HEADER VIRAL PROTEIN/IMMUNE SYSTEM 11-MAR-24 9AZT TITLE CH67 FAB BOUND TO A/MASSACHUSETTS/1/1990 INFLUENZA HEMAGGLUTININ HEAD TITLE 2 WITH A G189E MUTATION (1) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ HA1 CHAIN; COMPND 3 CHAIN: E; COMPND 4 FRAGMENT: HEAD DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: CH67 FAB HEAVY CHAIN; COMPND 9 CHAIN: H; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: CH67 FAB LIGHT CHAIN; COMPND 13 CHAIN: L; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 387165; SOURCE 4 STRAIN: A/MASSACHUSETTS/1/1990(H1N1); SOURCE 5 GENE: HA; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, INFLUENZA, HEMAGGLUTININ, UCA, ANTIVIRAL PROTEIN, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR D.P.MAURER,A.G.SCHMIDT REVDAT 1 12-MAR-25 9AZT 0 JRNL AUTH D.P.MAURER,M.VU,A.G.SCHMIDT JRNL TITL ANTIGENIC DRIFT EXPANDS INFLUENZA VIRAL ESCAPE PATHWAYS FROM JRNL TITL 2 RECALLED HUMORAL IMMUNITY. JRNL REF IMMUNITY 2025 JRNL REFN ISSN 1074-7613 JRNL PMID 40023162 JRNL DOI 10.1016/J.IMMUNI.2025.02.006 REMARK 2 REMARK 2 RESOLUTION. 2.94 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 2.94 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.20 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 17746 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.299 REMARK 3 R VALUE (WORKING SET) : 0.294 REMARK 3 FREE R VALUE : 0.338 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1774 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 47.2000 - 6.9200 1.00 1344 149 0.2453 0.3104 REMARK 3 2 6.9100 - 5.4900 1.00 1269 141 0.2818 0.3114 REMARK 3 3 5.4900 - 4.8000 1.00 1252 139 0.2600 0.2661 REMARK 3 4 4.8000 - 4.3600 1.00 1235 138 0.2671 0.3299 REMARK 3 5 4.3600 - 4.0500 1.00 1247 138 0.3124 0.3375 REMARK 3 6 4.0500 - 3.8100 1.00 1219 136 0.3232 0.3238 REMARK 3 7 3.8100 - 3.6200 1.00 1238 137 0.3449 0.4246 REMARK 3 8 3.6200 - 3.4600 1.00 1221 136 0.3578 0.4803 REMARK 3 9 3.4600 - 3.3300 1.00 1217 134 0.3762 0.4482 REMARK 3 10 3.3300 - 3.2100 1.00 1213 136 0.3859 0.4213 REMARK 3 11 3.2100 - 3.1100 1.00 1216 135 0.3835 0.4398 REMARK 3 12 3.1100 - 3.0200 1.00 1228 135 0.4153 0.4398 REMARK 3 13 3.0200 - 2.9400 0.89 1073 120 0.4958 0.5289 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) : 0.568 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.961 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 107.8 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 139.7 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 : 0.004 5111 REMARK 3 ANGLE : 0.755 6973 REMARK 3 CHIRALITY : 0.046 774 REMARK 3 PLANARITY : 0.007 891 REMARK 3 DIHEDRAL : 5.069 708 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 9AZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1000282331. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-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 : APS REMARK 200 BEAMLINE : 24-ID-E 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 EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17764 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.940 REMARK 200 RESOLUTION RANGE LOW (A) : 47.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 22.9200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.94 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.12 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.75 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8K, 100 MM HEPES, PH 7, 500 MM REMARK 280 NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 40.37600 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.85000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.37600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.85000 REMARK 290 SMTRY3 4 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: E, 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 GLY E 264 REMARK 465 ALA E 265 REMARK 465 GLY E 266 REMARK 465 SER E 267 REMARK 465 SER E 268 REMARK 465 LEU E 269 REMARK 465 GLU E 270 REMARK 465 VAL E 271 REMARK 465 LEU E 272 REMARK 465 PHE E 273 REMARK 465 GLN E 274 REMARK 465 LYS H 227 REMARK 465 SER H 228 REMARK 465 CYS H 229 REMARK 465 ASP H 230 REMARK 465 LYS H 231 REMARK 465 GLY H 232 REMARK 465 SER H 233 REMARK 465 SER H 234 REMARK 465 LEU H 235 REMARK 465 GLU H 236 REMARK 465 VAL H 237 REMARK 465 LEU H 238 REMARK 465 PHE H 239 REMARK 465 GLN H 240 REMARK 465 GLY H 241 REMARK 465 PRO H 242 REMARK 465 LEU H 243 REMARK 465 GLY H 244 REMARK 465 HIS H 245 REMARK 465 HIS H 246 REMARK 465 HIS H 247 REMARK 465 HIS H 248 REMARK 465 HIS H 249 REMARK 465 HIS H 250 REMARK 465 GLN L 1 REMARK 465 GLU L 49 REMARK 465 ASP L 50 REMARK 465 SER L 51 REMARK 465 ASP L 52 REMARK 465 ARG L 53 REMARK 465 PRO L 54 REMARK 465 SER L 55 REMARK 465 GLY L 56 REMARK 465 ILE L 57 REMARK 465 PRO L 58 REMARK 465 GLU L 212 REMARK 465 CYS L 213 REMARK 465 SER 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 ASP L 81 OH TYR L 85 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 E 55 73.10 46.89 REMARK 500 SER E 76 84.81 -165.85 REMARK 500 TYR E 82 -158.20 -116.33 REMARK 500 ILE E 83 -50.13 -124.64 REMARK 500 SER E 111 85.43 59.00 REMARK 500 ASN E 170 98.18 -61.28 REMARK 500 GLU E 173 -11.32 71.18 REMARK 500 HIS E 196 -57.41 67.77 REMARK 500 ASN E 199 68.21 -117.57 REMARK 500 LEU H 83 73.72 -104.58 REMARK 500 ARG H 85 88.83 66.04 REMARK 500 SER H 125 -24.15 -140.64 REMARK 500 ALA H 127 122.97 67.10 REMARK 500 ALA H 149 -158.73 -103.02 REMARK 500 ASP H 157 82.55 49.96 REMARK 500 THR H 204 -54.85 -134.16 REMARK 500 GLN L 16 -157.70 -100.91 REMARK 500 ALA L 83 -155.63 -173.04 REMARK 500 GLN L 110 131.94 -172.33 REMARK 500 GLN L 169 -154.61 -82.98 REMARK 500 ASN L 172 -16.96 67.42 REMARK 500 REMARK 500 REMARK: NULL DBREF 9AZT E 52 263 UNP Q07775 Q07775_9INFA 65 277 DBREF 9AZT H 1 250 PDB 9AZT 9AZT 1 250 DBREF 9AZT L 1 214 PDB 9AZT 9AZT 1 214 SEQADV 9AZT GLU E 189 UNP Q07775 GLY 203 ENGINEERED MUTATION SEQADV 9AZT GLY E 264 UNP Q07775 EXPRESSION TAG SEQADV 9AZT ALA E 265 UNP Q07775 EXPRESSION TAG SEQADV 9AZT GLY E 266 UNP Q07775 EXPRESSION TAG SEQADV 9AZT SER E 267 UNP Q07775 EXPRESSION TAG SEQADV 9AZT SER E 268 UNP Q07775 EXPRESSION TAG SEQADV 9AZT LEU E 269 UNP Q07775 EXPRESSION TAG SEQADV 9AZT GLU E 270 UNP Q07775 EXPRESSION TAG SEQADV 9AZT VAL E 271 UNP Q07775 EXPRESSION TAG SEQADV 9AZT LEU E 272 UNP Q07775 EXPRESSION TAG SEQADV 9AZT PHE E 273 UNP Q07775 EXPRESSION TAG SEQADV 9AZT GLN E 274 UNP Q07775 EXPRESSION TAG SEQRES 1 E 224 ALA PRO LEU GLN LEU GLY ASN CYS SER ILE ALA GLY TRP SEQRES 2 E 224 ILE LEU GLY ASN PRO GLU CYS GLU SER LEU PHE SER LYS SEQRES 3 E 224 GLU SER TRP SER TYR ILE ALA GLU THR PRO ASN SER GLU SEQRES 4 E 224 ASN GLY THR CYS TYR PRO GLY TYR PHE ALA ASP TYR GLU SEQRES 5 E 224 GLU LEU ARG GLU GLN LEU SER SER VAL SER SER PHE GLU SEQRES 6 E 224 ARG PHE GLU ILE PHE PRO LYS GLU SER SER TRP PRO ASN SEQRES 7 E 224 HIS THR VAL THR LYS GLY VAL THR ALA SER CYS SER HIS SEQRES 8 E 224 ASN GLY LYS SER SER PHE TYR ARG ASN LEU LEU TRP LEU SEQRES 9 E 224 THR GLU LYS ASN GLY LEU TYR PRO ASN LEU SER LYS SER SEQRES 10 E 224 TYR VAL ASN ASN LYS GLU LYS GLU VAL LEU VAL LEU TRP SEQRES 11 E 224 GLY VAL HIS HIS PRO SER ASN ILE GLU ASP GLN ARG ALA SEQRES 12 E 224 ILE TYR HIS THR GLU ASN ALA TYR VAL SER VAL VAL SER SEQRES 13 E 224 SER HIS TYR SER ARG ARG PHE THR PRO GLU ILE ALA LYS SEQRES 14 E 224 ARG PRO LYS VAL ARG ASP GLN GLU GLY ARG ILE ASN TYR SEQRES 15 E 224 TYR TRP THR LEU LEU GLU PRO GLY ASP THR ILE ILE PHE SEQRES 16 E 224 GLU ALA ASN GLY ASN LEU ILE ALA PRO TRP TYR ALA PHE SEQRES 17 E 224 ALA LEU SER ARG GLY GLY ALA GLY SER SER LEU GLU VAL SEQRES 18 E 224 LEU PHE GLN SEQRES 1 H 250 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL ARG LYS SEQRES 2 H 250 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 250 TYR THR PHE THR ASP ASN TYR ILE HIS TRP VAL ARG GLN SEQRES 4 H 250 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE HIS SEQRES 5 H 250 PRO ASN SER GLY ALA THR LYS TYR ALA GLN LYS PHE GLU SEQRES 6 H 250 GLY TRP VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 250 VAL TYR MET GLU LEU SER ARG SER ARG SER ASP ASP THR SEQRES 8 H 250 ALA VAL TYR TYR CYS ALA ARG ALA GLY LEU GLU PRO ARG SEQRES 9 H 250 SER VAL ASP TYR TYR PHE TYR GLY LEU ASP VAL TRP GLY SEQRES 10 H 250 GLN GLY THR ALA VAL THR VAL SER GLY ALA SER THR LYS SEQRES 11 H 250 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 H 250 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 H 250 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 H 250 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 H 250 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 H 250 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 H 250 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 H 250 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS GLY SER SER SEQRES 19 H 250 LEU GLU VAL LEU PHE GLN GLY PRO LEU GLY HIS HIS HIS SEQRES 20 H 250 HIS HIS HIS SEQRES 1 L 214 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER VAL ALA SEQRES 2 L 214 PRO GLY GLN THR ALA THR ILE THR CYS GLY GLY ASN ASN SEQRES 3 L 214 ILE GLY ARG LYS ARG VAL ASP TRP PHE GLN GLN LYS PRO SEQRES 4 L 214 GLY GLN ALA PRO VAL LEU VAL VAL TYR GLU ASP SER ASP SEQRES 5 L 214 ARG PRO SER GLY ILE PRO GLU ARG PHE SER ASP SER ASN SEQRES 6 L 214 SER GLY THR THR ALA THR LEU THR ILE SER ARG VAL GLU SEQRES 7 L 214 ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP ASP SEQRES 8 L 214 SER ASP SER ASP HIS VAL VAL PHE GLY GLY GLY THR LYS SEQRES 9 L 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 L 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 L 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 L 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 L 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 L 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 L 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS SEQRES 16 L 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 L 214 ALA PRO THR GLU CYS SER HET NAG A 1 14 HET NAG A 2 14 HET NAG E 301 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 4 NAG 3(C8 H15 N O6) HELIX 1 AA1 SER E 60 GLY E 67 1 8 HELIX 2 AA2 CYS E 71 PHE E 75 5 5 HELIX 3 AA3 ASP E 101 SER E 110 1 10 HELIX 4 AA4 ASN E 187 HIS E 196 1 10 HELIX 5 AA5 ARG H 87 THR H 91 5 5 HELIX 6 AA6 SER H 169 ALA H 171 5 3 HELIX 7 AA7 LYS H 214 ASN H 217 5 4 HELIX 8 AA8 SER L 123 GLN L 128 1 6 HELIX 9 AA9 THR L 183 SER L 189 1 7 SHEET 1 AA1 5 SER E 114 PHE E 118 0 SHEET 2 AA1 5 ALA E 257 SER E 261 -1 O ALA E 259 N GLU E 116 SHEET 3 AA1 5 GLU E 175 HIS E 184 -1 N LEU E 177 O PHE E 258 SHEET 4 AA1 5 LEU E 251 PRO E 254 -1 O ILE E 252 N GLY E 181 SHEET 5 AA1 5 LEU E 151 TRP E 153 -1 N LEU E 152 O ALA E 253 SHEET 1 AA2 4 SER E 114 PHE E 118 0 SHEET 2 AA2 4 ALA E 257 SER E 261 -1 O ALA E 259 N GLU E 116 SHEET 3 AA2 4 GLU E 175 HIS E 184 -1 N LEU E 177 O PHE E 258 SHEET 4 AA2 4 ARG E 229 LEU E 237 -1 O ARG E 229 N HIS E 184 SHEET 1 AA3 2 THR E 136 HIS E 141 0 SHEET 2 AA3 2 LYS E 144 SER E 146 -1 O LYS E 144 N HIS E 141 SHEET 1 AA4 4 LEU E 164 VAL E 169 0 SHEET 2 AA4 4 THR E 242 ALA E 247 -1 O PHE E 245 N LYS E 166 SHEET 3 AA4 4 VAL E 202 SER E 206 -1 N SER E 203 O GLU E 246 SHEET 4 AA4 4 SER E 210 PHE E 213 -1 O PHE E 213 N VAL E 202 SHEET 1 AA5 4 GLN H 3 GLN H 6 0 SHEET 2 AA5 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA5 4 THR H 78 LEU H 83 -1 O LEU H 83 N VAL H 18 SHEET 4 AA5 4 VAL H 68 ASP H 73 -1 N THR H 69 O GLU H 82 SHEET 1 AA6 6 VAL H 11 ARG H 12 0 SHEET 2 AA6 6 THR H 120 VAL H 124 1 O THR H 123 N ARG H 12 SHEET 3 AA6 6 ALA H 92 ALA H 99 -1 N TYR H 94 O THR H 120 SHEET 4 AA6 6 TYR H 33 GLN H 39 -1 N HIS H 35 O ALA H 97 SHEET 5 AA6 6 LEU H 45 ILE H 51 -1 O GLY H 49 N TRP H 36 SHEET 6 AA6 6 THR H 58 TYR H 60 -1 O LYS H 59 N TRP H 50 SHEET 1 AA7 4 SER H 133 LEU H 137 0 SHEET 2 AA7 4 LEU H 151 TYR H 158 -1 O LEU H 154 N PHE H 135 SHEET 3 AA7 4 TYR H 189 VAL H 195 -1 O TYR H 189 N TYR H 158 SHEET 4 AA7 4 VAL H 176 THR H 178 -1 N HIS H 177 O VAL H 194 SHEET 1 AA8 4 SER H 133 LEU H 137 0 SHEET 2 AA8 4 LEU H 151 TYR H 158 -1 O LEU H 154 N PHE H 135 SHEET 3 AA8 4 TYR H 189 VAL H 195 -1 O TYR H 189 N TYR H 158 SHEET 4 AA8 4 VAL H 182 LEU H 183 -1 N VAL H 182 O SER H 190 SHEET 1 AA9 3 THR H 164 TRP H 167 0 SHEET 2 AA9 3 TYR H 207 HIS H 213 -1 O ASN H 210 N SER H 166 SHEET 3 AA9 3 THR H 218 VAL H 224 -1 O VAL H 224 N TYR H 207 SHEET 1 AB1 5 SER L 9 VAL L 12 0 SHEET 2 AB1 5 THR L 103 VAL L 107 1 O THR L 106 N VAL L 10 SHEET 3 AB1 5 ASP L 84 ASP L 91 -1 N TYR L 85 O THR L 103 SHEET 4 AB1 5 ASP L 33 GLN L 37 -1 N GLN L 37 O ASP L 84 SHEET 5 AB1 5 VAL L 44 LEU L 45 -1 O VAL L 44 N GLN L 36 SHEET 1 AB2 4 SER L 9 VAL L 12 0 SHEET 2 AB2 4 THR L 103 VAL L 107 1 O THR L 106 N VAL L 10 SHEET 3 AB2 4 ASP L 84 ASP L 91 -1 N TYR L 85 O THR L 103 SHEET 4 AB2 4 HIS L 96 PHE L 99 -1 O VAL L 98 N VAL L 89 SHEET 1 AB3 3 THR L 17 GLY L 23 0 SHEET 2 AB3 3 THR L 69 SER L 75 -1 O ILE L 74 N ALA L 18 SHEET 3 AB3 3 PHE L 61 SER L 66 -1 N SER L 62 O THR L 73 SHEET 1 AB4 4 SER L 116 PHE L 120 0 SHEET 2 AB4 4 ALA L 132 PHE L 141 -1 O LEU L 137 N THR L 118 SHEET 3 AB4 4 TYR L 174 LEU L 182 -1 O LEU L 182 N ALA L 132 SHEET 4 AB4 4 VAL L 161 THR L 163 -1 N GLU L 162 O TYR L 179 SHEET 1 AB5 4 SER L 116 PHE L 120 0 SHEET 2 AB5 4 ALA L 132 PHE L 141 -1 O LEU L 137 N THR L 118 SHEET 3 AB5 4 TYR L 174 LEU L 182 -1 O LEU L 182 N ALA L 132 SHEET 4 AB5 4 SER L 167 LYS L 168 -1 N SER L 167 O ALA L 175 SHEET 1 AB6 4 PRO L 156 VAL L 157 0 SHEET 2 AB6 4 THR L 147 ALA L 152 -1 N TRP L 150 O VAL L 157 SHEET 3 AB6 4 TYR L 193 HIS L 199 -1 O SER L 194 N LYS L 151 SHEET 4 AB6 4 SER L 202 VAL L 208 -1 O VAL L 204 N VAL L 197 SSBOND 1 CYS E 59 CYS E 71 1555 1555 2.03 SSBOND 2 CYS E 94 CYS E 139 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 4 CYS H 153 CYS H 209 1555 1555 2.03 SSBOND 5 CYS L 22 CYS L 87 1555 1555 2.04 SSBOND 6 CYS L 136 CYS L 195 1555 1555 2.03 LINK ND2 ASN E 129 C1 NAG E 301 1555 1555 1.45 LINK ND2 ASN E 163 C1 NAG A 1 1555 1555 1.44 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.45 CISPEP 1 PHE H 159 PRO H 160 0 -4.38 CISPEP 2 GLU H 161 PRO H 162 0 -2.03 CISPEP 3 TYR L 142 PRO L 143 0 1.12 CRYST1 80.752 91.700 110.102 90.00 90.00 90.00 P 21 21 2 4 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 0.012384 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010905 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009082 0.00000