HEADER ANTIVIRAL PROTEIN 30-AUG-24 9JCY TITLE CRYSTAL STRUCTURE OF THE HCOV-HKU1 RBD IN COMPLEX WITH FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: WE CHOOSE THE SEGMENT OF SPIKE (RESIDUES 323-609) FOR COMPND 6 EXPRESSION. THE RECOMBINANT PROTEIN ENCOMPASSES A C-TERMINAL LINKER COMPND 7 ("SGLEVLFQGPGGS") FOLLOWED BY AN 8 X HIS TAG.; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: HEAVY CHAIN OF FAB; COMPND 10 CHAIN: C; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: THE HEAVY CHAIN OF FAB WAS EXPRESSED WITH A C-TERMIANL COMPND 13 LINKER ("GS") FOLLOWED BY A 6 X HIS TAG.; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: LIGHT CHAIN OF FAB; COMPND 16 CHAIN: B; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN CORONAVIRUS HKU1 (ISOLATE N1); SOURCE 3 ORGANISM_TAXID: 443239; SOURCE 4 GENE: S, 3; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS COMPLEX, ANTIBODY, HCOV-HKU1, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR H.WANG,Z.ZHAO,X.LIU,Y.DUAN,H.YANG REVDAT 1 30-JUL-25 9JCY 0 JRNL AUTH Z.ZHAO,Q.YANG,X.LIU,M.LI,Y.DUAN,M.DU,A.ZHOU,H.LIU,Y.HE, JRNL AUTH 2 W.WANG,Y.LU,X.ZHANG,H.WANG,X.YANG,H.ZHANG,X.CHEN,Z.RAO, JRNL AUTH 3 H.YANG JRNL TITL THE CRYSTAL STRUCTURE OF CORONAVIRUS RBD-TMPRSS2 COMPLEX JRNL TITL 2 PROVIDES BASIS FOR THE DISCOVERY OF THERAPEUTIC ANTIBODIES. JRNL REF NAT COMMUN V. 16 6636 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40681508 JRNL DOI 10.1038/S41467-025-62023-2 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21_5207-000) 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) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.74 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 79025 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.173 REMARK 3 FREE R VALUE : 0.203 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3955 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 30.7400 - 5.4500 1.00 2723 143 0.1833 0.1945 REMARK 3 2 5.4500 - 4.3300 1.00 2705 143 0.1442 0.1451 REMARK 3 3 4.3300 - 3.7900 1.00 2697 142 0.1435 0.1784 REMARK 3 4 3.7900 - 3.4400 1.00 2716 143 0.1560 0.1662 REMARK 3 5 3.4400 - 3.1900 1.00 2679 141 0.1561 0.1939 REMARK 3 6 3.1900 - 3.0100 1.00 2666 140 0.1676 0.2029 REMARK 3 7 3.0100 - 2.8600 1.00 2697 142 0.1721 0.2214 REMARK 3 8 2.8600 - 2.7300 1.00 2669 140 0.1762 0.2085 REMARK 3 9 2.7300 - 2.6300 1.00 2710 143 0.1753 0.2167 REMARK 3 10 2.6300 - 2.5400 1.00 2706 143 0.1814 0.2026 REMARK 3 11 2.5400 - 2.4600 1.00 2703 142 0.1761 0.2217 REMARK 3 12 2.4600 - 2.3900 1.00 2637 139 0.1805 0.2157 REMARK 3 13 2.3900 - 2.3200 1.00 2723 143 0.1823 0.2138 REMARK 3 14 2.3200 - 2.2700 1.00 2650 139 0.1851 0.2337 REMARK 3 15 2.2700 - 2.2200 1.00 2712 143 0.1879 0.2311 REMARK 3 16 2.2200 - 2.1700 1.00 2674 141 0.1869 0.2442 REMARK 3 17 2.1700 - 2.1200 1.00 2688 142 0.1902 0.2551 REMARK 3 18 2.1200 - 2.0800 1.00 2644 139 0.1923 0.2472 REMARK 3 19 2.0800 - 2.0500 1.00 2701 142 0.1801 0.2189 REMARK 3 20 2.0500 - 2.0100 1.00 2649 139 0.1805 0.1908 REMARK 3 21 2.0100 - 1.9800 1.00 2719 144 0.1854 0.2350 REMARK 3 22 1.9800 - 1.9500 1.00 2653 139 0.1861 0.2285 REMARK 3 23 1.9500 - 1.9200 1.00 2651 140 0.1978 0.2404 REMARK 3 24 1.9200 - 1.8900 1.00 2695 142 0.2068 0.2414 REMARK 3 25 1.8900 - 1.8700 1.00 2694 141 0.2251 0.2824 REMARK 3 26 1.8700 - 1.8400 0.99 2627 139 0.2325 0.2812 REMARK 3 27 1.8400 - 1.8200 1.00 2720 143 0.2620 0.2818 REMARK 3 28 1.8200 - 1.8000 0.99 2615 138 0.2764 0.3195 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) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.800 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 5727 REMARK 3 ANGLE : 0.860 7795 REMARK 3 CHIRALITY : 0.056 867 REMARK 3 PLANARITY : 0.007 1003 REMARK 3 DIHEDRAL : 13.044 2063 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 9JCY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 03-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1300050854. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79102 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 30.740 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : 0.09300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.6500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.60100 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 (%): 53.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2% (W/V) ALA-ALA, 0.2% (W/V) ALA REMARK 280 -GLN, 0.2% (W/V) GLY-GLU, 0.2% (W/V) GLY-L-ALA, 0.2% (W/V) GLY-L- REMARK 280 ASP, 0.2% (W/V) GLY-SAR, 0.2% (W/V) L-CARNOSINE, 0.2% (W/V) LEU- REMARK 280 ALA HYDRATE, 0.1 M BUFFER SYSTEM 3 [TRIS (BASE); BICINE] PH 8.5, REMARK 280 20% (V/V) PEG 500* MME, 10 % W/V PEG 20,000; FOR TMPRSS2:VHH77, REMARK 280 0.2 M SODIUM MALONATE PH 6.0, 10% (W/V) POLYETHYLENE GLYCOL 3, REMARK 280 350, EVAPORATION, TEMPERATURE 293K 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 80.64300 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7060 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30720 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 611 REMARK 465 LEU A 612 REMARK 465 GLU A 613 REMARK 465 VAL A 614 REMARK 465 LEU A 615 REMARK 465 PHE A 616 REMARK 465 GLN A 617 REMARK 465 GLY A 618 REMARK 465 PRO A 619 REMARK 465 GLY A 620 REMARK 465 GLY A 621 REMARK 465 SER A 622 REMARK 465 HIS A 623 REMARK 465 HIS A 624 REMARK 465 HIS A 625 REMARK 465 HIS A 626 REMARK 465 HIS A 627 REMARK 465 HIS A 628 REMARK 465 HIS A 629 REMARK 465 HIS A 630 REMARK 465 SER C 141 REMARK 465 THR C 142 REMARK 465 LYS C 225 REMARK 465 SER C 226 REMARK 465 CYS C 227 REMARK 465 GLY C 228 REMARK 465 SER C 229 REMARK 465 HIS C 230 REMARK 465 HIS C 231 REMARK 465 HIS C 232 REMARK 465 HIS C 233 REMARK 465 HIS C 234 REMARK 465 HIS C 235 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 LYS C 65 CG CD CE NZ REMARK 470 SER C 138 OG REMARK 470 SER C 139 OG REMARK 470 LYS C 140 CG CD CE NZ REMARK 470 LYS B 107 CG CD CE NZ 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 ASN A 413 -58.70 -139.19 REMARK 500 ASP C 155 62.86 67.45 REMARK 500 SER B 30 -123.45 53.60 REMARK 500 ALA B 51 -35.65 73.67 REMARK 500 ALA B 84 170.70 178.70 REMARK 500 REMARK 500 REMARK: NULL DBREF 9JCY A 323 609 UNP Q5MQD0 SPIKE_CVHN1 323 609 DBREF 9JCY C 1 235 PDB 9JCY 9JCY 1 235 DBREF 9JCY B 1 214 PDB 9JCY 9JCY 1 214 SEQADV 9JCY SER A 610 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY GLY A 611 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY LEU A 612 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY GLU A 613 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY VAL A 614 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY LEU A 615 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY PHE A 616 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY GLN A 617 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY GLY A 618 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY PRO A 619 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY GLY A 620 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY GLY A 621 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY SER A 622 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY HIS A 623 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY HIS A 624 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY HIS A 625 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY HIS A 626 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY HIS A 627 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY HIS A 628 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY HIS A 629 UNP Q5MQD0 EXPRESSION TAG SEQADV 9JCY HIS A 630 UNP Q5MQD0 EXPRESSION TAG SEQRES 1 A 308 ASP LEU PRO ASP CYS ASP ILE ASP LYS TRP LEU ASN ASN SEQRES 2 A 308 PHE ASN VAL PRO SER PRO LEU ASN TRP GLU ARG LYS ILE SEQRES 3 A 308 PHE SER ASN CYS ASN PHE ASN LEU SER THR LEU LEU ARG SEQRES 4 A 308 LEU VAL HIS THR ASP SER PHE SER CYS ASN ASN PHE ASP SEQRES 5 A 308 GLU SER LYS ILE TYR GLY SER CYS PHE LYS SER ILE VAL SEQRES 6 A 308 LEU ASP LYS PHE ALA ILE PRO ASN SER ARG ARG SER ASP SEQRES 7 A 308 LEU GLN LEU GLY SER SER GLY PHE LEU GLN SER SER ASN SEQRES 8 A 308 TYR LYS ILE ASP THR THR SER SER SER CYS GLN LEU TYR SEQRES 9 A 308 TYR SER LEU PRO ALA ILE ASN VAL THR ILE ASN ASN TYR SEQRES 10 A 308 ASN PRO SER SER TRP ASN ARG ARG TYR GLY PHE ASN ASN SEQRES 11 A 308 PHE ASN LEU SER SER HIS SER VAL VAL TYR SER ARG TYR SEQRES 12 A 308 CYS PHE SER VAL ASN ASN THR PHE CYS PRO CYS ALA LYS SEQRES 13 A 308 PRO SER PHE ALA SER SER CYS LYS SER HIS LYS PRO PRO SEQRES 14 A 308 SER ALA SER CYS PRO ILE GLY THR ASN TYR ARG SER CYS SEQRES 15 A 308 GLU SER THR THR VAL LEU ASP HIS THR ASP TRP CYS ARG SEQRES 16 A 308 CYS SER CYS LEU PRO ASP PRO ILE THR ALA TYR ASP PRO SEQRES 17 A 308 ARG SER CYS SER GLN LYS LYS SER LEU VAL GLY VAL GLY SEQRES 18 A 308 GLU HIS CYS ALA GLY PHE GLY VAL ASP GLU GLU LYS CYS SEQRES 19 A 308 GLY VAL LEU ASP GLY SER TYR ASN VAL SER CYS LEU CYS SEQRES 20 A 308 SER THR ASP ALA PHE LEU GLY TRP SER TYR ASP THR CYS SEQRES 21 A 308 VAL SER ASN ASN ARG CYS ASN ILE PHE SER ASN PHE ILE SEQRES 22 A 308 LEU ASN GLY ILE ASN SER GLY THR THR CYS SER ASN ASP SEQRES 23 A 308 LEU SER GLY LEU GLU VAL LEU PHE GLN GLY PRO GLY GLY SEQRES 24 A 308 SER HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 C 235 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 C 235 PRO SER GLY THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 C 235 GLY SER ILE SER SER SER ASN TRP TRP SER TRP VAL ARG SEQRES 4 C 235 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY SER MET SEQRES 5 C 235 HIS TYR SER GLY SER SER HIS TYR LYS PRO SER LEU LYS SEQRES 6 C 235 SER ARG ILE ALA MET SER VAL ASP THR SER LYS ASN GLN SEQRES 7 C 235 PHE SER LEU ASN LEU ASN SER VAL THR ALA ALA ASP THR SEQRES 8 C 235 ALA VAL TYR TYR CYS ALA ARG GLU GLY GLY SER SER GLY SEQRES 9 C 235 TYR ASP TYR VAL TYR TYR PHE ASP ASP TRP GLY GLN GLY SEQRES 10 C 235 THR THR VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 C 235 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 C 235 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 C 235 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 C 235 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 C 235 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 C 235 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 C 235 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 C 235 VAL GLU PRO LYS SER CYS GLY SER HIS HIS HIS HIS HIS SEQRES 19 C 235 HIS SEQRES 1 B 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 214 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 B 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 B 214 TYR SER THR PRO ARG THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS HET NAG A 701 14 HET NAG A 702 14 HET GOL A 703 6 HET GOL A 704 6 HET GOL B 301 6 HET GOL B 302 6 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM GOL GLYCEROL 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 GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 NAG 2(C8 H15 N O6) FORMUL 6 GOL 4(C3 H8 O3) FORMUL 10 HOH *640(H2 O) HELIX 1 AA1 ASP A 328 ASN A 334 1 7 HELIX 2 AA2 PRO A 341 TRP A 344 5 4 HELIX 3 AA3 ASN A 355 VAL A 363 1 9 HELIX 4 AA4 ASP A 374 ILE A 378 5 5 HELIX 5 AA5 PRO A 394 GLN A 402 5 9 HELIX 6 AA6 GLY A 407 ASN A 413 1 7 HELIX 7 AA7 SER A 442 TYR A 448 1 7 HELIX 8 AA8 LYS A 478 SER A 483 1 6 HELIX 9 AA9 ASP A 552 CYS A 556 5 5 HELIX 10 AB1 SER A 570 PHE A 574 5 5 HELIX 11 AB2 PRO C 62 LYS C 65 5 4 HELIX 12 AB3 THR C 87 THR C 91 5 5 HELIX 13 AB4 SER C 167 ALA C 169 5 3 HELIX 14 AB5 SER C 198 LEU C 200 5 3 HELIX 15 AB6 LYS C 212 ASN C 215 5 4 HELIX 16 AB7 GLN B 79 PHE B 83 5 5 HELIX 17 AB8 SER B 121 SER B 127 1 7 HELIX 18 AB9 LYS B 183 GLU B 187 1 5 SHEET 1 AA1 2 ASN A 337 PRO A 339 0 SHEET 2 AA1 2 THR A 435 ASN A 437 1 O ASN A 437 N VAL A 338 SHEET 1 AA2 5 GLU A 345 PHE A 349 0 SHEET 2 AA2 5 SER A 385 ALA A 392 -1 O ILE A 386 N PHE A 349 SHEET 3 AA2 5 ARG A 587 ASN A 597 -1 O PHE A 591 N PHE A 391 SHEET 4 AA2 5 SER A 422 PRO A 430 -1 N TYR A 427 O ILE A 590 SHEET 5 AA2 5 HIS A 364 ASN A 371 -1 N ASN A 371 O SER A 422 SHEET 1 AA3 4 GLU A 345 PHE A 349 0 SHEET 2 AA3 4 SER A 385 ALA A 392 -1 O ILE A 386 N PHE A 349 SHEET 3 AA3 4 ARG A 587 ASN A 597 -1 O PHE A 591 N PHE A 391 SHEET 4 AA3 4 VAL A 583 SER A 584 -1 N SER A 584 O ARG A 587 SHEET 1 AA4 3 CYS A 352 PHE A 354 0 SHEET 2 AA4 3 THR A 604 SER A 606 1 O CYS A 605 N PHE A 354 SHEET 3 AA4 3 CYS A 382 PHE A 383 -1 N PHE A 383 O THR A 604 SHEET 1 AA5 2 SER A 459 SER A 463 0 SHEET 2 AA5 2 TRP A 577 THR A 581 -1 O ASP A 580 N VAL A 460 SHEET 1 AA6 2 PHE A 467 SER A 468 0 SHEET 2 AA6 2 LYS A 536 LYS A 537 -1 O LYS A 536 N SER A 468 SHEET 1 AA7 2 CYS A 504 VAL A 509 0 SHEET 2 AA7 2 HIS A 512 CYS A 518 -1 O ARG A 517 N GLU A 505 SHEET 1 AA8 4 GLN C 3 SER C 7 0 SHEET 2 AA8 4 LEU C 18 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 3 AA8 4 GLN C 78 LEU C 83 -1 O PHE C 79 N CYS C 22 SHEET 4 AA8 4 ILE C 68 ASP C 73 -1 N ASP C 73 O GLN C 78 SHEET 1 AA9 6 LEU C 11 VAL C 12 0 SHEET 2 AA9 6 THR C 118 VAL C 122 1 O THR C 121 N VAL C 12 SHEET 3 AA9 6 ALA C 92 GLY C 101 -1 N ALA C 92 O VAL C 120 SHEET 4 AA9 6 TRP C 34 GLN C 40 -1 N VAL C 38 O TYR C 95 SHEET 5 AA9 6 GLU C 47 MET C 52 -1 O GLU C 47 N ARG C 39 SHEET 6 AA9 6 SER C 58 TYR C 60 -1 O HIS C 59 N SER C 51 SHEET 1 AB1 4 LEU C 11 VAL C 12 0 SHEET 2 AB1 4 THR C 118 VAL C 122 1 O THR C 121 N VAL C 12 SHEET 3 AB1 4 ALA C 92 GLY C 101 -1 N ALA C 92 O VAL C 120 SHEET 4 AB1 4 TYR C 109 ASP C 112 -1 O ASP C 112 N ARG C 98 SHEET 1 AB2 4 SER C 131 LEU C 135 0 SHEET 2 AB2 4 THR C 146 TYR C 156 -1 O LEU C 152 N PHE C 133 SHEET 3 AB2 4 TYR C 187 PRO C 196 -1 O LEU C 189 N VAL C 153 SHEET 4 AB2 4 VAL C 174 THR C 176 -1 N HIS C 175 O VAL C 192 SHEET 1 AB3 4 SER C 131 LEU C 135 0 SHEET 2 AB3 4 THR C 146 TYR C 156 -1 O LEU C 152 N PHE C 133 SHEET 3 AB3 4 TYR C 187 PRO C 196 -1 O LEU C 189 N VAL C 153 SHEET 4 AB3 4 VAL C 180 LEU C 181 -1 N VAL C 180 O SER C 188 SHEET 1 AB4 3 THR C 162 TRP C 165 0 SHEET 2 AB4 3 ILE C 206 HIS C 211 -1 O ASN C 208 N SER C 164 SHEET 3 AB4 3 THR C 216 LYS C 221 -1 O VAL C 218 N VAL C 209 SHEET 1 AB5 4 MET B 4 SER B 7 0 SHEET 2 AB5 4 VAL B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AB5 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AB5 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AB6 6 SER B 10 SER B 14 0 SHEET 2 AB6 6 THR B 102 LYS B 107 1 O GLU B 105 N LEU B 11 SHEET 3 AB6 6 ALA B 84 GLN B 90 -1 N ALA B 84 O VAL B 104 SHEET 4 AB6 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AB6 6 LYS B 45 TYR B 49 -1 O LYS B 45 N GLN B 37 SHEET 6 AB6 6 SER B 53 LEU B 54 -1 O SER B 53 N TYR B 49 SHEET 1 AB7 4 SER B 10 SER B 14 0 SHEET 2 AB7 4 THR B 102 LYS B 107 1 O GLU B 105 N LEU B 11 SHEET 3 AB7 4 ALA B 84 GLN B 90 -1 N ALA B 84 O VAL B 104 SHEET 4 AB7 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AB8 4 SER B 114 PHE B 118 0 SHEET 2 AB8 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AB8 4 TYR B 173 SER B 182 -1 O LEU B 179 N VAL B 132 SHEET 4 AB8 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 SHEET 1 AB9 4 ALA B 153 LEU B 154 0 SHEET 2 AB9 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB9 4 VAL B 191 THR B 197 -1 O GLU B 195 N GLN B 147 SHEET 4 AB9 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SSBOND 1 CYS A 327 CYS A 352 1555 1555 2.03 SSBOND 2 CYS A 370 CYS A 423 1555 1555 2.07 SSBOND 3 CYS A 382 CYS A 605 1555 1555 2.05 SSBOND 4 CYS A 466 CYS A 546 1555 1555 2.08 SSBOND 5 CYS A 474 CYS A 495 1555 1555 2.03 SSBOND 6 CYS A 476 CYS A 567 1555 1555 2.04 SSBOND 7 CYS A 485 CYS A 516 1555 1555 2.04 SSBOND 8 CYS A 504 CYS A 518 1555 1555 2.04 SSBOND 9 CYS A 520 CYS A 533 1555 1555 2.06 SSBOND 10 CYS A 556 CYS A 569 1555 1555 2.04 SSBOND 11 CYS A 582 CYS A 588 1555 1555 2.07 SSBOND 12 CYS C 22 CYS C 96 1555 1555 2.09 SSBOND 13 CYS C 151 CYS C 207 1555 1555 2.04 SSBOND 14 CYS B 23 CYS B 88 1555 1555 2.09 SSBOND 15 CYS B 134 CYS B 194 1555 1555 2.06 LINK ND2 ASN A 355 C1 NAG A 701 1555 1555 1.44 LINK ND2 ASN A 470 C1 NAG A 702 1555 1555 1.44 CISPEP 1 LEU A 521 PRO A 522 0 3.69 CISPEP 2 PHE C 157 PRO C 158 0 -5.01 CISPEP 3 GLU C 159 PRO C 160 0 1.17 CISPEP 4 SER B 7 PRO B 8 0 -8.37 CISPEP 5 THR B 94 PRO B 95 0 -3.99 CISPEP 6 TYR B 140 PRO B 141 0 -0.02 CRYST1 50.235 161.286 57.060 90.00 108.94 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 0.019906 0.000000 0.006831 0.00000 SCALE2 0.000000 0.006200 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018529 0.00000