HEADER VIRAL PROTEIN 15-AUG-24 9GHI TITLE MACHUPO VIRUS GP1-GP2 HETERODIMER IN COMPLEX WITH FAB OF MAC1 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: MAC1 HEAVY CHAIN; COMPND 15 CHAIN: H; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: MAC1 LIGHT CHAIN; COMPND 19 CHAIN: L; COMPND 20 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MAMMARENAVIRUS MACHUPOENSE; SOURCE 3 ORGANISM_TAXID: 3052317; 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 MACHUPOENSE; SOURCE 9 ORGANISM_TAXID: 3052317; 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 MACHUPO VIRUS GLYCOPROTEIN PREFUSION FAB, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.A.BOWDEN,G.C.PAESEN REVDAT 1 11-JUN-25 9GHI 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. 2.41 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) : 2.41 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.25 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 48641 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.232 REMARK 3 R VALUE (WORKING SET) : 0.230 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030 REMARK 3 FREE R VALUE TEST SET COUNT : 2449 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 47.2500 - 6.1900 1.00 2814 147 0.2024 0.2074 REMARK 3 2 6.1900 - 4.9200 1.00 2793 115 0.1857 0.2536 REMARK 3 3 4.9200 - 4.2900 1.00 2719 149 0.1601 0.1824 REMARK 3 4 4.2900 - 3.9000 1.00 2730 140 0.1828 0.2286 REMARK 3 5 3.9000 - 3.6200 1.00 2717 146 0.2174 0.2382 REMARK 3 6 3.6200 - 3.4100 1.00 2758 145 0.2493 0.2966 REMARK 3 7 3.4100 - 3.2400 1.00 2716 141 0.2616 0.2944 REMARK 3 8 3.2400 - 3.1000 1.00 2704 130 0.2547 0.3192 REMARK 3 9 3.1000 - 2.9800 1.00 2727 142 0.2643 0.3251 REMARK 3 10 2.9800 - 2.8800 1.00 2712 151 0.2920 0.3317 REMARK 3 11 2.8800 - 2.7900 1.00 2706 129 0.3210 0.4073 REMARK 3 12 2.7900 - 2.7100 1.00 2679 164 0.3306 0.3714 REMARK 3 13 2.7100 - 2.6300 1.00 2669 139 0.3106 0.2981 REMARK 3 14 2.6300 - 2.5700 1.00 2726 131 0.3094 0.3656 REMARK 3 15 2.5700 - 2.5100 1.00 2705 167 0.3386 0.3327 REMARK 3 16 2.5100 - 2.4600 1.00 2628 166 0.3497 0.3865 REMARK 3 17 2.4600 - 2.4100 0.98 2689 147 0.3618 0.3836 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) : 0.423 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.631 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 53.84 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.74 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 : 0.003 6452 REMARK 3 ANGLE : 0.533 8749 REMARK 3 CHIRALITY : 0.043 1012 REMARK 3 PLANARITY : 0.004 1089 REMARK 3 DIHEDRAL : 15.170 2568 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 5.9837 15.7275 37.6184 REMARK 3 T TENSOR REMARK 3 T11: 0.5859 T22: 0.3329 REMARK 3 T33: 0.4937 T12: -0.0014 REMARK 3 T13: 0.0270 T23: 0.0171 REMARK 3 L TENSOR REMARK 3 L11: 0.2672 L22: 0.2462 REMARK 3 L33: 2.6257 L12: -0.0469 REMARK 3 L13: -0.3000 L23: 0.3683 REMARK 3 S TENSOR REMARK 3 S11: -0.0596 S12: -0.0443 S13: 0.0067 REMARK 3 S21: 0.3246 S22: 0.0473 S23: -0.0147 REMARK 3 S31: 0.1813 S32: -0.0346 S33: 0.0075 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 9GHI 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_1292140982. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-NOV-21 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 : I04-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9179 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48718 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.410 REMARK 200 RESOLUTION RANGE LOW (A) : 184.930 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45 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: 90 MM LI2SO4, 90 MM NA2SO4, 90 MM REMARK 280 K2SO4 12.5 % W/V PEG 4000, 20% W/V 1,2,6-HEXANETRIOL 0.1 M GLY- REMARK 280 GLY/AMPD PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293.65K 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 36.79250 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: 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 ASP A 59 REMARK 465 LYS A 252 REMARK 465 THR A 253 REMARK 465 HIS A 254 REMARK 465 LEU A 255 REMARK 465 ASN A 256 REMARK 465 PHE A 257 REMARK 465 SER A 258 REMARK 465 ARG A 259 REMARK 465 ARG A 260 REMARK 465 LYS A 261 REMARK 465 ARG A 262 REMARK 465 SER B 263 REMARK 465 PHE B 264 REMARK 465 ASP B 271 REMARK 465 SER B 272 REMARK 465 SER B 273 REMARK 465 GLY B 274 REMARK 465 LYS B 275 REMARK 465 ASP B 276 REMARK 465 MET B 277 REMARK 465 PRO B 278 REMARK 465 GLY B 279 REMARK 465 GLY B 280 REMARK 465 ILE B 326 REMARK 465 LYS B 327 REMARK 465 THR B 328 REMARK 465 LEU B 329 REMARK 465 ASN B 330 REMARK 465 ASP B 331 REMARK 465 PRO B 332 REMARK 465 SER B 333 REMARK 465 LYS B 334 REMARK 465 LYS B 335 REMARK 465 LYS B 428 REMARK 465 SER B 429 REMARK 465 GLY B 430 REMARK 465 ASP B 431 REMARK 465 ASP B 432 REMARK 465 ASP B 433 REMARK 465 ASP B 434 REMARK 465 LYS B 435 REMARK 465 GLY B 436 REMARK 465 SER B 437 REMARK 465 GLY B 438 REMARK 465 TRP B 439 REMARK 465 SER B 440 REMARK 465 HIS B 441 REMARK 465 PRO B 442 REMARK 465 GLN B 443 REMARK 465 PHE B 444 REMARK 465 GLU B 445 REMARK 465 LYS B 446 REMARK 465 GLY B 447 REMARK 465 GLY B 448 REMARK 465 GLY B 449 REMARK 465 SER B 450 REMARK 465 GLY B 451 REMARK 465 GLY B 452 REMARK 465 GLY B 453 REMARK 465 SER B 454 REMARK 465 GLY B 455 REMARK 465 GLY B 456 REMARK 465 SER B 457 REMARK 465 ALA B 458 REMARK 465 TRP B 459 REMARK 465 SER B 460 REMARK 465 HIS B 461 REMARK 465 PRO B 462 REMARK 465 GLN B 463 REMARK 465 PHE B 464 REMARK 465 GLU B 465 REMARK 465 LYS B 466 REMARK 465 GLU H -2 REMARK 465 THR H -1 REMARK 465 GLY H 0 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 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 ND2 ASN A 86 O GLY A 103 2.19 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 ILE A 64 -62.09 -90.44 REMARK 500 LEU A 94 -80.02 -106.98 REMARK 500 ASN A 95 -168.57 -77.95 REMARK 500 SER A 97 -14.27 -143.68 REMARK 500 ASN A 174 107.75 -166.20 REMARK 500 ALA A 182 143.70 179.29 REMARK 500 ASP A 183 -140.45 61.66 REMARK 500 PHE A 226 -135.14 50.58 REMARK 500 THR B 370 -71.14 -129.72 REMARK 500 ALA H 88 -171.74 -174.44 REMARK 500 THR H 99 84.47 -161.44 REMARK 500 THR H 132 72.40 -107.80 REMARK 500 THR L 51 -57.68 75.75 REMARK 500 PHE L 67 139.14 -175.03 REMARK 500 ALA L 84 -172.49 -170.96 REMARK 500 ASN L 138 60.65 60.09 REMARK 500 ASN L 190 -53.74 -122.93 REMARK 500 REMARK 500 REMARK: NULL DBREF 9GHI A 59 262 UNP Q8AZ57 Q8AZ57_MACHU 59 262 DBREF 9GHI B 263 428 UNP Q6IUF7 GLYC_MACHU 263 428 DBREF 9GHI H -2 224 PDB 9GHI 9GHI -2 224 DBREF 9GHI L -2 214 PDB 9GHI 9GHI -2 214 SEQADV 9GHI CYS A 88 UNP Q8AZ57 LEU 88 ENGINEERED MUTATION SEQADV 9GHI ALA A 138 UNP Q8AZ57 LYS 138 CONFLICT SEQADV 9GHI GLU A 227 UNP Q8AZ57 ASP 227 CONFLICT SEQADV 9GHI SER A 258 UNP Q8AZ57 GLU 258 ENGINEERED MUTATION SEQADV 9GHI ARG A 260 UNP Q8AZ57 SER 260 ENGINEERED MUTATION SEQADV 9GHI LYS A 261 UNP Q8AZ57 LEU 261 ENGINEERED MUTATION SEQADV 9GHI ARG A 262 UNP Q8AZ57 LYS 262 ENGINEERED MUTATION SEQADV 9GHI SER B 263 UNP Q6IUF7 ALA 263 ENGINEERED MUTATION SEQADV 9GHI ASP B 307 UNP Q6IUF7 ASN 307 CONFLICT SEQADV 9GHI PRO B 332 UNP Q6IUF7 GLU 332 ENGINEERED MUTATION SEQADV 9GHI CYS B 340 UNP Q6IUF7 LEU 340 ENGINEERED MUTATION SEQADV 9GHI SER B 429 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 430 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI ASP B 431 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI ASP B 432 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI ASP B 433 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI ASP B 434 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI LYS B 435 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 436 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI SER B 437 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 438 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI TRP B 439 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI SER B 440 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI HIS B 441 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI PRO B 442 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLN B 443 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI PHE B 444 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLU B 445 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI LYS B 446 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 447 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 448 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 449 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI SER B 450 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 451 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 452 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 453 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI SER B 454 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 455 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLY B 456 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI SER B 457 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI ALA B 458 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI TRP B 459 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI SER B 460 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI HIS B 461 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI PRO B 462 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLN B 463 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI PHE B 464 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI GLU B 465 UNP Q6IUF7 EXPRESSION TAG SEQADV 9GHI LYS B 466 UNP Q6IUF7 EXPRESSION TAG SEQRES 1 A 204 ASP GLY THR PHE LYS ILE GLY LEU HIS THR GLU PHE GLN SEQRES 2 A 204 SER VAL THR LEU THR MET GLN ARG LEU LEU ALA ASN HIS SEQRES 3 A 204 SER ASN GLU CYS PRO SER LEU CYS MET LEU ASN ASN SER SEQRES 4 A 204 PHE TYR TYR MET ARG GLY GLY VAL ASN THR PHE LEU ILE SEQRES 5 A 204 ARG VAL SER ASP ILE SER VAL LEU MET LYS GLU TYR ASP SEQRES 6 A 204 VAL SER ILE TYR GLU PRO GLU ASP LEU GLY ASN CYS LEU SEQRES 7 A 204 ASN ALA SER ASP SER SER TRP ALA ILE HIS TRP PHE SER SEQRES 8 A 204 ASN ALA LEU GLY HIS ASP TRP LEU MET ASP PRO PRO MET SEQRES 9 A 204 LEU CYS ARG ASN LYS THR LYS LYS GLU GLY SER ASN ILE SEQRES 10 A 204 GLN PHE ASN ILE SER LYS ALA ASP ASP ALA ARG VAL TYR SEQRES 11 A 204 GLY LYS LYS ILE ARG ASN GLY MET ARG HIS LEU PHE ARG SEQRES 12 A 204 GLY PHE HIS ASP PRO CYS GLU GLU GLY LYS VAL CYS TYR SEQRES 13 A 204 LEU THR ILE ASN GLN CYS GLY ASP PRO SER SER PHE GLU SEQRES 14 A 204 TYR CYS GLY VAL ASN HIS LEU SER LYS CYS GLN PHE ASP SEQRES 15 A 204 HIS VAL ASN THR LEU HIS PHE LEU VAL ARG SER LYS THR SEQRES 16 A 204 HIS LEU ASN PHE SER ARG ARG LYS ARG SEQRES 1 B 204 SER PHE PHE SER TRP SER LEU THR ASP SER SER GLY LYS SEQRES 2 B 204 ASP MET PRO GLY GLY TYR CYS LEU GLU GLU TRP MET LEU SEQRES 3 B 204 ILE ALA ALA LYS MET LYS CYS PHE GLY ASN THR ALA VAL SEQRES 4 B 204 ALA LYS CYS ASN GLN ASP HIS ASP SER GLU PHE CYS ASP SEQRES 5 B 204 MET LEU ARG LEU PHE ASP TYR ASN LYS ASN ALA ILE LYS SEQRES 6 B 204 THR LEU ASN ASP PRO SER LYS LYS GLU ILE ASN LEU CYS SEQRES 7 B 204 SER GLN THR VAL ASN ALA LEU ILE SER ASP ASN LEU LEU SEQRES 8 B 204 MET LYS ASN LYS ILE LYS GLU LEU MET SER ILE PRO TYR SEQRES 9 B 204 CYS ASN TYR THR LYS PHE TRP TYR VAL ASN HIS THR LEU SEQRES 10 B 204 THR GLY GLN HIS THR LEU PRO ARG CYS TRP LEU ILE ARG SEQRES 11 B 204 ASN GLY SER TYR LEU ASN THR SER GLU PHE ARG ASN ASP SEQRES 12 B 204 TRP ILE LEU GLU SER ASP HIS LEU ILE SER GLU MET LEU SEQRES 13 B 204 SER LYS GLU TYR ALA GLU ARG GLN GLY LYS SER GLY ASP SEQRES 14 B 204 ASP ASP ASP LYS GLY SER GLY TRP SER HIS PRO GLN PHE SEQRES 15 B 204 GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SER SEQRES 16 B 204 ALA TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 H 234 GLU THR GLY GLN VAL GLN LEU GLN GLN SER GLY ALA GLU SEQRES 2 H 234 LEU VAL LYS PRO GLY ALA SER VAL LYS ILE SER CYS LYS SEQRES 3 H 234 ALA SER GLY TYR ALA PHE GLY SER HIS TRP MET ASN TRP SEQRES 4 H 234 VAL LYS GLN ARG PRO GLY LYS GLY LEU GLU TRP ILE GLY SEQRES 5 H 234 GLN ILE TYR PRO GLY ASP GLY ASP THR ASN TYR ASN GLY SEQRES 6 H 234 LYS PHE LYS GLY LYS ALA THR LEU THR ALA ASP LYS SER SEQRES 7 H 234 SER SER THR ALA TYR MET GLN PHE SER SER LEU THR SER SEQRES 8 H 234 GLU ASP SER ALA VAL TYR PHE CYS ALA ARG ASP ASP TYR SEQRES 9 H 234 GLY THR ARG TYR TYR PHE ASP TYR TRP GLY GLN GLY THR SEQRES 10 H 234 THR LEU THR VAL SER SER ALA THR THR LYS GLY PRO SER SEQRES 11 H 234 VAL TYR PRO LEU ALA PRO SER ALA ALA ALA GLN THR ASN SEQRES 12 H 234 SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE SEQRES 13 H 234 PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SEQRES 14 H 234 SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 234 ASP LEU TYR THR LEU SER SER SER VAL THR VAL PRO SER SEQRES 16 H 234 SER THR TRP PRO SER GLN THR VAL THR CYS ASN VAL ALA SEQRES 17 H 234 HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL SEQRES 18 H 234 PRO ARG ASP CYS GLY THR LYS HIS HIS HIS HIS HIS HIS SEQRES 1 L 217 GLU THR GLY ASP ILE GLN MET THR GLN THR THR SER SER SEQRES 2 L 217 LEU SER ALA SER LEU GLY ASP ARG VAL SER ILE SER CYS SEQRES 3 L 217 ARG ALA SER GLN ASP ILE ASN ASN TYR LEU ASN TRP TYR SEQRES 4 L 217 GLN GLN LYS PRO ASP GLY THR VAL LYS LEU LEU ILE HIS SEQRES 5 L 217 TYR THR SER ARG LEU ARG SER GLY VAL PRO SER ARG PHE SEQRES 6 L 217 SER GLY SER GLY PHE GLY THR ASP TYR SER LEU THR ILE SEQRES 7 L 217 THR ASN LEU GLU GLN GLU ASP ILE ALA THR TYR PHE CYS SEQRES 8 L 217 GLN GLN GLY LYS THR LEU PRO LEU THR PHE GLY ALA GLY SEQRES 9 L 217 THR LYS LEU GLU ILE 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 14 HET NAG C 2 14 HET NAG D 1 14 HET NAG D 2 14 HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET MAN E 4 11 HET FUC E 5 10 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET MAN F 4 11 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET NAG A 301 14 HET NAG B 501 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 5 NAG 12(C8 H15 N O6) FORMUL 7 BMA 3(C6 H12 O6) FORMUL 7 MAN 2(C6 H12 O6) FORMUL 7 FUC C6 H12 O5 FORMUL 12 HOH *115(H2 O) HELIX 1 AA1 MET A 77 ALA A 82 1 6 HELIX 2 AA2 GLU A 128 CYS A 135 5 8 HELIX 3 AA3 ALA A 138 GLY A 153 1 16 HELIX 4 AA4 ALA A 182 ASP A 184 5 3 HELIX 5 AA5 ALA A 185 PHE A 200 1 16 HELIX 6 AA6 ASP A 222 PHE A 226 5 5 HELIX 7 AA7 GLY A 230 SER A 235 1 6 HELIX 8 AA8 ASP A 240 SER A 251 1 12 HELIX 9 AA9 GLU B 284 LEU B 288 5 5 HELIX 10 AB1 GLY B 297 GLN B 306 1 10 HELIX 11 AB2 SER B 310 ALA B 325 1 16 HELIX 12 AB3 THR B 343 LEU B 347 5 5 HELIX 13 AB4 SER B 349 MET B 362 1 14 HELIX 14 AB5 ASN B 398 GLU B 401 5 4 HELIX 15 AB6 PHE B 402 GLN B 426 1 25 HELIX 16 AB7 ALA H 28 HIS H 32 5 5 HELIX 17 AB8 THR H 83 SER H 87 5 5 HELIX 18 AB9 SER H 156 SER H 158 5 3 HELIX 19 AC1 PRO H 200 SER H 203 5 4 HELIX 20 AC2 GLU L 79 ILE L 83 5 5 HELIX 21 AC3 SER L 121 GLY L 128 1 8 HELIX 22 AC4 LYS L 183 ARG L 188 1 6 HELIX 23 AC5 ASN L 212 CYS L 214 5 3 SHEET 1 AA1 3 THR A 68 THR A 74 0 SHEET 2 AA1 3 LYS B 371 HIS B 377 -1 O TYR B 374 N GLN A 71 SHEET 3 AA1 3 ARG B 387 CYS B 388 -1 O ARG B 387 N TRP B 373 SHEET 1 AA2 7 SER A 90 MET A 93 0 SHEET 2 AA2 7 PHE A 98 GLY A 103 -1 O TYR A 100 N CYS A 92 SHEET 3 AA2 7 ASN A 106 SER A 113 -1 O ASN A 106 N GLY A 103 SHEET 4 AA2 7 TYR A 214 GLN A 219 -1 O ASN A 218 N LEU A 109 SHEET 5 AA2 7 ILE A 175 ASN A 178 -1 N ILE A 175 O ILE A 217 SHEET 6 AA2 7 MET 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 MET A 162 SHEET 1 AA3 2 CYS B 282 LEU B 283 0 SHEET 2 AA3 2 LYS B 294 CYS B 295 -1 O LYS B 294 N LEU B 283 SHEET 1 AA4 2 ILE B 391 ARG B 392 0 SHEET 2 AA4 2 SER B 395 TYR B 396 -1 O SER B 395 N ARG B 392 SHEET 1 AA5 4 GLN H 3 GLN H 6 0 SHEET 2 AA5 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA5 4 THR H 77 PHE H 82 -1 O PHE H 82 N VAL H 18 SHEET 4 AA5 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA6 6 GLU H 10 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 ASP H 95 -1 N ALA H 88 O LEU H 109 SHEET 4 AA6 6 MET H 34 GLN H 39 -1 N GLN H 39 O VAL H 89 SHEET 5 AA6 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA6 6 THR H 57 TYR H 59 -1 O ASN H 58 N GLN H 50 SHEET 1 AA7 4 GLU H 10 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 ASP H 95 -1 N ALA H 88 O LEU H 109 SHEET 4 AA7 4 PHE H 100C TRP H 103 -1 O TYR H 102 N ARG H 94 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 VAL H 193 HIS H 199 -1 O ASN H 196 N THR H 153 SHEET 3 AB1 3 THR H 204 ILE H 210 -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 ARG 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 PHE L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB3 6 SER L 10 ALA L 13 0 SHEET 2 AB3 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AB3 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB3 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB3 6 VAL L 44 HIS L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AB3 6 ARG L 53 LEU L 54 -1 O ARG L 53 N HIS L 49 SHEET 1 AB4 4 SER L 10 ALA L 13 0 SHEET 2 AB4 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AB4 4 THR 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 PHE L 135 N SER L 116 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 ILE L 144 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 AB6 4 SER L 191 HIS L 198 -1 O GLU L 195 N LYS L 147 SHEET 4 AB6 4 SER L 201 ASN L 210 -1 O ILE L 205 N ALA L 196 SSBOND 1 CYS A 88 CYS B 340 1555 1555 2.03 SSBOND 2 CYS A 92 CYS A 237 1555 1555 2.03 SSBOND 3 CYS A 135 CYS A 164 1555 1555 2.03 SSBOND 4 CYS A 207 CYS A 213 1555 1555 2.04 SSBOND 5 CYS A 220 CYS A 229 1555 1555 2.03 SSBOND 6 CYS B 282 CYS B 295 1555 1555 2.03 SSBOND 7 CYS B 304 CYS B 313 1555 1555 2.03 SSBOND 8 CYS B 367 CYS B 388 1555 1555 2.03 SSBOND 9 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 10 CYS H 140 CYS H 195 1555 1555 2.03 SSBOND 11 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 12 CYS L 134 CYS L 194 1555 1555 2.04 LINK ND2 ASN A 83 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN A 95 C1 NAG A 301 1555 1555 1.44 LINK ND2 ASN A 137 C1 NAG D 1 1555 1555 1.45 LINK ND2 ASN A 166 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 178 C1 NAG F 1 1555 1555 1.45 LINK ND2 ASN B 368 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN B 376 C1 NAG B 501 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O6 NAG E 1 C1 FUC E 5 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 1.44 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.45 LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.45 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45 CISPEP 1 PHE H 146 PRO H 147 0 -3.28 CISPEP 2 GLU H 148 PRO H 149 0 -2.44 CISPEP 3 TRP H 188 PRO H 189 0 1.85 CISPEP 4 LEU L 94 PRO L 95 0 -0.12 CISPEP 5 TYR L 140 PRO L 141 0 2.32 CRYST1 46.682 73.585 184.958 90.00 91.00 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 0.021422 0.000000 0.000375 0.00000 SCALE2 0.000000 0.013590 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005407 0.00000