HEADER VIRAL PROTEIN/IMMUNE SYSTEM 30-NOV-23 8V5A TITLE PREFUSION-STABILIZED RESPIROVIRUS TYPE 3 FUSION PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: FUSION GLYCOPROTEIN F0; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CAMELID NANOBODY 4C06; COMPND 7 CHAIN: Y, W, U; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN RESPIROVIRUS 3; SOURCE 3 ORGANISM_TAXID: 11216; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 9 ORGANISM_TAXID: 9844; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PCB4 KEYWDS FUSION PROTEIN, VIRAL GLYCOPROTEIN, MEMBRANE FUSION, VIRAL PROTEIN, KEYWDS 2 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR N.V.JOHNSON,J.S.MCLELLAN JRNL AUTH J.P.M.LANGEDIJK,F.COX,N.V.JOHNSON,D.VAN OVERVELD,L.LE, JRNL AUTH 2 W.VAN DEN HOOGEN,R.VOORZAAT,R.ZAHN,L.VAN DER FITS, JRNL AUTH 3 J.JURASZEK,J.S.MCLELLAN,M.J.G.BAKKERS JRNL TITL UNIVERSAL PARAMYXOVIRUS VACCINE DESIGN BY STABILIZING JRNL TITL 2 REGIONS INVOLVED IN STRUCTURAL TRANSFORMATION OF THE FUSION JRNL TITL 3 PROTEIN. JRNL REF NAT COMMUN V. 15 4629 2024 JRNL REFN ESSN 2041-1723 JRNL PMID 38821950 JRNL DOI 10.1038/S41467-024-48059-W REMARK 2 REMARK 2 RESOLUTION. 3.00 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 193265 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8V5A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000279557. 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 : TRIMERIC HUMAN RESPIROVIRUS 3 REMARK 245 FUSION PROTEIN BOUND TO 3 REMARK 245 COPIES OF NANOBODY 4C06 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 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) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 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) : 70.00 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, Y, B, W, C, U 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 MET A 1 REMARK 465 PRO A 2 REMARK 465 ILE A 3 REMARK 465 SER A 4 REMARK 465 ILE A 5 REMARK 465 LEU A 6 REMARK 465 LEU A 7 REMARK 465 ILE A 8 REMARK 465 ILE A 9 REMARK 465 THR A 10 REMARK 465 THR A 11 REMARK 465 MET A 12 REMARK 465 ILE A 13 REMARK 465 MET A 14 REMARK 465 ALA A 15 REMARK 465 SER A 16 REMARK 465 HIS A 17 REMARK 465 CYS A 18 REMARK 465 THR A 95 REMARK 465 ASN A 96 REMARK 465 GLN A 97 REMARK 465 GLU A 98 REMARK 465 SER A 99 REMARK 465 ASN A 100 REMARK 465 GLU A 101 REMARK 465 ASN A 102 REMARK 465 THR A 103 REMARK 465 ASP A 104 REMARK 465 PRO A 105 REMARK 465 ARG A 106 REMARK 465 THR A 245 REMARK 465 SER A 246 REMARK 465 THR A 247 REMARK 465 VAL A 248 REMARK 465 ASP A 249 REMARK 465 LYS A 250 REMARK 465 TYR A 251 REMARK 465 GLU A 488 REMARK 465 PRO A 489 REMARK 465 GLU A 490 REMARK 465 ALA A 491 REMARK 465 MET B 1 REMARK 465 PRO B 2 REMARK 465 ILE B 3 REMARK 465 SER B 4 REMARK 465 ILE B 5 REMARK 465 LEU B 6 REMARK 465 LEU B 7 REMARK 465 ILE B 8 REMARK 465 ILE B 9 REMARK 465 THR B 10 REMARK 465 THR B 11 REMARK 465 MET B 12 REMARK 465 ILE B 13 REMARK 465 MET B 14 REMARK 465 ALA B 15 REMARK 465 SER B 16 REMARK 465 HIS B 17 REMARK 465 CYS B 18 REMARK 465 THR B 95 REMARK 465 ASN B 96 REMARK 465 GLN B 97 REMARK 465 GLU B 98 REMARK 465 SER B 99 REMARK 465 ASN B 100 REMARK 465 GLU B 101 REMARK 465 ASN B 102 REMARK 465 THR B 103 REMARK 465 ASP B 104 REMARK 465 PRO B 105 REMARK 465 ARG B 106 REMARK 465 THR B 245 REMARK 465 SER B 246 REMARK 465 THR B 247 REMARK 465 VAL B 248 REMARK 465 ASP B 249 REMARK 465 LYS B 250 REMARK 465 TYR B 251 REMARK 465 GLU B 488 REMARK 465 PRO B 489 REMARK 465 GLU B 490 REMARK 465 ALA B 491 REMARK 465 MET C 1 REMARK 465 PRO C 2 REMARK 465 ILE C 3 REMARK 465 SER C 4 REMARK 465 ILE C 5 REMARK 465 LEU C 6 REMARK 465 LEU C 7 REMARK 465 ILE C 8 REMARK 465 ILE C 9 REMARK 465 THR C 10 REMARK 465 THR C 11 REMARK 465 MET C 12 REMARK 465 ILE C 13 REMARK 465 MET C 14 REMARK 465 ALA C 15 REMARK 465 SER C 16 REMARK 465 HIS C 17 REMARK 465 CYS C 18 REMARK 465 THR C 95 REMARK 465 ASN C 96 REMARK 465 GLN C 97 REMARK 465 GLU C 98 REMARK 465 SER C 99 REMARK 465 ASN C 100 REMARK 465 GLU C 101 REMARK 465 ASN C 102 REMARK 465 THR C 103 REMARK 465 ASP C 104 REMARK 465 PRO C 105 REMARK 465 ARG C 106 REMARK 465 THR C 245 REMARK 465 SER C 246 REMARK 465 THR C 247 REMARK 465 VAL C 248 REMARK 465 ASP C 249 REMARK 465 LYS C 250 REMARK 465 TYR C 251 REMARK 465 GLU C 488 REMARK 465 PRO C 489 REMARK 465 GLU C 490 REMARK 465 ALA C 491 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 NE2 GLN A 139 O GLU Y 1 2.11 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 ASP A 21 68.62 -100.13 REMARK 500 GLU A 108 154.75 -49.79 REMARK 500 CYS A 387 5.88 -68.86 REMARK 500 ASP B 21 68.58 -100.05 REMARK 500 GLU B 108 154.74 -49.76 REMARK 500 CYS B 387 5.83 -68.84 REMARK 500 ASP C 21 68.56 -100.03 REMARK 500 GLU C 108 154.79 -49.82 REMARK 500 CYS C 387 5.85 -68.88 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-42981 RELATED DB: EMDB REMARK 900 PREFUSION-STABILIZED RESPIROVIRUS TYPE 3 FUSION PROTEIN DBREF1 8V5A A 1 486 UNP A0A023PFZ0_9MONO DBREF2 8V5A A A0A023PFZ0 1 486 DBREF 8V5A Y 1 117 PDB 8V5A 8V5A 1 117 DBREF1 8V5A B 1 486 UNP A0A023PFZ0_9MONO DBREF2 8V5A B A0A023PFZ0 1 486 DBREF 8V5A W 1 117 PDB 8V5A 8V5A 1 117 DBREF1 8V5A C 1 486 UNP A0A023PFZ0_9MONO DBREF2 8V5A C A0A023PFZ0 1 486 DBREF 8V5A U 1 117 PDB 8V5A 8V5A 1 117 SEQADV 8V5A PRO A 41 UNP A0A023PFZ SER 41 CONFLICT SEQADV 8V5A MET A 89 UNP A0A023PFZ GLN 89 CONFLICT SEQADV 8V5A PRO A 167 UNP A0A023PFZ ASN 167 CONFLICT SEQADV 8V5A PRO A 168 UNP A0A023PFZ LEU 168 CONFLICT SEQADV 8V5A ILE A 222 UNP A0A023PFZ GLN 222 CONFLICT SEQADV 8V5A PRO A 335 UNP A0A023PFZ PHE 335 CONFLICT SEQADV 8V5A ASN A 452 UNP A0A023PFZ ASP 452 CONFLICT SEQADV 8V5A VAL A 470 UNP A0A023PFZ SER 470 CONFLICT SEQADV 8V5A VAL A 477 UNP A0A023PFZ SER 477 CONFLICT SEQADV 8V5A GLY A 487 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A GLU A 488 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A PRO A 489 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A GLU A 490 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A ALA A 491 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A PRO B 41 UNP A0A023PFZ SER 41 CONFLICT SEQADV 8V5A MET B 89 UNP A0A023PFZ GLN 89 CONFLICT SEQADV 8V5A PRO B 167 UNP A0A023PFZ ASN 167 CONFLICT SEQADV 8V5A PRO B 168 UNP A0A023PFZ LEU 168 CONFLICT SEQADV 8V5A ILE B 222 UNP A0A023PFZ GLN 222 CONFLICT SEQADV 8V5A PRO B 335 UNP A0A023PFZ PHE 335 CONFLICT SEQADV 8V5A ASN B 452 UNP A0A023PFZ ASP 452 CONFLICT SEQADV 8V5A VAL B 470 UNP A0A023PFZ SER 470 CONFLICT SEQADV 8V5A VAL B 477 UNP A0A023PFZ SER 477 CONFLICT SEQADV 8V5A GLY B 487 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A GLU B 488 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A PRO B 489 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A GLU B 490 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A ALA B 491 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A PRO C 41 UNP A0A023PFZ SER 41 CONFLICT SEQADV 8V5A MET C 89 UNP A0A023PFZ GLN 89 CONFLICT SEQADV 8V5A PRO C 167 UNP A0A023PFZ ASN 167 CONFLICT SEQADV 8V5A PRO C 168 UNP A0A023PFZ LEU 168 CONFLICT SEQADV 8V5A ILE C 222 UNP A0A023PFZ GLN 222 CONFLICT SEQADV 8V5A PRO C 335 UNP A0A023PFZ PHE 335 CONFLICT SEQADV 8V5A ASN C 452 UNP A0A023PFZ ASP 452 CONFLICT SEQADV 8V5A VAL C 470 UNP A0A023PFZ SER 470 CONFLICT SEQADV 8V5A VAL C 477 UNP A0A023PFZ SER 477 CONFLICT SEQADV 8V5A GLY C 487 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A GLU C 488 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A PRO C 489 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A GLU C 490 UNP A0A023PFZ EXPRESSION TAG SEQADV 8V5A ALA C 491 UNP A0A023PFZ EXPRESSION TAG SEQRES 1 A 491 MET PRO ILE SER ILE LEU LEU ILE ILE THR THR MET ILE SEQRES 2 A 491 MET ALA SER HIS CYS GLN ILE ASP ILE THR LYS LEU GLN SEQRES 3 A 491 HIS VAL GLY VAL LEU VAL ASN SER PRO LYS GLY MET LYS SEQRES 4 A 491 ILE PRO GLN ASN PHE GLU THR ARG TYR LEU ILE LEU SER SEQRES 5 A 491 LEU ILE PRO LYS ILE GLU ASP SER ASN SER CYS GLY ASP SEQRES 6 A 491 GLN GLN ILE LYS GLN TYR LYS ARG LEU LEU ASP ARG LEU SEQRES 7 A 491 ILE ILE PRO LEU TYR ASP GLY LEU ARG LEU MET LYS ASP SEQRES 8 A 491 VAL ILE VAL THR ASN GLN GLU SER ASN GLU ASN THR ASP SEQRES 9 A 491 PRO ARG THR GLU ARG PHE PHE GLY GLY VAL ILE GLY THR SEQRES 10 A 491 ILE ALA LEU GLY VAL ALA THR SER ALA GLN ILE THR ALA SEQRES 11 A 491 ALA VAL ALA LEU VAL GLU ALA LYS GLN ALA ARG SER ASP SEQRES 12 A 491 ILE GLU LYS LEU LYS GLU ALA ILE ARG ASP THR ASN LYS SEQRES 13 A 491 ALA VAL GLN SER VAL GLN SER SER VAL GLY PRO PRO ILE SEQRES 14 A 491 VAL ALA ILE LYS SER VAL GLN ASP TYR VAL ASN LYS GLU SEQRES 15 A 491 ILE VAL PRO SER ILE ALA ARG LEU GLY CYS GLU ALA ALA SEQRES 16 A 491 GLY LEU GLN LEU GLY ILE ALA LEU THR GLN HIS TYR SER SEQRES 17 A 491 GLU LEU THR ASN ILE PHE GLY ASP ASN ILE GLY SER LEU SEQRES 18 A 491 ILE GLU LYS GLY ILE LYS LEU GLN GLY ILE ALA SER LEU SEQRES 19 A 491 TYR ARG THR ASN ILE THR GLU ILE PHE THR THR SER THR SEQRES 20 A 491 VAL ASP LYS TYR ASP ILE TYR ASP LEU LEU PHE THR GLU SEQRES 21 A 491 SER ILE LYS VAL ARG VAL ILE ASP VAL ASP LEU ASN ASP SEQRES 22 A 491 TYR SER ILE THR LEU GLN VAL ARG LEU PRO LEU LEU THR SEQRES 23 A 491 ARG LEU LEU ASN THR GLN ILE TYR LYS VAL ASP SER ILE SEQRES 24 A 491 SER TYR ASN ILE GLN ASN ARG GLU TRP TYR ILE PRO LEU SEQRES 25 A 491 PRO SER HIS ILE MET THR LYS GLY ALA PHE LEU GLY GLY SEQRES 26 A 491 ALA ASP VAL LYS GLU CYS ILE GLU ALA PRO SER SER TYR SEQRES 27 A 491 ILE CYS PRO SER ASP PRO GLY PHE VAL LEU ASN HIS GLU SEQRES 28 A 491 MET GLU SER CYS LEU SER GLY ASN ILE SER GLN CYS PRO SEQRES 29 A 491 ARG THR THR VAL THR SER ASP ILE VAL PRO ARG TYR ALA SEQRES 30 A 491 PHE VAL ASN GLY GLY VAL VAL ALA ASN CYS ILE THR THR SEQRES 31 A 491 THR CYS THR CYS ASN GLY ILE GLY ASN ARG ILE ASN GLN SEQRES 32 A 491 PRO PRO ASP GLN GLY VAL LYS ILE ILE THR HIS LYS GLU SEQRES 33 A 491 CYS ASN THR ILE GLY ILE ASN GLY MET LEU PHE ASN THR SEQRES 34 A 491 ASN LYS GLU GLY THR LEU ALA PHE TYR THR PRO ASP ASP SEQRES 35 A 491 ILE THR LEU ASN ASN SER VAL ALA LEU ASN PRO ILE ASP SEQRES 36 A 491 ILE SER ILE GLU LEU ASN LYS ALA LYS SER ASP LEU GLU SEQRES 37 A 491 GLU VAL LYS GLU TRP ILE ARG ARG VAL ASN GLN LYS LEU SEQRES 38 A 491 ASP SER ILE GLY SER GLY GLU PRO GLU ALA SEQRES 1 Y 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 Y 117 PRO GLY GLY SER LEU ARG LEU SER CYS SER ALA SER GLY SEQRES 3 Y 117 SER LEU SER THR ILE LYS ALA LEU GLY TRP TYR ARG ARG SEQRES 4 Y 117 ALA PRO GLY ARG GLU ARG GLU LEU VAL ALA SER ILE THR SEQRES 5 Y 117 SER ALA GLY GLU THR ASN TYR ALA ASP SER ALA LYS GLY SEQRES 6 Y 117 ARG PHE THR VAL SER THR ASP ASN ALA LYS ASN THR VAL SEQRES 7 Y 117 ASP LEU ARG MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 Y 117 VAL TYR TYR CYS TYR ALA GLU SER PHE VAL LEU ASN ILE SEQRES 9 Y 117 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY SEQRES 1 B 491 MET PRO ILE SER ILE LEU LEU ILE ILE THR THR MET ILE SEQRES 2 B 491 MET ALA SER HIS CYS GLN ILE ASP ILE THR LYS LEU GLN SEQRES 3 B 491 HIS VAL GLY VAL LEU VAL ASN SER PRO LYS GLY MET LYS SEQRES 4 B 491 ILE PRO GLN ASN PHE GLU THR ARG TYR LEU ILE LEU SER SEQRES 5 B 491 LEU ILE PRO LYS ILE GLU ASP SER ASN SER CYS GLY ASP SEQRES 6 B 491 GLN GLN ILE LYS GLN TYR LYS ARG LEU LEU ASP ARG LEU SEQRES 7 B 491 ILE ILE PRO LEU TYR ASP GLY LEU ARG LEU MET LYS ASP SEQRES 8 B 491 VAL ILE VAL THR ASN GLN GLU SER ASN GLU ASN THR ASP SEQRES 9 B 491 PRO ARG THR GLU ARG PHE PHE GLY GLY VAL ILE GLY THR SEQRES 10 B 491 ILE ALA LEU GLY VAL ALA THR SER ALA GLN ILE THR ALA SEQRES 11 B 491 ALA VAL ALA LEU VAL GLU ALA LYS GLN ALA ARG SER ASP SEQRES 12 B 491 ILE GLU LYS LEU LYS GLU ALA ILE ARG ASP THR ASN LYS SEQRES 13 B 491 ALA VAL GLN SER VAL GLN SER SER VAL GLY PRO PRO ILE SEQRES 14 B 491 VAL ALA ILE LYS SER VAL GLN ASP TYR VAL ASN LYS GLU SEQRES 15 B 491 ILE VAL PRO SER ILE ALA ARG LEU GLY CYS GLU ALA ALA SEQRES 16 B 491 GLY LEU GLN LEU GLY ILE ALA LEU THR GLN HIS TYR SER SEQRES 17 B 491 GLU LEU THR ASN ILE PHE GLY ASP ASN ILE GLY SER LEU SEQRES 18 B 491 ILE GLU LYS GLY ILE LYS LEU GLN GLY ILE ALA SER LEU SEQRES 19 B 491 TYR ARG THR ASN ILE THR GLU ILE PHE THR THR SER THR SEQRES 20 B 491 VAL ASP LYS TYR ASP ILE TYR ASP LEU LEU PHE THR GLU SEQRES 21 B 491 SER ILE LYS VAL ARG VAL ILE ASP VAL ASP LEU ASN ASP SEQRES 22 B 491 TYR SER ILE THR LEU GLN VAL ARG LEU PRO LEU LEU THR SEQRES 23 B 491 ARG LEU LEU ASN THR GLN ILE TYR LYS VAL ASP SER ILE SEQRES 24 B 491 SER TYR ASN ILE GLN ASN ARG GLU TRP TYR ILE PRO LEU SEQRES 25 B 491 PRO SER HIS ILE MET THR LYS GLY ALA PHE LEU GLY GLY SEQRES 26 B 491 ALA ASP VAL LYS GLU CYS ILE GLU ALA PRO SER SER TYR SEQRES 27 B 491 ILE CYS PRO SER ASP PRO GLY PHE VAL LEU ASN HIS GLU SEQRES 28 B 491 MET GLU SER CYS LEU SER GLY ASN ILE SER GLN CYS PRO SEQRES 29 B 491 ARG THR THR VAL THR SER ASP ILE VAL PRO ARG TYR ALA SEQRES 30 B 491 PHE VAL ASN GLY GLY VAL VAL ALA ASN CYS ILE THR THR SEQRES 31 B 491 THR CYS THR CYS ASN GLY ILE GLY ASN ARG ILE ASN GLN SEQRES 32 B 491 PRO PRO ASP GLN GLY VAL LYS ILE ILE THR HIS LYS GLU SEQRES 33 B 491 CYS ASN THR ILE GLY ILE ASN GLY MET LEU PHE ASN THR SEQRES 34 B 491 ASN LYS GLU GLY THR LEU ALA PHE TYR THR PRO ASP ASP SEQRES 35 B 491 ILE THR LEU ASN ASN SER VAL ALA LEU ASN PRO ILE ASP SEQRES 36 B 491 ILE SER ILE GLU LEU ASN LYS ALA LYS SER ASP LEU GLU SEQRES 37 B 491 GLU VAL LYS GLU TRP ILE ARG ARG VAL ASN GLN LYS LEU SEQRES 38 B 491 ASP SER ILE GLY SER GLY GLU PRO GLU ALA SEQRES 1 W 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 W 117 PRO GLY GLY SER LEU ARG LEU SER CYS SER ALA SER GLY SEQRES 3 W 117 SER LEU SER THR ILE LYS ALA LEU GLY TRP TYR ARG ARG SEQRES 4 W 117 ALA PRO GLY ARG GLU ARG GLU LEU VAL ALA SER ILE THR SEQRES 5 W 117 SER ALA GLY GLU THR ASN TYR ALA ASP SER ALA LYS GLY SEQRES 6 W 117 ARG PHE THR VAL SER THR ASP ASN ALA LYS ASN THR VAL SEQRES 7 W 117 ASP LEU ARG MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 W 117 VAL TYR TYR CYS TYR ALA GLU SER PHE VAL LEU ASN ILE SEQRES 9 W 117 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY SEQRES 1 C 491 MET PRO ILE SER ILE LEU LEU ILE ILE THR THR MET ILE SEQRES 2 C 491 MET ALA SER HIS CYS GLN ILE ASP ILE THR LYS LEU GLN SEQRES 3 C 491 HIS VAL GLY VAL LEU VAL ASN SER PRO LYS GLY MET LYS SEQRES 4 C 491 ILE PRO GLN ASN PHE GLU THR ARG TYR LEU ILE LEU SER SEQRES 5 C 491 LEU ILE PRO LYS ILE GLU ASP SER ASN SER CYS GLY ASP SEQRES 6 C 491 GLN GLN ILE LYS GLN TYR LYS ARG LEU LEU ASP ARG LEU SEQRES 7 C 491 ILE ILE PRO LEU TYR ASP GLY LEU ARG LEU MET LYS ASP SEQRES 8 C 491 VAL ILE VAL THR ASN GLN GLU SER ASN GLU ASN THR ASP SEQRES 9 C 491 PRO ARG THR GLU ARG PHE PHE GLY GLY VAL ILE GLY THR SEQRES 10 C 491 ILE ALA LEU GLY VAL ALA THR SER ALA GLN ILE THR ALA SEQRES 11 C 491 ALA VAL ALA LEU VAL GLU ALA LYS GLN ALA ARG SER ASP SEQRES 12 C 491 ILE GLU LYS LEU LYS GLU ALA ILE ARG ASP THR ASN LYS SEQRES 13 C 491 ALA VAL GLN SER VAL GLN SER SER VAL GLY PRO PRO ILE SEQRES 14 C 491 VAL ALA ILE LYS SER VAL GLN ASP TYR VAL ASN LYS GLU SEQRES 15 C 491 ILE VAL PRO SER ILE ALA ARG LEU GLY CYS GLU ALA ALA SEQRES 16 C 491 GLY LEU GLN LEU GLY ILE ALA LEU THR GLN HIS TYR SER SEQRES 17 C 491 GLU LEU THR ASN ILE PHE GLY ASP ASN ILE GLY SER LEU SEQRES 18 C 491 ILE GLU LYS GLY ILE LYS LEU GLN GLY ILE ALA SER LEU SEQRES 19 C 491 TYR ARG THR ASN ILE THR GLU ILE PHE THR THR SER THR SEQRES 20 C 491 VAL ASP LYS TYR ASP ILE TYR ASP LEU LEU PHE THR GLU SEQRES 21 C 491 SER ILE LYS VAL ARG VAL ILE ASP VAL ASP LEU ASN ASP SEQRES 22 C 491 TYR SER ILE THR LEU GLN VAL ARG LEU PRO LEU LEU THR SEQRES 23 C 491 ARG LEU LEU ASN THR GLN ILE TYR LYS VAL ASP SER ILE SEQRES 24 C 491 SER TYR ASN ILE GLN ASN ARG GLU TRP TYR ILE PRO LEU SEQRES 25 C 491 PRO SER HIS ILE MET THR LYS GLY ALA PHE LEU GLY GLY SEQRES 26 C 491 ALA ASP VAL LYS GLU CYS ILE GLU ALA PRO SER SER TYR SEQRES 27 C 491 ILE CYS PRO SER ASP PRO GLY PHE VAL LEU ASN HIS GLU SEQRES 28 C 491 MET GLU SER CYS LEU SER GLY ASN ILE SER GLN CYS PRO SEQRES 29 C 491 ARG THR THR VAL THR SER ASP ILE VAL PRO ARG TYR ALA SEQRES 30 C 491 PHE VAL ASN GLY GLY VAL VAL ALA ASN CYS ILE THR THR SEQRES 31 C 491 THR CYS THR CYS ASN GLY ILE GLY ASN ARG ILE ASN GLN SEQRES 32 C 491 PRO PRO ASP GLN GLY VAL LYS ILE ILE THR HIS LYS GLU SEQRES 33 C 491 CYS ASN THR ILE GLY ILE ASN GLY MET LEU PHE ASN THR SEQRES 34 C 491 ASN LYS GLU GLY THR LEU ALA PHE TYR THR PRO ASP ASP SEQRES 35 C 491 ILE THR LEU ASN ASN SER VAL ALA LEU ASN PRO ILE ASP SEQRES 36 C 491 ILE SER ILE GLU LEU ASN LYS ALA LYS SER ASP LEU GLU SEQRES 37 C 491 GLU VAL LYS GLU TRP ILE ARG ARG VAL ASN GLN LYS LEU SEQRES 38 C 491 ASP SER ILE GLY SER GLY GLU PRO GLU ALA SEQRES 1 U 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 U 117 PRO GLY GLY SER LEU ARG LEU SER CYS SER ALA SER GLY SEQRES 3 U 117 SER LEU SER THR ILE LYS ALA LEU GLY TRP TYR ARG ARG SEQRES 4 U 117 ALA PRO GLY ARG GLU ARG GLU LEU VAL ALA SER ILE THR SEQRES 5 U 117 SER ALA GLY GLU THR ASN TYR ALA ASP SER ALA LYS GLY SEQRES 6 U 117 ARG PHE THR VAL SER THR ASP ASN ALA LYS ASN THR VAL SEQRES 7 U 117 ASP LEU ARG MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 U 117 VAL TYR TYR CYS TYR ALA GLU SER PHE VAL LEU ASN ILE SEQRES 9 U 117 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLY HELIX 1 AA1 ASP A 21 GLN A 26 1 6 HELIX 2 AA2 GLY A 64 MET A 89 1 26 HELIX 3 AA3 SER A 125 LYS A 138 1 14 HELIX 4 AA4 GLN A 139 ARG A 152 1 14 HELIX 5 AA5 VAL A 175 GLU A 182 1 8 HELIX 6 AA6 GLU A 182 LEU A 190 1 9 HELIX 7 AA7 LEU A 190 GLY A 215 1 26 HELIX 8 AA8 ASN A 217 LYS A 224 1 8 HELIX 9 AA9 LEU A 228 ARG A 236 1 9 HELIX 10 AB1 ASN A 238 THR A 244 1 7 HELIX 11 AB2 ILE A 253 ILE A 262 1 10 HELIX 12 AB3 VAL A 328 CYS A 331 5 4 HELIX 13 AB4 GLU A 351 SER A 357 1 7 HELIX 14 AB5 ASN A 359 CYS A 363 5 5 HELIX 15 AB6 ASN A 452 GLY A 487 1 36 HELIX 16 AB7 LYS Y 86 THR Y 90 5 5 HELIX 17 AB8 ASP B 21 GLN B 26 1 6 HELIX 18 AB9 GLY B 64 MET B 89 1 26 HELIX 19 AC1 SER B 125 LYS B 138 1 14 HELIX 20 AC2 GLN B 139 ARG B 152 1 14 HELIX 21 AC3 VAL B 175 GLU B 182 1 8 HELIX 22 AC4 GLU B 182 LEU B 190 1 9 HELIX 23 AC5 LEU B 190 GLY B 215 1 26 HELIX 24 AC6 ASN B 217 LYS B 224 1 8 HELIX 25 AC7 LEU B 228 ARG B 236 1 9 HELIX 26 AC8 ASN B 238 THR B 244 1 7 HELIX 27 AC9 ILE B 253 ILE B 262 1 10 HELIX 28 AD1 VAL B 328 CYS B 331 5 4 HELIX 29 AD2 GLU B 351 SER B 357 1 7 HELIX 30 AD3 ASN B 359 CYS B 363 5 5 HELIX 31 AD4 ASN B 452 GLY B 487 1 36 HELIX 32 AD5 LYS W 86 THR W 90 5 5 HELIX 33 AD6 ASP C 21 GLN C 26 1 6 HELIX 34 AD7 GLY C 64 MET C 89 1 26 HELIX 35 AD8 SER C 125 LYS C 138 1 14 HELIX 36 AD9 GLN C 139 ARG C 152 1 14 HELIX 37 AE1 VAL C 175 GLU C 182 1 8 HELIX 38 AE2 GLU C 182 LEU C 190 1 9 HELIX 39 AE3 LEU C 190 GLY C 215 1 26 HELIX 40 AE4 ASN C 217 LYS C 224 1 8 HELIX 41 AE5 LEU C 228 ARG C 236 1 9 HELIX 42 AE6 ASN C 238 THR C 244 1 7 HELIX 43 AE7 ILE C 253 ILE C 262 1 10 HELIX 44 AE8 VAL C 328 CYS C 331 5 4 HELIX 45 AE9 GLU C 351 SER C 357 1 7 HELIX 46 AF1 ASN C 359 CYS C 363 5 5 HELIX 47 AF2 ASN C 452 GLY C 487 1 36 HELIX 48 AF3 LYS U 86 THR U 90 5 5 SHEET 1 AA118 VAL A 30 SER A 52 0 SHEET 2 AA118 VAL A 158 VAL A 161 0 SHEET 3 AA118 ILE A 169 LYS A 173 -1 O ALA A 171 N GLN A 159 SHEET 4 AA118 ILE A 226 LYS A 227 0 SHEET 5 AA118 LYS A 263 ASP A 270 -1 O VAL A 264 N ILE A 226 SHEET 6 AA118 SER A 275 SER A 298 -1 O SER A 275 N ASP A 270 SHEET 7 AA118 HIS A 315 LYS A 319 -1 O ILE A 316 N TYR A 294 SHEET 8 AA118 PHE A 322 ALA A 326 -1 O GLY A 324 N MET A 317 SHEET 9 AA118 ILE A 332 GLU A 333 0 SHEET 10 AA118 SER A 337 ILE A 339 -1 O ILE A 339 N ILE A 332 SHEET 11 AA118 GLY A 345 VAL A 347 -1 O PHE A 346 N GLY A 325 SHEET 12 AA118 GLY Y 10 VAL Y 12 0 SHEET 13 AA118 ILE Y 31 ARG Y 39 0 SHEET 14 AA118 GLU Y 46 THR Y 52 -1 O ILE Y 51 N LEU Y 34 SHEET 15 AA118 THR Y 57 TYR Y 59 -1 O ASN Y 58 N SER Y 50 SHEET 16 AA118 ALA Y 91 SER Y 99 -1 O TYR Y 94 N TYR Y 37 SHEET 17 AA118 ASN Y 103 TRP Y 106 -1 O ASN Y 103 N SER Y 99 SHEET 18 AA118 THR Y 110 VAL Y 114 -1 O THR Y 110 N TYR Y 93 SHEET 1 AA2 5 VAL A 92 ILE A 93 0 SHEET 2 AA2 5 GLY A 116 ILE A 118 -1 O THR A 117 N ILE A 93 SHEET 3 AA2 5 MET B 425 ASN B 428 1 O ASN B 428 N ILE A 118 SHEET 4 AA2 5 GLY B 421 ILE B 422 -1 N ILE B 422 O MET B 425 SHEET 5 AA2 5 CYS B 392 THR B 393 -1 N THR B 393 O GLY B 421 SHEET 1 AA3 4 VAL A 122 THR A 124 0 SHEET 2 AA3 4 TYR B 376 VAL B 379 -1 O PHE B 378 N ALA A 123 SHEET 3 AA3 4 GLY B 382 ALA B 385 -1 O GLY B 382 N VAL B 379 SHEET 4 AA3 4 LYS B 410 ILE B 412 -1 O LYS B 410 N ALA B 385 SHEET 1 AA4 3 TYR A 301 ILE A 303 0 SHEET 2 AA4 3 ARG A 306 TYR A 309 -1 O TRP A 308 N TYR A 301 SHEET 3 AA4 3 THR A 366 THR A 367 -1 O THR A 366 N TYR A 309 SHEET 1 AA5 4 LYS A 410 ILE A 412 0 SHEET 2 AA5 4 GLY A 382 ALA A 385 -1 N ALA A 385 O LYS A 410 SHEET 3 AA5 4 TYR A 376 VAL A 379 -1 N VAL A 379 O GLY A 382 SHEET 4 AA5 4 VAL C 122 THR C 124 -1 O ALA C 123 N PHE A 378 SHEET 1 AA6 5 CYS A 392 THR A 393 0 SHEET 2 AA6 5 GLY A 421 ILE A 422 -1 O GLY A 421 N THR A 393 SHEET 3 AA6 5 MET A 425 ASN A 428 -1 O MET A 425 N ILE A 422 SHEET 4 AA6 5 GLY C 116 ILE C 118 1 O ILE C 118 N ASN A 428 SHEET 5 AA6 5 VAL C 92 ILE C 93 -1 N ILE C 93 O THR C 117 SHEET 1 AA7 4 VAL Y 2 VAL Y 5 0 SHEET 2 AA7 4 LEU Y 18 GLY Y 26 -1 O SER Y 25 N GLN Y 3 SHEET 3 AA7 4 THR Y 77 MET Y 82 -1 O MET Y 82 N LEU Y 18 SHEET 4 AA7 4 THR Y 68 ASP Y 72 -1 N SER Y 70 O ASP Y 79 SHEET 1 AA818 VAL B 30 SER B 52 0 SHEET 2 AA818 VAL B 158 VAL B 161 0 SHEET 3 AA818 ILE B 169 LYS B 173 -1 O ALA B 171 N GLN B 159 SHEET 4 AA818 ILE B 226 LYS B 227 0 SHEET 5 AA818 LYS B 263 ASP B 270 -1 O VAL B 264 N ILE B 226 SHEET 6 AA818 SER B 275 SER B 298 -1 O SER B 275 N ASP B 270 SHEET 7 AA818 HIS B 315 LYS B 319 -1 O ILE B 316 N TYR B 294 SHEET 8 AA818 PHE B 322 ALA B 326 -1 O GLY B 324 N MET B 317 SHEET 9 AA818 ILE B 332 GLU B 333 0 SHEET 10 AA818 SER B 337 ILE B 339 -1 O ILE B 339 N ILE B 332 SHEET 11 AA818 GLY B 345 VAL B 347 -1 O PHE B 346 N GLY B 325 SHEET 12 AA818 GLY W 10 VAL W 12 0 SHEET 13 AA818 ILE W 31 ARG W 39 0 SHEET 14 AA818 GLU W 46 THR W 52 -1 O ILE W 51 N LEU W 34 SHEET 15 AA818 THR W 57 TYR W 59 -1 O ASN W 58 N SER W 50 SHEET 16 AA818 ALA W 91 SER W 99 -1 O TYR W 94 N TYR W 37 SHEET 17 AA818 ASN W 103 TRP W 106 -1 O ASN W 103 N SER W 99 SHEET 18 AA818 THR W 110 VAL W 114 -1 O THR W 110 N TYR W 93 SHEET 1 AA9 5 VAL B 92 ILE B 93 0 SHEET 2 AA9 5 GLY B 116 ILE B 118 -1 O THR B 117 N ILE B 93 SHEET 3 AA9 5 MET C 425 ASN C 428 1 O ASN C 428 N ILE B 118 SHEET 4 AA9 5 GLY C 421 ILE C 422 -1 N ILE C 422 O MET C 425 SHEET 5 AA9 5 CYS C 392 THR C 393 -1 N THR C 393 O GLY C 421 SHEET 1 AB1 4 VAL B 122 THR B 124 0 SHEET 2 AB1 4 TYR C 376 VAL C 379 -1 O PHE C 378 N ALA B 123 SHEET 3 AB1 4 GLY C 382 ALA C 385 -1 O GLY C 382 N VAL C 379 SHEET 4 AB1 4 LYS C 410 ILE C 412 -1 O LYS C 410 N ALA C 385 SHEET 1 AB2 3 TYR B 301 ILE B 303 0 SHEET 2 AB2 3 ARG B 306 TYR B 309 -1 O TRP B 308 N TYR B 301 SHEET 3 AB2 3 THR B 366 THR B 367 -1 O THR B 366 N TYR B 309 SHEET 1 AB3 4 VAL W 2 VAL W 5 0 SHEET 2 AB3 4 LEU W 18 GLY W 26 -1 O SER W 25 N GLN W 3 SHEET 3 AB3 4 THR W 77 MET W 82 -1 O MET W 82 N LEU W 18 SHEET 4 AB3 4 THR W 68 ASP W 72 -1 N SER W 70 O ASP W 79 SHEET 1 AB418 VAL C 30 SER C 52 0 SHEET 2 AB418 VAL C 158 VAL C 161 0 SHEET 3 AB418 ILE C 169 LYS C 173 -1 O ILE C 169 N VAL C 161 SHEET 4 AB418 ILE C 226 LYS C 227 0 SHEET 5 AB418 LYS C 263 ASP C 270 -1 O VAL C 264 N ILE C 226 SHEET 6 AB418 SER C 275 SER C 298 -1 O SER C 275 N ASP C 270 SHEET 7 AB418 HIS C 315 LYS C 319 -1 O ILE C 316 N TYR C 294 SHEET 8 AB418 PHE C 322 ALA C 326 -1 O GLY C 324 N MET C 317 SHEET 9 AB418 ILE C 332 GLU C 333 0 SHEET 10 AB418 SER C 337 ILE C 339 -1 O ILE C 339 N ILE C 332 SHEET 11 AB418 GLY C 345 VAL C 347 -1 O PHE C 346 N GLY C 325 SHEET 12 AB418 GLY U 10 VAL U 12 0 SHEET 13 AB418 ILE U 31 ARG U 39 0 SHEET 14 AB418 GLU U 46 THR U 52 -1 O ILE U 51 N LEU U 34 SHEET 15 AB418 THR U 57 TYR U 59 -1 O ASN U 58 N SER U 50 SHEET 16 AB418 ALA U 91 SER U 99 -1 O TYR U 94 N TYR U 37 SHEET 17 AB418 ASN U 103 TRP U 106 -1 O ASN U 103 N SER U 99 SHEET 18 AB418 THR U 110 VAL U 114 -1 O THR U 110 N TYR U 93 SHEET 1 AB5 3 TYR C 301 ILE C 303 0 SHEET 2 AB5 3 ARG C 306 TYR C 309 -1 O TRP C 308 N TYR C 301 SHEET 3 AB5 3 THR C 366 THR C 367 -1 O THR C 366 N TYR C 309 SHEET 1 AB6 4 VAL U 2 VAL U 5 0 SHEET 2 AB6 4 LEU U 18 GLY U 26 -1 O SER U 25 N GLN U 3 SHEET 3 AB6 4 THR U 77 MET U 82 -1 O MET U 82 N LEU U 18 SHEET 4 AB6 4 THR U 68 ASP U 72 -1 N SER U 70 O ASP U 79 SSBOND 1 CYS A 63 CYS A 192 1555 1555 2.03 SSBOND 2 CYS A 331 CYS A 340 1555 1555 2.02 SSBOND 3 CYS A 355 CYS A 363 1555 1555 2.03 SSBOND 4 CYS A 387 CYS A 392 1555 1555 2.04 SSBOND 5 CYS A 394 CYS A 417 1555 1555 2.03 SSBOND 6 CYS Y 22 CYS Y 95 1555 1555 2.03 SSBOND 7 CYS B 63 CYS B 192 1555 1555 2.03 SSBOND 8 CYS B 331 CYS B 340 1555 1555 2.02 SSBOND 9 CYS B 355 CYS B 363 1555 1555 2.03 SSBOND 10 CYS B 387 CYS B 392 1555 1555 2.04 SSBOND 11 CYS B 394 CYS B 417 1555 1555 2.03 SSBOND 12 CYS W 22 CYS W 95 1555 1555 2.03 SSBOND 13 CYS C 63 CYS C 192 1555 1555 2.03 SSBOND 14 CYS C 331 CYS C 340 1555 1555 2.02 SSBOND 15 CYS C 355 CYS C 363 1555 1555 2.03 SSBOND 16 CYS C 387 CYS C 392 1555 1555 2.04 SSBOND 17 CYS C 394 CYS C 417 1555 1555 2.03 SSBOND 18 CYS U 22 CYS U 95 1555 1555 2.03 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