HEADER VIRAL PROTEIN 13-FEB-23 8IDI TITLE CRYSTAL STRUCTURE OF NANOBODY VHH-T71 WITH MERS-COV RBD COMPND MOL_ID: 1; COMPND 2 MOLECULE: VHH-T71; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SPIKE PROTEIN S1; COMPND 7 CHAIN: B, D; COMPND 8 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS; SOURCE 3 ORGANISM_TAXID: 9838; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MIDDLE EAST RESPIRATORY SYNDROME-RELATED SOURCE 8 CORONAVIRUS; SOURCE 9 ORGANISM_COMMON: MERS-COV; SOURCE 10 ORGANISM_TAXID: 1335626; SOURCE 11 GENE: S; SOURCE 12 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS MERS-COV, NANOBODY, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX, VIRAL KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR X.WANG,L.TIAN REVDAT 1 28-FEB-24 8IDI 0 JRNL AUTH F.IDOUDI,R.WANG,L.TIAN,L.ZHANG,X.WANG JRNL TITL STRUCTURAL DEFINITION OF A NOVEL NANOBODY BINDING SITE JRNL TITL 2 SPECIFICALLY TARGETING THE MERS-COV RBD CORE-DOMAIN WITH JRNL TITL 3 NEUTRALIZING CAPACITY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.18.2_3874 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.55 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 77659 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.175 REMARK 3 R VALUE (WORKING SET) : 0.173 REMARK 3 FREE R VALUE : 0.207 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 3933 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 1.9240 - 1.9010 0.97 2525 161 0.2319 0.2739 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) : 0.180 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.700 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 : 0.006 5450 REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL 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): 68.4725 48.5948 48.4270 REMARK 3 T TENSOR REMARK 3 T11: 0.1691 T22: 0.1808 REMARK 3 T33: 0.1711 T12: -0.0087 REMARK 3 T13: 0.0014 T23: 0.0272 REMARK 3 L TENSOR REMARK 3 L11: 0.1167 L22: 0.0734 REMARK 3 L33: 0.0179 L12: 0.0398 REMARK 3 L13: -0.0818 L23: 0.0099 REMARK 3 S TENSOR REMARK 3 S11: 0.0256 S12: -0.0333 S13: 0.0069 REMARK 3 S21: 0.0074 S22: -0.0302 S23: -0.0342 REMARK 3 S31: 0.0071 S32: 0.0477 S33: 0.0049 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 8IDI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 22-FEB-23. REMARK 100 THE DEPOSITION ID IS D_1300035387. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-JUN-20 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 : BL17U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.987 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77670 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.901 REMARK 200 RESOLUTION RANGE LOW (A) : 36.551 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 6.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.1600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97 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 (%): 60.09 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 4% V/V TACSIMATE, PH 6.0, 12% W/V PEG REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291.15K 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 119.27450 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.41750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 119.27450 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.41750 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2360 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15950 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2430 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16130 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 A 0 REMARK 465 GLN A 1 REMARK 465 HIS A 131 REMARK 465 HIS A 132 REMARK 465 HIS A 133 REMARK 465 HIS A 134 REMARK 465 HIS A 135 REMARK 465 HIS A 136 REMARK 465 GLU B 367 REMARK 465 ALA B 368 REMARK 465 LYS B 369 REMARK 465 PRO B 370 REMARK 465 SER B 371 REMARK 465 GLY B 372 REMARK 465 SER B 373 REMARK 465 VAL B 374 REMARK 465 VAL B 375 REMARK 465 GLU B 376 REMARK 465 GLN B 377 REMARK 465 ALA B 378 REMARK 465 GLU B 379 REMARK 465 GLY B 380 REMARK 465 GLU B 589 REMARK 465 HIS B 590 REMARK 465 HIS B 591 REMARK 465 HIS B 592 REMARK 465 HIS B 593 REMARK 465 HIS B 594 REMARK 465 HIS B 595 REMARK 465 HIS C 131 REMARK 465 HIS C 132 REMARK 465 HIS C 133 REMARK 465 HIS C 134 REMARK 465 HIS C 135 REMARK 465 HIS C 136 REMARK 465 GLU D 367 REMARK 465 ALA D 368 REMARK 465 LYS D 369 REMARK 465 PRO D 370 REMARK 465 SER D 371 REMARK 465 GLY D 372 REMARK 465 SER D 373 REMARK 465 VAL D 374 REMARK 465 VAL D 375 REMARK 465 GLU D 376 REMARK 465 GLN D 377 REMARK 465 ALA D 378 REMARK 465 GLU D 379 REMARK 465 GLY D 380 REMARK 465 GLU D 589 REMARK 465 HIS D 590 REMARK 465 HIS D 591 REMARK 465 HIS D 592 REMARK 465 HIS D 593 REMARK 465 HIS D 594 REMARK 465 HIS D 595 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 O6 NAG F 2 O2 MAN F 4 1.93 REMARK 500 O ASP B 455 O HOH B 601 2.06 REMARK 500 O6 NAG E 1 O5 MAN E 5 2.10 REMARK 500 O HOH B 676 O HOH B 735 2.11 REMARK 500 OD2 ASP D 455 O HOH D 601 2.15 REMARK 500 C3 NAG E 1 C1 MAN E 4 2.19 REMARK 500 O HOH C 329 O HOH C 330 2.19 REMARK 500 OG SER D 583 O HOH D 602 2.19 REMARK 500 O HOH D 605 O HOH D 771 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 GLN A 3 -38.43 -147.92 REMARK 500 SER A 25 150.67 -47.81 REMARK 500 ASN A 33 -136.80 -142.17 REMARK 500 ASP A 67 -0.85 73.42 REMARK 500 ARG B 511 -48.50 -131.26 REMARK 500 SER C 26 -130.07 50.74 REMARK 500 ASN C 33 -137.09 -145.84 REMARK 500 ASP C 67 -5.39 77.29 REMARK 500 SER D 459 -133.59 54.31 REMARK 500 ASN D 468 -53.73 -125.24 REMARK 500 ARG D 511 -74.35 -131.43 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 321 DISTANCE = 6.16 ANGSTROMS REMARK 525 HOH A 322 DISTANCE = 6.37 ANGSTROMS REMARK 525 HOH A 323 DISTANCE = 6.66 ANGSTROMS REMARK 525 HOH A 324 DISTANCE = 6.92 ANGSTROMS REMARK 525 HOH A 325 DISTANCE = 7.08 ANGSTROMS REMARK 525 HOH B 857 DISTANCE = 6.11 ANGSTROMS REMARK 525 HOH B 858 DISTANCE = 6.33 ANGSTROMS REMARK 525 HOH B 859 DISTANCE = 6.42 ANGSTROMS REMARK 525 HOH B 860 DISTANCE = 6.55 ANGSTROMS REMARK 525 HOH B 861 DISTANCE = 6.87 ANGSTROMS REMARK 525 HOH B 862 DISTANCE = 7.09 ANGSTROMS REMARK 525 HOH B 863 DISTANCE = 7.24 ANGSTROMS REMARK 525 HOH B 864 DISTANCE = 7.30 ANGSTROMS REMARK 525 HOH B 865 DISTANCE = 7.33 ANGSTROMS REMARK 525 HOH B 866 DISTANCE = 7.35 ANGSTROMS REMARK 525 HOH B 867 DISTANCE = 9.34 ANGSTROMS REMARK 525 HOH C 373 DISTANCE = 6.51 ANGSTROMS REMARK 525 HOH C 374 DISTANCE = 6.87 ANGSTROMS REMARK 525 HOH D 842 DISTANCE = 5.97 ANGSTROMS REMARK 525 HOH D 843 DISTANCE = 6.36 ANGSTROMS REMARK 525 HOH D 844 DISTANCE = 6.95 ANGSTROMS REMARK 525 HOH D 845 DISTANCE = 7.14 ANGSTROMS REMARK 525 HOH D 846 DISTANCE = 7.22 ANGSTROMS REMARK 525 HOH D 847 DISTANCE = 7.29 ANGSTROMS REMARK 525 HOH D 848 DISTANCE = 7.61 ANGSTROMS REMARK 525 HOH D 849 DISTANCE = 7.92 ANGSTROMS REMARK 525 HOH D 850 DISTANCE = 10.62 ANGSTROMS DBREF 8IDI A 0 136 PDB 8IDI 8IDI 0 136 DBREF 8IDI B 367 588 UNP R9UQ53 R9UQ53_MERS 367 588 DBREF 8IDI C 0 136 PDB 8IDI 8IDI 0 136 DBREF 8IDI D 367 588 UNP R9UQ53 R9UQ53_MERS 367 588 SEQADV 8IDI GLU B 589 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS B 590 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS B 591 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS B 592 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS B 593 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS B 594 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS B 595 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI GLU D 589 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS D 590 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS D 591 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS D 592 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS D 593 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS D 594 UNP R9UQ53 EXPRESSION TAG SEQADV 8IDI HIS D 595 UNP R9UQ53 EXPRESSION TAG SEQRES 1 A 137 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL SEQRES 2 A 137 GLN ALA GLY GLY SER LEU THR LEU SER CYS THR PHE SER SEQRES 3 A 137 SER GLU TYR THR PHE THR HIS ASN ALA VAL GLY TRP PHE SEQRES 4 A 137 ARG GLN ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA ALA SEQRES 5 A 137 ILE ASN GLY GLY GLY GLY SER THR TYR TYR ALA ASP SER SEQRES 6 A 137 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASN ALA ASN SEQRES 7 A 137 THR VAL ALA SER LEU ILE MET LYS ASN LEU LYS PRO GLU SEQRES 8 A 137 ASP SER GLY ILE TYR TYR CYS ALA THR ASP VAL ARG LEU SEQRES 9 A 137 ILE ASP TRP TYR SER GLY ASP TRP SER LEU ALA ARG LEU SEQRES 10 A 137 TYR SER THR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 11 A 137 SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 229 GLU ALA LYS PRO SER GLY SER VAL VAL GLU GLN ALA GLU SEQRES 2 B 229 GLY VAL GLU CYS ASP PHE SER PRO LEU LEU SER GLY THR SEQRES 3 B 229 PRO PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR SEQRES 4 B 229 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE SEQRES 5 B 229 SER VAL ASN ASP PHE THR CYS SER GLN ILE SER PRO ALA SEQRES 6 B 229 ALA ILE ALA SER ASN CYS TYR SER SER LEU ILE LEU ASP SEQRES 7 B 229 TYR PHE SER TYR PRO LEU SER MET LYS SER ASP LEU SER SEQRES 8 B 229 VAL SER SER ALA GLY PRO ILE SER GLN PHE ASN TYR LYS SEQRES 9 B 229 GLN SER PHE SER ASN PRO THR CYS LEU ILE LEU ALA THR SEQRES 10 B 229 VAL PRO HIS ASN LEU THR THR ILE THR LYS PRO LEU LYS SEQRES 11 B 229 TYR SER TYR ILE ASN LYS CYS SER ARG LEU LEU SER ASP SEQRES 12 B 229 ASP ARG THR GLU VAL PRO GLN LEU VAL ASN ALA ASN GLN SEQRES 13 B 229 TYR SER PRO CYS VAL SER ILE VAL PRO SER THR VAL TRP SEQRES 14 B 229 GLU ASP GLY ASP TYR TYR ARG LYS GLN LEU SER PRO LEU SEQRES 15 B 229 GLU GLY GLY GLY TRP LEU VAL ALA SER GLY SER THR VAL SEQRES 16 B 229 ALA MET THR GLU GLN LEU GLN MET GLY PHE GLY ILE THR SEQRES 17 B 229 VAL GLN TYR GLY THR ASP THR ASN SER VAL CYS PRO LYS SEQRES 18 B 229 LEU GLU HIS HIS HIS HIS HIS HIS SEQRES 1 C 137 SER GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL SEQRES 2 C 137 GLN ALA GLY GLY SER LEU THR LEU SER CYS THR PHE SER SEQRES 3 C 137 SER GLU TYR THR PHE THR HIS ASN ALA VAL GLY TRP PHE SEQRES 4 C 137 ARG GLN ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA ALA SEQRES 5 C 137 ILE ASN GLY GLY GLY GLY SER THR TYR TYR ALA ASP SER SEQRES 6 C 137 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASN ALA ASN SEQRES 7 C 137 THR VAL ALA SER LEU ILE MET LYS ASN LEU LYS PRO GLU SEQRES 8 C 137 ASP SER GLY ILE TYR TYR CYS ALA THR ASP VAL ARG LEU SEQRES 9 C 137 ILE ASP TRP TYR SER GLY ASP TRP SER LEU ALA ARG LEU SEQRES 10 C 137 TYR SER THR TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 11 C 137 SER HIS HIS HIS HIS HIS HIS SEQRES 1 D 229 GLU ALA LYS PRO SER GLY SER VAL VAL GLU GLN ALA GLU SEQRES 2 D 229 GLY VAL GLU CYS ASP PHE SER PRO LEU LEU SER GLY THR SEQRES 3 D 229 PRO PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR SEQRES 4 D 229 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE SEQRES 5 D 229 SER VAL ASN ASP PHE THR CYS SER GLN ILE SER PRO ALA SEQRES 6 D 229 ALA ILE ALA SER ASN CYS TYR SER SER LEU ILE LEU ASP SEQRES 7 D 229 TYR PHE SER TYR PRO LEU SER MET LYS SER ASP LEU SER SEQRES 8 D 229 VAL SER SER ALA GLY PRO ILE SER GLN PHE ASN TYR LYS SEQRES 9 D 229 GLN SER PHE SER ASN PRO THR CYS LEU ILE LEU ALA THR SEQRES 10 D 229 VAL PRO HIS ASN LEU THR THR ILE THR LYS PRO LEU LYS SEQRES 11 D 229 TYR SER TYR ILE ASN LYS CYS SER ARG LEU LEU SER ASP SEQRES 12 D 229 ASP ARG THR GLU VAL PRO GLN LEU VAL ASN ALA ASN GLN SEQRES 13 D 229 TYR SER PRO CYS VAL SER ILE VAL PRO SER THR VAL TRP SEQRES 14 D 229 GLU ASP GLY ASP TYR TYR ARG LYS GLN LEU SER PRO LEU SEQRES 15 D 229 GLU GLY GLY GLY TRP LEU VAL ALA SER GLY SER THR VAL SEQRES 16 D 229 ALA MET THR GLU GLN LEU GLN MET GLY PHE GLY ILE THR SEQRES 17 D 229 VAL GLN TYR GLY THR ASP THR ASN SER VAL CYS PRO LYS SEQRES 18 D 229 LEU GLU HIS HIS HIS HIS HIS HIS HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET MAN E 4 11 HET MAN E 5 11 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET MAN F 4 11 HET MAN F 5 11 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 NAG 4(C8 H15 N O6) FORMUL 5 BMA 2(C6 H12 O6) FORMUL 5 MAN 4(C6 H12 O6) FORMUL 7 HOH *818(H2 O) HELIX 1 AA1 ASP A 63 LYS A 66 5 4 HELIX 2 AA2 LYS A 88 SER A 92 5 5 HELIX 3 AA3 ARG A 102 SER A 108 1 7 HELIX 4 AA4 LEU A 113 ARG A 115 5 3 HELIX 5 AA5 PHE B 385 SER B 390 5 6 HELIX 6 AA6 GLN B 395 PHE B 399 5 5 HELIX 7 AA7 ASN B 410 SER B 416 1 7 HELIX 8 AA8 SER B 429 ALA B 434 1 6 HELIX 9 AA9 PRO B 449 ALA B 461 5 13 HELIX 10 AB1 GLY B 462 ASN B 468 1 7 HELIX 11 AB2 GLY C 55 GLY C 57 5 3 HELIX 12 AB3 ASP C 63 LYS C 66 5 4 HELIX 13 AB4 LYS C 88 SER C 92 5 5 HELIX 14 AB5 ARG C 102 SER C 108 1 7 HELIX 15 AB6 LEU C 113 ARG C 115 5 3 HELIX 16 AB7 PHE D 385 SER D 390 5 6 HELIX 17 AB8 GLN D 395 PHE D 399 5 5 HELIX 18 AB9 ASN D 410 SER D 416 1 7 HELIX 19 AC1 SER D 429 ALA D 434 1 6 HELIX 20 AC2 PRO D 449 SER D 451 5 3 HELIX 21 AC3 MET D 452 VAL D 458 1 7 HELIX 22 AC4 SER D 459 ALA D 461 5 3 HELIX 23 AC5 GLY D 462 ASN D 468 1 7 SHEET 1 AA1 4 LEU A 4 SER A 7 0 SHEET 2 AA1 4 LEU A 18 PHE A 24 -1 O SER A 21 N SER A 7 SHEET 3 AA1 4 VAL A 79 MET A 84 -1 O MET A 84 N LEU A 18 SHEET 4 AA1 4 PHE A 69 ARG A 73 -1 N THR A 70 O ILE A 83 SHEET 1 AA2 6 GLY A 10 GLN A 13 0 SHEET 2 AA2 6 THR A 124 SER A 129 1 O THR A 127 N VAL A 12 SHEET 3 AA2 6 GLY A 93 VAL A 101 -1 N TYR A 95 O THR A 124 SHEET 4 AA2 6 ALA A 34 GLN A 40 -1 N PHE A 38 O TYR A 96 SHEET 5 AA2 6 GLU A 47 ASN A 53 -1 O ALA A 50 N TRP A 37 SHEET 6 AA2 6 THR A 59 TYR A 61 -1 O TYR A 60 N ALA A 51 SHEET 1 AA3 4 GLY A 10 GLN A 13 0 SHEET 2 AA3 4 THR A 124 SER A 129 1 O THR A 127 N VAL A 12 SHEET 3 AA3 4 GLY A 93 VAL A 101 -1 N TYR A 95 O THR A 124 SHEET 4 AA3 4 TYR A 117 TRP A 120 -1 O THR A 119 N THR A 99 SHEET 1 AA4 5 LYS B 400 PHE B 404 0 SHEET 2 AA4 5 SER B 440 SER B 447 -1 O LEU B 443 N LEU B 402 SHEET 3 AA4 5 GLN B 568 GLN B 576 -1 O GLY B 572 N ASP B 444 SHEET 4 AA4 5 THR B 477 THR B 483 -1 N ALA B 482 O MET B 569 SHEET 5 AA4 5 SER B 419 SER B 426 -1 N THR B 424 O LEU B 479 SHEET 1 AA5 2 ASN B 408 TYR B 409 0 SHEET 2 AA5 2 CYS B 585 PRO B 586 1 O CYS B 585 N TYR B 409 SHEET 1 AA6 4 GLU B 513 PRO B 515 0 SHEET 2 AA6 4 LYS B 496 LEU B 506 -1 N ARG B 505 O VAL B 514 SHEET 3 AA6 4 TRP B 553 ALA B 562 -1 O VAL B 555 N SER B 504 SHEET 4 AA6 4 TYR B 540 GLN B 544 -1 N TYR B 541 O ALA B 556 SHEET 1 AA7 4 LEU C 4 SER C 7 0 SHEET 2 AA7 4 LEU C 18 PHE C 24 -1 O SER C 21 N SER C 7 SHEET 3 AA7 4 VAL C 79 MET C 84 -1 O MET C 84 N LEU C 18 SHEET 4 AA7 4 PHE C 69 ARG C 73 -1 N THR C 70 O ILE C 83 SHEET 1 AA8 6 GLY C 10 GLN C 13 0 SHEET 2 AA8 6 THR C 124 SER C 129 1 O THR C 127 N GLY C 10 SHEET 3 AA8 6 GLY C 93 VAL C 101 -1 N TYR C 95 O THR C 124 SHEET 4 AA8 6 ALA C 34 GLN C 40 -1 N PHE C 38 O TYR C 96 SHEET 5 AA8 6 GLU C 47 ASN C 53 -1 O ALA C 50 N TRP C 37 SHEET 6 AA8 6 THR C 59 TYR C 61 -1 O TYR C 60 N ALA C 51 SHEET 1 AA9 4 GLY C 10 GLN C 13 0 SHEET 2 AA9 4 THR C 124 SER C 129 1 O THR C 127 N GLY C 10 SHEET 3 AA9 4 GLY C 93 VAL C 101 -1 N TYR C 95 O THR C 124 SHEET 4 AA9 4 TYR C 117 TRP C 120 -1 O THR C 119 N THR C 99 SHEET 1 AB1 5 LYS D 400 PHE D 404 0 SHEET 2 AB1 5 SER D 440 SER D 447 -1 O LEU D 441 N PHE D 404 SHEET 3 AB1 5 GLN D 568 GLN D 576 -1 O GLY D 572 N ASP D 444 SHEET 4 AB1 5 THR D 477 THR D 483 -1 N ILE D 480 O PHE D 571 SHEET 5 AB1 5 SER D 419 SER D 426 -1 N SER D 426 O THR D 477 SHEET 1 AB2 2 CYS D 407 TYR D 409 0 SHEET 2 AB2 2 VAL D 584 PRO D 586 1 O CYS D 585 N TYR D 409 SHEET 1 AB3 4 GLU D 513 PRO D 515 0 SHEET 2 AB3 4 LYS D 496 LEU D 506 -1 N ARG D 505 O VAL D 514 SHEET 3 AB3 4 TRP D 553 ALA D 562 -1 O VAL D 555 N SER D 504 SHEET 4 AB3 4 TYR D 540 GLN D 544 -1 N TYR D 541 O ALA D 556 SSBOND 1 CYS A 22 CYS A 97 1555 1555 2.06 SSBOND 2 CYS B 383 CYS B 407 1555 1555 2.05 SSBOND 3 CYS B 425 CYS B 478 1555 1555 2.05 SSBOND 4 CYS B 437 CYS B 585 1555 1555 2.09 SSBOND 5 CYS B 503 CYS B 526 1555 1555 2.04 SSBOND 6 CYS C 22 CYS C 97 1555 1555 2.07 SSBOND 7 CYS D 383 CYS D 407 1555 1555 2.02 SSBOND 8 CYS D 425 CYS D 478 1555 1555 2.06 SSBOND 9 CYS D 437 CYS D 585 1555 1555 2.08 SSBOND 10 CYS D 503 CYS D 526 1555 1555 2.03 LINK ND2 ASN B 487 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN D 487 C1 NAG F 1 1555 1555 1.47 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.38 LINK O3 NAG E 1 C1 MAN E 4 1555 1555 1.37 LINK O6 NAG E 1 C1 MAN E 5 1555 1555 1.38 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.38 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45 LINK O3 NAG F 1 C1 MAN F 4 1555 1555 1.43 LINK O6 NAG F 1 C1 MAN F 5 1555 1555 1.43 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.37 CRYST1 238.549 46.835 95.946 90.00 112.52 90.00 C 1 2 1 8 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 0.004192 0.000000 0.001738 0.00000 SCALE2 0.000000 0.021352 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011283 0.00000