HEADER VIRAL PROTEIN/IMMUNE SYSTEM 26-SEP-24 9DRU TITLE CRYSTAL STRUCTURE OF 04709_4F04 FAB IN COMPLEX WITH H1 HA FROM TITLE 2 A/CALIFORNIA/04/2009(H1N1) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ HA1 CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMAGGLUTININ HA2 CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 04709_4F04, HEAVY CHAIN; COMPND 11 CHAIN: H; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: 04709_4F04, LIGHT CHAIN; COMPND 15 CHAIN: L; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 GENE: HA; SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 9 ORGANISM_TAXID: 11320; SOURCE 10 GENE: HA; SOURCE 11 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS H1N1, ANTIBODY, HEMAGGLUTININ, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.H.LIN,I.A.WILSON REVDAT 1 19-MAR-25 9DRU 0 JRNL AUTH T.H.LIN,C.D.LEE,M.L.FERNANDEZ-QUINTERO,J.A.FERGUSON,J.HAN, JRNL AUTH 2 X.ZHU,W.YU,J.J.GUTHMILLER,F.KRAMMER,P.C.WILSON,A.B.WARD, JRNL AUTH 3 I.A.WILSON JRNL TITL STRUCTURALLY CONVERGENT ANTIBODIES DERIVED FROM DIFFERENT JRNL TITL 2 VACCINE STRATEGIES TARGET THE INFLUENZA VIRUS HA ANCHOR JRNL TITL 3 EPITOPE WITH A SUBSET OF V H 3 AND V K 3 GENES. JRNL REF NAT COMMUN V. 16 1268 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 39894881 JRNL DOI 10.1038/S41467-025-56496-4 REMARK 2 REMARK 2 RESOLUTION. 2.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21RC1_5127: ???) 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) : 2.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.98 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 3 NUMBER OF REFLECTIONS : 41068 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.265 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930 REMARK 3 FREE R VALUE TEST SET COUNT : 2026 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 29.9800 - 6.6100 1.00 3036 169 0.2157 0.2437 REMARK 3 2 6.6100 - 5.2600 1.00 2873 175 0.2052 0.2590 REMARK 3 3 5.2600 - 4.5900 1.00 2908 146 0.1740 0.2206 REMARK 3 4 4.5900 - 4.1800 1.00 2845 152 0.1694 0.2182 REMARK 3 5 4.1700 - 3.8800 1.00 2824 146 0.1790 0.2560 REMARK 3 6 3.8800 - 3.6500 1.00 2888 113 0.1973 0.2421 REMARK 3 7 3.6500 - 3.4700 1.00 2817 154 0.2165 0.2762 REMARK 3 8 3.4700 - 3.3200 1.00 2865 113 0.2280 0.2426 REMARK 3 9 3.3200 - 3.1900 1.00 2816 142 0.2469 0.3262 REMARK 3 10 3.1900 - 3.0800 1.00 2831 132 0.2361 0.3084 REMARK 3 11 3.0800 - 2.9800 1.00 2796 167 0.2590 0.3616 REMARK 3 12 2.9800 - 2.9000 0.99 2779 133 0.2901 0.3003 REMARK 3 13 2.9000 - 2.8200 0.96 2672 151 0.2767 0.3509 REMARK 3 14 2.8200 - 2.7500 0.76 2092 133 0.3001 0.3182 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) : 0.390 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.410 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 : 0.003 7466 REMARK 3 ANGLE : 0.607 10137 REMARK 3 CHIRALITY : 0.043 1122 REMARK 3 PLANARITY : 0.005 1304 REMARK 3 DIHEDRAL : 14.711 2686 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 9DRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288648. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-SEP-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 : SSRL REMARK 200 BEAMLINE : BL12-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 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 : 41068 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 20.00 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 46.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 2.60000 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 (%): 67.96 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, PH 6.4, 18% REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 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: DODECAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 50810 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 114320 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -255.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L 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 BIOMT1 2 -0.500000 -0.866025 0.000000 115.40400 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 57.70200 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 99.94280 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 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 A 501 O HOH A 537 2.17 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 196 -9.04 71.13 REMARK 500 SER A 266 168.57 62.53 REMARK 500 ALA B 5 -61.80 -99.75 REMARK 500 LYS B 127 -126.65 52.20 REMARK 500 ASP B 174 55.35 -91.37 REMARK 500 VAL H 48 -61.32 -105.53 REMARK 500 SER H 55 -0.28 71.67 REMARK 500 SER L 30 -124.47 59.07 REMARK 500 ALA L 51 -14.58 71.37 REMARK 500 PHE L 99 -64.66 -96.27 REMARK 500 PRO L 142 -169.86 -79.11 REMARK 500 VAL L 151 -85.64 -78.94 REMARK 500 ASN L 153 44.80 -148.78 REMARK 500 ASN L 159 -168.55 66.53 REMARK 500 SER L 160 68.02 60.95 REMARK 500 LYS L 189 42.66 -83.56 REMARK 500 LYS L 190 151.50 177.63 REMARK 500 LYS L 191 22.15 -144.06 REMARK 500 SER L 202 32.51 -90.48 REMARK 500 VAL L 205 -57.29 -134.33 REMARK 500 THR L 206 -179.79 -171.36 REMARK 500 REMARK 500 REMARK: NULL DBREF1 9DRU A 11 328 UNP A0A6M3Z334_9INFA DBREF2 9DRU A A0A6M3Z334 18 343 DBREF1 9DRU B 1 174 UNP A0A6J3XB93_9INFA DBREF2 9DRU B A0A6J3XB93 345 518 DBREF 9DRU H 1 227 PDB 9DRU 9DRU 1 227 DBREF 9DRU L 1 209 PDB 9DRU 9DRU 1 209 SEQADV 9DRU ASP A 8 UNP A0A6M3Z33 EXPRESSION TAG SEQADV 9DRU PRO A 9 UNP A0A6M3Z33 EXPRESSION TAG SEQADV 9DRU GLY A 10 UNP A0A6M3Z33 EXPRESSION TAG SEQADV 9DRU ASP A 131 UNP A0A6M3Z33 GLU 144 CONFLICT SEQADV 9DRU LEU A 194 UNP A0A6M3Z33 ILE 208 CONFLICT SEQADV 9DRU ILE A 329 UNP A0A6M3Z33 EXPRESSION TAG SEQADV 9DRU SER B 175 UNP A0A6J3XB9 EXPRESSION TAG SEQRES 1 A 330 ASP PRO GLY ASP THR LEU CYS ILE GLY TYR HIS ALA ASN SEQRES 2 A 330 ASN SER THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN SEQRES 3 A 330 VAL THR VAL THR HIS SER VAL ASN LEU LEU GLU ASP LYS SEQRES 4 A 330 HIS ASN GLY LYS LEU CYS LYS LEU ARG GLY VAL ALA PRO SEQRES 5 A 330 LEU HIS LEU GLY LYS CYS ASN ILE ALA GLY TRP ILE LEU SEQRES 6 A 330 GLY ASN PRO GLU CYS GLU SER LEU SER THR ALA SER SER SEQRES 7 A 330 TRP SER TYR ILE VAL GLU THR PRO SER SER ASP ASN GLY SEQRES 8 A 330 THR CYS TYR PRO GLY ASP PHE ILE ASP TYR GLU GLU LEU SEQRES 9 A 330 ARG GLU GLN LEU SER SER VAL SER SER PHE GLU ARG PHE SEQRES 10 A 330 GLU ILE PHE PRO LYS THR SER SER TRP PRO ASN HIS ASP SEQRES 11 A 330 SER ASN LYS GLY VAL THR ALA ALA CYS PRO HIS ALA GLY SEQRES 12 A 330 ALA LYS SER PHE TYR LYS ASN LEU ILE TRP LEU VAL LYS SEQRES 13 A 330 LYS GLY ASN SER TYR PRO LYS LEU SER LYS SER TYR ILE SEQRES 14 A 330 ASN ASP LYS GLY LYS GLU VAL LEU VAL LEU TRP GLY ILE SEQRES 15 A 330 HIS HIS PRO SER THR SER ALA ASP GLN GLN SER LEU TYR SEQRES 16 A 330 GLN ASN ALA ASP THR TYR VAL PHE VAL GLY SER SER ARG SEQRES 17 A 330 TYR SER LYS LYS PHE LYS PRO GLU ILE ALA ILE ARG PRO SEQRES 18 A 330 LYS VAL ARG ASP GLN GLU GLY ARG MET ASN TYR TYR TRP SEQRES 19 A 330 THR LEU VAL GLU PRO GLY ASP LYS ILE THR PHE GLU ALA SEQRES 20 A 330 THR GLY ASN LEU VAL VAL PRO ARG TYR ALA PHE ALA MET SEQRES 21 A 330 GLU ARG ASN ALA GLY SER GLY ILE ILE ILE SER ASP THR SEQRES 22 A 330 PRO VAL HIS ASP CYS ASN THR THR CYS GLN THR PRO LYS SEQRES 23 A 330 GLY ALA ILE ASN THR SER LEU PRO PHE GLN ASN ILE HIS SEQRES 24 A 330 PRO ILE THR ILE GLY LYS CYS PRO LYS TYR VAL LYS SER SEQRES 25 A 330 THR LYS LEU ARG LEU ALA THR GLY LEU ARG ASN ILE PRO SEQRES 26 A 330 SER ILE GLN SER ILE SEQRES 1 B 175 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY SEQRES 2 B 175 TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS SEQRES 3 B 175 GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP LEU LYS SEQRES 4 B 175 SER THR GLN ASN ALA ILE ASP GLY ILE THR ASN LYS VAL SEQRES 5 B 175 ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA SEQRES 6 B 175 VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG ILE GLU SEQRES 7 B 175 ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU ASP ILE SEQRES 8 B 175 TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN SEQRES 9 B 175 GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL LYS ASN SEQRES 10 B 175 LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN ASN ALA SEQRES 11 B 175 LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS SEQRES 12 B 175 CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN GLY THR SEQRES 13 B 175 TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS LEU ASN SEQRES 14 B 175 ARG GLU GLU ILE ASP SER SEQRES 1 H 227 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 227 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 227 PHE THR PHE ASN THR TYR ASN MET ASN TRP VAL ARG GLN SEQRES 4 H 227 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE SER SEQRES 5 H 227 SER SER SER LEU SER ARG TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 227 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 227 LEU PHE LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 227 ALA VAL TYR TYR CYS ALA ARG GLY ALA GLN ALA GLY TYR SEQRES 9 H 227 SER SER PHE PHE PRO PRO THR THR PHE TRP GLY GLN GLY SEQRES 10 H 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 H 227 VAL GLU PRO LYS SER CYS SEQRES 1 L 209 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 L 209 SER PRO GLY GLU GLY VAL THR LEU SER CYS ARG ALA SER SEQRES 3 L 209 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 209 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 209 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 209 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 209 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 L 209 TYR ASN TRP PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 L 209 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 209 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 209 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 209 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 209 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 209 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 209 SER LYS ALA ASP TYR GLU LYS LYS LYS VAL TYR ALA CYS SEQRES 16 L 209 GLU VAL THR HIS GLN GLY SER SER PRO VAL THR LYS SER SEQRES 17 L 209 PHE HET NAG A 401 14 HET NAG B 201 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 5 NAG 2(C8 H15 N O6) FORMUL 7 HOH *120(H2 O) HELIX 1 AA1 ASN A 65 GLY A 72 1 8 HELIX 2 AA2 ASN A 73 GLU A 77 5 5 HELIX 3 AA3 ASP A 104 LEU A 112 1 9 HELIX 4 AA4 PRO A 122 TRP A 127 1 6 HELIX 5 AA5 THR A 187 GLN A 196 1 10 HELIX 6 AA6 ASP B 37 LYS B 58 1 22 HELIX 7 AA7 GLU B 74 LYS B 127 1 54 HELIX 8 AA8 ASP B 145 ASN B 154 1 10 HELIX 9 AA9 ASP B 158 ASP B 174 1 17 HELIX 10 AB1 THR H 28 ASN H 30 5 3 HELIX 11 AB2 ASN H 74 LYS H 76 5 3 HELIX 12 AB3 ARG H 87 THR H 91 5 5 HELIX 13 AB4 TRP H 165 ALA H 169 5 5 HELIX 14 AB5 SER H 198 LEU H 200 5 3 HELIX 15 AB6 GLN L 79 PHE L 83 5 5 HELIX 16 AB7 GLU L 124 SER L 128 5 5 HELIX 17 AB8 LYS L 184 GLU L 188 1 5 SHEET 1 AA1 5 GLY B 31 ALA B 36 0 SHEET 2 AA1 5 TYR B 22 ASN B 28 -1 N TYR B 24 O ALA B 35 SHEET 3 AA1 5 THR A 12 TYR A 17 -1 N CYS A 14 O HIS B 25 SHEET 4 AA1 5 CYS B 137 PHE B 140 -1 O PHE B 138 N LEU A 13 SHEET 5 AA1 5 ALA B 130 GLY B 134 -1 N LYS B 131 O GLU B 139 SHEET 1 AA2 2 THR A 25 VAL A 26 0 SHEET 2 AA2 2 VAL A 34 THR A 35 -1 O VAL A 34 N VAL A 26 SHEET 1 AA3 2 SER A 39 ASN A 41 0 SHEET 2 AA3 2 ARG A 315 ALA A 317 -1 O LEU A 316 N VAL A 40 SHEET 1 AA4 3 LEU A 43 GLU A 44 0 SHEET 2 AA4 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLU A 44 SHEET 3 AA4 3 LYS A 307 TYR A 308 1 O LYS A 307 N GLN A 295 SHEET 1 AA5 2 LEU A 51 LEU A 54 0 SHEET 2 AA5 2 VAL A 274 THR A 279 1 O CYS A 277 N LYS A 53 SHEET 1 AA6 3 LEU A 59 HIS A 60 0 SHEET 2 AA6 3 ILE A 87 GLU A 89 1 O VAL A 88 N LEU A 59 SHEET 3 AA6 3 ILE A 267 ILE A 269 1 O ILE A 268 N GLU A 89 SHEET 1 AA7 5 VAL A 115 PHE A 118 0 SHEET 2 AA7 5 ALA A 257 ARG A 262 -1 O GLU A 261 N SER A 116 SHEET 3 AA7 5 GLU A 175 HIS A 184 -1 N GLU A 175 O MET A 260 SHEET 4 AA7 5 LEU A 251 PRO A 254 -1 O VAL A 252 N GLY A 181 SHEET 5 AA7 5 LEU A 151 TRP A 153 -1 N ILE A 152 O VAL A 253 SHEET 1 AA8 4 VAL A 115 PHE A 118 0 SHEET 2 AA8 4 ALA A 257 ARG A 262 -1 O GLU A 261 N SER A 116 SHEET 3 AA8 4 GLU A 175 HIS A 184 -1 N GLU A 175 O MET A 260 SHEET 4 AA8 4 ARG A 229 VAL A 237 -1 O ARG A 229 N HIS A 184 SHEET 1 AA9 2 THR A 136 HIS A 141 0 SHEET 2 AA9 2 ALA A 144 SER A 146 -1 O ALA A 144 N HIS A 141 SHEET 1 AB1 4 LEU A 164 ILE A 169 0 SHEET 2 AB1 4 LYS A 242 ALA A 247 -1 O ALA A 247 N LEU A 164 SHEET 3 AB1 4 VAL A 202 GLY A 205 -1 N PHE A 203 O GLU A 246 SHEET 4 AB1 4 SER A 210 PHE A 213 -1 O PHE A 213 N VAL A 202 SHEET 1 AB2 3 CYS A 281 GLN A 282 0 SHEET 2 AB2 3 ILE A 302 GLY A 303 -1 O ILE A 302 N GLN A 282 SHEET 3 AB2 3 THR B 64 ALA B 65 -1 O THR B 64 N GLY A 303 SHEET 1 AB3 4 GLN H 3 SER H 7 0 SHEET 2 AB3 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AB3 4 SER H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB3 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AB4 6 LEU H 11 VAL H 12 0 SHEET 2 AB4 6 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AB4 6 ALA H 92 GLN H 101 -1 N TYR H 94 O THR H 118 SHEET 4 AB4 6 TYR H 32 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB4 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AB4 6 ARG H 58 TYR H 60 -1 O TYR H 59 N TYR H 50 SHEET 1 AB5 4 LEU H 11 VAL H 12 0 SHEET 2 AB5 4 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AB5 4 ALA H 92 GLN H 101 -1 N TYR H 94 O THR H 118 SHEET 4 AB5 4 PHE H 113 TRP H 114 -1 O PHE H 113 N ARG H 98 SHEET 1 AB6 4 SER H 131 LEU H 135 0 SHEET 2 AB6 4 THR H 146 TYR H 156 -1 O LYS H 154 N SER H 131 SHEET 3 AB6 4 TYR H 187 PRO H 196 -1 O VAL H 195 N ALA H 147 SHEET 4 AB6 4 VAL H 174 THR H 176 -1 N HIS H 175 O VAL H 192 SHEET 1 AB7 4 SER H 131 LEU H 135 0 SHEET 2 AB7 4 THR H 146 TYR H 156 -1 O LYS H 154 N SER H 131 SHEET 3 AB7 4 TYR H 187 PRO H 196 -1 O VAL H 195 N ALA H 147 SHEET 4 AB7 4 VAL H 180 LEU H 181 -1 N VAL H 180 O SER H 188 SHEET 1 AB8 3 VAL H 161 THR H 162 0 SHEET 2 AB8 3 ILE H 206 HIS H 211 -1 O ASN H 210 N THR H 162 SHEET 3 AB8 3 THR H 216 LYS H 221 -1 O THR H 216 N HIS H 211 SHEET 1 AB9 4 MET L 4 THR L 5 0 SHEET 2 AB9 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB9 4 GLU L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AB9 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AC1 6 THR L 10 VAL L 13 0 SHEET 2 AC1 6 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 11 SHEET 3 AC1 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 103 SHEET 4 AC1 6 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AC1 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AC1 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AC2 3 PHE L 117 ILE L 118 0 SHEET 2 AC2 3 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AC2 3 TYR L 174 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 1 AC3 2 VAL L 147 LYS L 150 0 SHEET 2 AC3 2 ALA L 194 VAL L 197 -1 O ALA L 194 N LYS L 150 SSBOND 1 CYS A 14 CYS B 137 1555 1555 2.04 SSBOND 2 CYS A 52 CYS A 277 1555 1555 2.04 SSBOND 3 CYS A 64 CYS A 76 1555 1555 2.04 SSBOND 4 CYS A 97 CYS A 139 1555 1555 2.03 SSBOND 5 CYS A 281 CYS A 305 1555 1555 2.04 SSBOND 6 CYS B 144 CYS B 148 1555 1555 2.04 SSBOND 7 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 8 CYS H 151 CYS H 207 1555 1555 2.03 SSBOND 9 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 10 CYS L 135 CYS L 195 1555 1555 2.04 LINK ND2 ASN A 94 C1 NAG A 401 1555 1555 1.44 LINK ND2 ASN B 154 C1 NAG B 201 1555 1555 1.44 CISPEP 1 PHE H 157 PRO H 158 0 -5.16 CISPEP 2 GLU H 159 PRO H 160 0 -6.04 CISPEP 3 SER L 7 PRO L 8 0 -3.40 CISPEP 4 TRP L 94 PRO L 95 0 5.35 CISPEP 5 PRO L 95 PRO L 96 0 -1.97 CISPEP 6 TYR L 141 PRO L 142 0 -1.54 CRYST1 115.404 115.404 206.330 90.00 90.00 120.00 P 3 2 1 6 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 0.008665 0.005003 0.000000 0.00000 SCALE2 0.000000 0.010006 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004847 0.00000