR H 52 -1 O MET H 48 N TRP H 36 SHEET 6 AB4 6 ASP H 57 ARG H 59 -1 O ASP H 57 N TYR H 52 SHEET 1 AB5 4 GLU H 10 LYS H 12 0 SHEET 2 AB5 4 THR H 112 VAL H 116 1 O THR H 115 N GLU H 10 SHEET 3 AB5 4 ALA H 92 SER H 99 -1 N ALA H 92 O VAL H 114 SHEET 4 AB5 4 THR H 105 TRP H 108 -1 O ASP H 106 N ARG H 98 SHEET 1 AB6 5 SER L 9 VAL L 12 0 SHEET 2 AB6 5 THR L 105 VAL L 109 1 O LYS L 106 N VAL L 10 SHEET 3 AB6 5 ASP L 84 ALA L 90 -1 N TYR L 85 O THR L 105 SHEET 4 AB6 5 PHE L 33 GLN L 37 -1 N GLN L 37 O ASP L 84 SHEET 5 AB6 5 VAL L 44 ILE L 47 -1 O VAL L 46 N TRP L 34 SHEET 1 AB7 4 SER L 9 VAL L 12 0 SHEET 2 AB7 4 THR L 105 VAL L 109 1 O LYS L 106 N VAL L 10 SHEET 3 AB7 4 ASP L 84 ALA L 90 -1 N TYR L 85 O THR L 105 SHEET 4 AB7 4 TYR L 99 PHE L 101 -1 O VAL L 100 N SER L 89 SHEET 1 AB8 3 ALA L 18 SER L 23 0 SHEET 2 AB8 3 THR L 69 ILE L 74 -1 O VAL L 70 N CYS L 22 SHEET 3 AB8 3 PHE L 61 SER L 66 -1 N SER L 66 O THR L 69 SHEET 1 AB9 3 TYR A 38 HIS A 39 0 SHEET 2 AB9 3 VAL A 171 VAL A 175 1 O LEU A 173 N HIS A 39 SHEET 3 AB9 3 PHE A 157 ASP A 161 -1 N GLU A 160 O TRP A 172 SHEET 1 AC1 4 VAL A 92 VAL A 94 0 SHEET 2 AC1 4 PHE A 137 VAL A 139 1 O PHE A 137 N VAL A 93 SHEET 3 AC1 4 GLY A 60 ILE A 61 1 N ILE A 61 O VAL A 138 SHEET 4 AC1 4 ARG A 152 ALA A 153 1 O ALA A 153 N GLY A 60 SHEET 1 AC2 3 LYS A 288 VAL A 291 0 SHEET 2 AC2 3 GLU A 314 CYS A 317 1 O TRP A 315 N LYS A 288 SHEET 3 AC2 3 ARG A 340 PRO A 341 -1 O ARG A 340 N CYS A 316 SSBOND 1 CYS a 8 CYS a 19 1555 1555 2.03 SSBOND 2 CYS a 59 CYS a 147 1555 1555 2.03 SSBOND 3 CYS a 183 CYS a 227 1555 1555 2.04 SSBOND 4 CYS a 284 CYS a 333 1555 1555 2.01 SSBOND 5 CYS a 295 CYS a 316 1555 1555 2.04 SSBOND 6 CYS a 317 CYS a 320 1555 1555 2.03 SSBOND 7 CYS h 22 CYS h 96 1555 1555 2.03 SSBOND 8 CYS l 22 CYS l 87 1555 1555 2.04 SSBOND 9 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 10 CYS L 22 CYS L 87 1555 1555 2.04 SSBOND 11 CYS A 8 CYS A 19 1555 1555 2.14 SSBOND 12 CYS A 59 CYS A 147 1555 1555 2.03 SSBOND 13 CYS A 183 CYS A 227 1555 1555 2.04 SSBOND 14 CYS A 284 CYS A 333 1555 1555 2.00 SSBOND 15 CYS A 295 CYS A 316 1555 1555 2.04 SSBOND 16 CYS A 317 CYS A 320 1555 1555 2.03 CISPEP 1 ASN a 99 PRO a 100 0 -7.89 CISPEP 2 MET a 322 PRO a 323 0 0.02 CISPEP 3 ASN A 99 PRO A 100 0 -4.54 CISPEP 4 MET A 322 PRO A 323 0 0.29 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