HEADER VIRUS 09-MAY-20 7C2S TITLE HELICAL RECONSTRUCTION OF DENGUE VIRUS SEROTYPE 3 COMPLEXED WITH FAB TITLE 2 C10 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE PROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: ECTODOMAIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEAVY CHAIN OF FAB C10; COMPND 7 CHAIN: G, I; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LIGHT CHAIN OF FAB C10; COMPND 11 CHAIN: H, M; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DENGUE VIRUS 3; SOURCE 3 ORGANISM_TAXID: 11069; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 6 ORGANISM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 10 MOL_ID: 3; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: HEK293T KEYWDS ANTIBODY, NEUTRALIZATION, VIRUS EXPDTA ELECTRON MICROSCOPY MDLTYP CA ATOMS ONLY, CHAIN A, B, G, H, I, M AUTHOR S.MORRONE,S.V.CHEW,X.N.LIM,T.S.NG,V.A.KOSTYUCHENKO,S.ZHANG,S.M.LOK REVDAT 2 13-JAN-21 7C2S 1 REMARK REVDAT 1 08-JUL-20 7C2S 0 JRNL AUTH S.R.MORRONE,V.S.Y.CHEW,X.N.LIM,T.S.NG,V.A.KOSTYUCHENKO, JRNL AUTH 2 S.ZHANG,M.WIRAWAN,P.L.CHEW,J.LEE,J.L.TAN,J.WANG,T.Y.TAN, JRNL AUTH 3 J.SHI,G.SCREATON,M.C.MORAIS,S.M.LOK JRNL TITL HIGH FLAVIVIRUS STRUCTURAL PLASTICITY DEMONSTRATED BY A JRNL TITL 2 NON-SPHERICAL MORPHOLOGICAL VARIANT. JRNL REF NAT COMMUN V. 11 3112 2020 JRNL REFN ESSN 2041-1723 JRNL PMID 32561757 JRNL DOI 10.1038/S41467-020-16925-Y REMARK 2 REMARK 2 RESOLUTION. 10.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 10.40 REMARK 3 NUMBER OF PARTICLES : 7051 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 7C2S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAY-20. REMARK 100 THE DEPOSITION ID IS D_1300016924. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : HELICAL REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : FILAMENT REMARK 245 PARTICLE TYPE : HELICAL REMARK 245 NAME OF SAMPLE : HELICAL RECONSTRUCTION OF REMARK 245 DENGUE VIRUS SEROTYPE 3 REMARK 245 COMPLEXED WITH FAB C10; C10 FAB; REMARK 245 DENGUE VIRUS SEROTYPE 3 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON II (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL 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) : 18.00 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 96-MERIC REMARK 350 SOFTWARE USED: UCSF CHIMERA 1.13.1_B41965. REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, H, I, M 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 350 BIOMT1 2 0.997684 -0.068015 0.000000 15.39405 REMARK 350 BIOMT2 2 0.068015 0.997684 0.000000 -14.38032 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -129.50000 REMARK 350 BIOMT1 3 -0.278991 -0.960294 0.000000 490.13466 REMARK 350 BIOMT2 3 0.960294 -0.278991 0.000000 69.75649 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 -111.00000 REMARK 350 BIOMT1 4 -0.878817 0.477159 0.000000 306.79498 REMARK 350 BIOMT2 4 -0.477159 -0.878817 0.000000 515.67600 REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 -92.50000 REMARK 350 BIOMT1 5 0.653421 0.756995 0.000000 -89.83178 REMARK 350 BIOMT2 5 -0.756995 0.653421 0.000000 241.55038 REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 -74.00000 REMARK 350 BIOMT1 6 0.600420 -0.799685 0.000000 262.49500 REMARK 350 BIOMT2 6 0.799685 0.600420 0.000000 -87.57496 REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 -55.50000 REMARK 350 BIOMT1 7 -0.909236 -0.416281 0.000000 509.00914 REMARK 350 BIOMT2 7 0.416281 -0.909236 0.000000 326.77806 REMARK 350 BIOMT3 7 0.000000 0.000000 1.000000 -37.00000 REMARK 350 BIOMT1 8 -0.213030 0.977046 0.000000 51.65236 REMARK 350 BIOMT2 8 -0.977046 -0.213030 0.000000 479.36383 REMARK 350 BIOMT3 8 0.000000 0.000000 1.000000 -18.50000 REMARK 350 BIOMT1 9 -0.213030 -0.977046 0.000000 479.36383 REMARK 350 BIOMT2 9 0.977046 -0.213030 0.000000 51.65236 REMARK 350 BIOMT3 9 0.000000 0.000000 1.000000 18.50000 REMARK 350 BIOMT1 10 -0.909236 0.416281 0.000000 326.77806 REMARK 350 BIOMT2 10 -0.416281 -0.909236 0.000000 509.00914 REMARK 350 BIOMT3 10 0.000000 0.000000 1.000000 37.00000 REMARK 350 BIOMT1 11 0.600420 0.799685 0.000000 -87.57496 REMARK 350 BIOMT2 11 -0.799685 0.600420 0.000000 262.49500 REMARK 350 BIOMT3 11 0.000000 0.000000 1.000000 55.50000 REMARK 350 BIOMT1 12 0.653421 -0.756995 0.000000 241.55038 REMARK 350 BIOMT2 12 0.756995 0.653421 0.000000 -89.83178 REMARK 350 BIOMT3 12 0.000000 0.000000 1.000000 74.00000 REMARK 350 BIOMT1 13 -0.878817 -0.477159 0.000000 515.67600 REMARK 350 BIOMT2 13 0.477159 -0.878817 0.000000 306.79498 REMARK 350 BIOMT3 13 0.000000 0.000000 1.000000 92.50000 REMARK 350 BIOMT1 14 -0.278991 0.960294 0.000000 69.75649 REMARK 350 BIOMT2 14 -0.960294 -0.278991 0.000000 490.13466 REMARK 350 BIOMT3 14 0.000000 0.000000 1.000000 111.00000 REMARK 350 BIOMT1 15 0.997684 0.068015 0.000000 -14.38032 REMARK 350 BIOMT2 15 -0.068015 0.997684 0.000000 15.39405 REMARK 350 BIOMT3 15 0.000000 0.000000 1.000000 129.50000 REMARK 350 BIOMT1 16 -0.146083 -0.989272 0.000000 467.38658 REMARK 350 BIOMT2 16 0.989272 -0.146083 0.000000 34.32273 REMARK 350 BIOMT3 16 0.000000 0.000000 1.000000 148.00000 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-30278 RELATED DB: EMDB REMARK 900 HELICAL RECONSTRUCTION OF DENGUE VIRUS SEROTYPE 3 COMPLEXED WITH REMARK 900 FAB C10 DBREF 7C2S A 1 394 UNP Q07019 Q07019_9FLAV 167 560 DBREF 7C2S B 1 394 UNP Q07019 Q07019_9FLAV 167 560 DBREF 7C2S G 1 112 PDB 7C2S 7C2S 1 112 DBREF 7C2S H 2 106 PDB 7C2S 7C2S 2 106 DBREF 7C2S I 1 112 PDB 7C2S 7C2S 1 112 DBREF 7C2S M 2 106 PDB 7C2S 7C2S 2 106 SEQRES 1 A 394 MET ARG CYS VAL GLY VAL GLY ASN ARG ASP PHE VAL GLU SEQRES 2 A 394 GLY LEU SER GLY ALA THR TRP VAL ASP VAL VAL LEU GLU SEQRES 3 A 394 HIS GLY GLY CYS VAL THR THR MET ALA LYS ASN LYS PRO SEQRES 4 A 394 THR LEU ASP ILE GLU LEU GLN LYS THR GLU ALA THR GLN SEQRES 5 A 394 LEU ALA THR LEU ARG LYS LEU CYS ILE GLU GLY LYS ILE SEQRES 6 A 394 THR ASN ILE THR THR ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 A 394 GLU ALA ILE LEU PRO GLU GLU GLN ASP GLN ASN TYR VAL SEQRES 8 A 394 CYS LYS HIS THR TYR VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 A 394 CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 A 394 LYS PHE GLN CYS LEU GLU SER ILE GLU GLY LYS VAL VAL SEQRES 11 A 394 GLN HIS GLU ASN LEU LYS TYR THR VAL ILE ILE THR VAL SEQRES 12 A 394 HIS THR GLY ASP GLN HIS GLN VAL GLY ASN GLU THR GLN SEQRES 13 A 394 GLY VAL THR ALA GLU ILE THR PRO GLN ALA SER THR VAL SEQRES 14 A 394 GLU ALA ILE LEU PRO GLU TYR GLY THR LEU GLY LEU GLU SEQRES 15 A 394 CYS SER PRO ARG THR GLY LEU ASP PHE ASN GLU MET ILE SEQRES 16 A 394 LEU LEU THR MET LYS ASN LYS ALA TRP MET VAL HIS ARG SEQRES 17 A 394 GLN TRP PHE PHE ASP LEU PRO LEU PRO TRP THR SER GLY SEQRES 18 A 394 ALA THR THR GLU THR PRO THR TRP ASN ARG LYS GLU LEU SEQRES 19 A 394 LEU VAL THR PHE LYS ASN ALA HIS ALA LYS LYS GLN GLU SEQRES 20 A 394 VAL VAL VAL LEU GLY SER GLN GLU GLY ALA MET HIS THR SEQRES 21 A 394 ALA LEU THR GLY ALA THR GLU ILE GLN ASN SER GLY GLY SEQRES 22 A 394 THR SER ILE PHE ALA GLY HIS LEU LYS CYS ARG LEU LYS SEQRES 23 A 394 MET ASP LYS LEU GLU LEU LYS GLY MET SER TYR ALA MET SEQRES 24 A 394 CYS LEU ASN THR PHE VAL LEU LYS LYS GLU VAL SER GLU SEQRES 25 A 394 THR GLN HIS GLY THR ILE LEU ILE LYS VAL GLU TYR LYS SEQRES 26 A 394 GLY GLU ASP ALA PRO CYS LYS ILE PRO PHE SER THR GLU SEQRES 27 A 394 ASP GLY GLN GLY LYS ALA HIS ASN GLY ARG LEU ILE THR SEQRES 28 A 394 ALA ASN PRO VAL VAL THR LYS LYS GLU GLU PRO VAL ASN SEQRES 29 A 394 ILE GLU ALA GLU PRO PRO PHE GLY GLU SER ASN ILE VAL SEQRES 30 A 394 ILE GLY ILE GLY ASP LYS ALA LEU LYS ILE ASN TRP TYR SEQRES 31 A 394 LYS LYS GLY SER SEQRES 1 B 394 MET ARG CYS VAL GLY VAL GLY ASN ARG ASP PHE VAL GLU SEQRES 2 B 394 GLY LEU SER GLY ALA THR TRP VAL ASP VAL VAL LEU GLU SEQRES 3 B 394 HIS GLY GLY CYS VAL THR THR MET ALA LYS ASN LYS PRO SEQRES 4 B 394 THR LEU ASP ILE GLU LEU GLN LYS THR GLU ALA THR GLN SEQRES 5 B 394 LEU ALA THR LEU ARG LYS LEU CYS ILE GLU GLY LYS ILE SEQRES 6 B 394 THR ASN ILE THR THR ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 B 394 GLU ALA ILE LEU PRO GLU GLU GLN ASP GLN ASN TYR VAL SEQRES 8 B 394 CYS LYS HIS THR TYR VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 B 394 CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 B 394 LYS PHE GLN CYS LEU GLU SER ILE GLU GLY LYS VAL VAL SEQRES 11 B 394 GLN HIS GLU ASN LEU LYS TYR THR VAL ILE ILE THR VAL SEQRES 12 B 394 HIS THR GLY ASP GLN HIS GLN VAL GLY ASN GLU THR GLN SEQRES 13 B 394 GLY VAL THR ALA GLU ILE THR PRO GLN ALA SER THR VAL SEQRES 14 B 394 GLU ALA ILE LEU PRO GLU TYR GLY THR LEU GLY LEU GLU SEQRES 15 B 394 CYS SER PRO ARG THR GLY LEU ASP PHE ASN GLU MET ILE SEQRES 16 B 394 LEU LEU THR MET LYS ASN LYS ALA TRP MET VAL HIS ARG SEQRES 17 B 394 GLN TRP PHE PHE ASP LEU PRO LEU PRO TRP THR SER GLY SEQRES 18 B 394 ALA THR THR GLU THR PRO THR TRP ASN ARG LYS GLU LEU SEQRES 19 B 394 LEU VAL THR PHE LYS ASN ALA HIS ALA LYS LYS GLN GLU SEQRES 20 B 394 VAL VAL VAL LEU GLY SER GLN GLU GLY ALA MET HIS THR SEQRES 21 B 394 ALA LEU THR GLY ALA THR GLU ILE GLN ASN SER GLY GLY SEQRES 22 B 394 THR SER ILE PHE ALA GLY HIS LEU LYS CYS ARG LEU LYS SEQRES 23 B 394 MET ASP LYS LEU GLU LEU LYS GLY MET SER TYR ALA MET SEQRES 24 B 394 CYS LEU ASN THR PHE VAL LEU LYS LYS GLU VAL SER GLU SEQRES 25 B 394 THR GLN HIS GLY THR ILE LEU ILE LYS VAL GLU TYR LYS SEQRES 26 B 394 GLY GLU ASP ALA PRO CYS LYS ILE PRO PHE SER THR GLU SEQRES 27 B 394 ASP GLY GLN GLY LYS ALA HIS ASN GLY ARG LEU ILE THR SEQRES 28 B 394 ALA ASN PRO VAL VAL THR LYS LYS GLU GLU PRO VAL ASN SEQRES 29 B 394 ILE GLU ALA GLU PRO PRO PHE GLY GLU SER ASN ILE VAL SEQRES 30 B 394 ILE GLY ILE GLY ASP LYS ALA LEU LYS ILE ASN TRP TYR SEQRES 31 B 394 LYS LYS GLY SER SEQRES 1 G 127 GLU VAL GLN LEU VAL GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 G 127 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 G 127 TYR THR PHE THR SER TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 G 127 ALA PRO GLY GLN ARG LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 G 127 ALA GLY ASN GLY ASN THR LYS TYR SER GLN LYS PHE GLN SEQRES 6 G 127 ASP ARG VAL THR ILE THR ARG ASP THR SER ALA SER THR SEQRES 7 G 127 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 G 127 ALA ILE TYR TYR CYS ALA ARG ASP LYS VAL ASP ASP TYR SEQRES 9 G 127 GLY ASP TYR TRP PHE PRO THR LEU TRP TYR PHE ASP TYR SEQRES 10 G 127 TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1 H 109 SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER PRO SEQRES 2 H 109 GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SER SEQRES 3 H 109 ASP VAL GLY GLY PHE ASN TYR VAL SER TRP PHE GLN GLN SEQRES 4 H 109 HIS PRO GLY LYS ALA PRO LYS LEU MET LEU TYR ASP VAL SEQRES 5 H 109 THR SER ARG PRO SER GLY VAL SER SER ARG PHE SER GLY SEQRES 6 H 109 SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY SEQRES 7 H 109 LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER SEQRES 8 H 109 HIS THR SER ARG GLY THR TRP VAL PHE GLY GLY GLY THR SEQRES 9 H 109 LYS LEU THR VAL LEU SEQRES 1 I 127 GLU VAL GLN LEU VAL GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 I 127 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 I 127 TYR THR PHE THR SER TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 I 127 ALA PRO GLY GLN ARG LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 I 127 ALA GLY ASN GLY ASN THR LYS TYR SER GLN LYS PHE GLN SEQRES 6 I 127 ASP ARG VAL THR ILE THR ARG ASP THR SER ALA SER THR SEQRES 7 I 127 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 I 127 ALA ILE TYR TYR CYS ALA ARG ASP LYS VAL ASP ASP TYR SEQRES 9 I 127 GLY ASP TYR TRP PHE PRO THR LEU TRP TYR PHE ASP TYR SEQRES 10 I 127 TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 1 M 109 SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER PRO SEQRES 2 M 109 GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER SER SEQRES 3 M 109 ASP VAL GLY GLY PHE ASN TYR VAL SER TRP PHE GLN GLN SEQRES 4 M 109 HIS PRO GLY LYS ALA PRO LYS LEU MET LEU TYR ASP VAL SEQRES 5 M 109 THR SER ARG PRO SER GLY VAL SER SER ARG PHE SER GLY SEQRES 6 M 109 SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY SEQRES 7 M 109 LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SER SER SEQRES 8 M 109 HIS THR SER ARG GLY THR TRP VAL PHE GLY GLY GLY THR SEQRES 9 M 109 LYS LEU THR VAL LEU 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