HEADER VIRAL PROTEIN/IMMUNE SYSTEM 01-JUN-23 8JKH TITLE CRYOEM STRUCTURE OF SNS1 COMPLEXED WITH FAB 4B8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NS1; COMPND 3 CHAIN: A, a, B, b; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: THE HEAVY CHAIN OF ANTIBODY 4B8; COMPND 7 CHAIN: h, H, m, M; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: THE LIGHT CHAIN OF ANTIBODY 4B8; COMPND 11 CHAIN: l, L, n, N; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ZIKA VIRUS; SOURCE 3 ORGANISM_TAXID: 64320; SOURCE 4 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7111; 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: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ZIKV VIRUS, NON-STRUCTURAL PROTEIN 1, ANTIBODY, IMMUNE SYSTEM, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Q.CHEN,Q.PAN REVDAT 1 04-DEC-24 8JKH 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. 2.64 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) : 2.640 REMARK 3 NUMBER OF PARTICLES : 126116 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 8JKH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUN-23. REMARK 100 THE DEPOSITION ID IS D_1300038075. 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 4B8; ZIKV NS1; REMARK 245 ANTIBODY 4B8 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, a, h, l, H, L, B, b, m, n, REMARK 350 AND CHAINS: M, 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 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 HIS a -1 REMARK 465 HIS a 0 REMARK 465 GLU a 26 REMARK 465 ALA a 27 REMARK 465 TRP a 28 REMARK 465 ARG a 29 REMARK 465 LYS a 116 REMARK 465 ALA a 117 REMARK 465 TRP a 118 REMARK 465 GLY a 119 REMARK 465 LYS a 120 REMARK 465 SER a 121 REMARK 465 TYR a 122 REMARK 465 PHE a 123 REMARK 465 GLY a 353 REMARK 465 SER a 354 REMARK 465 GLU h 1 REMARK 465 LYS l 107 REMARK 465 GLU H 1 REMARK 465 SER H 117 REMARK 465 HIS B -3 REMARK 465 HIS B -2 REMARK 465 HIS B -1 REMARK 465 HIS B 0 REMARK 465 GLY B 353 REMARK 465 SER B 354 REMARK 465 HIS b -3 REMARK 465 HIS b -2 REMARK 465 HIS b -1 REMARK 465 HIS b 0 REMARK 465 GLU b 26 REMARK 465 ALA b 27 REMARK 465 TRP b 28 REMARK 465 ARG b 29 REMARK 465 ASP b 30 REMARK 465 ARG b 31 REMARK 465 LYS b 116 REMARK 465 ALA b 117 REMARK 465 TRP b 118 REMARK 465 GLY b 119 REMARK 465 LYS b 120 REMARK 465 SER b 121 REMARK 465 TYR b 122 REMARK 465 PHE b 123 REMARK 465 GLY b 353 REMARK 465 SER b 354 REMARK 465 GLU m 1 REMARK 465 LYS n 107 REMARK 465 GLU M 1 REMARK 465 SER M 117 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 10 CG CD CE NZ REMARK 470 LYS A 11 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 128 CG CD CE NZ REMARK 470 LYS A 284 CG CD CE NZ REMARK 470 GLU A 289 CG CD OE1 OE2 REMARK 470 LYS a 33 CG CD CE NZ REMARK 470 ARG a 125 CG CD NE CZ NH1 NH2 REMARK 470 LYS a 128 CG CD CE NZ REMARK 470 GLU a 173 CG CD OE1 OE2 REMARK 470 GLU a 237 CG CD OE1 OE2 REMARK 470 LYS a 339 CG CD CE NZ REMARK 470 LYS h 43 CG CD CE NZ REMARK 470 GLU l 81 CG CD OE1 OE2 REMARK 470 GLN H 13 CG CD OE1 NE2 REMARK 470 LYS L 42 CG CD CE NZ REMARK 470 LYS B 10 CG CD CE NZ REMARK 470 LYS B 11 CG CD CE NZ REMARK 470 LYS B 116 CG CD CE NZ REMARK 470 LYS B 120 CG CD CE NZ REMARK 470 LYS B 128 CG CD CE NZ REMARK 470 GLU B 173 CG CD OE1 OE2 REMARK 470 LYS B 284 CG CD CE NZ REMARK 470 GLU B 289 CG CD OE1 OE2 REMARK 470 LYS b 33 CG CD CE NZ REMARK 470 ARG b 125 CG CD NE CZ NH1 NH2 REMARK 470 LYS b 128 CG CD CE NZ REMARK 470 GLU b 173 CG CD OE1 OE2 REMARK 470 GLU b 237 CG CD OE1 OE2 REMARK 470 LYS b 339 CG CD CE NZ REMARK 470 GLN m 13 CG CD OE1 NE2 REMARK 470 LYS m 43 CG CD CE NZ REMARK 470 GLU n 81 CG CD OE1 OE2 REMARK 470 GLN M 13 CG CD OE1 NE2 REMARK 470 LYS N 42 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 CD1 TRP A 28 CD1 TRP B 28 1.75 REMARK 500 NE1 TRP A 28 CG TRP B 28 1.99 REMARK 500 NE1 TRP A 28 CB TRP B 28 2.06 REMARK 500 OH TYR A 122 O SER B 304 2.06 REMARK 500 CD1 TRP A 28 CG TRP B 28 2.11 REMARK 500 CG2 THR A 13 CG2 THR B 13 2.12 REMARK 500 OG SER B 297 O TYR B 331 2.13 REMARK 500 CG TRP A 28 NE1 TRP B 28 2.14 REMARK 500 O LEU b 231 OG SER b 252 2.15 REMARK 500 O SER A 304 OH TYR B 122 2.15 REMARK 500 OH TYR A 175 O GLY H 101 2.18 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 GLU A 12 -147.79 -160.44 REMARK 500 PRO A 112 42.82 -89.59 REMARK 500 TYR A 122 110.48 74.32 REMARK 500 ASP A 138 52.93 -92.63 REMARK 500 LEU A 140 46.80 -83.57 REMARK 500 LYS A 141 -37.68 -133.45 REMARK 500 HIS A 164 23.99 -143.43 REMARK 500 ASN A 207 -156.58 -83.73 REMARK 500 PRO a 36 -172.66 -66.04 REMARK 500 ASP a 136 125.25 -39.86 REMARK 500 ASP a 157 -75.65 -31.82 REMARK 500 HIS a 158 43.75 -103.41 REMARK 500 SER a 166 101.61 159.28 REMARK 500 ASN a 207 -63.81 -96.65 REMARK 500 TRP a 232 67.00 60.09 REMARK 500 GLU a 272 115.84 -161.03 REMARK 500 GLU a 315 31.48 -140.19 REMARK 500 VAL h 48 -61.38 -106.79 REMARK 500 SER h 102 44.54 -141.50 REMARK 500 GLN l 27 -149.32 -148.70 REMARK 500 SER l 30 127.10 -35.38 REMARK 500 THR l 31 1.85 52.28 REMARK 500 TRP l 32 72.57 -106.89 REMARK 500 ALA l 50 19.11 59.14 REMARK 500 ALA l 51 -10.59 73.46 REMARK 500 SER l 76 -70.31 -80.30 REMARK 500 ALA l 84 -168.66 -166.66 REMARK 500 GLU l 105 -157.18 -127.25 REMARK 500 ALA H 91 -175.33 -170.27 REMARK 500 SER H 102 46.40 -142.27 REMARK 500 SER L 30 -13.19 76.53 REMARK 500 THR L 31 -25.95 -143.49 REMARK 500 ALA L 51 -10.68 71.32 REMARK 500 SER L 52 -16.06 -141.04 REMARK 500 ALA L 84 -168.12 -160.12 REMARK 500 LYS B 11 98.33 -69.44 REMARK 500 PRO B 112 45.67 -86.11 REMARK 500 LYS B 120 109.61 -53.09 REMARK 500 TYR B 122 103.78 70.58 REMARK 500 LEU B 140 47.61 -83.06 REMARK 500 LYS B 141 -38.13 -130.24 REMARK 500 HIS B 164 26.12 -142.48 REMARK 500 ASN B 207 -157.86 -85.72 REMARK 500 ASP B 208 -39.26 -38.32 REMARK 500 GLU B 278 146.10 -172.88 REMARK 500 PRO b 36 104.33 -53.59 REMARK 500 ASP b 37 -101.70 32.93 REMARK 500 ASP b 136 124.94 -38.96 REMARK 500 SER b 166 115.19 -163.57 REMARK 500 ASN b 207 -61.33 -96.48 REMARK 500 REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-36372 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF SNS1 COMPLEXED WITH FAB 3G2 DBREF1 8JKH A 3 354 UNP A0A7U3RUT3_ZIKV DBREF2 8JKH A A0A7U3RUT3 797 1148 DBREF1 8JKH a 3 354 UNP A0A7U3RUT3_ZIKV DBREF2 8JKH a A0A7U3RUT3 797 1148 DBREF 8JKH h 1 117 PDB 8JKH 8JKH 1 117 DBREF 8JKH l 1 107 PDB 8JKH 8JKH 1 107 DBREF 8JKH H 1 117 PDB 8JKH 8JKH 1 117 DBREF 8JKH L 1 107 PDB 8JKH 8JKH 1 107 DBREF1 8JKH B 3 354 UNP A0A7U3RUT3_ZIKV DBREF2 8JKH B A0A7U3RUT3 797 1148 DBREF1 8JKH b 3 354 UNP A0A7U3RUT3_ZIKV DBREF2 8JKH b A0A7U3RUT3 797 1148 DBREF 8JKH m 1 117 PDB 8JKH 8JKH 1 117 DBREF 8JKH n 1 107 PDB 8JKH 8JKH 1 107 DBREF 8JKH M 1 117 PDB 8JKH 8JKH 1 117 DBREF 8JKH N 1 107 PDB 8JKH 8JKH 1 107 SEQADV 8JKH HIS A -3 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS A -2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS A -1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS A 0 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS A 1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS A 2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS a -3 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS a -2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS a -1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS a 0 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS a 1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS a 2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS B -3 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS B -2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS B -1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS B 0 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS B 1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS B 2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS b -3 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS b -2 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS b -1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS b 0 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS b 1 UNP A0A7U3RUT EXPRESSION TAG SEQADV 8JKH HIS b 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 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 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ILE GLN SEQRES 2 h 117 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 h 117 PHE THR ILE SER SER LYS TYR MET SER TRP VAL ARG GLN SEQRES 4 h 117 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ILE ILE TYR SEQRES 5 h 117 SER SER GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 h 117 ARG PHE THR ILE SER ARG ASP ILE SER LYS ASN THR LEU SEQRES 7 h 117 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 h 117 VAL TYR TYR CYS ALA SER LEU GLY SER GLY SER ALA PHE SEQRES 9 h 117 GLY TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 l 107 ASP ILE VAL MET THR GLN SER PRO SER SER VAL SER ALA SEQRES 2 l 107 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 l 107 GLN GLY ILE SER THR TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 l 107 PRO GLY LYS ALA PRO ARG LEU LEU ILE TYR ALA ALA SER SEQRES 5 l 107 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 l 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 l 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN ALA SEQRES 8 l 107 ASN SER PHE PRO PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 l 107 GLU ILE LYS SEQRES 1 H 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ILE GLN SEQRES 2 H 117 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 117 PHE THR ILE SER SER LYS TYR MET SER TRP VAL ARG GLN SEQRES 4 H 117 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ILE ILE TYR SEQRES 5 H 117 SER SER GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 H 117 ARG PHE THR ILE SER ARG ASP ILE SER LYS ASN THR LEU SEQRES 7 H 117 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 H 117 VAL TYR TYR CYS ALA SER LEU GLY SER GLY SER ALA PHE SEQRES 9 H 117 GLY TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 L 107 ASP ILE VAL MET THR GLN SER PRO SER SER VAL SER ALA SEQRES 2 L 107 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 107 GLN GLY ILE SER THR TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 107 PRO GLY LYS ALA PRO ARG LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 107 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN ALA SEQRES 8 L 107 ASN SER PHE PRO PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 L 107 GLU ILE LYS SEQRES 1 B 358 HIS HIS HIS HIS HIS HIS GLY CYS SER VAL ASP PHE SER SEQRES 2 B 358 LYS LYS GLU THR ARG CYS GLY THR GLY VAL PHE VAL TYR SEQRES 3 B 358 ASN ASP VAL GLU ALA TRP ARG ASP ARG TYR LYS TYR HIS SEQRES 4 B 358 PRO ASP SER PRO ARG ARG LEU ALA ALA ALA VAL LYS GLN SEQRES 5 B 358 ALA TRP GLU ASP GLY ILE CYS GLY ILE SER SER VAL SER SEQRES 6 B 358 ARG MET GLU ASN ILE MET TRP ARG SER VAL GLU GLY GLU SEQRES 7 B 358 LEU ASN ALA ILE LEU GLU GLU ASN GLY VAL GLN LEU THR SEQRES 8 B 358 VAL VAL VAL GLY SER VAL LYS ASN PRO MET TRP ARG GLY SEQRES 9 B 358 PRO GLN ARG LEU PRO VAL PRO VAL ASN GLU LEU PRO HIS SEQRES 10 B 358 GLY TRP LYS ALA TRP GLY LYS SER TYR PHE VAL ARG ALA SEQRES 11 B 358 ALA LYS THR ASN ASN SER PHE VAL VAL ASP GLY ASP THR SEQRES 12 B 358 LEU LYS GLU CYS PRO LEU LYS HIS ARG ALA TRP ASN SER SEQRES 13 B 358 PHE LEU VAL GLU ASP HIS GLY PHE GLY VAL PHE HIS THR SEQRES 14 B 358 SER VAL TRP LEU LYS VAL ARG GLU ASP TYR SER LEU GLU SEQRES 15 B 358 CYS ASP PRO ALA VAL ILE GLY THR ALA VAL LYS GLY LYS SEQRES 16 B 358 GLU ALA VAL HIS SER ASP LEU GLY TYR TRP ILE GLU SER SEQRES 17 B 358 GLU LYS ASN ASP THR TRP ARG LEU LYS ARG ALA HIS LEU SEQRES 18 B 358 ILE GLU MET LYS THR CYS GLU TRP PRO LYS SER HIS THR SEQRES 19 B 358 LEU TRP THR ASP GLY ILE GLU GLU SER ASP LEU ILE ILE SEQRES 20 B 358 PRO LYS SER LEU ALA GLY PRO LEU SER HIS HIS ASN THR SEQRES 21 B 358 ARG GLU GLY TYR ARG THR GLN MET LYS GLY PRO TRP HIS SEQRES 22 B 358 SER GLU GLU LEU GLU ILE ARG PHE GLU GLU CYS PRO GLY SEQRES 23 B 358 THR LYS VAL HIS VAL GLU GLU THR CYS GLY THR ARG GLY SEQRES 24 B 358 PRO SER LEU ARG SER THR THR ALA SER GLY ARG VAL ILE SEQRES 25 B 358 GLU GLU TRP CYS CYS ARG GLU CYS THR MET PRO PRO LEU SEQRES 26 B 358 SER PHE ARG ALA LYS ASP GLY CYS TRP TYR GLY MET GLU SEQRES 27 B 358 ILE ARG PRO ARG LYS GLU PRO GLU SER ASN LEU VAL ARG SEQRES 28 B 358 SER MET VAL THR ALA GLY SER SEQRES 1 b 358 HIS HIS HIS HIS HIS HIS GLY CYS SER VAL ASP PHE SER SEQRES 2 b 358 LYS LYS GLU THR ARG CYS GLY THR GLY VAL PHE VAL TYR SEQRES 3 b 358 ASN ASP VAL GLU ALA TRP ARG ASP ARG TYR LYS TYR HIS SEQRES 4 b 358 PRO ASP SER PRO ARG ARG LEU ALA ALA ALA VAL LYS GLN SEQRES 5 b 358 ALA TRP GLU ASP GLY ILE CYS GLY ILE SER SER VAL SER SEQRES 6 b 358 ARG MET GLU ASN ILE MET TRP ARG SER VAL GLU GLY GLU SEQRES 7 b 358 LEU ASN ALA ILE LEU GLU GLU ASN GLY VAL GLN LEU THR SEQRES 8 b 358 VAL VAL VAL GLY SER VAL LYS ASN PRO MET TRP ARG GLY SEQRES 9 b 358 PRO GLN ARG LEU PRO VAL PRO VAL ASN GLU LEU PRO HIS SEQRES 10 b 358 GLY TRP LYS ALA TRP GLY LYS SER TYR PHE VAL ARG ALA SEQRES 11 b 358 ALA LYS THR ASN ASN SER PHE VAL VAL ASP GLY ASP THR SEQRES 12 b 358 LEU LYS GLU CYS PRO LEU LYS HIS ARG ALA TRP ASN SER SEQRES 13 b 358 PHE LEU VAL GLU ASP HIS GLY PHE GLY VAL PHE HIS THR SEQRES 14 b 358 SER VAL TRP LEU LYS VAL ARG GLU ASP TYR SER LEU GLU SEQRES 15 b 358 CYS ASP PRO ALA VAL ILE GLY THR ALA VAL LYS GLY LYS SEQRES 16 b 358 GLU ALA VAL HIS SER ASP LEU GLY TYR TRP ILE GLU SER SEQRES 17 b 358 GLU LYS ASN ASP THR TRP ARG LEU LYS ARG ALA HIS LEU SEQRES 18 b 358 ILE GLU MET LYS THR CYS GLU TRP PRO LYS SER HIS THR SEQRES 19 b 358 LEU TRP THR ASP GLY ILE GLU GLU SER ASP LEU ILE ILE SEQRES 20 b 358 PRO LYS SER LEU ALA GLY PRO LEU SER HIS HIS ASN THR SEQRES 21 b 358 ARG GLU GLY TYR ARG THR GLN MET LYS GLY PRO TRP HIS SEQRES 22 b 358 SER GLU GLU LEU GLU ILE ARG PHE GLU GLU CYS PRO GLY SEQRES 23 b 358 THR LYS VAL HIS VAL GLU GLU THR CYS GLY THR ARG GLY SEQRES 24 b 358 PRO SER LEU ARG SER THR THR ALA SER GLY ARG VAL ILE SEQRES 25 b 358 GLU GLU TRP CYS CYS ARG GLU CYS THR MET PRO PRO LEU SEQRES 26 b 358 SER PHE ARG ALA LYS ASP GLY CYS TRP TYR GLY MET GLU SEQRES 27 b 358 ILE ARG PRO ARG LYS GLU PRO GLU SER ASN LEU VAL ARG SEQRES 28 b 358 SER MET VAL THR ALA GLY SER SEQRES 1 m 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ILE GLN SEQRES 2 m 117 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 m 117 PHE THR ILE SER SER LYS TYR MET SER TRP VAL ARG GLN SEQRES 4 m 117 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ILE ILE TYR SEQRES 5 m 117 SER SER GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 m 117 ARG PHE THR ILE SER ARG ASP ILE SER LYS ASN THR LEU SEQRES 7 m 117 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 m 117 VAL TYR TYR CYS ALA SER LEU GLY SER GLY SER ALA PHE SEQRES 9 m 117 GLY TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 n 107 ASP ILE VAL MET THR GLN SER PRO SER SER VAL SER ALA SEQRES 2 n 107 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 n 107 GLN GLY ILE SER THR TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 n 107 PRO GLY LYS ALA PRO ARG LEU LEU ILE TYR ALA ALA SER SEQRES 5 n 107 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 n 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 n 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN ALA SEQRES 8 n 107 ASN SER PHE PRO PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 n 107 GLU ILE LYS SEQRES 1 M 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ILE GLN SEQRES 2 M 117 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 M 117 PHE THR ILE SER SER LYS TYR MET SER TRP VAL ARG GLN SEQRES 4 M 117 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ILE ILE TYR SEQRES 5 M 117 SER SER GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 M 117 ARG PHE THR ILE SER ARG ASP ILE SER LYS ASN THR LEU SEQRES 7 M 117 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 M 117 VAL TYR TYR CYS ALA SER LEU GLY SER GLY SER ALA PHE SEQRES 9 M 117 GLY TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 N 107 ASP ILE VAL MET THR GLN SER PRO SER SER VAL SER ALA SEQRES 2 N 107 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 N 107 GLN GLY ILE SER THR TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 N 107 PRO GLY LYS ALA PRO ARG LEU LEU ILE TYR ALA ALA SER SEQRES 5 N 107 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 N 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 N 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN ALA SEQRES 8 N 107 ASN SER PHE PRO PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 N 107 GLU ILE LYS HELIX 1 AA1 SER A 38 GLY A 53 1 16 HELIX 2 AA2 SER A 61 GLU A 81 1 21 HELIX 3 AA3 PRO A 144 LYS A 146 5 3 HELIX 4 AA4 PRO A 226 THR A 230 5 5 HELIX 5 AA5 GLU A 237 LEU A 241 5 5 HELIX 6 AA6 PRO A 244 ALA A 248 5 5 HELIX 7 AA7 SER A 252 THR A 256 5 5 HELIX 8 AA8 PRO A 341 LEU A 345 5 5 HELIX 9 AA9 ARG a 41 GLY a 53 1 13 HELIX 10 AB1 SER a 61 ASN a 82 1 22 HELIX 11 AB2 PRO a 144 LYS a 146 5 3 HELIX 12 AB3 ASP a 180 VAL a 183 5 4 HELIX 13 AB4 PRO a 226 THR a 230 5 5 HELIX 14 AB5 PRO a 244 ALA a 248 5 5 HELIX 15 AB6 SER a 252 THR a 256 5 5 HELIX 16 AB7 THR h 28 LYS h 32 5 5 HELIX 17 AB8 ASP h 61 LYS h 64 5 4 HELIX 18 AB9 ARG h 86 THR h 90 5 5 HELIX 19 AC1 THR H 28 LYS H 32 5 5 HELIX 20 AC2 ASP H 61 LYS H 64 5 4 HELIX 21 AC3 ARG H 86 THR H 90 5 5 HELIX 22 AC4 SER B 38 GLY B 53 1 16 HELIX 23 AC5 SER B 61 ASN B 82 1 22 HELIX 24 AC6 PRO B 144 LYS B 146 5 3 HELIX 25 AC7 ASP B 180 VAL B 183 5 4 HELIX 26 AC8 PRO B 226 THR B 230 5 5 HELIX 27 AC9 PRO B 244 ALA B 248 5 5 HELIX 28 AD1 SER B 252 THR B 256 5 5 HELIX 29 AD2 PRO B 341 LEU B 345 5 5 HELIX 30 AD3 SER b 38 GLY b 53 1 16 HELIX 31 AD4 SER b 61 ASN b 82 1 22 HELIX 32 AD5 PRO b 144 LYS b 146 5 3 HELIX 33 AD6 ASP b 180 VAL b 183 5 4 HELIX 34 AD7 PRO b 226 THR b 230 5 5 HELIX 35 AD8 PRO b 244 ALA b 248 5 5 HELIX 36 AD9 SER b 252 THR b 256 5 5 HELIX 37 AE1 PRO b 341 LEU b 345 5 5 HELIX 38 AE2 THR m 28 LYS m 32 5 5 HELIX 39 AE3 ASP m 61 LYS m 64 5 4 HELIX 40 AE4 ARG m 86 THR m 90 5 5 HELIX 41 AE5 THR M 28 LYS M 32 5 5 HELIX 42 AE6 ASP M 61 LYS M 64 5 4 HELIX 43 AE7 ARG M 86 THR M 90 5 5 HELIX 44 AE8 GLN N 79 PHE N 83 5 5 SHEET 1 AA1 5 HIS A 2 ASP A 7 0 SHEET 2 AA1 5 GLU A 12 TYR A 22 -1 O ARG A 14 N SER A 5 SHEET 3 AA1 5 GLU a 12 TYR a 22 -1 O VAL a 21 N VAL A 19 SHEET 4 AA1 5 HIS a 2 ASP a 7 -1 N ASP a 7 O GLU a 12 SHEET 5 AA1 5 HIS A 2 ASP A 7 -1 N HIS A 2 O VAL a 6 SHEET 1 AA2 3 LYS A 33 HIS A 35 0 SHEET 2 AA2 3 SER A 166 VAL A 171 1 O VAL A 167 N HIS A 35 SHEET 3 AA2 3 PHE A 153 ASP A 157 -1 N GLU A 156 O TRP A 168 SHEET 1 AA3 4 THR A 87 VAL A 90 0 SHEET 2 AA3 4 SER A 132 VAL A 135 1 O PHE A 133 N THR A 87 SHEET 3 AA3 4 GLY A 56 ILE A 57 1 N ILE A 57 O VAL A 134 SHEET 4 AA3 4 ARG A 148 ALA A 149 1 O ALA A 149 N GLY A 56 SHEET 1 AA415 LEU A 298 ARG A 299 0 SHEET 2 AA415 CYS A 329 TYR A 331 -1 O TYR A 331 N LEU A 298 SHEET 3 AA415 LEU A 321 ARG A 324 -1 N PHE A 323 O TRP A 330 SHEET 4 AA415 LEU A 273 PHE A 277 -1 N ARG A 276 O SER A 322 SHEET 5 AA415 TRP A 210 LEU A 217 -1 N ALA A 215 O ILE A 275 SHEET 6 AA415 TYR A 200 LYS A 206 -1 N GLU A 203 O ARG A 214 SHEET 7 AA415 GLU A 192 SER A 196 -1 N HIS A 195 O ILE A 202 SHEET 8 AA415 GLY A 185 LYS A 189 -1 N ALA A 187 O VAL A 194 SHEET 9 AA415 GLY a 185 LYS a 189 -1 O THR a 186 N VAL A 188 SHEET 10 AA415 GLU a 192 SER a 196 -1 O GLU a 192 N LYS a 189 SHEET 11 AA415 TYR a 200 LYS a 206 -1 O ILE a 202 N HIS a 195 SHEET 12 AA415 TRP a 210 LEU a 217 -1 O ARG a 214 N GLU a 203 SHEET 13 AA415 LEU a 273 PHE a 277 -1 O ILE a 275 N ALA a 215 SHEET 14 AA415 LEU a 321 PHE a 323 -1 O SER a 322 N ARG a 276 SHEET 15 AA415 TRP a 330 TYR a 331 -1 O TRP a 330 N PHE a 323 SHEET 1 AA5 3 LYS A 284 VAL A 287 0 SHEET 2 AA5 3 GLU A 310 CYS A 313 1 O TRP A 311 N LYS A 284 SHEET 3 AA5 3 ARG A 336 PRO A 337 -1 O ARG A 336 N CYS A 312 SHEET 1 AA6 2 GLY a 56 ILE a 57 0 SHEET 2 AA6 2 ARG a 148 ALA a 149 1 O ALA a 149 N GLY a 56 SHEET 1 AA7 2 THR a 87 VAL a 90 0 SHEET 2 AA7 2 SER a 132 VAL a 135 1 O VAL a 135 N VAL a 89 SHEET 1 AA8 2 PHE a 153 VAL a 155 0 SHEET 2 AA8 2 LEU a 169 VAL a 171 -1 O LYS a 170 N LEU a 154 SHEET 1 AA9 3 LYS a 284 VAL a 287 0 SHEET 2 AA9 3 GLU a 310 CYS a 313 1 O TRP a 311 N LYS a 284 SHEET 3 AA9 3 ILE a 335 PRO a 337 -1 O ARG a 336 N CYS a 312 SHEET 1 AB1 4 GLN h 3 GLU h 6 0 SHEET 2 AB1 4 LEU h 18 SER h 25 -1 O SER h 25 N GLN h 3 SHEET 3 AB1 4 THR h 77 MET h 82 -1 O LEU h 78 N CYS h 22 SHEET 4 AB1 4 THR h 68 ASP h 72 -1 N ASP h 72 O THR h 77 SHEET 1 AB2 6 LEU h 11 ILE h 12 0 SHEET 2 AB2 6 LEU h 112 VAL h 115 1 O THR h 114 N ILE h 12 SHEET 3 AB2 6 ALA h 91 LEU h 98 -1 N ALA h 91 O VAL h 113 SHEET 4 AB2 6 TYR h 33 GLN h 39 -1 N VAL h 37 O TYR h 94 SHEET 5 AB2 6 LEU h 45 ILE h 51 -1 O ILE h 51 N MET h 34 SHEET 6 AB2 6 THR h 57 TYR h 59 -1 O TYR h 58 N ILE h 50 SHEET 1 AB3 4 MET l 4 SER l 7 0 SHEET 2 AB3 4 VAL l 19 ALA l 25 -1 O ARG l 24 N THR l 5 SHEET 3 AB3 4 ASP l 70 ILE l 75 -1 O LEU l 73 N ILE l 21 SHEET 4 AB3 4 PHE l 62 SER l 67 -1 N SER l 63 O THR l 74 SHEET 1 AB4 6 SER l 10 SER l 12 0 SHEET 2 AB4 6 THR l 102 GLU l 105 1 O LYS l 103 N VAL l 11 SHEET 3 AB4 6 THR l 85 GLN l 90 -1 N TYR l 86 O THR l 102 SHEET 4 AB4 6 LEU l 33 GLN l 38 -1 N GLN l 38 O THR l 85 SHEET 5 AB4 6 ARG l 45 TYR l 49 -1 O LEU l 47 N TRP l 35 SHEET 6 AB4 6 SER l 53 LEU l 54 -1 O SER l 53 N TYR l 49 SHEET 1 AB5 4 GLN H 3 VAL H 5 0 SHEET 2 AB5 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AB5 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AB5 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AB6 6 LEU H 11 ILE H 12 0 SHEET 2 AB6 6 THR H 111 VAL H 115 1 O THR H 114 N ILE H 12 SHEET 3 AB6 6 ALA H 91 SER H 100 -1 N TYR H 93 O THR H 111 SHEET 4 AB6 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 94 SHEET 5 AB6 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AB6 6 THR H 57 TYR H 59 -1 O TYR H 58 N ILE H 50 SHEET 1 AB7 4 LEU H 11 ILE H 12 0 SHEET 2 AB7 4 THR H 111 VAL H 115 1 O THR H 114 N ILE H 12 SHEET 3 AB7 4 ALA H 91 SER H 100 -1 N TYR H 93 O THR H 111 SHEET 4 AB7 4 ALA H 103 TRP H 107 -1 O GLY H 105 N SER H 97 SHEET 1 AB8 4 MET L 4 SER L 7 0 SHEET 2 AB8 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB8 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB8 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB9 6 SER L 10 ALA L 13 0 SHEET 2 AB9 6 THR L 102 ILE L 106 1 O GLU L 105 N VAL L 11 SHEET 3 AB9 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB9 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB9 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB9 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AC1 4 SER L 10 ALA L 13 0 SHEET 2 AC1 4 THR L 102 ILE L 106 1 O GLU L 105 N VAL L 11 SHEET 3 AC1 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC1 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AC2 5 HIS B 2 ASP B 7 0 SHEET 2 AC2 5 GLU B 12 TYR B 22 -1 O ARG B 14 N SER B 5 SHEET 3 AC2 5 GLU b 12 TYR b 22 -1 O VAL b 21 N VAL B 19 SHEET 4 AC2 5 HIS b 2 ASP b 7 -1 N SER b 5 O ARG b 14 SHEET 5 AC2 5 HIS B 2 ASP B 7 -1 N HIS B 2 O VAL b 6 SHEET 1 AC3 3 LYS B 33 PRO B 36 0 SHEET 2 AC3 3 SER B 166 VAL B 171 1 O VAL B 167 N HIS B 35 SHEET 3 AC3 3 PHE B 153 ASP B 157 -1 N GLU B 156 O TRP B 168 SHEET 1 AC4 2 GLY B 56 ILE B 57 0 SHEET 2 AC4 2 ARG B 148 ALA B 149 1 O ALA B 149 N GLY B 56 SHEET 1 AC5 2 THR B 87 VAL B 90 0 SHEET 2 AC5 2 SER B 132 VAL B 135 1 O PHE B 133 N THR B 87 SHEET 1 AC614 CYS B 329 TYR B 331 0 SHEET 2 AC614 LEU B 321 ARG B 324 -1 N PHE B 323 O TRP B 330 SHEET 3 AC614 LEU B 273 PHE B 277 -1 N ARG B 276 O SER B 322 SHEET 4 AC614 TRP B 210 LEU B 217 -1 N LEU B 217 O LEU B 273 SHEET 5 AC614 TYR B 200 LYS B 206 -1 N GLU B 203 O ARG B 214 SHEET 6 AC614 GLU B 192 SER B 196 -1 N HIS B 195 O ILE B 202 SHEET 7 AC614 GLY B 185 LYS B 189 -1 N ALA B 187 O VAL B 194 SHEET 8 AC614 GLY b 185 LYS b 189 -1 O VAL b 188 N THR B 186 SHEET 9 AC614 GLU b 192 SER b 196 -1 O GLU b 192 N LYS b 189 SHEET 10 AC614 TYR b 200 LYS b 206 -1 O ILE b 202 N HIS b 195 SHEET 11 AC614 TRP b 210 LEU b 217 -1 O ARG b 214 N GLU b 203 SHEET 12 AC614 LEU b 273 PHE b 277 -1 O LEU b 273 N LEU b 217 SHEET 13 AC614 LEU b 321 ALA b 325 -1 O SER b 322 N ARG b 276 SHEET 14 AC614 GLY b 328 TYR b 331 -1 O TRP b 330 N PHE b 323 SHEET 1 AC7 3 LYS B 284 VAL B 287 0 SHEET 2 AC7 3 GLU B 310 CYS B 313 1 O TRP B 311 N HIS B 286 SHEET 3 AC7 3 ILE B 335 PRO B 337 -1 O ARG B 336 N CYS B 312 SHEET 1 AC8 3 HIS b 35 PRO b 36 0 SHEET 2 AC8 3 TRP b 168 VAL b 171 1 O LEU b 169 N HIS b 35 SHEET 3 AC8 3 PHE b 153 VAL b 155 -1 N LEU b 154 O LYS b 170 SHEET 1 AC9 2 GLY b 56 ILE b 57 0 SHEET 2 AC9 2 ARG b 148 ALA b 149 1 O ALA b 149 N GLY b 56 SHEET 1 AD1 2 THR b 87 VAL b 89 0 SHEET 2 AD1 2 SER b 132 VAL b 134 1 O PHE b 133 N THR b 87 SHEET 1 AD2 3 VAL b 285 VAL b 287 0 SHEET 2 AD2 3 TRP b 311 CYS b 313 1 O CYS b 313 N HIS b 286 SHEET 3 AD2 3 ARG b 336 PRO b 337 -1 O ARG b 336 N CYS b 312 SHEET 1 AD3 4 GLN m 3 GLU m 6 0 SHEET 2 AD3 4 LEU m 18 SER m 25 -1 O ALA m 23 N VAL m 5 SHEET 3 AD3 4 THR m 77 MET m 82 -1 O MET m 82 N LEU m 18 SHEET 4 AD3 4 THR m 68 ASP m 72 -1 N THR m 68 O GLN m 81 SHEET 1 AD4 6 LEU m 11 ILE m 12 0 SHEET 2 AD4 6 THR m 111 VAL m 115 1 O THR m 114 N ILE m 12 SHEET 3 AD4 6 ALA m 91 GLY m 99 -1 N TYR m 93 O THR m 111 SHEET 4 AD4 6 TYR m 33 GLN m 39 -1 N VAL m 37 O TYR m 94 SHEET 5 AD4 6 LEU m 45 ILE m 51 -1 O VAL m 48 N TRP m 36 SHEET 6 AD4 6 THR m 57 TYR m 59 -1 O TYR m 58 N ILE m 50 SHEET 1 AD5 4 LEU m 11 ILE m 12 0 SHEET 2 AD5 4 THR m 111 VAL m 115 1 O THR m 114 N ILE m 12 SHEET 3 AD5 4 ALA m 91 GLY m 99 -1 N TYR m 93 O THR m 111 SHEET 4 AD5 4 ALA m 103 PHE m 104 -1 O ALA m 103 N GLY m 99 SHEET 1 AD6 4 THR n 5 SER n 7 0 SHEET 2 AD6 4 VAL n 19 ARG n 24 -1 O ARG n 24 N THR n 5 SHEET 3 AD6 4 ASP n 70 ILE n 75 -1 O LEU n 73 N ILE n 21 SHEET 4 AD6 4 PHE n 62 SER n 67 -1 N SER n 63 O THR n 74 SHEET 1 AD7 6 SER n 10 SER n 12 0 SHEET 2 AD7 6 THR n 102 GLU n 105 1 O GLU n 105 N VAL n 11 SHEET 3 AD7 6 THR n 85 GLN n 90 -1 N TYR n 86 O THR n 102 SHEET 4 AD7 6 LEU n 33 GLN n 38 -1 N GLN n 38 O THR n 85 SHEET 5 AD7 6 ARG n 45 TYR n 49 -1 O LEU n 47 N TRP n 35 SHEET 6 AD7 6 SER n 53 LEU n 54 -1 O SER n 53 N TYR n 49 SHEET 1 AD8 4 GLN M 3 VAL M 5 0 SHEET 2 AD8 4 LEU M 18 SER M 25 -1 O ALA M 23 N VAL M 5 SHEET 3 AD8 4 THR M 77 MET M 82 -1 O MET M 82 N LEU M 18 SHEET 4 AD8 4 PHE M 67 ASP M 72 -1 N THR M 68 O GLN M 81 SHEET 1 AD9 6 LEU M 11 ILE M 12 0 SHEET 2 AD9 6 THR M 111 VAL M 115 1 O THR M 114 N ILE M 12 SHEET 3 AD9 6 ALA M 91 SER M 100 -1 N TYR M 93 O THR M 111 SHEET 4 AD9 6 TYR M 33 GLN M 39 -1 N VAL M 37 O TYR M 94 SHEET 5 AD9 6 LEU M 45 ILE M 51 -1 O GLU M 46 N ARG M 38 SHEET 6 AD9 6 THR M 57 TYR M 59 -1 O TYR M 58 N ILE M 50 SHEET 1 AE1 4 LEU M 11 ILE M 12 0 SHEET 2 AE1 4 THR M 111 VAL M 115 1 O THR M 114 N ILE M 12 SHEET 3 AE1 4 ALA M 91 SER M 100 -1 N TYR M 93 O THR M 111 SHEET 4 AE1 4 ALA M 103 TRP M 107 -1 O GLY M 105 N SER M 97 SHEET 1 AE2 4 MET N 4 SER N 7 0 SHEET 2 AE2 4 VAL N 19 ALA N 25 -1 O ARG N 24 N THR N 5 SHEET 3 AE2 4 ASP N 70 ILE N 75 -1 O PHE N 71 N CYS N 23 SHEET 4 AE2 4 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74 SHEET 1 AE3 6 SER N 10 ALA N 13 0 SHEET 2 AE3 6 THR N 102 ILE N 106 1 O GLU N 105 N VAL N 11 SHEET 3 AE3 6 THR N 85 GLN N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AE3 6 LEU N 33 GLN N 38 -1 N GLN N 38 O THR N 85 SHEET 5 AE3 6 ARG N 45 TYR N 49 -1 O LEU N 47 N TRP N 35 SHEET 6 AE3 6 SER N 53 LEU N 54 -1 O SER N 53 N TYR N 49 SSBOND 1 CYS A 4 CYS A 15 1555 1555 2.03 SSBOND 2 CYS A 55 CYS A 143 1555 1555 2.03 SSBOND 3 CYS A 179 CYS A 223 1555 1555 2.03 SSBOND 4 CYS A 280 CYS A 329 1555 1555 2.02 SSBOND 5 CYS A 291 CYS A 312 1555 1555 2.04 SSBOND 6 CYS A 313 CYS A 316 1555 1555 2.03 SSBOND 7 CYS a 4 CYS a 15 1555 1555 2.03 SSBOND 8 CYS a 55 CYS a 143 1555 1555 2.04 SSBOND 9 CYS a 179 CYS a 223 1555 1555 2.03 SSBOND 10 CYS a 280 CYS a 329 1555 1555 2.03 SSBOND 11 CYS a 291 CYS a 312 1555 1555 2.04 SSBOND 12 CYS a 313 CYS a 316 1555 1555 2.03 SSBOND 13 CYS h 22 CYS h 95 1555 1555 2.04 SSBOND 14 CYS l 23 CYS l 88 1555 1555 2.04 SSBOND 15 CYS H 22 CYS H 95 1555 1555 2.04 SSBOND 16 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 17 CYS B 4 CYS B 15 1555 1555 2.03 SSBOND 18 CYS B 55 CYS B 143 1555 1555 2.03 SSBOND 19 CYS B 179 CYS B 223 1555 1555 2.03 SSBOND 20 CYS B 280 CYS B 329 1555 1555 2.03 SSBOND 21 CYS B 291 CYS B 312 1555 1555 2.04 SSBOND 22 CYS B 313 CYS B 316 1555 1555 2.03 SSBOND 23 CYS b 4 CYS b 15 1555 1555 2.03 SSBOND 24 CYS b 55 CYS b 143 1555 1555 2.03 SSBOND 25 CYS b 179 CYS b 223 1555 1555 2.03 SSBOND 26 CYS b 280 CYS b 329 1555 1555 2.03 SSBOND 27 CYS b 291 CYS b 312 1555 1555 2.04 SSBOND 28 CYS b 313 CYS b 316 1555 1555 2.03 SSBOND 29 CYS m 22 CYS m 95 1555 1555 2.04 SSBOND 30 CYS n 23 CYS n 88 1555 1555 2.04 SSBOND 31 CYS M 22 CYS M 95 1555 1555 2.04 SSBOND 32 CYS N 23 CYS N 88 1555 1555 2.04 CISPEP 1 ASN A 95 PRO A 96 0 -7.11 CISPEP 2 MET A 318 PRO A 319 0 0.29 CISPEP 3 ASN a 95 PRO a 96 0 -5.14 CISPEP 4 MET a 318 PRO a 319 0 -2.88 CISPEP 5 SER l 7 PRO l 8 0 -2.77 CISPEP 6 PHE l 94 PRO l 95 0 -0.02 CISPEP 7 SER L 7 PRO L 8 0 -0.71 CISPEP 8 PHE L 94 PRO L 95 0 -1.55 CISPEP 9 ASN B 95 PRO B 96 0 -4.93 CISPEP 10 MET B 318 PRO B 319 0 -1.66 CISPEP 11 ASN b 95 PRO b 96 0 -2.98 CISPEP 12 MET b 318 PRO b 319 0 -2.11 CISPEP 13 SER n 7 PRO n 8 0 -0.63 CISPEP 14 PHE n 94 PRO n 95 0 -3.02 CISPEP 15 SER N 7 PRO N 8 0 -1.30 CISPEP 16 PHE N 94 PRO N 95 0 -2.42 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