HEADER VIRAL PROTEIN 04-JAN-24 8XPY TITLE STRUCTURE OF NIPAH VIRUS MALAYSIA STRING G PROTEIN ECTODOMAIN MONOMER TITLE 2 BOUND TO SINGLE-DOMAIN ANTIBODY N425 AT 3.63 ANGSTROMS OVERALL TITLE 3 RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLYCOPROTEIN G; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SINGLE-DOMAIN ANTIBODY N425; COMPND 7 CHAIN: B; COMPND 8 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: EXPI293F; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F KEYWDS ANTIBODY, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR L.SUN,Z.CHEN,Y.SUN,Q.MAO REVDAT 1 18-SEP-24 8XPY 0 JRNL AUTH Y.WANG,Y.SUN,Z.SHEN,C.WANG,J.QIAN,Q.MAO,Y.WANG,W.SONG, JRNL AUTH 2 Y.KONG,C.ZHAN,Z.CHEN,D.S.DIMITROV,Z.YANG,S.JIANG,F.WU,L.LU, JRNL AUTH 3 T.YING,L.SUN,Y.WU JRNL TITL FULLY HUMAN SINGLE-DOMAIN ANTIBODY TARGETING A HIGHLY JRNL TITL 2 CONSERVED CRYPTIC EPITOPE ON THE NIPAH VIRUS G PROTEIN. JRNL REF NAT COMMUN V. 15 6892 2024 JRNL REFN ESSN 2041-1723 JRNL PMID 39134522 JRNL DOI 10.1038/S41467-024-51066-6 REMARK 2 REMARK 2 RESOLUTION. 3.63 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) : 3.630 REMARK 3 NUMBER OF PARTICLES : 661646 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 8XPY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1300043983. 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 MALAYSIA STRING G REMARK 245 PROTEIN ECTODOMAIN MONOMER IN REMARK 245 COMPLEX WITH SINGLE-DOMAIN REMARK 245 ANTIBODY N425 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 IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 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) : 5000.00 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G 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 ALA A 3 REMARK 465 GLU A 4 REMARK 465 ASN A 5 REMARK 465 LYS A 6 REMARK 465 LYS A 7 REMARK 465 VAL A 8 REMARK 465 ARG A 9 REMARK 465 PHE A 10 REMARK 465 GLU A 11 REMARK 465 ASN A 12 REMARK 465 THR A 13 REMARK 465 THR A 14 REMARK 465 SER A 15 REMARK 465 ASP A 16 REMARK 465 LYS A 17 REMARK 465 GLY A 18 REMARK 465 LYS A 19 REMARK 465 ILE A 20 REMARK 465 PRO A 21 REMARK 465 SER A 22 REMARK 465 LYS A 23 REMARK 465 VAL A 24 REMARK 465 ILE A 25 REMARK 465 LYS A 26 REMARK 465 SER A 27 REMARK 465 TYR A 28 REMARK 465 TYR A 29 REMARK 465 GLY A 30 REMARK 465 THR A 31 REMARK 465 MET A 32 REMARK 465 ASP A 33 REMARK 465 ILE A 34 REMARK 465 LYS A 35 REMARK 465 LYS A 36 REMARK 465 ILE A 37 REMARK 465 ASN A 38 REMARK 465 GLU A 39 REMARK 465 GLY A 40 REMARK 465 LEU A 41 REMARK 465 LEU A 42 REMARK 465 ASP A 43 REMARK 465 SER A 44 REMARK 465 LYS A 45 REMARK 465 ILE A 46 REMARK 465 LEU A 47 REMARK 465 SER A 48 REMARK 465 ALA A 49 REMARK 465 PHE A 50 REMARK 465 ASN A 51 REMARK 465 THR A 52 REMARK 465 VAL A 53 REMARK 465 ILE A 54 REMARK 465 ALA A 55 REMARK 465 LEU A 56 REMARK 465 LEU A 57 REMARK 465 GLY A 58 REMARK 465 SER A 59 REMARK 465 ILE A 60 REMARK 465 VAL A 61 REMARK 465 ILE A 62 REMARK 465 ILE A 63 REMARK 465 VAL A 64 REMARK 465 MET A 65 REMARK 465 ASN A 66 REMARK 465 ILE A 67 REMARK 465 MET A 68 REMARK 465 ILE A 69 REMARK 465 ILE A 70 REMARK 465 GLN A 71 REMARK 465 ASN A 72 REMARK 465 TYR A 73 REMARK 465 THR A 74 REMARK 465 ARG A 75 REMARK 465 SER A 76 REMARK 465 THR A 77 REMARK 465 ASP A 78 REMARK 465 ASN A 79 REMARK 465 GLN A 80 REMARK 465 ALA A 81 REMARK 465 VAL A 82 REMARK 465 ILE A 83 REMARK 465 LYS A 84 REMARK 465 ASP A 85 REMARK 465 ALA A 86 REMARK 465 LEU A 87 REMARK 465 GLN A 88 REMARK 465 GLY A 89 REMARK 465 ILE A 90 REMARK 465 GLN A 91 REMARK 465 GLN A 92 REMARK 465 GLN A 93 REMARK 465 ILE A 94 REMARK 465 LYS A 95 REMARK 465 GLY A 96 REMARK 465 LEU A 97 REMARK 465 ALA A 98 REMARK 465 ASP A 99 REMARK 465 LYS A 100 REMARK 465 ILE A 101 REMARK 465 GLY A 102 REMARK 465 THR A 103 REMARK 465 GLU A 104 REMARK 465 ILE A 105 REMARK 465 GLY A 106 REMARK 465 PRO A 107 REMARK 465 LYS A 108 REMARK 465 VAL A 109 REMARK 465 SER A 110 REMARK 465 LEU A 111 REMARK 465 ILE A 112 REMARK 465 ASP A 113 REMARK 465 THR A 114 REMARK 465 SER A 115 REMARK 465 SER A 116 REMARK 465 THR A 117 REMARK 465 ILE A 118 REMARK 465 THR A 119 REMARK 465 ILE A 120 REMARK 465 PRO A 121 REMARK 465 ALA A 122 REMARK 465 ASN A 123 REMARK 465 ILE A 124 REMARK 465 GLY A 125 REMARK 465 LEU A 126 REMARK 465 LEU A 127 REMARK 465 GLY A 128 REMARK 465 SER A 129 REMARK 465 LYS A 130 REMARK 465 ILE A 131 REMARK 465 SER A 132 REMARK 465 GLN A 133 REMARK 465 SER A 134 REMARK 465 THR A 135 REMARK 465 ALA A 136 REMARK 465 SER A 137 REMARK 465 ILE A 138 REMARK 465 ASN A 139 REMARK 465 GLU A 140 REMARK 465 ASN A 141 REMARK 465 VAL A 142 REMARK 465 ASN A 143 REMARK 465 GLU A 144 REMARK 465 LYS A 145 REMARK 465 CYS A 146 REMARK 465 LYS A 147 REMARK 465 PHE A 148 REMARK 465 THR A 149 REMARK 465 LEU A 150 REMARK 465 PRO A 151 REMARK 465 PRO A 152 REMARK 465 LEU A 153 REMARK 465 LYS A 154 REMARK 465 ILE A 155 REMARK 465 HIS A 156 REMARK 465 GLU A 157 REMARK 465 CYS A 158 REMARK 465 ASN A 159 REMARK 465 ILE A 160 REMARK 465 SER A 161 REMARK 465 CYS A 162 REMARK 465 PRO A 163 REMARK 465 ASN A 164 REMARK 465 PRO A 165 REMARK 465 LEU A 166 REMARK 465 PRO A 167 REMARK 465 PHE A 168 REMARK 465 ARG A 169 REMARK 465 GLU A 170 REMARK 465 TYR A 171 REMARK 465 ARG A 172 REMARK 465 PRO A 173 REMARK 465 GLN A 174 REMARK 465 THR A 175 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 A 195 49.64 -87.93 REMARK 500 ASP A 219 71.44 52.66 REMARK 500 ASN A 287 -63.42 -94.13 REMARK 500 LYS A 322 70.60 57.28 REMARK 500 LYS A 324 70.88 57.86 REMARK 500 TYR A 330 48.36 -88.66 REMARK 500 ASN A 331 -16.41 -142.69 REMARK 500 GLN A 332 -8.54 -140.17 REMARK 500 LEU A 397 52.01 -91.42 REMARK 500 LEU A 448 46.09 37.71 REMARK 500 ASN A 534 73.38 52.80 REMARK 500 GLU A 544 169.75 177.71 REMARK 500 SER B 53 -166.37 -70.63 REMARK 500 SER B 54 128.97 -34.84 REMARK 500 SER B 55 106.95 -46.09 REMARK 500 ALA B 61 70.70 57.64 REMARK 500 ASP B 62 -36.41 -36.93 REMARK 500 ASN B 77 98.47 -69.91 REMARK 500 ALA B 101 -168.17 -165.44 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG C 1 REMARK 610 NAG D 1 REMARK 610 NAG E 1 REMARK 610 NAG F 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38563 RELATED DB: EMDB REMARK 900 STRUCTURE OF NIPAH VIRUS MALAYSIA STRING G PROTEIN ECTODOMAIN REMARK 900 MONOMER BOUND TO SINGLE-DOMAIN ANTIBODY N425 AT 3.63 ANGSTROMS REMARK 900 OVERALL RESOLUTION DBREF 8XPY A 1 602 UNP Q9IH62 GLYCP_NIPAV 1 602 DBREF 8XPY B 1 119 PDB 8XPY 8XPY 1 119 SEQRES 1 A 602 MET PRO ALA GLU ASN LYS LYS VAL ARG PHE GLU ASN THR SEQRES 2 A 602 THR SER ASP LYS GLY LYS ILE PRO SER LYS VAL ILE LYS SEQRES 3 A 602 SER TYR TYR GLY THR MET ASP ILE LYS LYS ILE ASN GLU SEQRES 4 A 602 GLY LEU LEU ASP SER LYS ILE LEU SER ALA PHE ASN THR SEQRES 5 A 602 VAL ILE ALA LEU LEU GLY SER ILE VAL ILE ILE VAL MET SEQRES 6 A 602 ASN ILE MET ILE ILE GLN ASN TYR THR ARG SER THR ASP SEQRES 7 A 602 ASN GLN ALA VAL ILE LYS ASP ALA LEU GLN GLY ILE GLN SEQRES 8 A 602 GLN GLN ILE LYS GLY LEU ALA ASP LYS ILE GLY THR GLU SEQRES 9 A 602 ILE GLY PRO LYS VAL SER LEU ILE ASP THR SER SER THR SEQRES 10 A 602 ILE THR ILE PRO ALA ASN ILE GLY LEU LEU GLY SER LYS SEQRES 11 A 602 ILE SER GLN SER THR ALA SER ILE ASN GLU ASN VAL ASN SEQRES 12 A 602 GLU LYS CYS LYS PHE THR LEU PRO PRO LEU LYS ILE HIS SEQRES 13 A 602 GLU CYS ASN ILE SER CYS PRO ASN PRO LEU PRO PHE ARG SEQRES 14 A 602 GLU TYR ARG PRO GLN THR GLU GLY VAL SER ASN LEU VAL SEQRES 15 A 602 GLY LEU PRO ASN ASN ILE CYS LEU GLN LYS THR SER ASN SEQRES 16 A 602 GLN ILE LEU LYS PRO LYS LEU ILE SER TYR THR LEU PRO SEQRES 17 A 602 VAL VAL GLY GLN SER GLY THR CYS ILE THR ASP PRO LEU SEQRES 18 A 602 LEU ALA MET ASP GLU GLY TYR PHE ALA TYR SER HIS LEU SEQRES 19 A 602 GLU ARG ILE GLY SER CYS SER ARG GLY VAL SER LYS GLN SEQRES 20 A 602 ARG ILE ILE GLY VAL GLY GLU VAL LEU ASP ARG GLY ASP SEQRES 21 A 602 GLU VAL PRO SER LEU PHE MET THR ASN VAL TRP THR PRO SEQRES 22 A 602 PRO ASN PRO ASN THR VAL TYR HIS CYS SER ALA VAL TYR SEQRES 23 A 602 ASN ASN GLU PHE TYR TYR VAL LEU CYS ALA VAL SER THR SEQRES 24 A 602 VAL GLY ASP PRO ILE LEU ASN SER THR TYR TRP SER GLY SEQRES 25 A 602 SER LEU MET MET THR ARG LEU ALA VAL LYS PRO LYS SER SEQRES 26 A 602 ASN GLY GLY GLY TYR ASN GLN HIS GLN LEU ALA LEU ARG SEQRES 27 A 602 SER ILE GLU LYS GLY ARG TYR ASP LYS VAL MET PRO TYR SEQRES 28 A 602 GLY PRO SER GLY ILE LYS GLN GLY ASP THR LEU TYR PHE SEQRES 29 A 602 PRO ALA VAL GLY PHE LEU VAL ARG THR GLU PHE LYS TYR SEQRES 30 A 602 ASN ASP SER ASN CYS PRO ILE THR LYS CYS GLN TYR SER SEQRES 31 A 602 LYS PRO GLU ASN CYS ARG LEU SER MET GLY ILE ARG PRO SEQRES 32 A 602 ASN SER HIS TYR ILE LEU ARG SER GLY LEU LEU LYS TYR SEQRES 33 A 602 ASN LEU SER ASP GLY GLU ASN PRO LYS VAL VAL PHE ILE SEQRES 34 A 602 GLU ILE SER ASP GLN ARG LEU SER ILE GLY SER PRO SER SEQRES 35 A 602 LYS ILE TYR ASP SER LEU GLY GLN PRO VAL PHE TYR GLN SEQRES 36 A 602 ALA SER PHE SER TRP ASP THR MET ILE LYS PHE GLY ASP SEQRES 37 A 602 VAL LEU THR VAL ASN PRO LEU VAL VAL ASN TRP ARG ASN SEQRES 38 A 602 ASN THR VAL ILE SER ARG PRO GLY GLN SER GLN CYS PRO SEQRES 39 A 602 ARG PHE ASN THR CYS PRO GLU ILE CYS TRP GLU GLY VAL SEQRES 40 A 602 TYR ASN ASP ALA PHE LEU ILE ASP ARG ILE ASN TRP ILE SEQRES 41 A 602 SER ALA GLY VAL PHE LEU ASP SER ASN GLN THR ALA GLU SEQRES 42 A 602 ASN PRO VAL PHE THR VAL PHE LYS ASP ASN GLU ILE LEU SEQRES 43 A 602 TYR ARG ALA GLN LEU ALA SER GLU ASP THR ASN ALA GLN SEQRES 44 A 602 LYS THR ILE THR ASN CYS PHE LEU LEU LYS ASN LYS ILE SEQRES 45 A 602 TRP CYS ILE SER LEU VAL GLU ILE TYR ASP THR GLY ASP SEQRES 46 A 602 ASN VAL ILE ARG PRO LYS LEU PHE ALA VAL LYS ILE PRO SEQRES 47 A 602 GLU GLN CYS THR SEQRES 1 B 119 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 119 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 119 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 B 119 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE SER SEQRES 5 B 119 SER SER SER SER TYR THR ASN TYR ALA ASP SER VAL LYS SEQRES 6 B 119 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 B 119 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 B 119 ALA SER TYR TYR CYS ALA ARG GLY LEU ALA GLY VAL TRP SEQRES 9 B 119 GLY ILE ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 B 119 SER SER HET NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET MAN C 4 11 HET MAN C 5 11 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET MAN D 4 11 HET MAN D 5 11 HET MAN D 6 11 HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET MAN E 4 11 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET MAN F 4 11 HET MAN F 5 11 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET MAN G 4 11 HET MAN G 5 11 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE 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 HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 3 NAG 10(C8 H15 N O6) FORMUL 3 BMA 5(C6 H12 O6) FORMUL 3 MAN 10(C6 H12 O6) HELIX 1 AA1 ASN A 275 ASN A 277 5 3 HELIX 2 AA2 THR A 373 PHE A 375 5 3 HELIX 3 AA3 LYS A 391 MET A 399 5 9 HELIX 4 AA4 ALA B 61 LYS B 65 5 5 HELIX 5 AA5 ARG B 87 THR B 91 5 5 SHEET 1 AA1 4 LYS A 201 LEU A 202 0 SHEET 2 AA1 4 ILE A 588 LYS A 596 -1 O ALA A 594 N LYS A 201 SHEET 3 AA1 4 ILE A 572 TYR A 581 -1 N VAL A 578 O LYS A 591 SHEET 4 AA1 4 THR A 561 LEU A 567 -1 N ASN A 564 O ILE A 575 SHEET 1 AA2 3 CYS A 216 THR A 218 0 SHEET 2 AA2 3 TYR A 228 GLY A 238 -1 O ARG A 236 N CYS A 216 SHEET 3 AA2 3 LEU A 222 ASP A 225 -1 N ASP A 225 O TYR A 228 SHEET 1 AA3 4 CYS A 216 THR A 218 0 SHEET 2 AA3 4 TYR A 228 GLY A 238 -1 O ARG A 236 N CYS A 216 SHEET 3 AA3 4 GLY A 243 ASP A 257 -1 O GLY A 251 N TYR A 231 SHEET 4 AA3 4 PRO A 263 TRP A 271 -1 O SER A 264 N LEU A 256 SHEET 1 AA4 3 VAL A 279 TYR A 280 0 SHEET 2 AA4 3 PHE A 290 VAL A 297 -1 O ALA A 296 N TYR A 280 SHEET 3 AA4 3 VAL A 285 TYR A 286 -1 N VAL A 285 O TYR A 292 SHEET 1 AA5 4 VAL A 279 TYR A 280 0 SHEET 2 AA5 4 PHE A 290 VAL A 297 -1 O ALA A 296 N TYR A 280 SHEET 3 AA5 4 LEU A 314 ALA A 320 -1 O LEU A 319 N TYR A 291 SHEET 4 AA5 4 GLN A 334 ALA A 336 -1 O LEU A 335 N MET A 316 SHEET 1 AA6 5 ILE A 340 GLU A 341 0 SHEET 2 AA6 5 VAL A 426 GLU A 430 1 O VAL A 426 N GLU A 341 SHEET 3 AA6 5 TYR A 407 TYR A 416 -1 N LEU A 413 O ILE A 429 SHEET 4 AA6 5 LEU A 362 VAL A 371 -1 N GLY A 368 O ARG A 410 SHEET 5 AA6 5 LYS A 347 PRO A 350 -1 N LYS A 347 O PHE A 369 SHEET 1 AA7 5 ILE A 340 GLU A 341 0 SHEET 2 AA7 5 VAL A 426 GLU A 430 1 O VAL A 426 N GLU A 341 SHEET 3 AA7 5 TYR A 407 TYR A 416 -1 N LEU A 413 O ILE A 429 SHEET 4 AA7 5 LEU A 362 VAL A 371 -1 N GLY A 368 O ARG A 410 SHEET 5 AA7 5 ILE A 356 LYS A 357 -1 N ILE A 356 O TYR A 363 SHEET 1 AA8 4 SER A 442 ASP A 446 0 SHEET 2 AA8 4 PRO A 451 GLN A 455 -1 O VAL A 452 N TYR A 445 SHEET 3 AA8 4 LYS A 465 THR A 471 -1 O LYS A 465 N GLN A 455 SHEET 4 AA8 4 VAL A 476 TRP A 479 -1 O VAL A 476 N LEU A 470 SHEET 1 AA9 4 PHE A 512 ASP A 515 0 SHEET 2 AA9 4 ILE A 520 LEU A 526 -1 O ALA A 522 N PHE A 512 SHEET 3 AA9 4 PRO A 535 PHE A 540 -1 O THR A 538 N GLY A 523 SHEET 4 AA9 4 TYR A 547 GLN A 550 -1 O TYR A 547 N VAL A 539 SHEET 1 AB1 2 SER B 17 LEU B 18 0 SHEET 2 AB1 2 MET B 83 ASN B 84 -1 O MET B 83 N LEU B 18 SHEET 1 AB2 5 THR B 58 ASN B 59 0 SHEET 2 AB2 5 LEU B 45 ILE B 51 -1 N TYR B 50 O ASN B 59 SHEET 3 AB2 5 SER B 35 GLN B 39 -1 N ARG B 38 O GLU B 46 SHEET 4 AB2 5 ALA B 92 ALA B 97 -1 O TYR B 95 N VAL B 37 SHEET 5 AB2 5 THR B 113 VAL B 115 -1 O VAL B 115 N ALA B 92 SSBOND 1 CYS A 189 CYS A 601 1555 1555 2.03 SSBOND 2 CYS A 216 CYS A 240 1555 1555 2.03 SSBOND 3 CYS A 282 CYS A 295 1555 1555 2.03 SSBOND 4 CYS A 382 CYS A 395 1555 1555 2.03 SSBOND 5 CYS A 387 CYS A 499 1555 1555 2.03 SSBOND 6 CYS A 493 CYS A 503 1555 1555 2.03 SSBOND 7 CYS A 565 CYS A 574 1555 1555 2.03 SSBOND 8 CYS B 22 CYS B 96 1555 1555 2.03 LINK ND2 ASN A 481 C1 NAG G 1 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45 LINK O6 BMA C 3 C1 MAN C 4 1555 1555 1.44 LINK O6 MAN C 4 C1 MAN C 5 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44 LINK O6 BMA D 3 C1 MAN D 4 1555 1555 1.45 LINK O3 BMA D 3 C1 MAN D 6 1555 1555 1.45 LINK O6 MAN D 4 C1 MAN D 5 1555 1555 1.45 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45 LINK O6 BMA E 3 C1 MAN E 4 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.45 LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.44 LINK O6 BMA F 3 C1 MAN F 5 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.44 LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.45 LINK O6 BMA G 3 C1 MAN G 5 1555 1555 1.44 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