HEADER VIRAL PROTEIN/IMMUNE SYSTEM 08-DEC-24 9MEV TITLE STRUCTURE OF H1H3:FLUA20 CHIMERIC ANTIGEN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: H1H3 HA; COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FLUA20 HEAVY CHAIN FAB; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FLUA20 LIGHT CHAIN FAB; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS INFLUENZA, HA, HEMAGGLUTININ, ANTIGEN, ANTIBODY, VIRAL PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR N.SERAJ REVDAT 1 19-MAR-25 9MEV 0 JRNL AUTH K.M.CASTRO,R.AYARDULABI,S.WEHRLE,H.CUI,S.GEORGEON,J.SCHMIDT, JRNL AUTH 2 S.XIAO,N.SERAJ,W.HARSHBARGER,C.P.MALLETT,V.VASSILEV, JRNL AUTH 3 X.SAELENS,B.E.CORREIA JRNL TITL STRUCTURE-BASED DESIGN OF CHIMERIC INFLUENZA HEMAGGLUTININS JRNL TITL 2 TO ELICIT CROSS-GROUP IMMUNITY. JRNL REF BIORXIV 2025 JRNL REFN ISSN 2692-8205 JRNL PMID 40027756 JRNL DOI 10.1101/2024.12.17.628867 REMARK 2 REMARK 2 RESOLUTION. 2.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 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) : 2.06 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.82 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 72.9 REMARK 3 NUMBER OF REFLECTIONS : 45825 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.209 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.390 REMARK 3 FREE R VALUE TEST SET COUNT : 3152 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 44.8200 - 5.8400 0.96 3920 186 0.1873 0.2348 REMARK 3 2 5.8400 - 4.6400 0.99 4029 186 0.1586 0.1525 REMARK 3 3 4.6400 - 4.0500 0.99 4066 190 0.1426 0.1571 REMARK 3 4 4.0500 - 3.6800 0.96 3946 179 0.1565 0.1889 REMARK 3 5 3.6800 - 3.4200 0.96 3907 190 0.1647 0.1815 REMARK 3 6 3.4200 - 3.2200 0.98 3960 181 0.1716 0.2367 REMARK 3 7 3.2200 - 3.0600 0.98 4091 176 0.1789 0.2521 REMARK 3 8 3.0600 - 2.9200 0.97 3986 180 0.1891 0.2231 REMARK 3 9 2.9200 - 2.8100 0.95 3831 186 0.1918 0.2174 REMARK 3 10 2.8100 - 2.7100 0.93 3852 165 0.2027 0.2153 REMARK 3 11 2.7100 - 2.6300 0.88 3570 179 0.2003 0.1996 REMARK 3 12 2.6300 - 2.5500 0.77 3158 125 0.1997 0.2469 REMARK 3 13 2.5500 - 2.4900 0.71 2941 139 0.2031 0.2180 REMARK 3 14 2.4900 - 2.4300 0.67 2725 130 0.2026 0.2327 REMARK 3 15 2.4300 - 2.3700 0.63 2571 113 0.2042 0.2518 REMARK 3 16 2.3700 - 2.3200 0.57 2318 120 0.2113 0.2329 REMARK 3 17 2.3200 - 2.2700 0.55 2265 99 0.2213 0.2586 REMARK 3 18 2.2700 - 2.2300 0.52 2157 100 0.2291 0.2475 REMARK 3 19 2.2300 - 2.1900 0.48 1989 88 0.2420 0.2646 REMARK 3 20 2.1900 - 2.1500 0.42 1722 69 0.2546 0.2611 REMARK 3 21 2.1500 - 2.1200 0.36 1457 70 0.2733 0.3226 REMARK 3 22 2.1200 - 2.0900 0.30 1242 56 0.2993 0.3280 REMARK 3 23 2.0900 - 2.0600 0.22 905 45 0.3106 0.3444 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) : 0.216 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.427 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.98 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.11 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 : 0.011 5270 REMARK 3 ANGLE : 1.290 7174 REMARK 3 CHIRALITY : 0.071 801 REMARK 3 PLANARITY : 0.006 919 REMARK 3 DIHEDRAL : 14.101 1962 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 9MEV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290839. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-FEB-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 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 : XDS REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45825 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060 REMARK 200 RESOLUTION RANGE LOW (A) : 44.820 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09 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 (%): 55.18 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M PCB, PH 6, 25% W/V PEG1500, REMARK 280 VAPOR DIFFUSION, SITTING DROP, 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 46.73250 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 APPLY THE FOLLOWING TO CHAINS: B, H, L, A 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 B 264 REMARK 465 GLY B 265 REMARK 465 LEU B 266 REMARK 465 VAL B 267 REMARK 465 PRO B 268 REMARK 465 ARG B 269 REMARK 465 GLY B 270 REMARK 465 SER B 271 REMARK 465 GLY B 272 REMARK 465 HIS B 273 REMARK 465 HIS B 274 REMARK 465 HIS B 275 REMARK 465 HIS B 276 REMARK 465 HIS B 277 REMARK 465 HIS B 278 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 HIS H 217 REMARK 465 HIS H 218 REMARK 465 HIS H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 CYS L 214 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH L 533 O HOH L 581 1.83 REMARK 500 O HOH L 526 O HOH L 576 1.84 REMARK 500 O HOH B 525 O HOH B 547 1.92 REMARK 500 O HOH B 529 O HOH B 543 1.96 REMARK 500 O HOH H 454 O HOH H 588 1.97 REMARK 500 O HOH L 474 O HOH L 502 1.99 REMARK 500 O HOH B 504 O HOH B 516 2.00 REMARK 500 O HOH H 533 O HOH H 557 2.05 REMARK 500 O HOH H 482 O HOH H 585 2.09 REMARK 500 O HOH B 474 O HOH B 485 2.11 REMARK 500 O HOH B 401 O HOH B 539 2.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD2 ASP H 56 O GLY H 133 2645 1.96 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 TYR B 82 127.42 77.57 REMARK 500 CYS B 139 57.27 -119.31 REMARK 500 SER B 146 -157.95 -143.90 REMARK 500 VAL B 196 -58.67 67.94 REMARK 500 SER B 210 116.04 -162.13 REMARK 500 SER H 15 -1.99 70.90 REMARK 500 ASN H 54 0.87 -67.96 REMARK 500 ASP H 98 67.95 -154.00 REMARK 500 ARG L 30 -119.68 57.31 REMARK 500 ALA L 51 -37.18 75.61 REMARK 500 SER L 52 -0.50 -143.23 REMARK 500 LYS L 126 0.26 -67.77 REMARK 500 ASN L 138 75.77 55.38 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 B 558 DISTANCE = 5.85 ANGSTROMS REMARK 525 HOH B 559 DISTANCE = 6.76 ANGSTROMS REMARK 525 HOH B 560 DISTANCE = 7.66 ANGSTROMS REMARK 525 HOH B 561 DISTANCE = 7.83 ANGSTROMS REMARK 525 HOH B 562 DISTANCE = 8.29 ANGSTROMS REMARK 525 HOH B 563 DISTANCE = 8.30 ANGSTROMS REMARK 525 HOH B 565 DISTANCE = 8.06 ANGSTROMS REMARK 525 HOH H 606 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH H 607 DISTANCE = 5.99 ANGSTROMS REMARK 525 HOH H 608 DISTANCE = 6.89 ANGSTROMS REMARK 525 HOH H 609 DISTANCE = 7.19 ANGSTROMS REMARK 525 HOH H 610 DISTANCE = 8.17 ANGSTROMS REMARK 525 HOH H 611 DISTANCE = 8.23 ANGSTROMS REMARK 525 HOH H 612 DISTANCE = 9.11 ANGSTROMS REMARK 525 HOH H 613 DISTANCE = 10.47 ANGSTROMS REMARK 525 HOH L 606 DISTANCE = 6.29 ANGSTROMS REMARK 525 HOH L 608 DISTANCE = 7.79 ANGSTROMS REMARK 525 HOH L 609 DISTANCE = 7.63 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 EDO H 301 DBREF 9MEV B 52 278 PDB 9MEV 9MEV 52 278 DBREF 9MEV H 1 222 PDB 9MEV 9MEV 1 222 DBREF 9MEV L 1 214 PDB 9MEV 9MEV 1 214 SEQRES 1 B 227 ALA PRO LEU GLN LEU GLY ASN CYS SER VAL ALA GLY TRP SEQRES 2 B 227 ILE LEU GLY ASN PRO GLU CYS GLU LEU LEU ILE SER ARG SEQRES 3 B 227 GLU SER TRP SER TYR ILE VAL GLU LYS PRO ASN PRO GLU SEQRES 4 B 227 ASN GLY THR CYS TYR PRO GLY HIS PHE ALA ASP TYR GLU SEQRES 5 B 227 GLU LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU SEQRES 6 B 227 ARG PHE GLU ILE PHE PRO LYS GLU SER SER TRP PRO ASN SEQRES 7 B 227 HIS THR GLN ASN GLY GLY SER ASN SER CYS SER HIS ASN SEQRES 8 B 227 GLY GLU SER SER PHE TYR LYS ASN LEU LEU TRP LEU THR SEQRES 9 B 227 LYS SER GLY SER LEU TYR PRO ASN LEU SER LYS SER TYR SEQRES 10 B 227 ALA ASN ASN LYS GLU LYS GLU VAL LEU VAL LEU TRP GLY SEQRES 11 B 227 VAL HIS HIS PRO PRO THR ILE GLN GLU GLN THR SER LEU SEQRES 12 B 227 TYR VAL LYS GLU ASN ALA TYR VAL SER VAL VAL SER SER SEQRES 13 B 227 HIS TYR SER ARG LYS PHE THR PRO GLU ILE ALA LYS ARG SEQRES 14 B 227 PRO LYS VAL ARG ASP GLN GLU GLY ARG ILE ASN TYR TYR SEQRES 15 B 227 TRP THR LEU LEU GLU PRO GLY ASP THR ILE ILE PHE GLU SEQRES 16 B 227 ALA ASN GLY ASN LEU ILE ALA PRO ARG TYR ALA PHE ALA SEQRES 17 B 227 LEU SER ARG GLY SER GLY LEU VAL PRO ARG GLY SER GLY SEQRES 18 B 227 HIS HIS HIS HIS HIS HIS SEQRES 1 H 235 GLN VAL GLN LEU GLU GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 235 PRO SER GLU THR LEU SER LEU THR CYS SER VAL SER GLY SEQRES 3 H 235 VAL SER VAL THR SER ASP ILE TYR TYR TRP THR TRP ILE SEQRES 4 H 235 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR SEQRES 5 H 235 ILE PHE TYR ASN GLY ASP THR ASN TYR ASN PRO SER LEU SEQRES 6 H 235 LYS SER ARG VAL THR MET SER ILE ASP THR SER LYS ASN SEQRES 7 H 235 GLU PHE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 H 235 THR ALA VAL TYR PHE CYS ALA ARG GLY THR GLU ASP LEU SEQRES 9 H 235 GLY TYR CYS SER SER GLY SER CYS PRO ASN HIS TRP GLY SEQRES 10 H 235 GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS SEQRES 11 H 235 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 H 235 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 H 235 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 H 235 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 H 235 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 H 235 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 H 235 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 H 235 LYS ARG VAL GLU PRO LYS SER CYS HIS HIS HIS HIS HIS SEQRES 19 H 235 HIS SEQRES 1 L 214 ASP ILE VAL MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER ILE GLY ASP ARG VAL THR ILE THR CYS ARG PRO SER SEQRES 3 L 214 GLN ASN ILE ARG SER PHE LEU ASN TRP PHE GLN HIS LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 214 ASN LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR GLU PHE THR LEU THR ILE ARG SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 214 TYR ASN THR PRO PRO THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HET NAG A 1 14 HET NAG A 2 14 HET NAG B 301 14 HET EDO H 301 3 HET EDO L 301 4 HET EDO L 302 4 HET EDO L 303 4 HET EDO L 304 4 HET EDO L 305 4 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM EDO 1,2-ETHANEDIOL 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 EDO ETHYLENE GLYCOL FORMUL 4 NAG 3(C8 H15 N O6) FORMUL 6 EDO 6(C2 H6 O2) FORMUL 12 HOH *589(H2 O) HELIX 1 AA1 SER B 60 GLY B 67 1 8 HELIX 2 AA2 ASN B 68 GLU B 72 5 5 HELIX 3 AA3 ASP B 101 LEU B 109 1 9 HELIX 4 AA4 PRO B 122 TRP B 127 1 6 HELIX 5 AA5 THR B 187 VAL B 196 1 10 HELIX 6 AA6 LEU H 63 SER H 65 5 3 HELIX 7 AA7 THR H 83 THR H 87 5 5 HELIX 8 AA8 SER H 127 THR H 131 5 5 HELIX 9 AA9 SER H 156 ALA H 158 5 3 HELIX 10 AB1 PRO H 185 LEU H 189 5 5 HELIX 11 AB2 LYS H 201 ASN H 204 5 4 HELIX 12 AB3 GLN L 79 PHE L 83 5 5 HELIX 13 AB4 SER L 121 LYS L 126 1 6 HELIX 14 AB5 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 2 LEU B 54 GLN B 55 0 SHEET 2 AA1 2 ILE B 83 VAL B 84 1 O VAL B 84 N LEU B 54 SHEET 1 AA2 7 TRP B 80 SER B 81 0 SHEET 2 AA2 7 SER B 111 PHE B 118 -1 O VAL B 112 N TRP B 80 SHEET 3 AA2 7 ALA B 257 ARG B 262 -1 O SER B 261 N SER B 113 SHEET 4 AA2 7 GLU B 175 HIS B 184 -1 N LEU B 177 O PHE B 258 SHEET 5 AA2 7 LEU B 251 PRO B 254 -1 O ILE B 252 N GLY B 181 SHEET 6 AA2 7 LEU B 151 THR B 155 -1 N LEU B 152 O ALA B 253 SHEET 7 AA2 7 THR B 131 GLN B 132 -1 N THR B 131 O THR B 155 SHEET 1 AA3 5 TRP B 80 SER B 81 0 SHEET 2 AA3 5 SER B 111 PHE B 118 -1 O VAL B 112 N TRP B 80 SHEET 3 AA3 5 ALA B 257 ARG B 262 -1 O SER B 261 N SER B 113 SHEET 4 AA3 5 GLU B 175 HIS B 184 -1 N LEU B 177 O PHE B 258 SHEET 5 AA3 5 ARG B 229 LEU B 237 -1 O LEU B 237 N VAL B 176 SHEET 1 AA4 2 SER B 136 HIS B 141 0 SHEET 2 AA4 2 GLU B 144 SER B 146 -1 O GLU B 144 N HIS B 141 SHEET 1 AA5 4 LEU B 164 ALA B 169 0 SHEET 2 AA5 4 THR B 242 ALA B 247 -1 O PHE B 245 N LYS B 166 SHEET 3 AA5 4 VAL B 202 VAL B 205 -1 N SER B 203 O GLU B 246 SHEET 4 AA5 4 SER B 210 PHE B 213 -1 O PHE B 213 N VAL B 202 SHEET 1 AA6 4 GLN H 3 GLU H 6 0 SHEET 2 AA6 4 LEU H 18 SER H 25 -1 O SER H 23 N GLU H 5 SHEET 3 AA6 4 GLU H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AA6 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLU H 77 SHEET 1 AA7 6 GLY H 10 VAL H 12 0 SHEET 2 AA7 6 THR H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA7 6 ALA H 88 THR H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA7 6 TYR H 34 GLN H 39 -1 N ILE H 37 O PHE H 91 SHEET 5 AA7 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA7 6 THR H 57 TYR H 59 -1 O ASN H 58 N TYR H 50 SHEET 1 AA8 4 GLY H 10 VAL H 12 0 SHEET 2 AA8 4 THR H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA8 4 ALA H 88 THR H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA8 4 HIS H 102 TRP H 103 -1 O HIS H 102 N ARG H 94 SHEET 1 AA9 4 SER H 120 LEU H 124 0 SHEET 2 AA9 4 ALA H 136 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA9 4 TYR H 176 VAL H 184 -1 O VAL H 184 N ALA H 136 SHEET 4 AA9 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB1 4 SER H 120 LEU H 124 0 SHEET 2 AB1 4 ALA H 136 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AB1 4 TYR H 176 VAL H 184 -1 O VAL H 184 N ALA H 136 SHEET 4 AB1 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB2 3 THR H 151 TRP H 154 0 SHEET 2 AB2 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB2 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AB3 4 MET L 4 SER L 7 0 SHEET 2 AB3 4 VAL L 19 PRO L 25 -1 O THR L 22 N SER L 7 SHEET 3 AB3 4 GLU L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AB3 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB4 6 SER L 10 SER L 14 0 SHEET 2 AB4 6 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 AB4 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AB4 6 LEU L 33 HIS L 38 -1 N PHE L 36 O TYR L 87 SHEET 5 AB4 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB4 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AB5 4 SER L 10 SER L 14 0 SHEET 2 AB5 4 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 AB5 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AB5 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB6 4 SER L 114 PHE L 118 0 SHEET 2 AB6 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB6 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AB6 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB7 3 LYS L 145 VAL L 150 0 SHEET 2 AB7 3 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 3 AB7 3 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS B 59 CYS B 71 1555 1555 2.01 SSBOND 2 CYS B 94 CYS B 139 1555 1555 2.05 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 4 CYS H 100B CYS H 100G 1555 1555 2.03 SSBOND 5 CYS H 140 CYS H 196 1555 1555 2.02 SSBOND 6 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 7 CYS L 134 CYS L 194 1555 1555 2.02 LINK ND2 ASN B 58 C1 NAG B 301 1555 1555 1.45 LINK ND2 ASN B 91 C1 NAG A 1 1555 1555 1.43 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.43 CISPEP 1 PHE H 146 PRO H 147 0 -12.22 CISPEP 2 GLU H 148 PRO H 149 0 11.11 CISPEP 3 SER L 7 PRO L 8 0 -0.70 CISPEP 4 THR L 94 PRO L 95 0 2.87 CISPEP 5 TYR L 140 PRO L 141 0 3.87 CRYST1 50.641 93.465 86.434 90.00 93.48 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 0.019747 0.000000 0.001202 0.00000 SCALE2 0.000000 0.010699 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011591 0.00000