HEADER VIRAL PROTEIN/IMMUNE SYSTEM 28-SEP-24 9JQU TITLE THE CRYSTAL STRUCTURE OF SFTSV GN AND SD4 ANTIBODY COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPMENT POLYPROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: M POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: SEQUENCE REFERENCE FOR SOURCE ORGANISM SFTS VIRUS JS4 COMPND 7 IS NOT AVAILABLE IN UNIPROT AT THE TIME OF BIOCURATION. CURRENT COMPND 8 SEQUENCE REFERENCE IS FROM UNIPROT ID A0A1S6K8S9.; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: SD4 LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: SD4 HEAVY CHAIN; COMPND 15 CHAIN: H; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SFTS VIRUS JS4; SOURCE 3 ORGANISM_TAXID: 992216; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SFTSV, GN, SD4, ANTIBODY, SEVERE FEVER WITH THROMBOCYTOPENIA SYNDROME KEYWDS 2 VIRUS, VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 3 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR W.F.SHI,C.S.QUAN,J.X.QI REVDAT 1 18-JUN-25 9JQU 0 JRNL AUTH C.S.QUAN,J.X.QI,W.F.SHI JRNL TITL HIGH AFFINITY HUMAN-DERIVED ANTIBODIES EFFECTIVELY RESCUE JRNL TITL 2 MORIBUND MICE WITH LETHAL SEVERE FEVER WITH THROMBOCYTOPENIA JRNL TITL 3 VIRUS INFECTION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.21 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1 REMARK 3 NUMBER OF REFLECTIONS : 11716 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.252 REMARK 3 R VALUE (WORKING SET) : 0.250 REMARK 3 FREE R VALUE : 0.289 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 587 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 32.2100 - 5.2300 0.97 2913 164 0.2356 0.2452 REMARK 3 2 5.2300 - 4.1600 0.97 2834 138 0.2282 0.2820 REMARK 3 3 4.1600 - 3.6300 0.97 2799 145 0.2718 0.3362 REMARK 3 4 3.6300 - 3.3000 0.89 2583 140 0.3106 0.3756 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.463 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.000 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 84.38 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 5923 REMARK 3 ANGLE : 0.789 8028 REMARK 3 CHIRALITY : 0.050 879 REMARK 3 PLANARITY : 0.006 1031 REMARK 3 DIHEDRAL : 13.290 2150 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN A AND RESID 21:341 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.723 -1.007 -26.940 REMARK 3 T TENSOR REMARK 3 T11: 0.5290 T22: 0.4961 REMARK 3 T33: 0.4590 T12: 0.0045 REMARK 3 T13: 0.0197 T23: 0.0057 REMARK 3 L TENSOR REMARK 3 L11: 0.6420 L22: 0.3937 REMARK 3 L33: 0.8429 L12: 0.0074 REMARK 3 L13: 0.2872 L23: -0.0891 REMARK 3 S TENSOR REMARK 3 S11: 0.0730 S12: -0.1340 S13: -0.0731 REMARK 3 S21: 0.0956 S22: -0.0359 S23: 0.0239 REMARK 3 S31: 0.0412 S32: -0.0476 S33: 0.7317 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN H AND RESID 2:223 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.339 -28.349 -70.512 REMARK 3 T TENSOR REMARK 3 T11: 0.5591 T22: 0.5572 REMARK 3 T33: 0.6575 T12: -0.0136 REMARK 3 T13: -0.0457 T23: -0.0431 REMARK 3 L TENSOR REMARK 3 L11: 0.1088 L22: 0.2545 REMARK 3 L33: 0.2474 L12: 0.1352 REMARK 3 L13: 0.0105 L23: 0.3577 REMARK 3 S TENSOR REMARK 3 S11: 0.0250 S12: 0.1244 S13: -0.1800 REMARK 3 S21: -0.0788 S22: 0.1568 S23: -0.1675 REMARK 3 S31: -0.1721 S32: 0.0725 S33: -4.5814 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN L AND RESID 1:211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.352 -36.926 -60.124 REMARK 3 T TENSOR REMARK 3 T11: 0.5375 T22: 0.6153 REMARK 3 T33: 0.5790 T12: 0.0151 REMARK 3 T13: 0.0298 T23: -0.0273 REMARK 3 L TENSOR REMARK 3 L11: 0.4536 L22: 0.7385 REMARK 3 L33: 0.3923 L12: 0.5364 REMARK 3 L13: 0.1120 L23: -0.1145 REMARK 3 S TENSOR REMARK 3 S11: 0.0512 S12: -0.0127 S13: 0.0106 REMARK 3 S21: 0.1677 S22: -0.0598 S23: 0.0676 REMARK 3 S31: 0.1102 S32: -0.0966 S33: -2.2095 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9JQU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 03-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1300052002. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-MAY-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11858 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : 4.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.6750 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 5Y10,7L2E REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M SODIUM REMARK 280 ACETATE TRIHYDRATE PH 4.6, 30% W/V POLYETHYLENE GLYCOL 4,000, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 23.18000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6080 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 32720 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H, B, C 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 GLY A 20 REMARK 465 HIS A 342 REMARK 465 HIS A 343 REMARK 465 HIS A 344 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 GLN H 1 REMARK 465 PRO H 134 REMARK 465 SER H 135 REMARK 465 SER H 136 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 GLY H 142 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 115 CG CD OE1 OE2 REMARK 470 THR A 299 OG1 CG2 REMARK 470 ARG L 79 CD NE CZ NH1 NH2 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 SER A 22 -102.89 30.00 REMARK 500 SER A 46 -77.49 154.16 REMARK 500 ARG A 75 -24.15 71.30 REMARK 500 LEU A 108 -179.97 -174.57 REMARK 500 PHE A 203 77.23 -109.72 REMARK 500 CYS A 217 -56.85 -123.34 REMARK 500 GLU A 218 -27.76 66.76 REMARK 500 GLU A 298 109.78 -50.15 REMARK 500 THR A 299 -75.29 -90.65 REMARK 500 SER A 300 -73.79 -103.94 REMARK 500 GLU A 301 -170.74 45.38 REMARK 500 ALA A 302 135.51 -171.71 REMARK 500 SER L 30 -138.61 65.80 REMARK 500 ASN L 31 38.69 -98.29 REMARK 500 LEU L 47 -61.11 -95.53 REMARK 500 ALA L 51 -5.27 66.16 REMARK 500 ASP L 82 3.48 -68.02 REMARK 500 SER H 7 148.26 -171.57 REMARK 500 VAL H 48 -63.05 -105.48 REMARK 500 SER H 63 -9.29 70.51 REMARK 500 SER H 123 -155.37 -78.58 REMARK 500 PRO H 193 46.59 -77.99 REMARK 500 SER H 194 -61.00 54.70 REMARK 500 LYS H 222 143.55 74.20 REMARK 500 REMARK 500 REMARK: NULL DBREF1 9JQU A 20 338 UNP A0A1S6K8S9_SFTS DBREF2 9JQU A A0A1S6K8S9 19 337 DBREF 9JQU L 1 214 PDB 9JQU 9JQU 1 214 DBREF 9JQU H 1 223 PDB 9JQU 9JQU 1 223 SEQADV 9JQU HIS A 339 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQU HIS A 340 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQU HIS A 341 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQU HIS A 342 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQU HIS A 343 UNP A0A1S6K8S EXPRESSION TAG SEQADV 9JQU HIS A 344 UNP A0A1S6K8S EXPRESSION TAG SEQRES 1 A 325 GLY ASP SER GLY PRO ILE ILE CYS ALA GLY PRO ILE HIS SEQRES 2 A 325 SER ASN LYS SER ALA GLY ILE PRO HIS LEU LEU GLY TYR SEQRES 3 A 325 SER GLU LYS ILE CYS GLN ILE ASP ARG LEU ILE HIS VAL SEQRES 4 A 325 SER SER TRP LEU ARG ASN HIS SER GLN PHE GLN GLY TYR SEQRES 5 A 325 VAL GLY GLN ARG GLY GLY ARG SER GLN VAL SER TYR TYR SEQRES 6 A 325 PRO ALA GLU ASN SER TYR SER ARG TRP SER GLY LEU LEU SEQRES 7 A 325 SER PRO CYS ASP ALA ASP TRP LEU GLY MET LEU VAL VAL SEQRES 8 A 325 LYS LYS ALA ARG GLU SER ASP MET ILE VAL PRO GLY PRO SEQRES 9 A 325 SER TYR LYS GLY LYS VAL PHE PHE GLU ARG PRO THR PHE SEQRES 10 A 325 ASP GLY TYR VAL GLY TRP GLY CYS GLY SER GLY LYS SER SEQRES 11 A 325 ARG THR GLU SER GLY GLU LEU CYS SER SER ASP SER GLY SEQRES 12 A 325 THR SER SER GLY LEU LEU PRO SER ASP ARG VAL LEU TRP SEQRES 13 A 325 ILE GLY ASP VAL ALA CYS GLN LEU MET THR PRO ILE PRO SEQRES 14 A 325 GLU GLU THR PHE LEU GLU LEU LYS SER PHE SER GLN SER SEQRES 15 A 325 GLU PHE PRO ASP ILE CYS LYS ILE ASP GLY ILE VAL PHE SEQRES 16 A 325 ASN GLN CYS GLU GLY GLU SER LEU PRO GLN PRO PHE ASP SEQRES 17 A 325 VAL ALA TRP MET ASP VAL GLY HIS SER HIS LYS ILE ILE SEQRES 18 A 325 MET ARG GLU HIS LYS THR LYS TRP VAL GLN GLU SER SER SEQRES 19 A 325 SER LYS ASP PHE VAL CYS TYR LYS GLU GLY THR GLY PRO SEQRES 20 A 325 CYS SER GLU SER GLU GLU LYS ALA CYS LYS THR SER GLY SEQRES 21 A 325 SER CYS ARG GLY ASP MET GLN PHE CYS LYS VAL ALA GLY SEQRES 22 A 325 CYS GLU HIS GLY GLU GLU THR SER GLU ALA LYS CYS ARG SEQRES 23 A 325 CYS SER LEU VAL HIS LYS PRO GLY GLU VAL VAL VAL SER SEQRES 24 A 325 TYR GLY GLY MET ARG VAL ARG PRO LYS CYS TYR GLY PHE SEQRES 25 A 325 SER ARG MET MET ALA THR LEU HIS HIS HIS HIS HIS HIS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 L 214 GLN HIS ILE SER ASN HIS LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY THR ALA PRO THR LEU LEU ILE TYR GLU ALA SER SEQRES 5 L 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE SER PHE THR ILE SER SER LEU SEQRES 7 L 214 ARG PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 ASP ASN PHE PRO LEU THR PHE GLY PRO GLY THR THR MET SEQRES 9 L 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 H 223 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 223 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 223 PHE PRO PHE SER GLY TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 H 223 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE SER SEQRES 5 H 223 TYR ASP GLY SER GLU LYS ASN TYR ALA ASP SER VAL LYS SEQRES 6 H 223 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 223 LEU TYR LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 H 223 ALA VAL TYR TYR CYS ALA LYS ASP ARG ASP TYR TYR GLY SEQRES 9 H 223 SER GLY PHE TYR ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 H 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 223 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 H 223 LYS SER HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET NAG C 1 14 HET NAG C 2 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-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 FORMUL 4 NAG 4(C8 H15 N O6) FORMUL 4 BMA C6 H12 O6 HELIX 1 AA1 SER A 46 ARG A 54 1 9 HELIX 2 AA2 LEU A 55 HIS A 65 1 11 HELIX 3 AA3 GLY A 77 VAL A 81 5 5 HELIX 4 AA4 SER A 98 LEU A 105 1 8 HELIX 5 AA5 SER A 161 SER A 164 5 4 HELIX 6 AA6 PRO A 169 ASP A 171 5 3 HELIX 7 AA7 PRO A 188 PHE A 203 1 16 HELIX 8 AA8 SER A 253 LYS A 255 5 3 HELIX 9 AA9 SER A 268 GLY A 279 1 12 HELIX 10 AB1 ASP A 284 GLY A 292 1 9 HELIX 11 AB2 ARG L 79 PHE L 83 5 5 HELIX 12 AB3 LYS L 183 GLU L 187 1 5 HELIX 13 AB4 PRO H 28 TYR H 32 5 5 HELIX 14 AB5 ARG H 87 THR H 91 5 5 HELIX 15 AB6 LYS H 209 ASN H 212 5 4 SHEET 1 AA1 2 TYR A 71 VAL A 72 0 SHEET 2 AA1 2 LEU A 167 LEU A 168 1 O LEU A 168 N TYR A 71 SHEET 1 AA2 5 SER A 82 TYR A 84 0 SHEET 2 AA2 5 VAL A 173 ILE A 176 1 O TRP A 175 N SER A 82 SHEET 3 AA2 5 PHE A 130 PRO A 134 1 N PHE A 130 O LEU A 174 SHEET 4 AA2 5 TYR A 139 GLY A 143 -1 O VAL A 140 N ARG A 133 SHEET 5 AA2 5 VAL A 110 LYS A 112 1 N LYS A 111 O GLY A 141 SHEET 1 AA3 2 LYS A 148 ARG A 150 0 SHEET 2 AA3 2 CYS A 157 SER A 159 -1 O SER A 158 N SER A 149 SHEET 1 AA4 4 ASP A 178 CYS A 181 0 SHEET 2 AA4 4 CYS A 328 ARG A 333 -1 O TYR A 329 N ALA A 180 SHEET 3 AA4 4 ASP A 227 MET A 231 -1 N TRP A 230 O GLY A 330 SHEET 4 AA4 4 ILE A 239 MET A 241 -1 O ILE A 239 N MET A 231 SHEET 1 AA5 3 ILE A 212 VAL A 213 0 SHEET 2 AA5 3 ILE A 206 ILE A 209 -1 N ILE A 209 O ILE A 212 SHEET 3 AA5 3 ALA A 336 LEU A 338 -1 O THR A 337 N CYS A 207 SHEET 1 AA6 3 LYS A 245 VAL A 249 0 SHEET 2 AA6 3 GLU A 314 TYR A 319 -1 O GLU A 314 N VAL A 249 SHEET 3 AA6 3 MET A 322 VAL A 324 -1 O VAL A 324 N VAL A 317 SHEET 1 AA7 4 GLY A 265 PRO A 266 0 SHEET 2 AA7 4 PHE A 257 LYS A 261 -1 N LYS A 261 O GLY A 265 SHEET 3 AA7 4 ARG A 305 LEU A 308 -1 O ARG A 305 N TYR A 260 SHEET 4 AA7 4 ARG A 282 GLY A 283 1 N ARG A 282 O CYS A 306 SHEET 1 AA8 4 MET L 4 SER L 7 0 SHEET 2 AA8 4 VAL L 19 ALA L 25 -1 O GLN L 24 N THR L 5 SHEET 3 AA8 4 PHE L 71 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AA8 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AA9 6 SER L 10 SER L 12 0 SHEET 2 AA9 6 THR L 102 ASP L 105 1 O ASP L 105 N LEU L 11 SHEET 3 AA9 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA9 6 THR L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA9 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AB1 4 PHE L 116 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 3 ALA L 144 VAL L 150 0 SHEET 2 AB2 3 TYR L 192 HIS L 198 -1 O ALA L 193 N LYS L 149 SHEET 3 AB2 3 VAL L 205 LYS L 207 -1 O VAL L 205 N VAL L 196 SHEET 1 AB3 4 GLN H 3 SER H 7 0 SHEET 2 AB3 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AB3 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB3 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AB4 6 VAL H 11 VAL H 12 0 SHEET 2 AB4 6 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AB4 6 ALA H 92 TYR H 95 -1 N TYR H 94 O THR H 115 SHEET 4 AB4 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB4 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AB4 6 LYS H 58 TYR H 60 -1 O ASN H 59 N VAL H 50 SHEET 1 AB5 2 ALA H 97 ASP H 99 0 SHEET 2 AB5 2 TYR H 108 TRP H 111 -1 O TYR H 110 N LYS H 98 SHEET 1 AB6 4 SER H 128 LEU H 132 0 SHEET 2 AB6 4 ALA H 144 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AB6 4 TYR H 184 VAL H 192 -1 O TYR H 184 N TYR H 153 SHEET 4 AB6 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 189 SHEET 1 AB7 4 SER H 128 LEU H 132 0 SHEET 2 AB7 4 ALA H 144 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AB7 4 TYR H 184 VAL H 192 -1 O TYR H 184 N TYR H 153 SHEET 4 AB7 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 185 SHEET 1 AB8 3 THR H 159 TRP H 162 0 SHEET 2 AB8 3 TYR H 202 HIS H 208 -1 O ASN H 205 N SER H 161 SHEET 3 AB8 3 THR H 213 VAL H 219 -1 O THR H 213 N HIS H 208 SSBOND 1 CYS A 27 CYS A 50 1555 1555 2.03 SSBOND 2 CYS A 144 CYS A 157 1555 1555 2.03 SSBOND 3 CYS A 181 CYS A 328 1555 1555 2.03 SSBOND 4 CYS A 207 CYS A 217 1555 1555 2.02 SSBOND 5 CYS A 259 CYS A 306 1555 1555 2.03 SSBOND 6 CYS A 267 CYS A 304 1555 1555 2.04 SSBOND 7 CYS A 275 CYS A 281 1555 1555 2.03 SSBOND 8 CYS A 288 CYS A 293 1555 1555 2.03 SSBOND 9 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 10 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 11 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 12 CYS H 148 CYS H 204 1555 1555 2.03 LINK ND2 ASN A 34 C1 NAG C 1 1555 1555 1.45 LINK ND2 ASN A 64 C1 NAG B 1 1555 1555 1.43 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.47 CISPEP 1 TYR A 84 PRO A 85 0 4.50 CISPEP 2 SER L 7 PRO L 8 0 -1.59 CISPEP 3 PHE L 94 PRO L 95 0 6.45 CISPEP 4 TYR L 140 PRO L 141 0 -3.08 CISPEP 5 PHE H 154 PRO H 155 0 0.64 CISPEP 6 GLU H 156 PRO H 157 0 3.34 CRYST1 96.856 46.360 97.322 90.00 113.30 90.00 P 1 21 1 2 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 0.010325 0.000000 0.004447 0.00000 SCALE2 0.000000 0.021570 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011188 0.00000