HEADER VIRAL PROTEIN 15-AUG-24 9GHJ TITLE JUNIN VIRUS GP1-GP2 HETERODIMER IN COMPLEX WITH FAB OF JUN1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PRE-GLYCOPROTEIN POLYPROTEIN GP COMPLEX; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PRE-GP-C; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GLYCOPROTEIN G2; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: GP2; COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: JUN1 HEAVY CHAIN; COMPND 15 CHAIN: H; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: JUN1 LIGHT CHAIN; COMPND 19 CHAIN: L; COMPND 20 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MAMMARENAVIRUS JUNINENSE; SOURCE 3 ORGANISM_TAXID: 2169991; SOURCE 4 GENE: GPC; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7106; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MAMMARENAVIRUS JUNINENSE; SOURCE 9 ORGANISM_TAXID: 2169991; SOURCE 10 GENE: GPC, GP-C; SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7106; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_TAXID: 10090; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 20 ORGANISM_TAXID: 10090; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS JUNIN VIRUS GLYCOPROTEIN PREFUSION FAB, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.A.BOWDEN,G.C.PAESEN REVDAT 1 11-JUN-25 9GHJ 0 JRNL AUTH G.C.PAESEN,W.M.NG,G.SUTTON,K.J.DOORES,T.A.BOWDEN JRNL TITL STRUCTURE AND STABILIZATION OF THE ANTIGENIC GLYCOPROTEIN JRNL TITL 2 BUILDING BLOCKS OF THE NEW WORLD MAMMARENAVIRUS SPIKE JRNL TITL 3 COMPLEX. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.09 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.1_5286 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) : 2.09 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 79.81 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 3 NUMBER OF REFLECTIONS : 75110 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.214 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 3680 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 79.8100 - 6.1900 1.00 2873 161 0.2034 0.2481 REMARK 3 2 6.1900 - 4.9100 1.00 2835 138 0.1775 0.2104 REMARK 3 3 4.9100 - 4.2900 1.00 2799 151 0.1458 0.1823 REMARK 3 4 4.2900 - 3.9000 1.00 2811 140 0.1617 0.1882 REMARK 3 5 3.9000 - 3.6200 1.00 2782 147 0.1821 0.2142 REMARK 3 6 3.6200 - 3.4100 1.00 2796 129 0.1989 0.1980 REMARK 3 7 3.4100 - 3.2400 1.00 2798 152 0.2031 0.2163 REMARK 3 8 3.2400 - 3.1000 1.00 2767 133 0.2183 0.2722 REMARK 3 9 3.1000 - 2.9800 1.00 2772 148 0.2294 0.2964 REMARK 3 10 2.9800 - 2.8700 1.00 2756 157 0.2452 0.2868 REMARK 3 11 2.8700 - 2.7800 1.00 2782 142 0.2203 0.2660 REMARK 3 12 2.7800 - 2.7000 1.00 2782 141 0.2093 0.2636 REMARK 3 13 2.7000 - 2.6300 1.00 2786 122 0.2154 0.2713 REMARK 3 14 2.6300 - 2.5700 1.00 2752 135 0.2298 0.2282 REMARK 3 15 2.5700 - 2.5100 1.00 2752 157 0.2468 0.2910 REMARK 3 16 2.5100 - 2.4600 1.00 2796 148 0.2669 0.3233 REMARK 3 17 2.4600 - 2.4100 1.00 2740 160 0.2898 0.3396 REMARK 3 18 2.4100 - 2.3600 1.00 2769 133 0.3149 0.3488 REMARK 3 19 2.3600 - 2.3200 1.00 2732 143 0.3065 0.3281 REMARK 3 20 2.3200 - 2.2800 1.00 2790 135 0.3138 0.3581 REMARK 3 21 2.2800 - 2.2400 0.98 2709 141 0.3109 0.3549 REMARK 3 22 2.2400 - 2.2100 0.96 2665 146 0.3289 0.3521 REMARK 3 23 2.2100 - 2.1800 0.96 2651 121 0.3466 0.3587 REMARK 3 24 2.1800 - 2.1500 0.95 2634 124 0.3544 0.3238 REMARK 3 25 2.1500 - 2.1200 0.94 2579 133 0.3743 0.4274 REMARK 3 26 2.1200 - 2.0900 0.90 2522 143 0.3982 0.3934 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) : 0.343 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.571 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 44.72 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.98 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 : 0.002 6335 REMARK 3 ANGLE : 0.555 8599 REMARK 3 CHIRALITY : 0.042 996 REMARK 3 PLANARITY : 0.004 1062 REMARK 3 DIHEDRAL : 12.426 2476 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 9GHJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1292140928. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-JAN-22 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 : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76048 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090 REMARK 200 RESOLUTION RANGE LOW (A) : 112.300 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% V/V 2-PROPANOL, 0.1 M TRIS PH 8.0, REMARK 280 5% W/V PEG 8,000, 6% 2-METHYL-2,4-PENTANEDIOL, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293.65K 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 112.89450 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.98700 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 112.89450 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.98700 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, 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 GLU A 59 REMARK 465 LYS A 241 REMARK 465 ASN A 242 REMARK 465 ILE A 243 REMARK 465 GLN A 244 REMARK 465 LEU A 245 REMARK 465 PRO A 246 REMARK 465 ARG A 247 REMARK 465 ARG A 248 REMARK 465 ARG A 249 REMARK 465 ARG A 250 REMARK 465 ARG A 251 REMARK 465 ALA B 252 REMARK 465 SER B 261 REMARK 465 SER B 262 REMARK 465 GLY B 263 REMARK 465 LYS B 264 REMARK 465 ASP B 265 REMARK 465 THR B 266 REMARK 465 PRO B 267 REMARK 465 GLY B 268 REMARK 465 ASN B 319 REMARK 465 ASP B 320 REMARK 465 PRO B 321 REMARK 465 THR B 322 REMARK 465 LYS B 323 REMARK 465 LYS B 324 REMARK 465 GLN B 325 REMARK 465 TYR B 411 REMARK 465 SER B 412 REMARK 465 ASP B 413 REMARK 465 ARG B 414 REMARK 465 GLN B 415 REMARK 465 GLY B 416 REMARK 465 SER B 417 REMARK 465 GLY B 418 REMARK 465 ASP B 419 REMARK 465 ASP B 420 REMARK 465 ASP B 421 REMARK 465 ASP B 422 REMARK 465 LYS B 423 REMARK 465 GLY B 424 REMARK 465 SER B 425 REMARK 465 GLY B 426 REMARK 465 TRP B 427 REMARK 465 SER B 428 REMARK 465 HIS B 429 REMARK 465 PRO B 430 REMARK 465 GLN B 431 REMARK 465 PHE B 432 REMARK 465 GLU B 433 REMARK 465 LYS B 434 REMARK 465 GLY B 435 REMARK 465 GLY B 436 REMARK 465 GLY B 437 REMARK 465 SER B 438 REMARK 465 GLY B 439 REMARK 465 GLY B 440 REMARK 465 GLY B 441 REMARK 465 SER B 442 REMARK 465 GLY B 443 REMARK 465 GLY B 444 REMARK 465 SER B 445 REMARK 465 ALA B 446 REMARK 465 TRP B 447 REMARK 465 SER B 448 REMARK 465 HIS B 449 REMARK 465 PRO B 450 REMARK 465 GLN B 451 REMARK 465 PHE B 452 REMARK 465 GLU B 453 REMARK 465 LYS B 454 REMARK 465 GLU H -5 REMARK 465 THR H -4 REMARK 465 SER H 128 REMARK 465 ALA H 129 REMARK 465 ALA H 130 REMARK 465 GLN H 131 REMARK 465 THR H 132 REMARK 465 ASN H 133 REMARK 465 ASP H 214 REMARK 465 CYS H 215 REMARK 465 GLY H 216 REMARK 465 THR H 217 REMARK 465 LYS H 218 REMARK 465 HIS H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 GLU L -2 REMARK 465 THR L -1 REMARK 465 ASN L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 A 61 146.16 -174.69 REMARK 500 ASN A 95 -168.14 -165.96 REMARK 500 PHE A 162 -167.37 -111.29 REMARK 500 THR B 359 -61.05 -124.34 REMARK 500 TYR H 100D 43.34 -95.37 REMARK 500 ALA L 51 -37.21 79.49 REMARK 500 ASN L 190 -50.84 -130.60 REMARK 500 REMARK 500 REMARK: NULL DBREF 9GHJ A 59 251 UNP C1K9J9 C1K9J9_JUNIN 59 251 DBREF 9GHJ B 252 416 UNP P26313 GLYC_JUNIN 252 416 DBREF 9GHJ H -5 224 PDB 9GHJ 9GHJ -5 224 DBREF 9GHJ L -2 214 PDB 9GHJ 9GHJ -2 214 SEQADV 9GHJ CYS A 88 UNP C1K9J9 LEU 88 ENGINEERED MUTATION SEQADV 9GHJ ARG A 249 UNP C1K9J9 SER 249 ENGINEERED MUTATION SEQADV 9GHJ ARG A 250 UNP C1K9J9 LEU 250 ENGINEERED MUTATION SEQADV 9GHJ ARG A 251 UNP C1K9J9 LYS 251 ENGINEERED MUTATION SEQADV 9GHJ PRO B 321 UNP P26313 GLU 321 ENGINEERED MUTATION SEQADV 9GHJ CYS B 329 UNP P26313 MET 329 ENGINEERED MUTATION SEQADV 9GHJ SER B 417 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 418 UNP P26313 EXPRESSION TAG SEQADV 9GHJ ASP B 419 UNP P26313 EXPRESSION TAG SEQADV 9GHJ ASP B 420 UNP P26313 EXPRESSION TAG SEQADV 9GHJ ASP B 421 UNP P26313 EXPRESSION TAG SEQADV 9GHJ ASP B 422 UNP P26313 EXPRESSION TAG SEQADV 9GHJ LYS B 423 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 424 UNP P26313 EXPRESSION TAG SEQADV 9GHJ SER B 425 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 426 UNP P26313 EXPRESSION TAG SEQADV 9GHJ TRP B 427 UNP P26313 EXPRESSION TAG SEQADV 9GHJ SER B 428 UNP P26313 EXPRESSION TAG SEQADV 9GHJ HIS B 429 UNP P26313 EXPRESSION TAG SEQADV 9GHJ PRO B 430 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLN B 431 UNP P26313 EXPRESSION TAG SEQADV 9GHJ PHE B 432 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLU B 433 UNP P26313 EXPRESSION TAG SEQADV 9GHJ LYS B 434 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 435 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 436 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 437 UNP P26313 EXPRESSION TAG SEQADV 9GHJ SER B 438 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 439 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 440 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 441 UNP P26313 EXPRESSION TAG SEQADV 9GHJ SER B 442 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 443 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLY B 444 UNP P26313 EXPRESSION TAG SEQADV 9GHJ SER B 445 UNP P26313 EXPRESSION TAG SEQADV 9GHJ ALA B 446 UNP P26313 EXPRESSION TAG SEQADV 9GHJ TRP B 447 UNP P26313 EXPRESSION TAG SEQADV 9GHJ SER B 448 UNP P26313 EXPRESSION TAG SEQADV 9GHJ HIS B 449 UNP P26313 EXPRESSION TAG SEQADV 9GHJ PRO B 450 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLN B 451 UNP P26313 EXPRESSION TAG SEQADV 9GHJ PHE B 452 UNP P26313 EXPRESSION TAG SEQADV 9GHJ GLU B 453 UNP P26313 EXPRESSION TAG SEQADV 9GHJ LYS B 454 UNP P26313 EXPRESSION TAG SEQRES 1 A 193 GLU GLU ALA PHE LYS ILE GLY LEU HIS THR GLU PHE GLN SEQRES 2 A 193 THR VAL SER PHE SER MET VAL GLY LEU PHE SER ASN ASN SEQRES 3 A 193 PRO HIS ASP CYS PRO LEU LEU CYS THR LEU ASN LYS SER SEQRES 4 A 193 HIS LEU TYR ILE LYS GLY GLY ASN ALA SER PHE GLN ILE SEQRES 5 A 193 SER PHE ASP ASP ILE ALA VAL LEU LEU PRO GLN TYR ASP SEQRES 6 A 193 VAL ILE ILE GLN HIS PRO ALA ASP MET SER TRP CYS SER SEQRES 7 A 193 LYS SER ASP ASP GLN ILE TRP LEU SER GLN TRP PHE MET SEQRES 8 A 193 ASN ALA VAL GLY HIS ASP TRP HIS LEU ASP PRO PRO PHE SEQRES 9 A 193 LEU CYS ARG ASN ARG THR LYS THR GLU GLY PHE ILE PHE SEQRES 10 A 193 GLN VAL ASN THR SER LYS THR GLY VAL ASN GLU ASN TYR SEQRES 11 A 193 ALA LYS LYS PHE LYS THR GLY MET HIS HIS LEU TYR ARG SEQRES 12 A 193 GLU TYR PRO ASP SER CYS LEU ASN GLY LYS LEU CYS LEU SEQRES 13 A 193 MET LYS ALA GLN PRO THR SER TRP PRO LEU GLN CYS PRO SEQRES 14 A 193 LEU ASP HIS VAL ASN THR LEU HIS PHE LEU THR ARG GLY SEQRES 15 A 193 LYS ASN ILE GLN LEU PRO ARG ARG ARG ARG ARG SEQRES 1 B 203 ALA PHE PHE SER TRP SER LEU THR ASP SER SER GLY LYS SEQRES 2 B 203 ASP THR PRO GLY GLY TYR CYS LEU GLU GLU TRP MET LEU SEQRES 3 B 203 VAL ALA ALA LYS MET LYS CYS PHE GLY ASN THR ALA VAL SEQRES 4 B 203 ALA LYS CYS ASN LEU ASN HIS ASP SER GLU PHE CYS ASP SEQRES 5 B 203 MET LEU ARG LEU PHE ASP TYR ASN LYS ASN ALA ILE LYS SEQRES 6 B 203 THR LEU ASN ASP PRO THR LYS LYS GLN VAL ASN LEU CYS SEQRES 7 B 203 GLY GLN THR ILE ASN ALA LEU ILE SER ASP ASN LEU LEU SEQRES 8 B 203 MET LYS ASN LYS ILE ARG GLU LEU MET SER VAL PRO TYR SEQRES 9 B 203 CYS ASN TYR THR LYS PHE TRP TYR VAL ASN HIS THR LEU SEQRES 10 B 203 SER GLY GLN HIS SER LEU PRO ARG CYS TRP LEU ILE LYS SEQRES 11 B 203 ASN ASN SER TYR LEU ASN ILE SER ASP PHE ARG ASN ASP SEQRES 12 B 203 TRP ILE LEU GLU SER ASP PHE LEU ILE SER GLU MET LEU SEQRES 13 B 203 SER LYS GLU TYR SER ASP ARG GLN GLY SER GLY ASP ASP SEQRES 14 B 203 ASP ASP LYS GLY SER GLY TRP SER HIS PRO GLN PHE GLU SEQRES 15 B 203 LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SER ALA SEQRES 16 B 203 TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 H 242 GLU THR GLY GLN ILE GLN LEU VAL GLN SER VAL GLU THR SEQRES 2 H 242 GLY GLY GLY LEU VAL ARG PRO GLY ASN SER LEU LYS LEU SEQRES 3 H 242 SER CYS VAL THR SER GLY PHE THR PHE SER ASN TYR GLN SEQRES 4 H 242 MET HIS TRP LEU ARG GLN PRO PRO GLY LYS ARG LEU GLU SEQRES 5 H 242 TRP ILE ALA VAL ILE THR VAL LYS SER ASP ASN TYR GLY SEQRES 6 H 242 ALA ASN TYR VAL GLU SER VAL LYS GLY ARG PHE ALA ILE SEQRES 7 H 242 SER ARG ASP ASP SER LYS SER SER VAL TYR LEU GLU MET SEQRES 8 H 242 ASN ARG LEU ARG GLU GLU ASP THR ALA THR TYR PHE CYS SEQRES 9 H 242 SER ARG SER GLY ILE TYR ASP GLY TYR TYR ALA TYR ALA SEQRES 10 H 242 MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SEQRES 11 H 242 SER ALA THR THR LYS GLY PRO SER VAL TYR PRO LEU ALA SEQRES 12 H 242 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 13 H 242 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 14 H 242 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 15 H 242 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 16 H 242 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 17 H 242 GLN THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 18 H 242 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY SEQRES 19 H 242 THR LYS HIS HIS HIS HIS HIS HIS SEQRES 1 L 217 GLU THR GLY SER VAL VAL MET THR GLN SER GLN LYS PHE SEQRES 2 L 217 MET SER THR SER VAL GLY ASP ARG VAL SER ILE THR CYS SEQRES 3 L 217 LYS ALA SER GLN ILE VAL GLY THR SER VAL ALA TRP TYR SEQRES 4 L 217 GLN GLN LYS ALA GLY GLN SER PRO LYS LEU LEU ILE TYR SEQRES 5 L 217 TRP ALA SER THR ARG HIS THR GLY VAL PRO ASP ARG PHE SEQRES 6 L 217 THR ALA GLY GLY SER GLY THR ASP PHE THR LEU THR ILE SEQRES 7 L 217 THR ASN VAL GLN SER GLU ASP LEU ALA ASP TYR PHE CYS SEQRES 8 L 217 GLN GLN TYR ALA THR TYR PRO LEU THR PHE GLY SER GLY SEQRES 9 L 217 THR LYS LEU GLU LEU LYS ARG THR ASP ALA ALA PRO THR SEQRES 10 L 217 VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SER SEQRES 11 L 217 GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR SEQRES 12 L 217 PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER SEQRES 13 L 217 GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN SEQRES 14 L 217 ASP SER LYS ASP SER THR TYR SER MET SER SER THR LEU SEQRES 15 L 217 THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR SEQRES 16 L 217 THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO ILE SEQRES 17 L 217 VAL LYS SER PHE ASN ARG ASN GLU CYS HET NAG C 1 25 HET NAG C 2 26 HET BMA C 3 21 HET FUC C 4 20 HET NAG D 1 14 HET NAG D 2 14 HET FUC D 3 10 HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET MAN E 4 11 HET NAG F 1 26 HET NAG F 2 27 HET NAG G 1 26 HET NAG G 2 27 HET PGE A 301 24 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM PGE TRIETHYLENE GLYCOL 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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 NAG 10(C8 H15 N O6) FORMUL 5 BMA 2(C6 H12 O6) FORMUL 5 FUC 2(C6 H12 O5) FORMUL 7 MAN C6 H12 O6 FORMUL 10 PGE C6 H14 O4 FORMUL 11 HOH *178(H2 O) HELIX 1 AA1 SER A 76 ASN A 83 1 8 HELIX 2 AA2 HIS A 128 CYS A 135 5 8 HELIX 3 AA3 SER A 138 GLY A 153 1 16 HELIX 4 AA4 THR A 182 VAL A 184 5 3 HELIX 5 AA5 ASN A 185 TYR A 200 1 16 HELIX 6 AA6 ASP A 229 GLY A 240 1 12 HELIX 7 AA7 GLU B 273 LEU B 277 5 5 HELIX 8 AA8 GLY B 286 ALA B 291 1 6 HELIX 9 AA9 LYS B 292 ASN B 294 5 3 HELIX 10 AB1 SER B 299 LEU B 318 1 20 HELIX 11 AB2 THR B 332 ILE B 337 1 6 HELIX 12 AB3 SER B 338 MET B 351 1 14 HELIX 13 AB4 ILE B 388 ASP B 390 5 3 HELIX 14 AB5 PHE B 391 GLU B 410 1 20 HELIX 15 AB6 THR H 28 TYR H 32 5 5 HELIX 16 AB7 VAL H 52A ASN H 54 5 5 HELIX 17 AB8 GLU H 61 LYS H 64 5 4 HELIX 18 AB9 ASP H 72A LYS H 72C 5 3 HELIX 19 AC1 ARG H 83 THR H 87 5 5 HELIX 20 AC2 SER H 156 SER H 158 5 3 HELIX 21 AC3 LEU H 159 SER H 161 5 3 HELIX 22 AC4 GLN L 79 LEU L 83 5 5 HELIX 23 AC5 SER L 121 GLY L 128 1 8 HELIX 24 AC6 LYS L 183 HIS L 189 1 7 SHEET 1 AA1 4 ALA A 61 LYS A 63 0 SHEET 2 AA1 4 GLU A 69 SER A 74 -1 O PHE A 70 N PHE A 62 SHEET 3 AA1 4 LYS B 360 ASN B 365 -1 O TYR B 363 N GLN A 71 SHEET 4 AA1 4 ARG B 376 CYS B 377 -1 O ARG B 376 N TRP B 362 SHEET 1 AA2 7 LEU A 90 THR A 93 0 SHEET 2 AA2 7 HIS A 98 GLY A 103 -1 O LYS A 102 N LEU A 90 SHEET 3 AA2 7 ALA A 106 ASP A 113 -1 O PHE A 108 N ILE A 101 SHEET 4 AA2 7 LEU A 214 PRO A 219 -1 O GLN A 218 N GLN A 109 SHEET 5 AA2 7 PHE A 175 ASN A 178 -1 N VAL A 177 O MET A 215 SHEET 6 AA2 7 PHE A 162 CYS A 164 -1 N LEU A 163 O GLN A 176 SHEET 7 AA2 7 VAL A 124 ILE A 126 -1 N ILE A 126 O PHE A 162 SHEET 1 AA3 2 TYR B 270 LEU B 272 0 SHEET 2 AA3 2 LYS B 283 PHE B 285 -1 O LYS B 283 N LEU B 272 SHEET 1 AA4 2 ILE B 380 LYS B 381 0 SHEET 2 AA4 2 SER B 384 TYR B 385 -1 O SER B 384 N LYS B 381 SHEET 1 AA5 4 GLN H 0 VAL H 5 0 SHEET 2 AA5 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 4 SHEET 3 AA5 4 SER H 74 MET H 79 -1 O MET H 79 N LEU H 18 SHEET 4 AA5 4 PHE H 67 ASP H 72 -1 N ALA H 68 O GLU H 78 SHEET 1 AA6 6 LEU H 11 VAL H 12 0 SHEET 2 AA6 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA6 6 ALA H 88 TYR H 98 -1 N TYR H 90 O THR H 107 SHEET 4 AA6 6 GLN H 33 GLN H 39 -1 N LEU H 37 O PHE H 91 SHEET 5 AA6 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA6 6 ALA H 57 TYR H 59 -1 O ASN H 58 N VAL H 50 SHEET 1 AA7 4 LEU H 11 VAL H 12 0 SHEET 2 AA7 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA7 4 ALA H 88 TYR H 98 -1 N TYR H 90 O THR H 107 SHEET 4 AA7 4 TYR H 100A TRP H 103 -1 O TYR H 100A N TYR H 98 SHEET 1 AA8 4 SER H 120 LEU H 124 0 SHEET 2 AA8 4 MET H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA8 4 LEU H 174 PRO H 184 -1 O TYR H 175 N TYR H 145 SHEET 4 AA8 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180 SHEET 1 AA9 4 SER H 120 LEU H 124 0 SHEET 2 AA9 4 MET H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA9 4 LEU H 174 PRO H 184 -1 O TYR H 175 N TYR H 145 SHEET 4 AA9 4 VAL H 169 GLN H 171 -1 N GLN H 171 O LEU H 174 SHEET 1 AB1 3 THR H 151 TRP H 154 0 SHEET 2 AB1 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153 SHEET 3 AB1 3 THR H 204 LYS H 209 -1 O VAL H 206 N VAL H 197 SHEET 1 AB2 4 MET L 4 THR L 5 0 SHEET 2 AB2 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AB2 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB2 4 PHE L 62 SER L 67 -1 N GLY L 65 O THR L 72 SHEET 1 AB3 6 PHE L 10 THR L 13 0 SHEET 2 AB3 6 THR L 102 LEU L 106 1 O GLU L 105 N MET L 11 SHEET 3 AB3 6 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB3 6 VAL L 33 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AB3 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB3 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AB4 4 PHE L 10 THR L 13 0 SHEET 2 AB4 4 THR L 102 LEU L 106 1 O GLU L 105 N MET L 11 SHEET 3 AB4 4 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB4 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB5 4 THR L 114 PHE L 118 0 SHEET 2 AB5 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB5 4 TYR L 173 THR L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AB5 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 AB6 4 SER L 153 ARG L 155 0 SHEET 2 AB6 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 AB6 4 TYR L 192 THR L 197 -1 O GLU L 195 N LYS L 147 SHEET 4 AB6 4 ILE L 205 PHE L 209 -1 O PHE L 209 N TYR L 192 SSBOND 1 CYS A 88 CYS B 329 1555 1555 2.03 SSBOND 2 CYS A 92 CYS A 226 1555 1555 2.03 SSBOND 3 CYS A 135 CYS A 164 1555 1555 2.02 SSBOND 4 CYS A 207 CYS A 213 1555 1555 2.04 SSBOND 5 CYS B 271 CYS B 284 1555 1555 2.04 SSBOND 6 CYS B 293 CYS B 302 1555 1555 2.03 SSBOND 7 CYS B 356 CYS B 377 1555 1555 2.03 SSBOND 8 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 9 CYS H 140 CYS H 195 1555 1555 2.04 SSBOND 10 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 11 CYS L 134 CYS L 194 1555 1555 2.03 LINK ND2 ASN A 95 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN A 166 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 178 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN B 357 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN B 365 C1 NAG G 1 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45 LINK O6 NAG C 1 C1 FUC C 4 1555 1555 1.44 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44 LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 CISPEP 1 PHE H 146 PRO H 147 0 -4.77 CISPEP 2 GLU H 148 PRO H 149 0 3.59 CISPEP 3 TRP H 188 PRO H 189 0 2.95 CISPEP 4 TYR L 94 PRO L 95 0 -4.08 CISPEP 5 TYR L 140 PRO L 141 0 0.47 CRYST1 225.789 71.974 80.231 90.00 95.90 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 0.004429 0.000000 0.000457 0.00000 SCALE2 0.000000 0.013894 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012530 0.00000