HEADER VIRAL PROTEIN 17-DEC-23 8XHE TITLE DUAL RECEPTOR-BINDING, INFECTIVITY, AND TRANSMISSIBILITY OF AN TITLE 2 EMERGING H2N2 AVIAN INFLUENZA VIRUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ; COMPND 3 CHAIN: C, A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 STRAIN: A/SINGAPORE/1/1957 H2N2; SOURCE 5 GENE: HA; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS H2N2, INFLUENZA VIRUS, RECEPTOR, REPLICATION, TRANSMISSION, MICE, KEYWDS 2 GUINEA PIG, FERRET, MUTATION, PUBLIC HEALTH RISK, VIRUS, VIRAL KEYWDS 3 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.SUN,T.Y.ZHENG REVDAT 1 18-DEC-24 8XHE 0 JRNL AUTH J.SUN JRNL TITL DUAL RECEPTOR-BINDING, INFECTIVITY, AND TRANSMISSIBILITY OF JRNL TITL 2 AN EMERGING H2N2 AVIAN INFLUENZA VIRUS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.64 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) : 2.640 REMARK 3 NUMBER OF PARTICLES : 202890 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 8XHE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-DEC-23. REMARK 100 THE DEPOSITION ID IS D_1300043431. 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 : THE STRUCTURE OF INFLUENZA H2 REMARK 245 HUMAN SINGAPORE R137M REMARK 245 HEMAGGLUTININ WITH HUMAN REMARK 245 RECEPTOR 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 : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, A, B, D, E, F 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 GLU C 328 REMARK 465 SER C 329 REMARK 465 ARG C 330 REMARK 465 GLY C 331 REMARK 465 LEU C 332 REMARK 465 PHE C 333 REMARK 465 GLY C 334 REMARK 465 GLU C 502 REMARK 465 GLU A 328 REMARK 465 SER A 329 REMARK 465 ARG A 330 REMARK 465 GLY A 331 REMARK 465 LEU A 332 REMARK 465 PHE A 333 REMARK 465 GLY A 334 REMARK 465 ALA A 335 REMARK 465 GLU A 502 REMARK 465 GLU B 328 REMARK 465 SER B 329 REMARK 465 ARG B 330 REMARK 465 GLY B 331 REMARK 465 LEU B 332 REMARK 465 PHE B 333 REMARK 465 GLY B 334 REMARK 465 GLU B 502 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 OE2 GLU A 190 O9 SIA F 4 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS C 467 CA - CB - SG ANGL. DEV. = 7.9 DEGREES 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 GLN C 7 148.00 -170.47 REMARK 500 CYS C 72 52.40 -92.72 REMARK 500 GLN C 196 -70.62 63.66 REMARK 500 THR C 206 -169.63 -125.89 REMARK 500 PRO C 307 170.39 -58.50 REMARK 500 ARG C 457 -130.89 68.09 REMARK 500 ASP C 475 -168.02 -126.65 REMARK 500 ASN A 28 60.32 61.06 REMARK 500 CYS A 72 51.41 -90.52 REMARK 500 LEU A 75 58.73 -96.41 REMARK 500 SER A 111 1.38 -67.82 REMARK 500 GLN A 196 -7.18 72.33 REMARK 500 VAL A 298 -61.48 -90.97 REMARK 500 LYS A 308 143.94 -174.15 REMARK 500 LYS A 311 36.03 -98.75 REMARK 500 ASP A 349 -16.56 -141.63 REMARK 500 SER A 357 47.14 -141.26 REMARK 500 ARG A 457 -131.02 64.93 REMARK 500 LEU B 94 93.32 -69.12 REMARK 500 LYS B 114 -8.63 73.47 REMARK 500 HIS B 115 148.61 -173.17 REMARK 500 GLN B 196 -4.45 68.82 REMARK 500 LYS B 314 115.33 -161.18 REMARK 500 LYS B 388 31.26 -93.28 REMARK 500 ARG B 457 -139.24 64.12 REMARK 500 THR B 486 58.83 -97.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38348 RELATED DB: EMDB REMARK 900 DUAL RECEPTOR-BINDING, INFECTIVITY, AND TRANSMISSIBILITY OF AN REMARK 900 EMERGING H2N2 AVIAN INFLUENZA VIRUS DBREF 8XHE C 6 502 UNP Q67333 HEMA_I57A5 16 512 DBREF 8XHE A 6 502 UNP Q67333 HEMA_I57A5 16 512 DBREF 8XHE B 6 502 UNP Q67333 HEMA_I57A5 16 512 SEQADV 8XHE THR C 20 UNP Q67333 LYS 30 CONFLICT SEQADV 8XHE MET C 137 UNP Q67333 ARG 147 CONFLICT SEQADV 8XHE LYS C 156 UNP Q67333 GLU 166 CONFLICT SEQADV 8XHE THR C 189 UNP Q67333 LYS 199 CONFLICT SEQADV 8XHE VAL C 348 UNP Q67333 ILE 358 CONFLICT SEQADV 8XHE THR A 20 UNP Q67333 LYS 30 CONFLICT SEQADV 8XHE MET A 137 UNP Q67333 ARG 147 CONFLICT SEQADV 8XHE LYS A 156 UNP Q67333 GLU 166 CONFLICT SEQADV 8XHE THR A 189 UNP Q67333 LYS 199 CONFLICT SEQADV 8XHE VAL A 348 UNP Q67333 ILE 358 CONFLICT SEQADV 8XHE THR B 20 UNP Q67333 LYS 30 CONFLICT SEQADV 8XHE MET B 137 UNP Q67333 ARG 147 CONFLICT SEQADV 8XHE LYS B 156 UNP Q67333 GLU 166 CONFLICT SEQADV 8XHE THR B 189 UNP Q67333 LYS 199 CONFLICT SEQADV 8XHE VAL B 348 UNP Q67333 ILE 358 CONFLICT SEQRES 1 C 497 ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 C 497 GLU THR VAL ASP THR ILE LEU GLU ARG ASN VAL THR VAL SEQRES 3 C 497 THR HIS ALA LYS ASP ILE LEU GLU LYS THR HIS ASN GLY SEQRES 4 C 497 LYS LEU CYS LYS LEU ASN GLY ILE PRO PRO LEU GLU LEU SEQRES 5 C 497 GLY ASP CYS SER ILE ALA GLY TRP LEU LEU GLY ASN PRO SEQRES 6 C 497 GLU CYS ASP ARG LEU LEU SER VAL PRO GLU TRP SER TYR SEQRES 7 C 497 ILE MET GLU LYS GLU ASN PRO ARG ASP GLY LEU CYS TYR SEQRES 8 C 497 PRO GLY SER PHE ASN ASP TYR GLU GLU LEU LYS HIS LEU SEQRES 9 C 497 LEU SER SER VAL LYS HIS PHE GLU LYS VAL LYS ILE LEU SEQRES 10 C 497 PRO LYS ASP ARG TRP THR GLN HIS THR THR THR GLY GLY SEQRES 11 C 497 SER MET ALA CYS ALA VAL SER GLY ASN PRO SER PHE PHE SEQRES 12 C 497 ARG ASN MET VAL TRP LEU THR LYS LYS GLY SER ASN TYR SEQRES 13 C 497 PRO VAL ALA LYS GLY SER TYR ASN ASN THR SER GLY GLU SEQRES 14 C 497 GLN MET LEU ILE ILE TRP GLY VAL HIS HIS PRO ASN ASP SEQRES 15 C 497 GLU THR GLU GLN ARG THR LEU TYR GLN ASN VAL GLY THR SEQRES 16 C 497 TYR VAL SER VAL GLY THR SER THR LEU ASN LYS ARG SER SEQRES 17 C 497 THR PRO ASP ILE ALA THR ARG PRO LYS VAL ASN GLY LEU SEQRES 18 C 497 GLY SER ARG MET GLU PHE SER TRP THR LEU LEU ASP MET SEQRES 19 C 497 TRP ASP THR ILE ASN PHE GLU SER THR GLY ASN LEU ILE SEQRES 20 C 497 ALA PRO GLU TYR GLY PHE LYS ILE SER LYS ARG GLY SER SEQRES 21 C 497 SER GLY ILE MET LYS THR GLU GLY THR LEU GLU ASN CYS SEQRES 22 C 497 GLU THR LYS CYS GLN THR PRO LEU GLY ALA ILE ASN THR SEQRES 23 C 497 THR LEU PRO PHE HIS ASN VAL HIS PRO LEU THR ILE GLY SEQRES 24 C 497 GLU CYS PRO LYS TYR VAL LYS SER GLU LYS LEU VAL LEU SEQRES 25 C 497 ALA THR GLY LEU ARG ASN VAL PRO GLN ILE GLU SER ARG SEQRES 26 C 497 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 27 C 497 TRP GLN GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 28 C 497 SER ASN ASP GLN GLY SER GLY TYR ALA ALA ASP LYS GLU SEQRES 29 C 497 SER THR GLN LYS ALA PHE ASP GLY ILE THR ASN LYS VAL SEQRES 30 C 497 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE GLU ALA SEQRES 31 C 497 VAL GLY LYS GLU PHE SER ASN LEU GLU ARG ARG LEU GLU SEQRES 32 C 497 ASN LEU ASN LYS LYS MET GLU ASP GLY PHE LEU ASP VAL SEQRES 33 C 497 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU MET GLU ASN SEQRES 34 C 497 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 35 C 497 LEU TYR ASP LYS VAL ARG MET GLN LEU ARG ASP ASN VAL SEQRES 36 C 497 LYS GLU LEU GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 37 C 497 CYS ASP ASP GLU CYS MET ASN SER VAL LYS ASN GLY THR SEQRES 38 C 497 TYR ASP TYR PRO LYS TYR GLU GLU GLU SER LYS LEU ASN SEQRES 39 C 497 ARG ASN GLU SEQRES 1 A 497 ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 A 497 GLU THR VAL ASP THR ILE LEU GLU ARG ASN VAL THR VAL SEQRES 3 A 497 THR HIS ALA LYS ASP ILE LEU GLU LYS THR HIS ASN GLY SEQRES 4 A 497 LYS LEU CYS LYS LEU ASN GLY ILE PRO PRO LEU GLU LEU SEQRES 5 A 497 GLY ASP CYS SER ILE ALA GLY TRP LEU LEU GLY ASN PRO SEQRES 6 A 497 GLU CYS ASP ARG LEU LEU SER VAL PRO GLU TRP SER TYR SEQRES 7 A 497 ILE MET GLU LYS GLU ASN PRO ARG ASP GLY LEU CYS TYR SEQRES 8 A 497 PRO GLY SER PHE ASN ASP TYR GLU GLU LEU LYS HIS LEU SEQRES 9 A 497 LEU SER SER VAL LYS HIS PHE GLU LYS VAL LYS ILE LEU SEQRES 10 A 497 PRO LYS ASP ARG TRP THR GLN HIS THR THR THR GLY GLY SEQRES 11 A 497 SER MET ALA CYS ALA VAL SER GLY ASN PRO SER PHE PHE SEQRES 12 A 497 ARG ASN MET VAL TRP LEU THR LYS LYS GLY SER ASN TYR SEQRES 13 A 497 PRO VAL ALA LYS GLY SER TYR ASN ASN THR SER GLY GLU SEQRES 14 A 497 GLN MET LEU ILE ILE TRP GLY VAL HIS HIS PRO ASN ASP SEQRES 15 A 497 GLU THR GLU GLN ARG THR LEU TYR GLN ASN VAL GLY THR SEQRES 16 A 497 TYR VAL SER VAL GLY THR SER THR LEU ASN LYS ARG SER SEQRES 17 A 497 THR PRO ASP ILE ALA THR ARG PRO LYS VAL ASN GLY LEU SEQRES 18 A 497 GLY SER ARG MET GLU PHE SER TRP THR LEU LEU ASP MET SEQRES 19 A 497 TRP ASP THR ILE ASN PHE GLU SER THR GLY ASN LEU ILE SEQRES 20 A 497 ALA PRO GLU TYR GLY PHE LYS ILE SER LYS ARG GLY SER SEQRES 21 A 497 SER GLY ILE MET LYS THR GLU GLY THR LEU GLU ASN CYS SEQRES 22 A 497 GLU THR LYS CYS GLN THR PRO LEU GLY ALA ILE ASN THR SEQRES 23 A 497 THR LEU PRO PHE HIS ASN VAL HIS PRO LEU THR ILE GLY SEQRES 24 A 497 GLU CYS PRO LYS TYR VAL LYS SER GLU LYS LEU VAL LEU SEQRES 25 A 497 ALA THR GLY LEU ARG ASN VAL PRO GLN ILE GLU SER ARG SEQRES 26 A 497 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 27 A 497 TRP GLN GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 28 A 497 SER ASN ASP GLN GLY SER GLY TYR ALA ALA ASP LYS GLU SEQRES 29 A 497 SER THR GLN LYS ALA PHE ASP GLY ILE THR ASN LYS VAL SEQRES 30 A 497 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE GLU ALA SEQRES 31 A 497 VAL GLY LYS GLU PHE SER ASN LEU GLU ARG ARG LEU GLU SEQRES 32 A 497 ASN LEU ASN LYS LYS MET GLU ASP GLY PHE LEU ASP VAL SEQRES 33 A 497 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU MET GLU ASN SEQRES 34 A 497 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 35 A 497 LEU TYR ASP LYS VAL ARG MET GLN LEU ARG ASP ASN VAL SEQRES 36 A 497 LYS GLU LEU GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 37 A 497 CYS ASP ASP GLU CYS MET ASN SER VAL LYS ASN GLY THR SEQRES 38 A 497 TYR ASP TYR PRO LYS TYR GLU GLU GLU SER LYS LEU ASN SEQRES 39 A 497 ARG ASN GLU SEQRES 1 B 497 ASP GLN ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR SEQRES 2 B 497 GLU THR VAL ASP THR ILE LEU GLU ARG ASN VAL THR VAL SEQRES 3 B 497 THR HIS ALA LYS ASP ILE LEU GLU LYS THR HIS ASN GLY SEQRES 4 B 497 LYS LEU CYS LYS LEU ASN GLY ILE PRO PRO LEU GLU LEU SEQRES 5 B 497 GLY ASP CYS SER ILE ALA GLY TRP LEU LEU GLY ASN PRO SEQRES 6 B 497 GLU CYS ASP ARG LEU LEU SER VAL PRO GLU TRP SER TYR SEQRES 7 B 497 ILE MET GLU LYS GLU ASN PRO ARG ASP GLY LEU CYS TYR SEQRES 8 B 497 PRO GLY SER PHE ASN ASP TYR GLU GLU LEU LYS HIS LEU SEQRES 9 B 497 LEU SER SER VAL LYS HIS PHE GLU LYS VAL LYS ILE LEU SEQRES 10 B 497 PRO LYS ASP ARG TRP THR GLN HIS THR THR THR GLY GLY SEQRES 11 B 497 SER MET ALA CYS ALA VAL SER GLY ASN PRO SER PHE PHE SEQRES 12 B 497 ARG ASN MET VAL TRP LEU THR LYS LYS GLY SER ASN TYR SEQRES 13 B 497 PRO VAL ALA LYS GLY SER TYR ASN ASN THR SER GLY GLU SEQRES 14 B 497 GLN MET LEU ILE ILE TRP GLY VAL HIS HIS PRO ASN ASP SEQRES 15 B 497 GLU THR GLU GLN ARG THR LEU TYR GLN ASN VAL GLY THR SEQRES 16 B 497 TYR VAL SER VAL GLY THR SER THR LEU ASN LYS ARG SER SEQRES 17 B 497 THR PRO ASP ILE ALA THR ARG PRO LYS VAL ASN GLY LEU SEQRES 18 B 497 GLY SER ARG MET GLU PHE SER TRP THR LEU LEU ASP MET SEQRES 19 B 497 TRP ASP THR ILE ASN PHE GLU SER THR GLY ASN LEU ILE SEQRES 20 B 497 ALA PRO GLU TYR GLY PHE LYS ILE SER LYS ARG GLY SER SEQRES 21 B 497 SER GLY ILE MET LYS THR GLU GLY THR LEU GLU ASN CYS SEQRES 22 B 497 GLU THR LYS CYS GLN THR PRO LEU GLY ALA ILE ASN THR SEQRES 23 B 497 THR LEU PRO PHE HIS ASN VAL HIS PRO LEU THR ILE GLY SEQRES 24 B 497 GLU CYS PRO LYS TYR VAL LYS SER GLU LYS LEU VAL LEU SEQRES 25 B 497 ALA THR GLY LEU ARG ASN VAL PRO GLN ILE GLU SER ARG SEQRES 26 B 497 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 27 B 497 TRP GLN GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 28 B 497 SER ASN ASP GLN GLY SER GLY TYR ALA ALA ASP LYS GLU SEQRES 29 B 497 SER THR GLN LYS ALA PHE ASP GLY ILE THR ASN LYS VAL SEQRES 30 B 497 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE GLU ALA SEQRES 31 B 497 VAL GLY LYS GLU PHE SER ASN LEU GLU ARG ARG LEU GLU SEQRES 32 B 497 ASN LEU ASN LYS LYS MET GLU ASP GLY PHE LEU ASP VAL SEQRES 33 B 497 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU MET GLU ASN SEQRES 34 B 497 GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN SEQRES 35 B 497 LEU TYR ASP LYS VAL ARG MET GLN LEU ARG ASP ASN VAL SEQRES 36 B 497 LYS GLU LEU GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 37 B 497 CYS ASP ASP GLU CYS MET ASN SER VAL LYS ASN GLY THR SEQRES 38 B 497 TYR ASP TYR PRO LYS TYR GLU GLU GLU SER LYS LEU ASN SEQRES 39 B 497 ARG ASN GLU HET GAL D 1 12 HET NAG D 2 14 HET GAL D 3 11 HET SIA D 4 20 HET GAL E 1 12 HET NAG E 2 14 HET GAL E 3 11 HET SIA E 4 20 HET GAL F 1 12 HET NAG F 2 14 HET GAL F 3 11 HET SIA F 4 20 HET NAG C 601 14 HET NAG C 602 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG B 601 14 HET NAG B 602 14 HET NAG B 603 14 HETNAM GAL BETA-D-GALACTOPYRANOSE HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE 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 SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC HETSYN 2 SIA ACID; O-SIALIC ACID FORMUL 4 GAL 6(C6 H12 O6) FORMUL 4 NAG 11(C8 H15 N O6) FORMUL 4 SIA 3(C11 H19 N O9) HELIX 1 AA1 SER C 61 GLY C 68 1 8 HELIX 2 AA2 CYS C 72 LEU C 76 5 5 HELIX 3 AA3 ASP C 102 SER C 111 1 10 HELIX 4 AA4 ASP C 187 GLN C 196 1 10 HELIX 5 AA5 ASP C 367 LYS C 388 1 22 HELIX 6 AA6 GLU C 404 ARG C 457 1 54 HELIX 7 AA7 ASP C 475 GLY C 485 1 11 HELIX 8 AA8 TYR C 489 LYS C 491 5 3 HELIX 9 AA9 TYR C 492 ASN C 501 1 10 HELIX 10 AB1 SER A 61 GLY A 68 1 8 HELIX 11 AB2 ASP A 102 SER A 111 1 10 HELIX 12 AB3 PRO A 123 TRP A 127 5 5 HELIX 13 AB4 ASP A 187 GLN A 196 1 10 HELIX 14 AB5 LYS A 368 GLU A 387 1 20 HELIX 15 AB6 GLU A 404 ARG A 457 1 54 HELIX 16 AB7 ASP A 475 GLY A 485 1 11 HELIX 17 AB8 TYR A 489 LYS A 491 5 3 HELIX 18 AB9 TYR A 492 ASN A 501 1 10 HELIX 19 AC1 SER B 61 GLY B 68 1 8 HELIX 20 AC2 ASN B 69 LEU B 76 5 8 HELIX 21 AC3 ASP B 102 SER B 111 1 10 HELIX 22 AC4 PRO B 123 TRP B 127 5 5 HELIX 23 AC5 ASP B 187 GLN B 196 1 10 HELIX 24 AC6 ASP B 367 LYS B 388 1 22 HELIX 25 AC7 GLU B 404 ARG B 457 1 54 HELIX 26 AC8 ASP B 475 LYS B 483 1 9 HELIX 27 AC9 ASP B 488 ASN B 501 1 14 SHEET 1 AA1 5 GLY C 361 TYR C 364 0 SHEET 2 AA1 5 TYR C 352 ASN C 358 -1 N HIS C 356 O GLY C 363 SHEET 3 AA1 5 ILE C 8 TYR C 12 -1 N CYS C 9 O HIS C 355 SHEET 4 AA1 5 CYS C 467 PHE C 470 -1 O PHE C 468 N ILE C 8 SHEET 5 AA1 5 VAL C 460 GLU C 462 -1 N LYS C 461 O GLU C 469 SHEET 1 AA2 2 GLU C 19 VAL C 21 0 SHEET 2 AA2 2 VAL C 29 VAL C 31 -1 O VAL C 29 N VAL C 21 SHEET 1 AA3 2 ALA C 34 ASP C 36 0 SHEET 2 AA3 2 VAL C 316 ALA C 318 -1 O LEU C 317 N LYS C 35 SHEET 1 AA4 3 LEU C 38 GLU C 39 0 SHEET 2 AA4 3 PHE C 295 HIS C 296 1 O PHE C 295 N GLU C 39 SHEET 3 AA4 3 LYS C 308 TYR C 309 1 O LYS C 308 N HIS C 296 SHEET 1 AA5 2 LEU C 46 LEU C 49 0 SHEET 2 AA5 2 LEU C 275 THR C 280 1 O THR C 280 N LYS C 48 SHEET 1 AA6 3 LEU C 55 GLU C 56 0 SHEET 2 AA6 3 ILE C 84 GLU C 86 1 O MET C 85 N LEU C 55 SHEET 3 AA6 3 ILE C 268 LYS C 270 1 O MET C 269 N ILE C 84 SHEET 1 AA7 5 GLY C 98 PHE C 100 0 SHEET 2 AA7 5 ARG C 229 LEU C 237 1 O PHE C 232 N SER C 99 SHEET 3 AA7 5 MET C 176 HIS C 184 -1 N TRP C 180 O SER C 233 SHEET 4 AA7 5 TYR C 256 ILE C 260 -1 O PHE C 258 N LEU C 177 SHEET 5 AA7 5 PHE C 116 LYS C 120 -1 N VAL C 119 O GLY C 257 SHEET 1 AA8 5 GLY C 98 PHE C 100 0 SHEET 2 AA8 5 ARG C 229 LEU C 237 1 O PHE C 232 N SER C 99 SHEET 3 AA8 5 MET C 176 HIS C 184 -1 N TRP C 180 O SER C 233 SHEET 4 AA8 5 LEU C 251 PRO C 254 -1 O ILE C 252 N GLY C 181 SHEET 5 AA8 5 MET C 151 TRP C 153 -1 N VAL C 152 O ALA C 253 SHEET 1 AA9 2 HIS C 130 THR C 131 0 SHEET 2 AA9 2 THR C 155 LYS C 156 -1 O THR C 155 N THR C 131 SHEET 1 AB1 2 SER C 136 VAL C 141 0 SHEET 2 AB1 2 ASN C 144 SER C 146 -1 O SER C 146 N CYS C 139 SHEET 1 AB2 4 ALA C 164 ASN C 169 0 SHEET 2 AB2 4 THR C 242 SER C 247 -1 O PHE C 245 N GLY C 166 SHEET 3 AB2 4 VAL C 202 GLY C 205 -1 N SER C 203 O GLU C 246 SHEET 4 AB2 4 ASN C 210 SER C 213 -1 O SER C 213 N VAL C 202 SHEET 1 AB3 3 ALA C 288 ILE C 289 0 SHEET 2 AB3 3 CYS C 282 GLN C 283 -1 N CYS C 282 O ILE C 289 SHEET 3 AB3 3 ILE C 303 GLY C 304 -1 O ILE C 303 N GLN C 283 SHEET 1 AB4 3 ILE A 8 TYR A 12 0 SHEET 2 AB4 3 TYR A 352 SER A 357 -1 O HIS A 355 N CYS A 9 SHEET 3 AB4 3 SER A 362 TYR A 364 -1 O GLY A 363 N HIS A 356 SHEET 1 AB5 2 GLU A 19 VAL A 21 0 SHEET 2 AB5 2 VAL A 29 VAL A 31 -1 O VAL A 31 N GLU A 19 SHEET 1 AB6 2 ALA A 34 ASP A 36 0 SHEET 2 AB6 2 VAL A 316 ALA A 318 -1 O LEU A 317 N LYS A 35 SHEET 1 AB7 2 LEU A 46 LEU A 49 0 SHEET 2 AB7 2 LEU A 275 THR A 280 1 O THR A 280 N LYS A 48 SHEET 1 AB8 3 LEU A 55 GLU A 56 0 SHEET 2 AB8 3 ILE A 84 GLU A 86 1 O MET A 85 N LEU A 55 SHEET 3 AB8 3 ILE A 268 LYS A 270 1 O MET A 269 N ILE A 84 SHEET 1 AB9 5 GLY A 98 PHE A 100 0 SHEET 2 AB9 5 ARG A 229 LEU A 237 1 O PHE A 232 N SER A 99 SHEET 3 AB9 5 MET A 176 HIS A 184 -1 N TRP A 180 O SER A 233 SHEET 4 AB9 5 TYR A 256 ARG A 263 -1 O PHE A 258 N LEU A 177 SHEET 5 AB9 5 VAL A 113 LYS A 120 -1 N VAL A 119 O GLY A 257 SHEET 1 AC1 5 GLY A 98 PHE A 100 0 SHEET 2 AC1 5 ARG A 229 LEU A 237 1 O PHE A 232 N SER A 99 SHEET 3 AC1 5 MET A 176 HIS A 184 -1 N TRP A 180 O SER A 233 SHEET 4 AC1 5 LEU A 251 PRO A 254 -1 O ILE A 252 N GLY A 181 SHEET 5 AC1 5 MET A 151 TRP A 153 -1 N VAL A 152 O ALA A 253 SHEET 1 AC2 2 SER A 136 VAL A 141 0 SHEET 2 AC2 2 ASN A 144 SER A 146 -1 O SER A 146 N SER A 136 SHEET 1 AC3 4 ALA A 164 ASN A 169 0 SHEET 2 AC3 4 THR A 242 SER A 247 -1 O PHE A 245 N GLY A 166 SHEET 3 AC3 4 VAL A 202 GLY A 205 -1 N SER A 203 O GLU A 246 SHEET 4 AC3 4 ASN A 210 SER A 213 -1 O LYS A 211 N VAL A 204 SHEET 1 AC4 3 ALA A 288 ILE A 289 0 SHEET 2 AC4 3 CYS A 282 GLN A 283 -1 N CYS A 282 O ILE A 289 SHEET 3 AC4 3 ILE A 303 GLY A 304 -1 O ILE A 303 N GLN A 283 SHEET 1 AC5 2 VAL A 460 GLU A 462 0 SHEET 2 AC5 2 PHE A 468 PHE A 470 -1 O GLU A 469 N LYS A 461 SHEET 1 AC6 5 GLY B 363 ALA B 366 0 SHEET 2 AC6 5 TYR B 352 HIS B 356 -1 N HIS B 356 O GLY B 363 SHEET 3 AC6 5 GLN B 7 TYR B 12 -1 N GLY B 11 O GLY B 353 SHEET 4 AC6 5 CYS B 467 PHE B 470 -1 O PHE B 468 N ILE B 8 SHEET 5 AC6 5 VAL B 460 GLU B 462 -1 N LYS B 461 O GLU B 469 SHEET 1 AC7 2 GLU B 19 VAL B 21 0 SHEET 2 AC7 2 VAL B 29 VAL B 31 -1 O VAL B 29 N VAL B 21 SHEET 1 AC8 2 ALA B 34 ASP B 36 0 SHEET 2 AC8 2 VAL B 316 ALA B 318 -1 O LEU B 317 N LYS B 35 SHEET 1 AC9 3 LEU B 38 GLU B 39 0 SHEET 2 AC9 3 PHE B 295 HIS B 296 1 O PHE B 295 N GLU B 39 SHEET 3 AC9 3 LYS B 308 TYR B 309 1 O LYS B 308 N HIS B 296 SHEET 1 AD1 2 LYS B 48 LEU B 49 0 SHEET 2 AD1 2 GLU B 279 THR B 280 1 O THR B 280 N LYS B 48 SHEET 1 AD2 3 LEU B 55 GLU B 56 0 SHEET 2 AD2 3 ILE B 84 GLU B 86 1 O MET B 85 N LEU B 55 SHEET 3 AD2 3 ILE B 268 LYS B 270 1 O MET B 269 N ILE B 84 SHEET 1 AD3 5 GLY B 98 PHE B 100 0 SHEET 2 AD3 5 ARG B 229 LEU B 237 1 O MET B 230 N SER B 99 SHEET 3 AD3 5 MET B 176 HIS B 184 -1 N MET B 176 O LEU B 237 SHEET 4 AD3 5 TYR B 256 ILE B 260 -1 O PHE B 258 N LEU B 177 SHEET 5 AD3 5 PHE B 116 LYS B 120 -1 N GLU B 117 O LYS B 259 SHEET 1 AD4 5 GLY B 98 PHE B 100 0 SHEET 2 AD4 5 ARG B 229 LEU B 237 1 O MET B 230 N SER B 99 SHEET 3 AD4 5 MET B 176 HIS B 184 -1 N MET B 176 O LEU B 237 SHEET 4 AD4 5 LEU B 251 PRO B 254 -1 O ILE B 252 N GLY B 181 SHEET 5 AD4 5 MET B 151 TRP B 153 -1 N VAL B 152 O ALA B 253 SHEET 1 AD5 2 SER B 136 VAL B 141 0 SHEET 2 AD5 2 ASN B 144 SER B 146 -1 O SER B 146 N SER B 136 SHEET 1 AD6 4 ALA B 164 ASN B 169 0 SHEET 2 AD6 4 THR B 242 SER B 247 -1 O PHE B 245 N GLY B 166 SHEET 3 AD6 4 VAL B 202 GLY B 205 -1 N SER B 203 O GLU B 246 SHEET 4 AD6 4 ASN B 210 SER B 213 -1 O LYS B 211 N VAL B 204 SSBOND 1 CYS C 9 CYS C 467 1555 1555 2.04 SSBOND 2 CYS C 47 CYS C 278 1555 1555 2.03 SSBOND 3 CYS C 60 CYS C 72 1555 1555 2.03 SSBOND 4 CYS C 95 CYS C 139 1555 1555 2.03 SSBOND 5 CYS C 282 CYS C 306 1555 1555 2.03 SSBOND 6 CYS C 474 CYS C 478 1555 1555 2.03 SSBOND 7 CYS A 9 CYS A 467 1555 1555 2.04 SSBOND 8 CYS A 47 CYS A 278 1555 1555 2.03 SSBOND 9 CYS A 60 CYS A 72 1555 1555 2.03 SSBOND 10 CYS A 95 CYS A 139 1555 1555 2.03 SSBOND 11 CYS A 282 CYS A 306 1555 1555 2.03 SSBOND 12 CYS A 474 CYS A 478 1555 1555 2.03 SSBOND 13 CYS B 9 CYS B 467 1555 1555 2.03 SSBOND 14 CYS B 47 CYS B 278 1555 1555 2.03 SSBOND 15 CYS B 60 CYS B 72 1555 1555 2.03 SSBOND 16 CYS B 95 CYS B 139 1555 1555 2.03 SSBOND 17 CYS B 282 CYS B 306 1555 1555 2.03 SSBOND 18 CYS B 474 CYS B 478 1555 1555 2.03 LINK ND2 ASN C 28 C1 NAG C 602 1555 1555 1.46 LINK ND2 ASN C 169 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN A 28 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 169 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 484 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN B 28 C1 NAG B 603 1555 1555 1.44 LINK ND2 ASN B 169 C1 NAG B 601 1555 1555 1.44 LINK ND2 ASN B 484 C1 NAG B 602 1555 1555 1.44 LINK O3 GAL D 1 C1 NAG D 2 1555 1555 1.39 LINK O4 NAG D 2 C1 GAL D 3 1555 1555 1.40 LINK O6 GAL D 3 C2 SIA D 4 1555 1555 1.38 LINK O3 GAL E 1 C1 NAG E 2 1555 1555 1.39 LINK O4 NAG E 2 C1 GAL E 3 1555 1555 1.40 LINK O6 GAL E 3 C2 SIA E 4 1555 1555 1.38 LINK O3 GAL F 1 C1 NAG F 2 1555 1555 1.39 LINK O4 NAG F 2 C1 GAL F 3 1555 1555 1.40 LINK O6 GAL F 3 C2 SIA F 4 1555 1555 1.38 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