HEADER VIRAL PROTEIN/IMMUNE SYSTEM 02-APR-24 8YXI TITLE CRYSTAL STRUCTURE OF SFTSV GN IN COMPLEX WITH A NEUTRALIZING ANTIBODY TITLE 2 40C10 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN; COMPND 3 CHAIN: C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: LIGHT CHAIN; COMPND 6 CHAIN: B; COMPND 7 MOL_ID: 3; COMPND 8 MOLECULE: ENVELOPMENT POLYPROTEIN; COMPND 9 CHAIN: A; COMPND 10 SYNONYM: M POLYPROTEIN; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_TAXID: 10090; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: SEVERE FEVER WITH THROMBOCYTOPENIA SYNDROME SOURCE 9 VIRUS; SOURCE 10 ORGANISM_TAXID: 1003835; SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS NEUTRALIZING ANTIBODY, SFTSV, COMPLEX, VIRAL PROTEIN/IMMUNE SYSTEM, KEYWDS 2 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR P.YANG,Y.GUO,N.ZHANG REVDAT 1 11-SEP-24 8YXI 0 JRNL AUTH P.YANG,Y.GUO,N.ZHANG JRNL TITL MOLECULAR MECHANISM AND STRUCTURE-GUIDED HUMANIZATION OF A JRNL TITL 2 BROADLY NEUTRALIZING ANTIBODY AGAINST SFTSV JRNL REF PLOS PATHOGENS 2024 JRNL REFN JRNL DOI 10.1371/JOURNAL.PPAT.1012550 REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.63 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 35511 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.208 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.770 REMARK 3 FREE R VALUE TEST SET COUNT : 1695 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 36.6300 - 5.4900 0.99 2868 166 0.2053 0.2243 REMARK 3 2 5.4900 - 4.3600 1.00 2846 148 0.1712 0.2045 REMARK 3 3 4.3600 - 3.8100 0.99 2843 122 0.1678 0.2073 REMARK 3 4 3.8100 - 3.4600 1.00 2857 123 0.1822 0.2614 REMARK 3 5 3.4600 - 3.2100 1.00 2799 148 0.2019 0.2629 REMARK 3 6 3.2100 - 3.0200 1.00 2820 142 0.2043 0.2310 REMARK 3 7 3.0200 - 2.8700 1.00 2822 145 0.2187 0.2651 REMARK 3 8 2.8700 - 2.7500 0.99 2771 136 0.2384 0.2854 REMARK 3 9 2.7500 - 2.6400 1.00 2824 116 0.2584 0.2892 REMARK 3 10 2.6400 - 2.5500 1.00 2807 152 0.2681 0.3300 REMARK 3 11 2.5500 - 2.4700 0.99 2774 148 0.2787 0.3084 REMARK 3 12 2.4700 - 2.4000 0.99 2785 149 0.2748 0.3046 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.280 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.150 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.010 NULL REMARK 3 ANGLE : 1.053 NULL REMARK 3 CHIRALITY : 0.064 893 REMARK 3 PLANARITY : 0.009 1035 REMARK 3 DIHEDRAL : 11.313 841 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 8YXI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 07-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300046569. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-APR-23 REMARK 200 TEMPERATURE (KELVIN) : 80 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 : BL10U2 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 EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35578 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 94.370 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 1.900 REMARK 200 R MERGE (I) : 0.16000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.90000 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: SAD REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.04 M CITRIC ACID, 0.06 M BIS-TRIS REMARK 280 PROPANE/PH 6.4, 20% W/V POLYETHYLENE GLYCOL 3,350, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 97.87650 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.95300 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 97.87650 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.95300 REMARK 290 SMTRY3 4 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: 6410 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, B, A, D, E 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 SER C 137 REMARK 465 ALA C 138 REMARK 465 ALA C 139 REMARK 465 GLN C 140 REMARK 465 GLY A 322 REMARK 465 LEU A 323 REMARK 465 ASN A 324 REMARK 465 ASP A 325 REMARK 465 ILE A 326 REMARK 465 PHE A 327 REMARK 465 GLU A 328 REMARK 465 ALA A 329 REMARK 465 GLN A 330 REMARK 465 LYS A 331 REMARK 465 ILE A 332 REMARK 465 GLU A 333 REMARK 465 TRP A 334 REMARK 465 HIS A 335 REMARK 465 GLU A 336 REMARK 465 ALA A 337 REMARK 465 ALA A 338 REMARK 465 ALA A 339 REMARK 465 HIS A 340 REMARK 465 HIS A 341 REMARK 465 HIS A 342 REMARK 465 HIS A 343 REMARK 465 HIS A 344 REMARK 465 HIS A 345 REMARK 465 HIS A 346 REMARK 465 HIS A 347 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 SER B 203 OG REMARK 470 GLU A 198 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 468 O HOH A 499 2.01 REMARK 500 NH1 ARG A 262 O HOH A 401 2.04 REMARK 500 O HOH A 543 O HOH A 544 2.07 REMARK 500 O HOH A 539 O HOH A 542 2.10 REMARK 500 NH1 ARG A 303 O HOH A 402 2.10 REMARK 500 O HOH A 451 O HOH A 523 2.10 REMARK 500 O ASN C 142 OG SER C 194 2.12 REMARK 500 NE2 GLN B 37 O HOH B 301 2.12 REMARK 500 OD1 ASP B 170 OG1 THR B 172 2.14 REMARK 500 OH TYR C 111 O HOH C 301 2.14 REMARK 500 O HOH A 483 O HOH A 494 2.15 REMARK 500 O HOH B 325 O HOH B 367 2.15 REMARK 500 O TYR B 67 O HOH B 302 2.15 REMARK 500 OE1 GLU A 278 O HOH A 403 2.15 REMARK 500 O VAL C 172 O HOH C 302 2.15 REMARK 500 O HOH C 310 O HOH C 406 2.16 REMARK 500 OG SER A 258 OG SER A 260 2.16 REMARK 500 O ALA A 8 NH1 ARG A 34 2.17 REMARK 500 O6 NAG E 1 O HOH A 529 2.17 REMARK 500 O HOH C 376 O HOH C 411 2.17 REMARK 500 O HOH B 377 O HOH B 382 2.17 REMARK 500 O HOH C 415 O HOH C 416 2.18 REMARK 500 O HOH C 385 O HOH C 392 2.19 REMARK 500 O THR B 126 O HOH B 303 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD2 ASP C 182 NH1 ARG B 188 2657 2.14 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 ALA C 92 174.65 178.33 REMARK 500 LEU C 147 -168.76 -103.72 REMARK 500 SER C 165 26.57 48.72 REMARK 500 SER C 181 -130.07 59.85 REMARK 500 TRP C 197 -74.10 -75.51 REMARK 500 ALA B 15 128.82 -38.12 REMARK 500 SER B 30 -139.64 54.98 REMARK 500 ALA B 51 -46.10 76.42 REMARK 500 PRO B 120 157.26 -48.34 REMARK 500 ARG B 211 127.47 179.51 REMARK 500 SER A 2 36.28 -97.40 REMARK 500 ILE A 6 -21.99 -147.17 REMARK 500 ARG A 55 -45.09 78.96 REMARK 500 LYS A 94 -159.94 -114.07 REMARK 500 CYS A 187 -70.45 -97.73 REMARK 500 HIS A 215 -152.16 -118.49 REMARK 500 ARG A 222 -95.52 -107.90 REMARK 500 SER A 232 19.78 57.92 REMARK 500 ASP A 264 -176.83 -68.65 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 PHE C 60 ASN C 61 148.83 REMARK 500 REMARK 500 REMARK: NULL DBREF 8YXI C 1 222 PDB 8YXI 8YXI 1 222 DBREF 8YXI B 1 212 PDB 8YXI 8YXI 1 212 DBREF1 8YXI A 1 321 UNP A0A2Z4HIM0_SFTS DBREF2 8YXI A A0A2Z4HIM0 20 340 SEQADV 8YXI GLY A 322 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI LEU A 323 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI ASN A 324 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI ASP A 325 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI ILE A 326 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI PHE A 327 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI GLU A 328 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI ALA A 329 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI GLN A 330 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI LYS A 331 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI ILE A 332 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI GLU A 333 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI TRP A 334 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI HIS A 335 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI GLU A 336 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI ALA A 337 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI ALA A 338 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI ALA A 339 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI HIS A 340 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI HIS A 341 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI HIS A 342 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI HIS A 343 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI HIS A 344 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI HIS A 345 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI HIS A 346 UNP A0A2Z4HIM EXPRESSION TAG SEQADV 8YXI HIS A 347 UNP A0A2Z4HIM EXPRESSION TAG SEQRES 1 C 222 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 C 222 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 C 222 TYR THR PHE THR SER HIS TYR MET TYR TRP VAL LYS GLN SEQRES 4 C 222 ARG PRO GLY GLN GLY PRO GLU TRP ILE GLY GLU ILE ASN SEQRES 5 C 222 PRO THR ASN GLY GLY THR LYS PHE ASN GLU LYS PHE LYS SEQRES 6 C 222 SER LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 C 222 ALA TYR ILE GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 C 222 ALA VAL TYR TYR CYS SER SER SER GLY TYR ASP TYR ASP SEQRES 9 C 222 GLY ARG ALA TYR PHE ASP TYR TRP GLY GLN GLY THR THR SEQRES 10 C 222 LEU THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL SEQRES 11 C 222 TYR PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER SEQRES 12 C 222 MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO SEQRES 13 C 222 GLU PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER SEQRES 14 C 222 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP SEQRES 15 C 222 LEU TYR THR LEU SER SER SER VAL THR VAL PRO SER SER SEQRES 16 C 222 THR TRP PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS SEQRES 17 C 222 PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 18 C 222 ARG SEQRES 1 B 212 ASP VAL VAL MET THR GLN THR PRO LYS PHE LEU LEU VAL SEQRES 2 B 212 SER ALA GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 B 212 GLN SER VAL SER ASN ASP VAL ALA TRP TYR GLN GLN LYS SEQRES 4 B 212 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TYR ALA SER SEQRES 5 B 212 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 B 212 GLY TYR GLY THR ASP PHE THR PHE THR ILE SER ALA VAL SEQRES 7 B 212 GLN ALA GLU ASP LEU ALA VAL TYR PHE CYS GLN GLN ASN SEQRES 8 B 212 TYR ASN SER PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 B 212 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 B 212 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 B 212 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 B 212 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 B 212 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 B 212 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 B 212 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 B 212 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 B 212 PHE ASN ARG GLY SEQRES 1 A 347 ASP SER GLY PRO ILE ILE CYS ALA GLY PRO ILE HIS SER SEQRES 2 A 347 ASN LYS SER ALA ASP ILE PRO HIS LEU LEU GLY TYR SER SEQRES 3 A 347 GLU LYS ILE CYS GLN ILE ASP ARG LEU ILE HIS VAL SER SEQRES 4 A 347 SER TRP LEU ARG ASN HIS SER GLN PHE GLN GLY TYR VAL SEQRES 5 A 347 GLY GLN ARG GLY GLY ARG SER GLN VAL SER TYR TYR PRO SEQRES 6 A 347 ALA GLU ASN SER TYR SER ARG TRP SER GLY LEU LEU SER SEQRES 7 A 347 PRO CYS ASP ALA ASP TRP LEU GLY MET LEU VAL VAL LYS SEQRES 8 A 347 LYS ALA LYS GLY SER ASP MET ILE VAL PRO GLY PRO SER SEQRES 9 A 347 TYR LYS GLY LYS VAL PHE PHE GLU ARG PRO THR PHE ASP SEQRES 10 A 347 GLY TYR VAL GLY TRP GLY CYS GLY SER GLY LYS SER ARG SEQRES 11 A 347 THR GLU SER GLY GLU LEU CYS SER SER ASP SER GLY THR SEQRES 12 A 347 SER SER GLY LEU LEU PRO SER ASN ARG VAL LEU TRP ILE SEQRES 13 A 347 GLY ASP VAL ALA CYS GLN PRO MET THR PRO ILE PRO GLU SEQRES 14 A 347 GLU THR PHE LEU GLU LEU LYS SER PHE SER GLN SER GLU SEQRES 15 A 347 PHE PRO ASP ILE CYS LYS ILE ASP GLY ILE VAL PHE ASN SEQRES 16 A 347 GLN CYS GLU GLY GLU SER LEU PRO GLN PRO PHE ASP VAL SEQRES 17 A 347 ALA TRP MET ASP VAL GLY HIS SER HIS LYS ILE ILE MET SEQRES 18 A 347 ARG GLU HIS LYS THR LYS TRP VAL GLN GLU SER SER SER SEQRES 19 A 347 LYS ASP PHE VAL CYS TYR LYS GLU GLY THR GLY PRO CYS SEQRES 20 A 347 SER GLU SER GLU GLU LYS THR CYS LYS THR SER GLY SER SEQRES 21 A 347 CYS ARG GLY ASP MET GLN PHE CYS LYS VAL ALA GLY CYS SEQRES 22 A 347 GLU HIS GLY GLU GLU ALA SER GLU ALA LYS CYS ARG CYS SEQRES 23 A 347 SER LEU VAL HIS LYS PRO GLY GLU VAL VAL VAL SER TYR SEQRES 24 A 347 GLY GLY MET ARG VAL ARG PRO LYS CYS TYR GLY PHE SER SEQRES 25 A 347 ARG MET MET ALA THR LEU GLU VAL ASN GLY LEU ASN ASP SEQRES 26 A 347 ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU ALA ALA SEQRES 27 A 347 ALA HIS HIS HIS HIS HIS HIS HIS HIS HET NAG D 1 14 HET NAG D 2 14 HET MAN D 3 11 HET NAG E 1 14 HET NAG E 2 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 4 NAG 4(C8 H15 N O6) FORMUL 4 MAN C6 H12 O6 FORMUL 6 HOH *355(H2 O) HELIX 1 AA1 THR C 28 HIS C 32 5 5 HELIX 2 AA2 GLU C 62 LYS C 65 5 4 HELIX 3 AA3 LYS C 74 SER C 76 5 3 HELIX 4 AA4 THR C 87 SER C 91 5 5 HELIX 5 AA5 SER C 165 SER C 167 5 3 HELIX 6 AA6 PRO C 209 SER C 212 5 4 HELIX 7 AA7 GLN B 79 LEU B 83 5 5 HELIX 8 AA8 SER B 121 SER B 127 1 7 HELIX 9 AA9 LYS B 183 ARG B 188 1 6 HELIX 10 AB1 GLY A 24 ARG A 34 1 11 HELIX 11 AB2 LEU A 35 SER A 46 1 12 HELIX 12 AB3 GLY A 57 VAL A 61 5 5 HELIX 13 AB4 SER A 69 TRP A 73 5 5 HELIX 14 AB5 SER A 78 LEU A 85 1 8 HELIX 15 AB6 SER A 141 SER A 144 5 4 HELIX 16 AB7 PRO A 149 ASN A 151 5 3 HELIX 17 AB8 PRO A 168 PHE A 183 1 16 HELIX 18 AB9 SER A 233 LYS A 235 5 3 HELIX 19 AC1 SER A 248 GLY A 259 1 12 HELIX 20 AC2 ASP A 264 GLY A 272 1 9 SHEET 1 AA1 4 GLN C 3 GLN C 6 0 SHEET 2 AA1 4 VAL C 18 SER C 25 -1 O LYS C 23 N GLN C 5 SHEET 3 AA1 4 THR C 78 LEU C 83 -1 O ILE C 81 N LEU C 20 SHEET 4 AA1 4 ALA C 68 ASP C 73 -1 N ASP C 73 O THR C 78 SHEET 1 AA2 6 GLU C 10 VAL C 12 0 SHEET 2 AA2 6 THR C 116 VAL C 120 1 O THR C 117 N GLU C 10 SHEET 3 AA2 6 ALA C 92 ASP C 102 -1 N ALA C 92 O LEU C 118 SHEET 4 AA2 6 MET C 34 GLN C 39 -1 N TYR C 35 O SER C 97 SHEET 5 AA2 6 PRO C 45 ILE C 51 -1 O GLU C 46 N LYS C 38 SHEET 6 AA2 6 THR C 58 PHE C 60 -1 O LYS C 59 N GLU C 50 SHEET 1 AA3 4 GLU C 10 VAL C 12 0 SHEET 2 AA3 4 THR C 116 VAL C 120 1 O THR C 117 N GLU C 10 SHEET 3 AA3 4 ALA C 92 ASP C 102 -1 N ALA C 92 O LEU C 118 SHEET 4 AA3 4 ALA C 107 TRP C 112 -1 O TYR C 111 N SER C 98 SHEET 1 AA4 4 SER C 129 PRO C 132 0 SHEET 2 AA4 4 MET C 144 TYR C 154 -1 O LEU C 150 N TYR C 131 SHEET 3 AA4 4 LEU C 183 PRO C 193 -1 O LEU C 186 N VAL C 151 SHEET 4 AA4 4 VAL C 172 GLN C 180 -1 N PHE C 175 O SER C 187 SHEET 1 AA5 3 THR C 160 TRP C 163 0 SHEET 2 AA5 3 THR C 203 HIS C 208 -1 O ASN C 205 N THR C 162 SHEET 3 AA5 3 THR C 213 LYS C 218 -1 O THR C 213 N HIS C 208 SHEET 1 AA6 4 MET B 4 THR B 7 0 SHEET 2 AA6 4 VAL B 19 ALA B 25 -1 O THR B 22 N THR B 7 SHEET 3 AA6 4 ASP B 70 ILE B 75 -1 O PHE B 73 N ILE B 21 SHEET 4 AA6 4 PHE B 62 TYR B 67 -1 N SER B 65 O THR B 72 SHEET 1 AA7 6 PHE B 10 VAL B 13 0 SHEET 2 AA7 6 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AA7 6 ALA B 84 GLN B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AA7 6 VAL B 33 GLN B 38 -1 N GLN B 38 O VAL B 85 SHEET 5 AA7 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA7 6 TYR B 53 ARG B 54 -1 O TYR B 53 N TYR B 49 SHEET 1 AA8 4 PHE B 10 VAL B 13 0 SHEET 2 AA8 4 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AA8 4 ALA B 84 GLN B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AA8 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AA9 4 THR B 114 PHE B 118 0 SHEET 2 AA9 4 GLY B 129 PHE B 139 -1 O PHE B 135 N SER B 116 SHEET 3 AA9 4 TYR B 173 THR B 182 -1 O MET B 175 N LEU B 136 SHEET 4 AA9 4 VAL B 159 TRP B 163 -1 N LEU B 160 O THR B 178 SHEET 1 AB1 4 SER B 153 ARG B 155 0 SHEET 2 AB1 4 ILE B 144 ILE B 150 -1 N ILE B 150 O SER B 153 SHEET 3 AB1 4 SER B 191 HIS B 198 -1 O THR B 197 N ASN B 145 SHEET 4 AB1 4 ILE B 205 ASN B 210 -1 O ILE B 205 N ALA B 196 SHEET 1 AB2 2 TYR A 51 VAL A 52 0 SHEET 2 AB2 2 LEU A 147 LEU A 148 1 O LEU A 148 N TYR A 51 SHEET 1 AB3 5 SER A 62 TYR A 64 0 SHEET 2 AB3 5 VAL A 153 ILE A 156 1 O TRP A 155 N SER A 62 SHEET 3 AB3 5 PHE A 110 PRO A 114 1 N GLU A 112 O ILE A 156 SHEET 4 AB3 5 TYR A 119 GLY A 123 -1 O TRP A 122 N PHE A 111 SHEET 5 AB3 5 VAL A 90 LYS A 92 1 N LYS A 91 O TYR A 119 SHEET 1 AB4 2 LYS A 128 ARG A 130 0 SHEET 2 AB4 2 CYS A 137 SER A 139 -1 O SER A 138 N SER A 129 SHEET 1 AB5 4 ASP A 158 CYS A 161 0 SHEET 2 AB5 4 CYS A 308 LEU A 318 -1 O TYR A 309 N ALA A 160 SHEET 3 AB5 4 ILE A 186 ILE A 189 -1 N LYS A 188 O THR A 317 SHEET 4 AB5 4 ILE A 192 VAL A 193 -1 O ILE A 192 N ILE A 189 SHEET 1 AB6 4 ASP A 158 CYS A 161 0 SHEET 2 AB6 4 CYS A 308 LEU A 318 -1 O TYR A 309 N ALA A 160 SHEET 3 AB6 4 GLN A 204 ASP A 212 -1 N GLN A 204 O ALA A 316 SHEET 4 AB6 4 ILE A 219 MET A 221 -1 O ILE A 219 N MET A 211 SHEET 1 AB7 3 LYS A 225 VAL A 229 0 SHEET 2 AB7 3 GLU A 294 TYR A 299 -1 O SER A 298 N LYS A 225 SHEET 3 AB7 3 MET A 302 VAL A 304 -1 O VAL A 304 N VAL A 297 SHEET 1 AB8 3 PHE A 237 TYR A 240 0 SHEET 2 AB8 3 ARG A 285 LEU A 288 -1 O SER A 287 N VAL A 238 SHEET 3 AB8 3 ARG A 262 GLY A 263 1 N ARG A 262 O CYS A 286 SSBOND 1 CYS C 22 CYS C 96 1555 1555 2.06 SSBOND 2 CYS C 149 CYS C 204 1555 1555 2.05 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.08 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.04 SSBOND 5 CYS A 7 CYS A 30 1555 1555 2.05 SSBOND 6 CYS A 124 CYS A 137 1555 1555 2.11 SSBOND 7 CYS A 161 CYS A 308 1555 1555 2.08 SSBOND 8 CYS A 187 CYS A 197 1555 1555 2.04 SSBOND 9 CYS A 239 CYS A 286 1555 1555 2.04 SSBOND 10 CYS A 247 CYS A 284 1555 1555 2.04 SSBOND 11 CYS A 255 CYS A 261 1555 1555 2.04 SSBOND 12 CYS A 268 CYS A 273 1555 1555 2.04 LINK ND2 ASN A 14 C1 NAG E 1 1555 1555 1.46 LINK ND2 ASN A 44 C1 NAG D 1 1555 1555 1.42 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG D 2 C1 MAN D 3 1555 1555 1.45 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.46 CISPEP 1 PHE C 155 PRO C 156 0 -7.88 CISPEP 2 GLU C 157 PRO C 158 0 5.88 CISPEP 3 THR B 7 PRO B 8 0 -2.59 CISPEP 4 SER B 94 PRO B 95 0 -2.94 CISPEP 5 TYR B 140 PRO B 141 0 -0.93 CISPEP 6 TYR A 64 PRO A 65 0 -0.32 CRYST1 195.753 65.906 73.738 90.00 105.38 90.00 C 1 2 1 4 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 0.005108 0.000000 0.001405 0.00000 SCALE2 0.000000 0.015173 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014065 0.00000