HEADER VIRAL PROTEIN/IMMUNE SYSTEM 31-MAR-25 9UA9 TITLE NIPAH VIRUS FUSION GLYCOPROTEIN IN COMPLEX WITH A BROADLY NEUTRALIZING TITLE 2 ANTIBODY 1D6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 1D6-VL; COMPND 3 CHAIN: F, E, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 1D6 VH; COMPND 7 CHAIN: H, G, I; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FUSION GLYCOPROTEIN F0; COMPND 11 CHAIN: A, C, B; COMPND 12 SYNONYM: PROTEIN F; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA; SOURCE 3 ORGANISM_TAXID: 9539; 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: HENIPAVIRUS NIPAHENSE; SOURCE 15 ORGANISM_TAXID: 3052225; 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 9UA9 0 SPRSDE 09-APR-25 9UA9 8XN9 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. 1.99 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) : 1.990 REMARK 3 NUMBER OF PARTICLES : 114162 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 9UA9 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_1300058042. 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 1D6; REMARK 245 NIPAH VIRUS FUSION GLYCOPROTEIN; REMARK 245 1D6 VH; 1D6 VL REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.03 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) : 400.00 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) : 4751.00 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: F, H, A, C, B, G, I, E, D, J, REMARK 350 AND CHAINS: K, L 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 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 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 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 OE1 GLU B 95 O HOH B 601 2.18 REMARK 500 O HOH B 601 O HOH B 693 2.19 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 ASN F 52 -19.36 72.38 REMARK 500 ASP F 53 2.14 -150.08 REMARK 500 SER H 15 -0.45 70.55 REMARK 500 ILE H 48 -62.28 -106.76 REMARK 500 ASN A 51 72.25 51.43 REMARK 500 ASP A 188 -8.56 75.11 REMARK 500 TYR A 274 61.32 60.66 REMARK 500 GLN A 290 36.88 -98.32 REMARK 500 ASN C 51 71.97 51.30 REMARK 500 LYS C 167 78.62 -100.05 REMARK 500 ASP C 188 -7.42 73.77 REMARK 500 ASN B 51 72.06 51.36 REMARK 500 LYS B 167 77.53 -100.14 REMARK 500 ASP B 188 -7.02 74.03 REMARK 500 TYR B 274 61.79 61.45 REMARK 500 GLN B 290 37.19 -97.55 REMARK 500 GLU B 441 -60.50 -94.16 REMARK 500 SER G 15 -0.68 70.77 REMARK 500 ILE G 48 -62.54 -105.19 REMARK 500 SER I 15 -0.56 70.77 REMARK 500 ILE I 48 -62.82 -105.32 REMARK 500 ASN E 52 -19.90 71.44 REMARK 500 ASN D 52 -19.18 71.78 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63982 RELATED DB: EMDB REMARK 900 NIPAH VIRUS FUSION GLYCOPROTEIN IN COMPLEX WITH A BROADLY REMARK 900 NEUTRALIZING ANTIBODY 1D6 DBREF 9UA9 F 2 110 PDB 9UA9 9UA9 2 110 DBREF 9UA9 H 1 125 PDB 9UA9 9UA9 1 125 DBREF 9UA9 A 27 476 UNP Q9IH63 FUS_NIPAV 27 476 DBREF 9UA9 C 27 476 UNP Q9IH63 FUS_NIPAV 27 476 DBREF 9UA9 B 27 476 UNP Q9IH63 FUS_NIPAV 27 476 DBREF 9UA9 G 1 125 PDB 9UA9 9UA9 1 125 DBREF 9UA9 I 1 125 PDB 9UA9 9UA9 1 125 DBREF 9UA9 E 2 110 PDB 9UA9 9UA9 2 110 DBREF 9UA9 D 2 110 PDB 9UA9 9UA9 2 110 SEQRES 1 F 109 PRO VAL LEU THR GLN PRO PRO SER ALA SER GLU ALA ALA SEQRES 2 F 109 ARG LYS SER VAL THR ILE SER CYS SER GLY SER SER SER SEQRES 3 F 109 ASN ILE GLY SER ASN SER VAL SER TRP TYR GLN GLN LEU SEQRES 4 F 109 PRO GLY THR ALA LEU LYS LEU LEU ILE SER TYR ASN ASP SEQRES 5 F 109 GLN ARG ALA SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 F 109 LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY LEU SEQRES 7 F 109 GLN THR GLU ASP GLU ALA ASP TYR TYR CYS ALA ALA TRP SEQRES 8 F 109 ASP ASP SER LEU SER GLY PRO VAL PHE GLY GLY GLY THR SEQRES 9 F 109 ARG LEU THR VAL LEU SEQRES 1 H 125 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 125 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 125 ALA SER ILE SER SER TYR TRP TRP GLY TRP ILE ARG GLN SEQRES 4 H 125 PRO PRO GLY LYS GLY LEU GLU TRP ILE ALA ASP ILE TYR SEQRES 5 H 125 PRO ASN SER GLY SER THR ASN TYR ASN PRO SER LEU LYS SEQRES 6 H 125 SER ARG VAL THR ASN SER LYS ASP ALA SER LYS ASN GLN SEQRES 7 H 125 PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR SEQRES 8 H 125 ALA MET TYR TYR CYS ALA ARG ALA PRO ARG GLY TYR SER SEQRES 9 H 125 TYR SER TYR VAL PHE GLY HIS ARG PHE ASP VAL TRP GLY SEQRES 10 H 125 PRO GLY VAL LEU VAL THR VAL SER SEQRES 1 A 450 ILE LEU HIS TYR GLU LYS LEU SER LYS ILE GLY LEU VAL SEQRES 2 A 450 LYS GLY VAL THR ARG LYS TYR LYS ILE LYS SER ASN PRO SEQRES 3 A 450 LEU THR LYS ASP ILE VAL ILE LYS MET ILE PRO ASN VAL SEQRES 4 A 450 SER ASN MET SER GLN CYS THR GLY SER VAL MET GLU ASN SEQRES 5 A 450 TYR LYS THR ARG LEU ASN GLY ILE LEU THR PRO ILE LYS SEQRES 6 A 450 GLY ALA LEU GLU ILE TYR LYS ASN ASN THR HIS ASP LEU SEQRES 7 A 450 VAL GLY ASP VAL ARG LEU ALA GLY VAL ILE MET ALA GLY SEQRES 8 A 450 VAL ALA ILE GLY ILE ALA THR ALA ALA GLN ILE THR ALA SEQRES 9 A 450 GLY VAL ALA LEU TYR GLU ALA MET LYS ASN ALA ASP ASN SEQRES 10 A 450 ILE ASN LYS LEU LYS SER SER ILE GLU SER THR ASN GLU SEQRES 11 A 450 ALA VAL VAL LYS LEU GLN GLU THR ALA GLU LYS THR VAL SEQRES 12 A 450 TYR VAL LEU THR ALA LEU GLN ASP TYR ILE ASN THR ASN SEQRES 13 A 450 LEU VAL PRO THR ILE ASP LYS ILE SER CYS LYS GLN THR SEQRES 14 A 450 GLU LEU SER LEU ASP LEU ALA LEU SER LYS TYR LEU SER SEQRES 15 A 450 ASP LEU LEU PHE VAL PHE GLY PRO ASN LEU GLN ASP PRO SEQRES 16 A 450 VAL SER ASN SER MET THR ILE GLN ALA ILE SER GLN ALA SEQRES 17 A 450 PHE GLY GLY ASN TYR GLU THR LEU LEU ARG THR LEU GLY SEQRES 18 A 450 TYR ALA THR GLU ASP PHE ASP ASP LEU LEU GLU SER ASP SEQRES 19 A 450 SER ILE THR GLY GLN ILE ILE TYR VAL ASP LEU SER SER SEQRES 20 A 450 TYR TYR ILE ILE VAL ARG VAL TYR PHE PRO ILE LEU THR SEQRES 21 A 450 GLU ILE GLN GLN ALA TYR ILE GLN GLU LEU LEU PRO VAL SEQRES 22 A 450 SER PHE ASN ASN ASP ASN SER GLU TRP ILE SER ILE VAL SEQRES 23 A 450 PRO ASN PHE ILE LEU VAL ARG ASN THR LEU ILE SER ASN SEQRES 24 A 450 ILE GLU ILE GLY PHE CYS LEU ILE THR LYS ARG SER VAL SEQRES 25 A 450 ILE CYS ASN GLN ASP TYR ALA THR PRO MET THR ASN ASN SEQRES 26 A 450 MET ARG GLU CYS LEU THR GLY SER THR GLU LYS CYS PRO SEQRES 27 A 450 ARG GLU LEU VAL VAL SER SER HIS VAL PRO ARG PHE ALA SEQRES 28 A 450 LEU SER ASN GLY VAL LEU PHE ALA ASN CYS ILE SER VAL SEQRES 29 A 450 THR CYS GLN CYS GLN THR THR GLY ARG ALA ILE SER GLN SEQRES 30 A 450 SER GLY GLU GLN THR LEU LEU MET ILE ASP ASN THR THR SEQRES 31 A 450 CYS PRO THR ALA VAL LEU GLY ASN VAL ILE ILE SER LEU SEQRES 32 A 450 GLY LYS TYR LEU GLY SER VAL ASN TYR ASN SER GLU GLY SEQRES 33 A 450 ILE ALA ILE GLY PRO PRO VAL PHE THR ASP LYS VAL ASP SEQRES 34 A 450 ILE SER SER GLN ILE SER SER MET ASN GLN SER LEU GLN SEQRES 35 A 450 GLN SER LYS ASP TYR ILE LYS GLU SEQRES 1 C 450 ILE LEU HIS TYR GLU LYS LEU SER LYS ILE GLY LEU VAL SEQRES 2 C 450 LYS GLY VAL THR ARG LYS TYR LYS ILE LYS SER ASN PRO SEQRES 3 C 450 LEU THR LYS ASP ILE VAL ILE LYS MET ILE PRO ASN VAL SEQRES 4 C 450 SER ASN MET SER GLN CYS THR GLY SER VAL MET GLU ASN SEQRES 5 C 450 TYR LYS THR ARG LEU ASN GLY ILE LEU THR PRO ILE LYS SEQRES 6 C 450 GLY ALA LEU GLU ILE TYR LYS ASN ASN THR HIS ASP LEU SEQRES 7 C 450 VAL GLY ASP VAL ARG LEU ALA GLY VAL ILE MET ALA GLY SEQRES 8 C 450 VAL ALA ILE GLY ILE ALA THR ALA ALA GLN ILE THR ALA SEQRES 9 C 450 GLY VAL ALA LEU TYR GLU ALA MET LYS ASN ALA ASP ASN SEQRES 10 C 450 ILE ASN LYS LEU LYS SER SER ILE GLU SER THR ASN GLU SEQRES 11 C 450 ALA VAL VAL LYS LEU GLN GLU THR ALA GLU LYS THR VAL SEQRES 12 C 450 TYR VAL LEU THR ALA LEU GLN ASP TYR ILE ASN THR ASN SEQRES 13 C 450 LEU VAL PRO THR ILE ASP LYS ILE SER CYS LYS GLN THR SEQRES 14 C 450 GLU LEU SER LEU ASP LEU ALA LEU SER LYS TYR LEU SER SEQRES 15 C 450 ASP LEU LEU PHE VAL PHE GLY PRO ASN LEU GLN ASP PRO SEQRES 16 C 450 VAL SER ASN SER MET THR ILE GLN ALA ILE SER GLN ALA SEQRES 17 C 450 PHE GLY GLY ASN TYR GLU THR LEU LEU ARG THR LEU GLY SEQRES 18 C 450 TYR ALA THR GLU ASP PHE ASP ASP LEU LEU GLU SER ASP SEQRES 19 C 450 SER ILE THR GLY GLN ILE ILE TYR VAL ASP LEU SER SER SEQRES 20 C 450 TYR TYR ILE ILE VAL ARG VAL TYR PHE PRO ILE LEU THR SEQRES 21 C 450 GLU ILE GLN GLN ALA TYR ILE GLN GLU LEU LEU PRO VAL SEQRES 22 C 450 SER PHE ASN ASN ASP ASN SER GLU TRP ILE SER ILE VAL SEQRES 23 C 450 PRO ASN PHE ILE LEU VAL ARG ASN THR LEU ILE SER ASN SEQRES 24 C 450 ILE GLU ILE GLY PHE CYS LEU ILE THR LYS ARG SER VAL SEQRES 25 C 450 ILE CYS ASN GLN ASP TYR ALA THR PRO MET THR ASN ASN SEQRES 26 C 450 MET ARG GLU CYS LEU THR GLY SER THR GLU LYS CYS PRO SEQRES 27 C 450 ARG GLU LEU VAL VAL SER SER HIS VAL PRO ARG PHE ALA SEQRES 28 C 450 LEU SER ASN GLY VAL LEU PHE ALA ASN CYS ILE SER VAL SEQRES 29 C 450 THR CYS GLN CYS GLN THR THR GLY ARG ALA ILE SER GLN SEQRES 30 C 450 SER GLY GLU GLN THR LEU LEU MET ILE ASP ASN THR THR SEQRES 31 C 450 CYS PRO THR ALA VAL LEU GLY ASN VAL ILE ILE SER LEU SEQRES 32 C 450 GLY LYS TYR LEU GLY SER VAL ASN TYR ASN SER GLU GLY SEQRES 33 C 450 ILE ALA ILE GLY PRO PRO VAL PHE THR ASP LYS VAL ASP SEQRES 34 C 450 ILE SER SER GLN ILE SER SER MET ASN GLN SER LEU GLN SEQRES 35 C 450 GLN SER LYS ASP TYR ILE LYS GLU SEQRES 1 B 450 ILE LEU HIS TYR GLU LYS LEU SER LYS ILE GLY LEU VAL SEQRES 2 B 450 LYS GLY VAL THR ARG LYS TYR LYS ILE LYS SER ASN PRO SEQRES 3 B 450 LEU THR LYS ASP ILE VAL ILE LYS MET ILE PRO ASN VAL SEQRES 4 B 450 SER ASN MET SER GLN CYS THR GLY SER VAL MET GLU ASN SEQRES 5 B 450 TYR LYS THR ARG LEU ASN GLY ILE LEU THR PRO ILE LYS SEQRES 6 B 450 GLY ALA LEU GLU ILE TYR LYS ASN ASN THR HIS ASP LEU SEQRES 7 B 450 VAL GLY ASP VAL ARG LEU ALA GLY VAL ILE MET ALA GLY SEQRES 8 B 450 VAL ALA ILE GLY ILE ALA THR ALA ALA GLN ILE THR ALA SEQRES 9 B 450 GLY VAL ALA LEU TYR GLU ALA MET LYS ASN ALA ASP ASN SEQRES 10 B 450 ILE ASN LYS LEU LYS SER SER ILE GLU SER THR ASN GLU SEQRES 11 B 450 ALA VAL VAL LYS LEU GLN GLU THR ALA GLU LYS THR VAL SEQRES 12 B 450 TYR VAL LEU THR ALA LEU GLN ASP TYR ILE ASN THR ASN SEQRES 13 B 450 LEU VAL PRO THR ILE ASP LYS ILE SER CYS LYS GLN THR SEQRES 14 B 450 GLU LEU SER LEU ASP LEU ALA LEU SER LYS TYR LEU SER SEQRES 15 B 450 ASP LEU LEU PHE VAL PHE GLY PRO ASN LEU GLN ASP PRO SEQRES 16 B 450 VAL SER ASN SER MET THR ILE GLN ALA ILE SER GLN ALA SEQRES 17 B 450 PHE GLY GLY ASN TYR GLU THR LEU LEU ARG THR LEU GLY SEQRES 18 B 450 TYR ALA THR GLU ASP PHE ASP ASP LEU LEU GLU SER ASP SEQRES 19 B 450 SER ILE THR GLY GLN ILE ILE TYR VAL ASP LEU SER SER SEQRES 20 B 450 TYR TYR ILE ILE VAL ARG VAL TYR PHE PRO ILE LEU THR SEQRES 21 B 450 GLU ILE GLN GLN ALA TYR ILE GLN GLU LEU LEU PRO VAL SEQRES 22 B 450 SER PHE ASN ASN ASP ASN SER GLU TRP ILE SER ILE VAL SEQRES 23 B 450 PRO ASN PHE ILE LEU VAL ARG ASN THR LEU ILE SER ASN SEQRES 24 B 450 ILE GLU ILE GLY PHE CYS LEU ILE THR LYS ARG SER VAL SEQRES 25 B 450 ILE CYS ASN GLN ASP TYR ALA THR PRO MET THR ASN ASN SEQRES 26 B 450 MET ARG GLU CYS LEU THR GLY SER THR GLU LYS CYS PRO SEQRES 27 B 450 ARG GLU LEU VAL VAL SER SER HIS VAL PRO ARG PHE ALA SEQRES 28 B 450 LEU SER ASN GLY VAL LEU PHE ALA ASN CYS ILE SER VAL SEQRES 29 B 450 THR CYS GLN CYS GLN THR THR GLY ARG ALA ILE SER GLN SEQRES 30 B 450 SER GLY GLU GLN THR LEU LEU MET ILE ASP ASN THR THR SEQRES 31 B 450 CYS PRO THR ALA VAL LEU GLY ASN VAL ILE ILE SER LEU SEQRES 32 B 450 GLY LYS TYR LEU GLY SER VAL ASN TYR ASN SER GLU GLY SEQRES 33 B 450 ILE ALA ILE GLY PRO PRO VAL PHE THR ASP LYS VAL ASP SEQRES 34 B 450 ILE SER SER GLN ILE SER SER MET ASN GLN SER LEU GLN SEQRES 35 B 450 GLN SER LYS ASP TYR ILE LYS GLU SEQRES 1 G 125 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 G 125 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 G 125 ALA SER ILE SER SER TYR TRP TRP GLY TRP ILE ARG GLN SEQRES 4 G 125 PRO PRO GLY LYS GLY LEU GLU TRP ILE ALA ASP ILE TYR SEQRES 5 G 125 PRO ASN SER GLY SER THR ASN TYR ASN PRO SER LEU LYS SEQRES 6 G 125 SER ARG VAL THR ASN SER LYS ASP ALA SER LYS ASN GLN SEQRES 7 G 125 PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR SEQRES 8 G 125 ALA MET TYR TYR CYS ALA ARG ALA PRO ARG GLY TYR SER SEQRES 9 G 125 TYR SER TYR VAL PHE GLY HIS ARG PHE ASP VAL TRP GLY SEQRES 10 G 125 PRO GLY VAL LEU VAL THR VAL SER SEQRES 1 I 125 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 I 125 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 I 125 ALA SER ILE SER SER TYR TRP TRP GLY TRP ILE ARG GLN SEQRES 4 I 125 PRO PRO GLY LYS GLY LEU GLU TRP ILE ALA ASP ILE TYR SEQRES 5 I 125 PRO ASN SER GLY SER THR ASN TYR ASN PRO SER LEU LYS SEQRES 6 I 125 SER ARG VAL THR ASN SER LYS ASP ALA SER LYS ASN GLN SEQRES 7 I 125 PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR SEQRES 8 I 125 ALA MET TYR TYR CYS ALA ARG ALA PRO ARG GLY TYR SER SEQRES 9 I 125 TYR SER TYR VAL PHE GLY HIS ARG PHE ASP VAL TRP GLY SEQRES 10 I 125 PRO GLY VAL LEU VAL THR VAL SER SEQRES 1 E 109 PRO VAL LEU THR GLN PRO PRO SER ALA SER GLU ALA ALA SEQRES 2 E 109 ARG LYS SER VAL THR ILE SER CYS SER GLY SER SER SER SEQRES 3 E 109 ASN ILE GLY SER ASN SER VAL SER TRP TYR GLN GLN LEU SEQRES 4 E 109 PRO GLY THR ALA LEU LYS LEU LEU ILE SER TYR ASN ASP SEQRES 5 E 109 GLN ARG ALA SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 E 109 LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY LEU SEQRES 7 E 109 GLN THR GLU ASP GLU ALA ASP TYR TYR CYS ALA ALA TRP SEQRES 8 E 109 ASP ASP SER LEU SER GLY PRO VAL PHE GLY GLY GLY THR SEQRES 9 E 109 ARG LEU THR VAL LEU SEQRES 1 D 109 PRO VAL LEU THR GLN PRO PRO SER ALA SER GLU ALA ALA SEQRES 2 D 109 ARG LYS SER VAL THR ILE SER CYS SER GLY SER SER SER SEQRES 3 D 109 ASN ILE GLY SER ASN SER VAL SER TRP TYR GLN GLN LEU SEQRES 4 D 109 PRO GLY THR ALA LEU LYS LEU LEU ILE SER TYR ASN ASP SEQRES 5 D 109 GLN ARG ALA SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 D 109 LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY LEU SEQRES 7 D 109 GLN THR GLU ASP GLU ALA ASP TYR TYR CYS ALA ALA TRP SEQRES 8 D 109 ASP ASP SER LEU SER GLY PRO VAL PHE GLY GLY GLY THR SEQRES 9 D 109 ARG LEU THR VAL LEU HET NAG J 1 14 HET NAG J 2 14 HET NAG K 1 14 HET NAG K 2 14 HET NAG L 1 14 HET NAG L 2 14 HET NAG A 501 14 HET NAG A 502 14 HET NAG A 503 14 HET NAG C 501 14 HET NAG C 502 14 HET NAG C 503 14 HET NAG B 501 14 HET NAG B 502 14 HET NAG B 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 15(C8 H15 N O6) FORMUL 22 HOH *553(H2 O) HELIX 1 AA1 GLN F 80 GLU F 84 5 5 HELIX 2 AA2 SER H 28 TYR H 32 5 5 HELIX 3 AA3 LEU H 64 SER H 66 5 3 HELIX 4 AA4 THR H 87 THR H 91 5 5 HELIX 5 AA5 HIS A 29 LYS A 35 1 7 HELIX 6 AA6 VAL A 65 THR A 72 5 8 HELIX 7 AA7 SER A 74 ASN A 99 1 26 HELIX 8 AA8 GLY A 117 GLY A 121 1 5 HELIX 9 AA9 ALA A 125 LYS A 146 1 22 HELIX 10 AB1 LEU A 147 SER A 153 1 7 HELIX 11 AB2 LEU A 175 ASN A 182 1 8 HELIX 12 AB3 LEU A 183 ILE A 187 5 5 HELIX 13 AB4 SER A 191 GLY A 215 1 25 HELIX 14 AB5 ILE A 228 SER A 232 1 5 HELIX 15 AB6 GLN A 233 GLY A 236 5 4 HELIX 16 AB7 ASN A 238 GLY A 247 1 10 HELIX 17 AB8 ASP A 252 SER A 259 1 8 HELIX 18 AB9 ILE A 328 CYS A 331 5 4 HELIX 19 AC1 THR A 349 THR A 357 1 9 HELIX 20 AC2 SER A 359 CYS A 363 5 5 HELIX 21 AC3 ASN A 437 GLU A 441 5 5 HELIX 22 AC4 ASP A 452 GLU A 476 1 25 HELIX 23 AC5 HIS C 29 LYS C 35 1 7 HELIX 24 AC6 VAL C 65 THR C 72 5 8 HELIX 25 AC7 SER C 74 ASN C 99 1 26 HELIX 26 AC8 GLY C 117 GLY C 121 1 5 HELIX 27 AC9 ALA C 125 LYS C 146 1 22 HELIX 28 AD1 LEU C 147 SER C 153 1 7 HELIX 29 AD2 LEU C 175 ASN C 182 1 8 HELIX 30 AD3 LEU C 183 ILE C 187 5 5 HELIX 31 AD4 SER C 191 GLY C 215 1 25 HELIX 32 AD5 THR C 227 SER C 232 1 6 HELIX 33 AD6 GLN C 233 GLY C 236 5 4 HELIX 34 AD7 ASN C 238 GLY C 247 1 10 HELIX 35 AD8 ASP C 252 SER C 259 1 8 HELIX 36 AD9 ILE C 328 CYS C 331 5 4 HELIX 37 AE1 THR C 349 THR C 357 1 9 HELIX 38 AE2 SER C 359 CYS C 363 5 5 HELIX 39 AE3 ASN C 437 GLU C 441 5 5 HELIX 40 AE4 ASP C 452 GLU C 476 1 25 HELIX 41 AE5 HIS B 29 LYS B 35 1 7 HELIX 42 AE6 VAL B 65 THR B 72 5 8 HELIX 43 AE7 SER B 74 ASN B 99 1 26 HELIX 44 AE8 GLY B 117 GLY B 121 1 5 HELIX 45 AE9 ALA B 125 LYS B 146 1 22 HELIX 46 AF1 LEU B 147 SER B 153 1 7 HELIX 47 AF2 LEU B 175 ASN B 182 1 8 HELIX 48 AF3 LEU B 183 ILE B 187 5 5 HELIX 49 AF4 SER B 191 GLY B 215 1 25 HELIX 50 AF5 ILE B 228 SER B 232 1 5 HELIX 51 AF6 GLN B 233 GLY B 236 5 4 HELIX 52 AF7 ASN B 238 GLY B 247 1 10 HELIX 53 AF8 ASP B 252 SER B 259 1 8 HELIX 54 AF9 ILE B 328 CYS B 331 5 4 HELIX 55 AG1 THR B 349 THR B 357 1 9 HELIX 56 AG2 SER B 359 CYS B 363 5 5 HELIX 57 AG3 ASN B 437 GLU B 441 5 5 HELIX 58 AG4 ASP B 452 GLU B 476 1 25 HELIX 59 AG5 SER G 28 TYR G 32 5 5 HELIX 60 AG6 LEU G 64 SER G 66 5 3 HELIX 61 AG7 THR G 87 THR G 91 5 5 HELIX 62 AG8 SER I 28 TYR I 32 5 5 HELIX 63 AG9 LEU I 64 SER I 66 5 3 HELIX 64 AH1 THR I 87 THR I 91 5 5 HELIX 65 AH2 GLN E 80 GLU E 84 5 5 HELIX 66 AH3 GLN D 80 GLU D 84 5 5 SHEET 1 AA1 6 SER F 9 ALA F 13 0 SHEET 2 AA1 6 THR F 105 LEU F 110 1 O THR F 108 N ALA F 10 SHEET 3 AA1 6 ASP F 86 ASP F 93 -1 N TYR F 87 O THR F 105 SHEET 4 AA1 6 VAL F 34 GLN F 39 -1 N SER F 35 O ALA F 90 SHEET 5 AA1 6 LYS F 46 SER F 50 -1 O LEU F 48 N TRP F 36 SHEET 6 AA1 6 GLN F 54 ARG F 55 -1 O GLN F 54 N SER F 50 SHEET 1 AA2 4 SER F 9 ALA F 13 0 SHEET 2 AA2 4 THR F 105 LEU F 110 1 O THR F 108 N ALA F 10 SHEET 3 AA2 4 ASP F 86 ASP F 93 -1 N TYR F 87 O THR F 105 SHEET 4 AA2 4 GLY F 98 PHE F 101 -1 O GLY F 98 N ASP F 93 SHEET 1 AA3 3 VAL F 18 SER F 23 0 SHEET 2 AA3 3 SER F 71 ILE F 76 -1 O ILE F 76 N VAL F 18 SHEET 3 AA3 3 PHE F 63 SER F 68 -1 N SER F 68 O SER F 71 SHEET 1 AA4 4 GLN H 3 SER H 7 0 SHEET 2 AA4 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA4 4 GLN H 78 LEU H 83 -1 O PHE H 79 N CYS H 22 SHEET 4 AA4 4 VAL H 68 ASP H 73 -1 N ASP H 73 O GLN H 78 SHEET 1 AA5 6 LEU H 11 VAL H 12 0 SHEET 2 AA5 6 VAL H 120 VAL H 124 1 O THR H 123 N VAL H 12 SHEET 3 AA5 6 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 122 SHEET 4 AA5 6 TRP H 34 GLN H 39 -1 N ILE H 37 O TYR H 95 SHEET 5 AA5 6 GLU H 46 TYR H 52 -1 O ILE H 51 N TRP H 34 SHEET 6 AA5 6 SER H 57 TYR H 60 -1 O SER H 57 N TYR H 52 SHEET 1 AA6 4 LEU H 11 VAL H 12 0 SHEET 2 AA6 4 VAL H 120 VAL H 124 1 O THR H 123 N VAL H 12 SHEET 3 AA6 4 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 122 SHEET 4 AA6 4 VAL H 115 TRP H 116 -1 O VAL H 115 N ARG H 98 SHEET 1 AA7 2 ARG H 101 TYR H 103 0 SHEET 2 AA7 2 PHE H 109 HIS H 111 -1 O GLY H 110 N GLY H 102 SHEET 1 AA8 5 VAL A 158 GLN A 162 0 SHEET 2 AA8 5 THR A 168 THR A 173 -1 O VAL A 171 N VAL A 159 SHEET 3 AA8 5 LEU A 38 LYS A 60 1 N LYS A 60 O LEU A 172 SHEET 4 AA8 5 SER A 337 CYS A 340 1 O VAL A 338 N LYS A 45 SHEET 5 AA8 5 LEU A 332 ILE A 333 -1 N LEU A 332 O ILE A 339 SHEET 1 AA9 8 MET A 226 THR A 227 0 SHEET 2 AA9 8 THR A 263 ASP A 270 -1 O GLY A 264 N MET A 226 SHEET 3 AA9 8 TYR A 275 GLU A 287 -1 O ILE A 277 N ILE A 267 SHEET 4 AA9 8 LEU A 38 LYS A 60 -1 N LYS A 55 O VAL A 280 SHEET 5 AA9 8 ALA A 291 PRO A 298 -1 O LEU A 297 N VAL A 39 SHEET 6 AA9 8 PHE A 315 ARG A 319 -1 O VAL A 318 N TYR A 292 SHEET 7 AA9 8 LEU A 322 ILE A 326 -1 O SER A 324 N LEU A 317 SHEET 8 AA9 8 ALA A 345 THR A 346 -1 O THR A 346 N ASN A 325 SHEET 1 AB1 5 THR A 101 HIS A 102 0 SHEET 2 AB1 5 ILE A 114 ALA A 116 -1 O ILE A 114 N HIS A 102 SHEET 3 AB1 5 VAL B 425 SER B 428 1 O SER B 428 N MET A 115 SHEET 4 AB1 5 THR B 419 LEU B 422 -1 N LEU B 422 O VAL B 425 SHEET 5 AB1 5 CYS B 392 CYS B 394 -1 N GLN B 393 O VAL B 421 SHEET 1 AB2 4 ALA A 123 THR A 124 0 SHEET 2 AB2 4 PHE B 376 SER B 379 -1 O LEU B 378 N ALA A 123 SHEET 3 AB2 4 VAL B 382 ALA B 385 -1 O VAL B 382 N SER B 379 SHEET 4 AB2 4 LEU B 410 ILE B 412 -1 O LEU B 410 N ALA B 385 SHEET 1 AB3 3 PHE A 301 ASN A 302 0 SHEET 2 AB3 3 GLU A 307 SER A 310 -1 O TRP A 308 N PHE A 301 SHEET 3 AB3 3 ARG A 365 LEU A 367 -1 O GLU A 366 N ILE A 309 SHEET 1 AB4 4 LEU A 410 ILE A 412 0 SHEET 2 AB4 4 VAL A 382 ALA A 385 -1 N ALA A 385 O LEU A 410 SHEET 3 AB4 4 PHE A 376 SER A 379 -1 N ALA A 377 O PHE A 384 SHEET 4 AB4 4 ALA C 123 THR C 124 -1 O ALA C 123 N LEU A 378 SHEET 1 AB5 5 CYS A 392 CYS A 394 0 SHEET 2 AB5 5 THR A 419 LEU A 422 -1 O VAL A 421 N GLN A 393 SHEET 3 AB5 5 VAL A 425 SER A 428 -1 O VAL A 425 N LEU A 422 SHEET 4 AB5 5 ILE C 114 ALA C 116 1 O MET C 115 N SER A 428 SHEET 5 AB5 5 THR C 101 HIS C 102 -1 N HIS C 102 O ILE C 114 SHEET 1 AB6 5 VAL C 158 GLN C 162 0 SHEET 2 AB6 5 THR C 168 THR C 173 -1 O VAL C 171 N VAL C 159 SHEET 3 AB6 5 LEU C 38 LYS C 60 1 N LYS C 60 O LEU C 172 SHEET 4 AB6 5 SER C 337 CYS C 340 1 O VAL C 338 N LYS C 45 SHEET 5 AB6 5 LEU C 332 ILE C 333 -1 N LEU C 332 O ILE C 339 SHEET 1 AB7 7 THR C 263 ASP C 270 0 SHEET 2 AB7 7 TYR C 275 GLU C 287 -1 O ILE C 277 N ILE C 267 SHEET 3 AB7 7 LEU C 38 LYS C 60 -1 N LYS C 55 O VAL C 280 SHEET 4 AB7 7 ALA C 291 PRO C 298 -1 O LEU C 297 N VAL C 39 SHEET 5 AB7 7 PHE C 315 ARG C 319 -1 O VAL C 318 N TYR C 292 SHEET 6 AB7 7 LEU C 322 ILE C 326 -1 O SER C 324 N LEU C 317 SHEET 7 AB7 7 ALA C 345 THR C 346 -1 O THR C 346 N ASN C 325 SHEET 1 AB8 3 PHE C 301 ASN C 302 0 SHEET 2 AB8 3 GLU C 307 SER C 310 -1 O TRP C 308 N PHE C 301 SHEET 3 AB8 3 ARG C 365 LEU C 367 -1 O GLU C 366 N ILE C 309 SHEET 1 AB9 4 LEU C 410 ILE C 412 0 SHEET 2 AB9 4 VAL C 382 ALA C 385 -1 N ALA C 385 O LEU C 410 SHEET 3 AB9 4 PHE C 376 SER C 379 -1 N SER C 379 O VAL C 382 SHEET 4 AB9 4 ALA B 123 THR B 124 -1 O ALA B 123 N LEU C 378 SHEET 1 AC1 5 CYS C 392 CYS C 394 0 SHEET 2 AC1 5 THR C 419 LEU C 422 -1 O VAL C 421 N GLN C 393 SHEET 3 AC1 5 VAL C 425 SER C 428 -1 O VAL C 425 N LEU C 422 SHEET 4 AC1 5 ILE B 114 ALA B 116 1 O MET B 115 N ILE C 426 SHEET 5 AC1 5 THR B 101 HIS B 102 -1 N HIS B 102 O ILE B 114 SHEET 1 AC2 5 VAL B 158 GLN B 162 0 SHEET 2 AC2 5 THR B 168 THR B 173 -1 O VAL B 171 N VAL B 159 SHEET 3 AC2 5 LEU B 38 LYS B 60 1 N LYS B 60 O LEU B 172 SHEET 4 AC2 5 SER B 337 CYS B 340 1 O VAL B 338 N LYS B 45 SHEET 5 AC2 5 LEU B 332 ILE B 333 -1 N LEU B 332 O ILE B 339 SHEET 1 AC3 8 MET B 226 THR B 227 0 SHEET 2 AC3 8 THR B 263 ASP B 270 -1 O GLY B 264 N MET B 226 SHEET 3 AC3 8 TYR B 275 GLU B 287 -1 O ILE B 277 N ILE B 267 SHEET 4 AC3 8 LEU B 38 LYS B 60 -1 N LYS B 55 O VAL B 280 SHEET 5 AC3 8 ALA B 291 PRO B 298 -1 O LEU B 297 N VAL B 39 SHEET 6 AC3 8 PHE B 315 ARG B 319 -1 O VAL B 318 N TYR B 292 SHEET 7 AC3 8 LEU B 322 ILE B 326 -1 O SER B 324 N LEU B 317 SHEET 8 AC3 8 ALA B 345 THR B 346 -1 O THR B 346 N ASN B 325 SHEET 1 AC4 3 PHE B 301 ASN B 302 0 SHEET 2 AC4 3 GLU B 307 SER B 310 -1 O TRP B 308 N PHE B 301 SHEET 3 AC4 3 ARG B 365 LEU B 367 -1 O GLU B 366 N ILE B 309 SHEET 1 AC5 4 GLN G 3 SER G 7 0 SHEET 2 AC5 4 LEU G 18 SER G 25 -1 O SER G 25 N GLN G 3 SHEET 3 AC5 4 GLN G 78 LEU G 83 -1 O PHE G 79 N CYS G 22 SHEET 4 AC5 4 VAL G 68 ASP G 73 -1 N ASP G 73 O GLN G 78 SHEET 1 AC6 6 LEU G 11 VAL G 12 0 SHEET 2 AC6 6 VAL G 120 VAL G 124 1 O THR G 123 N VAL G 12 SHEET 3 AC6 6 ALA G 92 ARG G 98 -1 N ALA G 92 O VAL G 122 SHEET 4 AC6 6 TRP G 34 GLN G 39 -1 N ILE G 37 O TYR G 95 SHEET 5 AC6 6 GLU G 46 TYR G 52 -1 O ILE G 51 N TRP G 34 SHEET 6 AC6 6 SER G 57 TYR G 60 -1 O SER G 57 N TYR G 52 SHEET 1 AC7 4 LEU G 11 VAL G 12 0 SHEET 2 AC7 4 VAL G 120 VAL G 124 1 O THR G 123 N VAL G 12 SHEET 3 AC7 4 ALA G 92 ARG G 98 -1 N ALA G 92 O VAL G 122 SHEET 4 AC7 4 VAL G 115 TRP G 116 -1 O VAL G 115 N ARG G 98 SHEET 1 AC8 2 ARG G 101 TYR G 103 0 SHEET 2 AC8 2 PHE G 109 HIS G 111 -1 O GLY G 110 N GLY G 102 SHEET 1 AC9 4 GLN I 3 SER I 7 0 SHEET 2 AC9 4 LEU I 18 SER I 25 -1 O SER I 25 N GLN I 3 SHEET 3 AC9 4 GLN I 78 LEU I 83 -1 O PHE I 79 N CYS I 22 SHEET 4 AC9 4 VAL I 68 ASP I 73 -1 N ASP I 73 O GLN I 78 SHEET 1 AD1 6 LEU I 11 VAL I 12 0 SHEET 2 AD1 6 VAL I 120 VAL I 124 1 O THR I 123 N VAL I 12 SHEET 3 AD1 6 ALA I 92 ARG I 98 -1 N ALA I 92 O VAL I 122 SHEET 4 AD1 6 TRP I 34 GLN I 39 -1 N ILE I 37 O TYR I 95 SHEET 5 AD1 6 GLU I 46 TYR I 52 -1 O ILE I 51 N TRP I 34 SHEET 6 AD1 6 SER I 57 TYR I 60 -1 O SER I 57 N TYR I 52 SHEET 1 AD2 4 LEU I 11 VAL I 12 0 SHEET 2 AD2 4 VAL I 120 VAL I 124 1 O THR I 123 N VAL I 12 SHEET 3 AD2 4 ALA I 92 ARG I 98 -1 N ALA I 92 O VAL I 122 SHEET 4 AD2 4 VAL I 115 TRP I 116 -1 O VAL I 115 N ARG I 98 SHEET 1 AD3 2 ARG I 101 TYR I 103 0 SHEET 2 AD3 2 PHE I 109 HIS I 111 -1 O GLY I 110 N GLY I 102 SHEET 1 AD4 6 SER E 9 ALA E 13 0 SHEET 2 AD4 6 THR E 105 LEU E 110 1 O THR E 108 N ALA E 10 SHEET 3 AD4 6 ASP E 86 ASP E 93 -1 N TYR E 87 O THR E 105 SHEET 4 AD4 6 VAL E 34 GLN E 39 -1 N SER E 35 O ALA E 90 SHEET 5 AD4 6 LYS E 46 SER E 50 -1 O LEU E 48 N TRP E 36 SHEET 6 AD4 6 GLN E 54 ARG E 55 -1 O GLN E 54 N SER E 50 SHEET 1 AD5 4 SER E 9 ALA E 13 0 SHEET 2 AD5 4 THR E 105 LEU E 110 1 O THR E 108 N ALA E 10 SHEET 3 AD5 4 ASP E 86 ASP E 93 -1 N TYR E 87 O THR E 105 SHEET 4 AD5 4 GLY E 98 PHE E 101 -1 O GLY E 98 N ASP E 93 SHEET 1 AD6 3 VAL E 18 SER E 23 0 SHEET 2 AD6 3 SER E 71 ILE E 76 -1 O ILE E 76 N VAL E 18 SHEET 3 AD6 3 PHE E 63 SER E 68 -1 N SER E 68 O SER E 71 SHEET 1 AD7 6 SER D 9 ALA D 13 0 SHEET 2 AD7 6 THR D 105 LEU D 110 1 O THR D 108 N ALA D 10 SHEET 3 AD7 6 ASP D 86 ASP D 93 -1 N TYR D 87 O THR D 105 SHEET 4 AD7 6 VAL D 34 GLN D 39 -1 N SER D 35 O ALA D 90 SHEET 5 AD7 6 LYS D 46 SER D 50 -1 O LEU D 48 N TRP D 36 SHEET 6 AD7 6 GLN D 54 ARG D 55 -1 O GLN D 54 N SER D 50 SHEET 1 AD8 4 SER D 9 ALA D 13 0 SHEET 2 AD8 4 THR D 105 LEU D 110 1 O THR D 108 N ALA D 10 SHEET 3 AD8 4 ASP D 86 ASP D 93 -1 N TYR D 87 O THR D 105 SHEET 4 AD8 4 GLY D 98 PHE D 101 -1 O GLY D 98 N ASP D 93 SHEET 1 AD9 3 VAL D 18 SER D 23 0 SHEET 2 AD9 3 SER D 71 ILE D 76 -1 O ILE D 76 N VAL D 18 SHEET 3 AD9 3 PHE D 63 SER D 68 -1 N SER D 68 O SER D 71 SSBOND 1 CYS F 22 CYS F 89 1555 1555 2.04 SSBOND 2 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 3 CYS A 331 CYS A 340 1555 1555 2.04 SSBOND 4 CYS A 355 CYS A 363 1555 1555 2.03 SSBOND 5 CYS A 387 CYS A 392 1555 1555 2.03 SSBOND 6 CYS C 71 CYS C 192 1555 1555 2.03 SSBOND 7 CYS C 331 CYS C 340 1555 1555 2.03 SSBOND 8 CYS C 355 CYS C 363 1555 1555 2.03 SSBOND 9 CYS C 387 CYS C 392 1555 1555 2.03 SSBOND 10 CYS C 394 CYS C 417 1555 1555 2.03 SSBOND 11 CYS B 71 CYS B 192 1555 1555 2.03 SSBOND 12 CYS B 331 CYS B 340 1555 1555 2.04 SSBOND 13 CYS B 355 CYS B 363 1555 1555 2.03 SSBOND 14 CYS B 387 CYS B 392 1555 1555 2.04 SSBOND 15 CYS B 394 CYS B 417 1555 1555 2.04 SSBOND 16 CYS G 22 CYS G 96 1555 1555 2.04 SSBOND 17 CYS I 22 CYS I 96 1555 1555 2.04 SSBOND 18 CYS E 22 CYS E 89 1555 1555 2.04 SSBOND 19 CYS D 22 CYS D 89 1555 1555 2.04 LINK ND2 ASN A 67 C1 NAG A 502 1555 1555 1.44 LINK ND2 ASN A 99 C1 NAG A 501 1555 1555 1.44 LINK ND2 ASN A 414 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN A 464 C1 NAG A 503 1555 1555 1.44 LINK ND2 ASN C 67 C1 NAG C 502 1555 1555 1.44 LINK ND2 ASN C 99 C1 NAG C 501 1555 1555 1.44 LINK ND2 ASN C 414 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN C 464 C1 NAG C 503 1555 1555 1.44 LINK ND2 ASN B 67 C1 NAG B 502 1555 1555 1.44 LINK ND2 ASN B 99 C1 NAG B 501 1555 1555 1.44 LINK ND2 ASN B 414 C1 NAG L 1 1555 1555 1.44 LINK ND2 ASN B 464 C1 NAG B 503 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45 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