HEADER VIRAL PROTEIN/IMMUNE SYSTEM 31-MAR-25 9UAA TITLE NIPAH VIRUS FUSION GLYCOPROTEIN IN COMPLEX WITH A BROADLY NEUTRALIZING TITLE 2 ANTIBODY 5C8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FUSION GLYCOPROTEIN F0; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: PROTEIN F; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 5C8-VL; COMPND 8 CHAIN: F, E, D; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: 5C8-VH; COMPND 12 CHAIN: G, H, I; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HENIPAVIRUS NIPAHENSE; SOURCE 3 ORGANISM_TAXID: 3052225; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MACACA; SOURCE 9 ORGANISM_TAXID: 9539; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MACACA; SOURCE 15 ORGANISM_TAXID: 9539; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: EXPI293 KEYWDS HENIPAVIRUS, FUSION GLYCOPROTEIN, ANTIBODY, ANTIVIRAL PROTEIN, VIRAL KEYWDS 2 PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR P.F.FAN,Y.REN,C.M.YU,W.CHEN REVDAT 1 09-APR-25 9UAA 0 SPRSDE 09-APR-25 9UAA 8XNH JRNL AUTH P.F.FAN,C.M.YU,W.CHEN,Y.REN JRNL TITL NIPAH VIRUS FUSION GLYCOPROTEIN IN COMPLEX WITH A BROADLY JRNL TITL 2 NEUTRALIZING ANTIBODY 1D6 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.22 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) : 2.220 REMARK 3 NUMBER OF PARTICLES : 462582 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 9UAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-25. REMARK 100 THE DEPOSITION ID IS D_1300058083. 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 : NIPAH VIRUS FUSION GLYCOPROTEIN REMARK 245 IN COMPLEX WITH A BROADLY REMARK 245 NEUTRALIZING ANTIBODY 5C8; REMARK 245 NIPAH VIRUS FUSION GLYCOPROTEIN; REMARK 245 5C8 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.02 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 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 : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2600.00 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) : 5191.00 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: NONAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, G, H, I, B, C, E, D 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 VAL A 105 REMARK 465 GLY A 106 REMARK 465 ASP A 107 REMARK 465 VAL A 108 REMARK 465 ARG A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 VAL B 105 REMARK 465 GLY B 106 REMARK 465 ASP B 107 REMARK 465 VAL B 108 REMARK 465 ARG B 109 REMARK 465 LEU B 110 REMARK 465 ALA B 111 REMARK 465 VAL C 105 REMARK 465 GLY C 106 REMARK 465 ASP C 107 REMARK 465 VAL C 108 REMARK 465 ARG C 109 REMARK 465 LEU C 110 REMARK 465 ALA C 111 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 GLY E 30 OH TYR E 71 2.11 REMARK 500 O GLY F 30 OH TYR F 71 2.12 REMARK 500 O GLY D 30 OH TYR D 71 2.13 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 MET A 68 32.87 -141.07 REMARK 500 ASN A 238 76.86 -100.14 REMARK 500 ASN A 437 33.23 -97.59 REMARK 500 ASN F 32 49.73 -82.41 REMARK 500 LYS F 42 -163.61 -164.36 REMARK 500 ALA F 51 -8.13 73.29 REMARK 500 THR G 88 -167.82 -128.41 REMARK 500 VAL G 108 -54.14 65.92 REMARK 500 TRP G 119 -168.84 -124.70 REMARK 500 VAL H 108 -53.95 64.19 REMARK 500 THR I 88 -168.33 -127.60 REMARK 500 VAL I 108 -54.36 66.32 REMARK 500 TRP I 119 -169.42 -125.00 REMARK 500 ASN B 238 75.98 -100.10 REMARK 500 ASN B 437 33.81 -98.39 REMARK 500 GLN C 290 43.87 -106.40 REMARK 500 ASN C 303 119.12 -160.13 REMARK 500 ASN C 437 33.47 -98.12 REMARK 500 LYS E 42 -165.26 -162.86 REMARK 500 ALA E 51 -9.39 73.09 REMARK 500 ASN D 32 49.31 -82.42 REMARK 500 LYS D 42 -164.93 -162.88 REMARK 500 ALA D 51 -8.23 72.82 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63983 RELATED DB: EMDB REMARK 900 NIPAH VIRUS FUSION GLYCOPROTEIN IN COMPLEX WITH A BROADLY REMARK 900 NEUTRALIZING ANTIBODY 5C8 DBREF 9UAA A 27 471 UNP Q9IH63 FUS_NIPAV 27 471 DBREF 9UAA F 1 106 PDB 9UAA 9UAA 1 106 DBREF 9UAA G 1 127 PDB 9UAA 9UAA 1 127 DBREF 9UAA H 1 127 PDB 9UAA 9UAA 1 127 DBREF 9UAA I 1 127 PDB 9UAA 9UAA 1 127 DBREF 9UAA B 27 471 UNP Q9IH63 FUS_NIPAV 27 471 DBREF 9UAA C 27 471 UNP Q9IH63 FUS_NIPAV 27 471 DBREF 9UAA E 1 106 PDB 9UAA 9UAA 1 106 DBREF 9UAA D 1 106 PDB 9UAA 9UAA 1 106 SEQRES 1 A 445 ILE LEU HIS TYR GLU LYS LEU SER LYS ILE GLY LEU VAL SEQRES 2 A 445 LYS GLY VAL THR ARG LYS TYR LYS ILE LYS SER ASN PRO SEQRES 3 A 445 LEU THR LYS ASP ILE VAL ILE LYS MET ILE PRO ASN VAL SEQRES 4 A 445 SER ASN MET SER GLN CYS THR GLY SER VAL MET GLU ASN SEQRES 5 A 445 TYR LYS THR ARG LEU ASN GLY ILE LEU THR PRO ILE LYS SEQRES 6 A 445 GLY ALA LEU GLU ILE TYR LYS ASN ASN THR HIS ASP LEU SEQRES 7 A 445 VAL GLY ASP VAL ARG LEU ALA GLY VAL ILE MET ALA GLY SEQRES 8 A 445 VAL ALA ILE GLY ILE ALA THR ALA ALA GLN ILE THR ALA SEQRES 9 A 445 GLY VAL ALA LEU TYR GLU ALA MET LYS ASN ALA ASP ASN SEQRES 10 A 445 ILE ASN LYS LEU LYS SER SER ILE GLU SER THR ASN GLU SEQRES 11 A 445 ALA VAL VAL LYS LEU GLN GLU THR ALA GLU LYS THR VAL SEQRES 12 A 445 TYR VAL LEU THR ALA LEU GLN ASP TYR ILE ASN THR ASN SEQRES 13 A 445 LEU VAL PRO THR ILE ASP LYS ILE SER CYS LYS GLN THR SEQRES 14 A 445 GLU LEU SER LEU ASP LEU ALA LEU SER LYS TYR LEU SER SEQRES 15 A 445 ASP LEU LEU PHE VAL PHE GLY PRO ASN LEU GLN ASP PRO SEQRES 16 A 445 VAL SER ASN SER MET THR ILE GLN ALA ILE SER GLN ALA SEQRES 17 A 445 PHE GLY GLY ASN TYR GLU THR LEU LEU ARG THR LEU GLY SEQRES 18 A 445 TYR ALA THR GLU ASP PHE ASP ASP LEU LEU GLU SER ASP SEQRES 19 A 445 SER ILE THR GLY GLN ILE ILE TYR VAL ASP LEU SER SER SEQRES 20 A 445 TYR TYR ILE ILE VAL ARG VAL TYR PHE PRO ILE LEU THR SEQRES 21 A 445 GLU ILE GLN GLN ALA TYR ILE GLN GLU LEU LEU PRO VAL SEQRES 22 A 445 SER PHE ASN ASN ASP ASN SER GLU TRP ILE SER ILE VAL SEQRES 23 A 445 PRO ASN PHE ILE LEU VAL ARG ASN THR LEU ILE SER ASN SEQRES 24 A 445 ILE GLU ILE GLY PHE CYS LEU ILE THR LYS ARG SER VAL SEQRES 25 A 445 ILE CYS ASN GLN ASP TYR ALA THR PRO MET THR ASN ASN SEQRES 26 A 445 MET ARG GLU CYS LEU THR GLY SER THR GLU LYS CYS PRO SEQRES 27 A 445 ARG GLU LEU VAL VAL SER SER HIS VAL PRO ARG PHE ALA SEQRES 28 A 445 LEU SER ASN GLY VAL LEU PHE ALA ASN CYS ILE SER VAL SEQRES 29 A 445 THR CYS GLN CYS GLN THR THR GLY ARG ALA ILE SER GLN SEQRES 30 A 445 SER GLY GLU GLN THR LEU LEU MET ILE ASP ASN THR THR SEQRES 31 A 445 CYS PRO THR ALA VAL LEU GLY ASN VAL ILE ILE SER LEU SEQRES 32 A 445 GLY LYS TYR LEU GLY SER VAL ASN TYR ASN SER GLU GLY SEQRES 33 A 445 ILE ALA ILE GLY PRO PRO VAL PHE THR ASP LYS VAL ASP SEQRES 34 A 445 ILE SER SER GLN ILE SER SER MET ASN GLN SER LEU GLN SEQRES 35 A 445 GLN SER LYS SEQRES 1 F 106 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 F 106 SER VAL GLY ASP THR VAL THR ILE THR CYS GLN ALA SER SEQRES 3 F 106 GLN GLY ILE GLY ASN ASN LEU HIS TRP TYR GLN GLN LYS SEQRES 4 F 106 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ARG ALA SER SEQRES 5 F 106 SER LEU GLN SER GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 F 106 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7 F 106 GLN PRO GLU ASP PHE ALA TYR TYR CYS GLN GLN GLY TYR SEQRES 8 F 106 SER TYR PRO PHE THR PHE GLY PRO GLY THR LYS VAL ASP SEQRES 9 F 106 ILE LYS SEQRES 1 G 127 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY VAL VAL LYS SEQRES 2 G 127 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 G 127 GLY SER ILE SER ASP SER TYR ARG TRP SER TRP ILE ARG SEQRES 4 G 127 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SEQRES 5 G 127 TYR GLY SER SER THR SER THR ASN TYR ASN PRO SER LEU SEQRES 6 G 127 LYS SER ARG VAL THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 G 127 GLN PHE SER LEU ASN LEU SER SER LEU THR ALA ALA ASP SEQRES 8 G 127 THR ALA VAL TYR TYR CYS VAL ARG VAL VAL GLN TYR LEU SEQRES 9 G 127 GLU TRP PHE VAL ASP LEU ILE GLU VAL ASN TRP PHE ASP SEQRES 10 G 127 VAL TRP GLY PRO GLY VAL LEU VAL THR VAL SEQRES 1 H 127 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY VAL VAL LYS SEQRES 2 H 127 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 127 GLY SER ILE SER ASP SER TYR ARG TRP SER TRP ILE ARG SEQRES 4 H 127 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SEQRES 5 H 127 TYR GLY SER SER THR SER THR ASN TYR ASN PRO SER LEU SEQRES 6 H 127 LYS SER ARG VAL THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 H 127 GLN PHE SER LEU ASN LEU SER SER LEU THR ALA ALA ASP SEQRES 8 H 127 THR ALA VAL TYR TYR CYS VAL ARG VAL VAL GLN TYR LEU SEQRES 9 H 127 GLU TRP PHE VAL ASP LEU ILE GLU VAL ASN TRP PHE ASP SEQRES 10 H 127 VAL TRP GLY PRO GLY VAL LEU VAL THR VAL SEQRES 1 I 127 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY VAL VAL LYS SEQRES 2 I 127 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 I 127 GLY SER ILE SER ASP SER TYR ARG TRP SER TRP ILE ARG SEQRES 4 I 127 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SEQRES 5 I 127 TYR GLY SER SER THR SER THR ASN TYR ASN PRO SER LEU SEQRES 6 I 127 LYS SER ARG VAL THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 I 127 GLN PHE SER LEU ASN LEU SER SER LEU THR ALA ALA ASP SEQRES 8 I 127 THR ALA VAL TYR TYR CYS VAL ARG VAL VAL GLN TYR LEU SEQRES 9 I 127 GLU TRP PHE VAL ASP LEU ILE GLU VAL ASN TRP PHE ASP SEQRES 10 I 127 VAL TRP GLY PRO GLY VAL LEU VAL THR VAL SEQRES 1 B 445 ILE LEU HIS TYR GLU LYS LEU SER LYS ILE GLY LEU VAL SEQRES 2 B 445 LYS GLY VAL THR ARG LYS TYR LYS ILE LYS SER ASN PRO SEQRES 3 B 445 LEU THR LYS ASP ILE VAL ILE LYS MET ILE PRO ASN VAL SEQRES 4 B 445 SER ASN MET SER GLN CYS THR GLY SER VAL MET GLU ASN SEQRES 5 B 445 TYR LYS THR ARG LEU ASN GLY ILE LEU THR PRO ILE LYS SEQRES 6 B 445 GLY ALA LEU GLU ILE TYR LYS ASN ASN THR HIS ASP LEU SEQRES 7 B 445 VAL GLY ASP VAL ARG LEU ALA GLY VAL ILE MET ALA GLY SEQRES 8 B 445 VAL ALA ILE GLY ILE ALA THR ALA ALA GLN ILE THR ALA SEQRES 9 B 445 GLY VAL ALA LEU TYR GLU ALA MET LYS ASN ALA ASP ASN SEQRES 10 B 445 ILE ASN LYS LEU LYS SER SER ILE GLU SER THR ASN GLU SEQRES 11 B 445 ALA VAL VAL LYS LEU GLN GLU THR ALA GLU LYS THR VAL SEQRES 12 B 445 TYR VAL LEU THR ALA LEU GLN ASP TYR ILE ASN THR ASN SEQRES 13 B 445 LEU VAL PRO THR ILE ASP LYS ILE SER CYS LYS GLN THR SEQRES 14 B 445 GLU LEU SER LEU ASP LEU ALA LEU SER LYS TYR LEU SER SEQRES 15 B 445 ASP LEU LEU PHE VAL PHE GLY PRO ASN LEU GLN ASP PRO SEQRES 16 B 445 VAL SER ASN SER MET THR ILE GLN ALA ILE SER GLN ALA SEQRES 17 B 445 PHE GLY GLY ASN TYR GLU THR LEU LEU ARG THR LEU GLY SEQRES 18 B 445 TYR ALA THR GLU ASP PHE ASP ASP LEU LEU GLU SER ASP SEQRES 19 B 445 SER ILE THR GLY GLN ILE ILE TYR VAL ASP LEU SER SER SEQRES 20 B 445 TYR TYR ILE ILE VAL ARG VAL TYR PHE PRO ILE LEU THR SEQRES 21 B 445 GLU ILE GLN GLN ALA TYR ILE GLN GLU LEU LEU PRO VAL SEQRES 22 B 445 SER PHE ASN ASN ASP ASN SER GLU TRP ILE SER ILE VAL SEQRES 23 B 445 PRO ASN PHE ILE LEU VAL ARG ASN THR LEU ILE SER ASN SEQRES 24 B 445 ILE GLU ILE GLY PHE CYS LEU ILE THR LYS ARG SER VAL SEQRES 25 B 445 ILE CYS ASN GLN ASP TYR ALA THR PRO MET THR ASN ASN SEQRES 26 B 445 MET ARG GLU CYS LEU THR GLY SER THR GLU LYS CYS PRO SEQRES 27 B 445 ARG GLU LEU VAL VAL SER SER HIS VAL PRO ARG PHE ALA SEQRES 28 B 445 LEU SER ASN GLY VAL LEU PHE ALA ASN CYS ILE SER VAL SEQRES 29 B 445 THR CYS GLN CYS GLN THR THR GLY ARG ALA ILE SER GLN SEQRES 30 B 445 SER GLY GLU GLN THR LEU LEU MET ILE ASP ASN THR THR SEQRES 31 B 445 CYS PRO THR ALA VAL LEU GLY ASN VAL ILE ILE SER LEU SEQRES 32 B 445 GLY LYS TYR LEU GLY SER VAL ASN TYR ASN SER GLU GLY SEQRES 33 B 445 ILE ALA ILE GLY PRO PRO VAL PHE THR ASP LYS VAL ASP SEQRES 34 B 445 ILE SER SER GLN ILE SER SER MET ASN GLN SER LEU GLN SEQRES 35 B 445 GLN SER LYS SEQRES 1 C 445 ILE LEU HIS TYR GLU LYS LEU SER LYS ILE GLY LEU VAL SEQRES 2 C 445 LYS GLY VAL THR ARG LYS TYR LYS ILE LYS SER ASN PRO SEQRES 3 C 445 LEU THR LYS ASP ILE VAL ILE LYS MET ILE PRO ASN VAL SEQRES 4 C 445 SER ASN MET SER GLN CYS THR GLY SER VAL MET GLU ASN SEQRES 5 C 445 TYR LYS THR ARG LEU ASN GLY ILE LEU THR PRO ILE LYS SEQRES 6 C 445 GLY ALA LEU GLU ILE TYR LYS ASN ASN THR HIS ASP LEU SEQRES 7 C 445 VAL GLY ASP VAL ARG LEU ALA GLY VAL ILE MET ALA GLY SEQRES 8 C 445 VAL ALA ILE GLY ILE ALA THR ALA ALA GLN ILE THR ALA SEQRES 9 C 445 GLY VAL ALA LEU TYR GLU ALA MET LYS ASN ALA ASP ASN SEQRES 10 C 445 ILE ASN LYS LEU LYS SER SER ILE GLU SER THR ASN GLU SEQRES 11 C 445 ALA VAL VAL LYS LEU GLN GLU THR ALA GLU LYS THR VAL SEQRES 12 C 445 TYR VAL LEU THR ALA LEU GLN ASP TYR ILE ASN THR ASN SEQRES 13 C 445 LEU VAL PRO THR ILE ASP LYS ILE SER CYS LYS GLN THR SEQRES 14 C 445 GLU LEU SER LEU ASP LEU ALA LEU SER LYS TYR LEU SER SEQRES 15 C 445 ASP LEU LEU PHE VAL PHE GLY PRO ASN LEU GLN ASP PRO SEQRES 16 C 445 VAL SER ASN SER MET THR ILE GLN ALA ILE SER GLN ALA SEQRES 17 C 445 PHE GLY GLY ASN TYR GLU THR LEU LEU ARG THR LEU GLY SEQRES 18 C 445 TYR ALA THR GLU ASP PHE ASP ASP LEU LEU GLU SER ASP SEQRES 19 C 445 SER ILE THR GLY GLN ILE ILE TYR VAL ASP LEU SER SER SEQRES 20 C 445 TYR TYR ILE ILE VAL ARG VAL TYR PHE PRO ILE LEU THR SEQRES 21 C 445 GLU ILE GLN GLN ALA TYR ILE GLN GLU LEU LEU PRO VAL SEQRES 22 C 445 SER PHE ASN ASN ASP ASN SER GLU TRP ILE SER ILE VAL SEQRES 23 C 445 PRO ASN PHE ILE LEU VAL ARG ASN THR LEU ILE SER ASN SEQRES 24 C 445 ILE GLU ILE GLY PHE CYS LEU ILE THR LYS ARG SER VAL SEQRES 25 C 445 ILE CYS ASN GLN ASP TYR ALA THR PRO MET THR ASN ASN SEQRES 26 C 445 MET ARG GLU CYS LEU THR GLY SER THR GLU LYS CYS PRO SEQRES 27 C 445 ARG GLU LEU VAL VAL SER SER HIS VAL PRO ARG PHE ALA SEQRES 28 C 445 LEU SER ASN GLY VAL LEU PHE ALA ASN CYS ILE SER VAL SEQRES 29 C 445 THR CYS GLN CYS GLN THR THR GLY ARG ALA ILE SER GLN SEQRES 30 C 445 SER GLY GLU GLN THR LEU LEU MET ILE ASP ASN THR THR SEQRES 31 C 445 CYS PRO THR ALA VAL LEU GLY ASN VAL ILE ILE SER LEU SEQRES 32 C 445 GLY LYS TYR LEU GLY SER VAL ASN TYR ASN SER GLU GLY SEQRES 33 C 445 ILE ALA ILE GLY PRO PRO VAL PHE THR ASP LYS VAL ASP SEQRES 34 C 445 ILE SER SER GLN ILE SER SER MET ASN GLN SER LEU GLN SEQRES 35 C 445 GLN SER LYS SEQRES 1 E 106 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 E 106 SER VAL GLY ASP THR VAL THR ILE THR CYS GLN ALA SER SEQRES 3 E 106 GLN GLY ILE GLY ASN ASN LEU HIS TRP TYR GLN GLN LYS SEQRES 4 E 106 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ARG ALA SER SEQRES 5 E 106 SER LEU GLN SER GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 E 106 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7 E 106 GLN PRO GLU ASP PHE ALA TYR TYR CYS GLN GLN GLY TYR SEQRES 8 E 106 SER TYR PRO PHE THR PHE GLY PRO GLY THR LYS VAL ASP SEQRES 9 E 106 ILE LYS SEQRES 1 D 106 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 106 SER VAL GLY ASP THR VAL THR ILE THR CYS GLN ALA SER SEQRES 3 D 106 GLN GLY ILE GLY ASN ASN LEU HIS TRP TYR GLN GLN LYS SEQRES 4 D 106 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ARG ALA SER SEQRES 5 D 106 SER LEU GLN SER GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 D 106 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7 D 106 GLN PRO GLU ASP PHE ALA TYR TYR CYS GLN GLN GLY TYR SEQRES 8 D 106 SER TYR PRO PHE THR PHE GLY PRO GLY THR LYS VAL ASP SEQRES 9 D 106 ILE LYS HET NAG A 501 14 HET NAG A 502 14 HET NAG A 503 14 HET NAG B 501 14 HET NAG B 502 14 HET NAG B 503 14 HET NAG C 501 14 HET NAG C 502 14 HET NAG C 503 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 10 NAG 9(C8 H15 N O6) FORMUL 19 HOH *340(H2 O) HELIX 1 AA1 HIS A 29 LYS A 35 1 7 HELIX 2 AA2 VAL A 65 THR A 72 5 8 HELIX 3 AA3 SER A 74 ASN A 99 1 26 HELIX 4 AA4 GLY A 117 GLY A 121 1 5 HELIX 5 AA5 ALA A 125 LYS A 146 1 22 HELIX 6 AA6 LEU A 147 SER A 153 1 7 HELIX 7 AA7 LEU A 175 ASN A 182 1 8 HELIX 8 AA8 LEU A 183 ILE A 187 5 5 HELIX 9 AA9 SER A 191 GLY A 215 1 25 HELIX 10 AB1 THR A 227 SER A 232 1 6 HELIX 11 AB2 GLN A 233 GLY A 236 5 4 HELIX 12 AB3 ASN A 238 GLY A 247 1 10 HELIX 13 AB4 ASP A 252 SER A 259 1 8 HELIX 14 AB5 ILE A 328 CYS A 331 5 4 HELIX 15 AB6 THR A 349 THR A 357 1 9 HELIX 16 AB7 SER A 359 CYS A 363 5 5 HELIX 17 AB8 ASN A 437 GLU A 441 5 5 HELIX 18 AB9 ASP A 452 LYS A 471 1 20 HELIX 19 AC1 THR G 88 THR G 92 5 5 HELIX 20 AC2 PRO H 63 LYS H 66 5 4 HELIX 21 AC3 THR H 88 THR H 92 5 5 HELIX 22 AC4 PRO I 63 LYS I 66 5 4 HELIX 23 AC5 THR I 88 THR I 92 5 5 HELIX 24 AC6 HIS B 29 LYS B 35 1 7 HELIX 25 AC7 VAL B 65 THR B 72 5 8 HELIX 26 AC8 SER B 74 ASN B 99 1 26 HELIX 27 AC9 GLY B 117 GLY B 121 1 5 HELIX 28 AD1 ALA B 125 LYS B 146 1 22 HELIX 29 AD2 LEU B 147 SER B 153 1 7 HELIX 30 AD3 LEU B 175 ASN B 182 1 8 HELIX 31 AD4 LEU B 183 ILE B 187 5 5 HELIX 32 AD5 SER B 191 GLY B 215 1 25 HELIX 33 AD6 ILE B 228 SER B 232 1 5 HELIX 34 AD7 GLN B 233 GLY B 236 5 4 HELIX 35 AD8 ASN B 238 GLY B 247 1 10 HELIX 36 AD9 ASP B 252 SER B 259 1 8 HELIX 37 AE1 ILE B 328 CYS B 331 5 4 HELIX 38 AE2 THR B 349 THR B 357 1 9 HELIX 39 AE3 SER B 359 CYS B 363 5 5 HELIX 40 AE4 ASN B 437 GLU B 441 5 5 HELIX 41 AE5 ASP B 452 LYS B 471 1 20 HELIX 42 AE6 HIS C 29 LYS C 35 1 7 HELIX 43 AE7 VAL C 65 THR C 72 5 8 HELIX 44 AE8 SER C 74 ASN C 99 1 26 HELIX 45 AE9 GLY C 117 GLY C 121 1 5 HELIX 46 AF1 ALA C 125 LYS C 146 1 22 HELIX 47 AF2 LEU C 147 SER C 153 1 7 HELIX 48 AF3 LEU C 175 ASN C 182 1 8 HELIX 49 AF4 LEU C 183 ILE C 187 5 5 HELIX 50 AF5 SER C 191 GLY C 215 1 25 HELIX 51 AF6 THR C 227 SER C 232 1 6 HELIX 52 AF7 GLN C 233 GLY C 236 5 4 HELIX 53 AF8 ASN C 238 GLY C 247 1 10 HELIX 54 AF9 ASP C 252 SER C 259 1 8 HELIX 55 AG1 ILE C 328 CYS C 331 5 4 HELIX 56 AG2 THR C 349 THR C 357 1 9 HELIX 57 AG3 SER C 359 CYS C 363 5 5 HELIX 58 AG4 ASN C 437 GLU C 441 5 5 HELIX 59 AG5 ASP C 452 LYS C 471 1 20 SHEET 1 AA1 5 VAL A 158 GLN A 162 0 SHEET 2 AA1 5 THR A 168 THR A 173 -1 O VAL A 171 N VAL A 159 SHEET 3 AA1 5 LEU A 38 LYS A 60 1 N LYS A 60 O LEU A 172 SHEET 4 AA1 5 SER A 337 CYS A 340 1 O VAL A 338 N LYS A 45 SHEET 5 AA1 5 LEU A 332 ILE A 333 -1 N LEU A 332 O ILE A 339 SHEET 1 AA2 7 THR A 263 ASP A 270 0 SHEET 2 AA2 7 TYR A 275 GLU A 287 -1 O ILE A 277 N ILE A 267 SHEET 3 AA2 7 LEU A 38 LYS A 60 -1 N LYS A 55 O VAL A 280 SHEET 4 AA2 7 ALA A 291 PRO A 298 -1 O LEU A 297 N VAL A 39 SHEET 5 AA2 7 PHE A 315 ARG A 319 -1 O VAL A 318 N TYR A 292 SHEET 6 AA2 7 LEU A 322 ILE A 326 -1 O SER A 324 N LEU A 317 SHEET 7 AA2 7 ALA A 345 THR A 346 -1 O THR A 346 N ASN A 325 SHEET 1 AA3 5 THR A 101 HIS A 102 0 SHEET 2 AA3 5 ILE A 114 ALA A 116 -1 O ILE A 114 N HIS A 102 SHEET 3 AA3 5 VAL B 425 SER B 428 1 O ILE B 426 N MET A 115 SHEET 4 AA3 5 THR B 419 LEU B 422 -1 N ALA B 420 O ILE B 427 SHEET 5 AA3 5 CYS B 392 CYS B 394 -1 N GLN B 393 O VAL B 421 SHEET 1 AA4 4 ALA A 123 THR A 124 0 SHEET 2 AA4 4 PHE B 376 SER B 379 -1 O LEU B 378 N ALA A 123 SHEET 3 AA4 4 VAL B 382 ALA B 385 -1 O PHE B 384 N ALA B 377 SHEET 4 AA4 4 LEU B 410 ILE B 412 -1 O LEU B 410 N ALA B 385 SHEET 1 AA5 3 PHE A 301 ASN A 302 0 SHEET 2 AA5 3 GLU A 307 SER A 310 -1 O TRP A 308 N PHE A 301 SHEET 3 AA5 3 ARG A 365 LEU A 367 -1 O GLU A 366 N ILE A 309 SHEET 1 AA6 4 LEU A 410 ILE A 412 0 SHEET 2 AA6 4 VAL A 382 ALA A 385 -1 N ALA A 385 O LEU A 410 SHEET 3 AA6 4 PHE A 376 SER A 379 -1 N ALA A 377 O PHE A 384 SHEET 4 AA6 4 ALA C 123 THR C 124 -1 O ALA C 123 N LEU A 378 SHEET 1 AA7 5 CYS A 392 CYS A 394 0 SHEET 2 AA7 5 THR A 419 LEU A 422 -1 O VAL A 421 N GLN A 393 SHEET 3 AA7 5 VAL A 425 SER A 428 -1 O ILE A 427 N ALA A 420 SHEET 4 AA7 5 ILE C 114 ALA C 116 1 O MET C 115 N ILE A 426 SHEET 5 AA7 5 THR C 101 HIS C 102 -1 N HIS C 102 O ILE C 114 SHEET 1 AA8 4 LEU F 4 SER F 7 0 SHEET 2 AA8 4 VAL F 19 ALA F 25 -1 O GLN F 24 N THR F 5 SHEET 3 AA8 4 ASP F 70 ILE F 75 -1 O ILE F 75 N VAL F 19 SHEET 4 AA8 4 SER F 63 SER F 67 -1 N SER F 63 O THR F 74 SHEET 1 AA9 5 SER F 53 LEU F 54 0 SHEET 2 AA9 5 LYS F 45 TYR F 49 -1 N TYR F 49 O SER F 53 SHEET 3 AA9 5 LEU F 33 GLN F 38 -1 N GLN F 37 O LYS F 45 SHEET 4 AA9 5 ALA F 84 GLN F 89 -1 O GLN F 88 N HIS F 34 SHEET 5 AA9 5 THR F 96 PHE F 97 -1 O THR F 96 N GLN F 89 SHEET 1 AB1 4 GLN G 3 SER G 7 0 SHEET 2 AB1 4 LEU G 18 SER G 25 -1 O SER G 25 N GLN G 3 SHEET 3 AB1 4 GLN G 79 LEU G 84 -1 O PHE G 80 N CYS G 22 SHEET 4 AB1 4 VAL G 69 ASP G 74 -1 N THR G 70 O ASN G 83 SHEET 1 AB2 5 THR G 59 TYR G 61 0 SHEET 2 AB2 5 GLU G 47 TYR G 53 -1 N TYR G 51 O ASN G 60 SHEET 3 AB2 5 ARG G 34 GLN G 40 -1 N ARG G 39 O GLU G 47 SHEET 4 AB2 5 ALA G 93 TRP G 106 -1 O VAL G 98 N SER G 36 SHEET 5 AB2 5 LEU G 110 VAL G 118 -1 O VAL G 113 N TYR G 103 SHEET 1 AB3 5 THR G 59 TYR G 61 0 SHEET 2 AB3 5 GLU G 47 TYR G 53 -1 N TYR G 51 O ASN G 60 SHEET 3 AB3 5 ARG G 34 GLN G 40 -1 N ARG G 39 O GLU G 47 SHEET 4 AB3 5 ALA G 93 TRP G 106 -1 O VAL G 98 N SER G 36 SHEET 5 AB3 5 VAL G 123 VAL G 125 -1 O VAL G 125 N ALA G 93 SHEET 1 AB4 4 GLN H 3 SER H 7 0 SHEET 2 AB4 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AB4 4 GLN H 79 LEU H 84 -1 O PHE H 80 N CYS H 22 SHEET 4 AB4 4 VAL H 69 ASP H 74 -1 N THR H 70 O ASN H 83 SHEET 1 AB5 5 THR H 59 TYR H 61 0 SHEET 2 AB5 5 GLU H 47 TYR H 53 -1 N TYR H 51 O ASN H 60 SHEET 3 AB5 5 ARG H 34 GLN H 40 -1 N ARG H 39 O GLU H 47 SHEET 4 AB5 5 ALA H 93 TRP H 106 -1 O TYR H 96 N ILE H 38 SHEET 5 AB5 5 LEU H 110 VAL H 118 -1 O VAL H 113 N TYR H 103 SHEET 1 AB6 5 THR H 59 TYR H 61 0 SHEET 2 AB6 5 GLU H 47 TYR H 53 -1 N TYR H 51 O ASN H 60 SHEET 3 AB6 5 ARG H 34 GLN H 40 -1 N ARG H 39 O GLU H 47 SHEET 4 AB6 5 ALA H 93 TRP H 106 -1 O TYR H 96 N ILE H 38 SHEET 5 AB6 5 VAL H 123 VAL H 125 -1 O VAL H 125 N ALA H 93 SHEET 1 AB7 4 GLN I 3 SER I 7 0 SHEET 2 AB7 4 LEU I 18 SER I 25 -1 O SER I 25 N GLN I 3 SHEET 3 AB7 4 GLN I 79 LEU I 84 -1 O PHE I 80 N CYS I 22 SHEET 4 AB7 4 VAL I 69 ASP I 74 -1 N THR I 70 O ASN I 83 SHEET 1 AB8 5 THR I 59 TYR I 61 0 SHEET 2 AB8 5 GLU I 47 TYR I 53 -1 N TYR I 51 O ASN I 60 SHEET 3 AB8 5 ARG I 34 GLN I 40 -1 N ARG I 39 O GLU I 47 SHEET 4 AB8 5 ALA I 93 TRP I 106 -1 O TYR I 96 N ILE I 38 SHEET 5 AB8 5 LEU I 110 VAL I 118 -1 O VAL I 113 N TYR I 103 SHEET 1 AB9 5 THR I 59 TYR I 61 0 SHEET 2 AB9 5 GLU I 47 TYR I 53 -1 N TYR I 51 O ASN I 60 SHEET 3 AB9 5 ARG I 34 GLN I 40 -1 N ARG I 39 O GLU I 47 SHEET 4 AB9 5 ALA I 93 TRP I 106 -1 O TYR I 96 N ILE I 38 SHEET 5 AB9 5 VAL I 123 VAL I 125 -1 O VAL I 123 N TYR I 95 SHEET 1 AC1 5 VAL B 158 LEU B 161 0 SHEET 2 AC1 5 VAL B 169 THR B 173 -1 O VAL B 171 N VAL B 159 SHEET 3 AC1 5 LEU B 38 LYS B 60 1 N LYS B 60 O LEU B 172 SHEET 4 AC1 5 SER B 337 CYS B 340 1 O VAL B 338 N LYS B 45 SHEET 5 AC1 5 LEU B 332 ILE B 333 -1 N LEU B 332 O ILE B 339 SHEET 1 AC2 8 MET B 226 THR B 227 0 SHEET 2 AC2 8 THR B 263 ASP B 270 -1 O GLY B 264 N MET B 226 SHEET 3 AC2 8 TYR B 275 GLU B 287 -1 O TYR B 275 N ASP B 270 SHEET 4 AC2 8 LEU B 38 LYS B 60 -1 N LYS B 55 O VAL B 280 SHEET 5 AC2 8 ALA B 291 PRO B 298 -1 O LEU B 297 N VAL B 39 SHEET 6 AC2 8 PHE B 315 ARG B 319 -1 O VAL B 318 N TYR B 292 SHEET 7 AC2 8 LEU B 322 ILE B 326 -1 O SER B 324 N LEU B 317 SHEET 8 AC2 8 ALA B 345 THR B 346 -1 O THR B 346 N ASN B 325 SHEET 1 AC3 5 THR B 101 HIS B 102 0 SHEET 2 AC3 5 ILE B 114 ALA B 116 -1 O ILE B 114 N HIS B 102 SHEET 3 AC3 5 VAL C 425 SER C 428 1 O ILE C 426 N MET B 115 SHEET 4 AC3 5 THR C 419 LEU C 422 -1 N ALA C 420 O ILE C 427 SHEET 5 AC3 5 CYS C 392 CYS C 394 -1 N GLN C 393 O VAL C 421 SHEET 1 AC4 4 ALA B 123 THR B 124 0 SHEET 2 AC4 4 PHE C 376 SER C 379 -1 O LEU C 378 N ALA B 123 SHEET 3 AC4 4 VAL C 382 ALA C 385 -1 O PHE C 384 N ALA C 377 SHEET 4 AC4 4 LEU C 410 ILE C 412 -1 O LEU C 410 N ALA C 385 SHEET 1 AC5 3 PHE B 301 ASN B 302 0 SHEET 2 AC5 3 GLU B 307 SER B 310 -1 O TRP B 308 N PHE B 301 SHEET 3 AC5 3 ARG B 365 LEU B 367 -1 O GLU B 366 N ILE B 309 SHEET 1 AC6 5 VAL C 158 GLN C 162 0 SHEET 2 AC6 5 THR C 168 THR C 173 -1 O VAL C 171 N VAL C 159 SHEET 3 AC6 5 LEU C 38 LYS C 60 1 N LYS C 60 O LEU C 172 SHEET 4 AC6 5 SER C 337 CYS C 340 1 O VAL C 338 N LYS C 45 SHEET 5 AC6 5 LEU C 332 ILE C 333 -1 N LEU C 332 O ILE C 339 SHEET 1 AC7 7 THR C 263 ASP C 270 0 SHEET 2 AC7 7 TYR C 275 GLU C 287 -1 O TYR C 275 N ASP C 270 SHEET 3 AC7 7 LEU C 38 LYS C 60 -1 N ILE C 48 O THR C 286 SHEET 4 AC7 7 ALA C 291 PRO C 298 -1 O LEU C 297 N VAL C 39 SHEET 5 AC7 7 PHE C 315 ARG C 319 -1 O VAL C 318 N TYR C 292 SHEET 6 AC7 7 LEU C 322 ILE C 326 -1 O LEU C 322 N ARG C 319 SHEET 7 AC7 7 ALA C 345 THR C 346 -1 O THR C 346 N ASN C 325 SHEET 1 AC8 3 PHE C 301 ASN C 302 0 SHEET 2 AC8 3 GLU C 307 SER C 310 -1 O TRP C 308 N PHE C 301 SHEET 3 AC8 3 ARG C 365 LEU C 367 -1 O GLU C 366 N ILE C 309 SHEET 1 AC9 4 LEU E 4 SER E 7 0 SHEET 2 AC9 4 VAL E 19 ALA E 25 -1 O GLN E 24 N THR E 5 SHEET 3 AC9 4 ASP E 70 ILE E 75 -1 O ILE E 75 N VAL E 19 SHEET 4 AC9 4 SER E 63 SER E 67 -1 N SER E 63 O THR E 74 SHEET 1 AD1 5 SER E 53 LEU E 54 0 SHEET 2 AD1 5 LYS E 45 TYR E 49 -1 N TYR E 49 O SER E 53 SHEET 3 AD1 5 LEU E 33 GLN E 38 -1 N GLN E 37 O LYS E 45 SHEET 4 AD1 5 ALA E 84 GLN E 89 -1 O GLN E 88 N HIS E 34 SHEET 5 AD1 5 THR E 96 PHE E 97 -1 O THR E 96 N GLN E 89 SHEET 1 AD2 4 LEU D 4 SER D 7 0 SHEET 2 AD2 4 VAL D 19 ALA D 25 -1 O GLN D 24 N THR D 5 SHEET 3 AD2 4 ASP D 70 ILE D 75 -1 O ILE D 75 N VAL D 19 SHEET 4 AD2 4 SER D 63 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AD3 5 SER D 53 LEU D 54 0 SHEET 2 AD3 5 LYS D 45 TYR D 49 -1 N TYR D 49 O SER D 53 SHEET 3 AD3 5 LEU D 33 GLN D 38 -1 N GLN D 37 O LYS D 45 SHEET 4 AD3 5 ALA D 84 GLN D 89 -1 O GLN D 88 N HIS D 34 SHEET 5 AD3 5 THR D 96 PHE D 97 -1 O THR D 96 N GLN D 89 SSBOND 1 CYS A 331 CYS A 340 1555 1555 2.03 SSBOND 2 CYS A 355 CYS A 363 1555 1555 2.03 SSBOND 3 CYS A 387 CYS A 392 1555 1555 2.04 SSBOND 4 CYS F 23 CYS F 87 1555 1555 2.05 SSBOND 5 CYS G 22 CYS G 97 1555 1555 2.04 SSBOND 6 CYS H 22 CYS H 97 1555 1555 2.04 SSBOND 7 CYS I 22 CYS I 97 1555 1555 2.04 SSBOND 8 CYS B 331 CYS B 340 1555 1555 2.03 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 C 331 CYS C 340 1555 1555 2.03 SSBOND 12 CYS C 355 CYS C 363 1555 1555 2.03 SSBOND 13 CYS C 387 CYS C 392 1555 1555 2.04 SSBOND 14 CYS E 23 CYS E 87 1555 1555 2.05 SSBOND 15 CYS D 23 CYS D 87 1555 1555 2.05 LINK ND2 ASN A 67 C1 NAG A 503 1555 1555 1.44 LINK ND2 ASN A 99 C1 NAG A 501 1555 1555 1.44 LINK ND2 ASN A 414 C1 NAG A 502 1555 1555 1.44 LINK ND2 ASN B 67 C1 NAG B 503 1555 1555 1.44 LINK ND2 ASN B 99 C1 NAG B 501 1555 1555 1.44 LINK ND2 ASN B 414 C1 NAG B 502 1555 1555 1.44 LINK ND2 ASN C 67 C1 NAG C 503 1555 1555 1.44 LINK ND2 ASN C 99 C1 NAG C 501 1555 1555 1.44 LINK ND2 ASN C 414 C1 NAG C 502 1555 1555 1.44 CISPEP 1 SER F 7 PRO F 8 0 -4.01 CISPEP 2 TYR F 93 PRO F 94 0 -0.80 CISPEP 3 SER E 7 PRO E 8 0 -3.68 CISPEP 4 TYR E 93 PRO E 94 0 -0.71 CISPEP 5 SER D 7 PRO D 8 0 -3.98 CISPEP 6 TYR D 93 PRO D 94 0 -0.17 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