HEADER VIRAL PROTEIN/IMMUNE SYSTEM 19-JUL-24 9CQA TITLE STRUCTURE OF ANTIBODY 1G1 BOUND TO THE CENTRAL CONSERVED REGION OF RSV TITLE 2 G COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 1G1 HEAVY CHAIN; COMPND 3 CHAIN: E, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB1G1 LIGHT CHAIN; COMPND 7 CHAIN: F, G; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MATURE SECRETED GLYCOPROTEIN G; COMPND 11 CHAIN: A, B; COMPND 12 SYNONYM: MATURE SG; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: RESPIRATORY SYNCYTIAL VIRUS A2; SOURCE 17 ORGANISM_TAXID: 1972429; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY, RESPIRATORY SYNCYTIAL VIRUS, G GLYCOPROTEIN, VIRAL PROTEIN, KEYWDS 2 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.G.JUAREZ,R.M.DUBOIS REVDAT 1 19-FEB-25 9CQA 0 JRNL AUTH M.J.JUAREZ,R.M.DUBOIS JRNL TITL STRUCTURES OF RESPIRATORY SYNCYTIAL VIRUS G BOUND TO JRNL TITL 2 BROADLY-REACTIVE ANTIBODIES PROVIDE INSIGHTS INTO VACCINE JRNL TITL 3 DESIGN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.74 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: 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) : 1.74 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.32 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 110700 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.211 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.810 REMARK 3 FREE R VALUE TEST SET COUNT : 2004 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 47.3200 - 4.1900 0.99 8179 152 0.1886 0.1944 REMARK 3 2 4.1900 - 3.3300 1.00 7945 144 0.1879 0.2115 REMARK 3 3 3.3300 - 2.9100 0.99 7858 143 0.2091 0.2074 REMARK 3 4 2.9100 - 2.6400 0.99 7785 159 0.2173 0.2293 REMARK 3 5 2.6400 - 2.4500 1.00 7839 131 0.2194 0.2263 REMARK 3 6 2.4500 - 2.3100 1.00 7790 154 0.2171 0.2488 REMARK 3 7 2.3100 - 2.1900 1.00 7770 134 0.2207 0.2568 REMARK 3 8 2.1900 - 2.1000 0.99 7737 144 0.2144 0.2314 REMARK 3 9 2.1000 - 2.0200 1.00 7715 147 0.2262 0.2563 REMARK 3 10 2.0200 - 1.9500 0.99 7766 148 0.2433 0.2944 REMARK 3 11 1.9500 - 1.8900 1.00 7709 130 0.2496 0.2683 REMARK 3 12 1.8900 - 1.8300 1.00 7782 147 0.2669 0.2631 REMARK 3 13 1.8300 - 1.7800 0.99 7673 142 0.3035 0.3059 REMARK 3 14 1.7800 - 1.7400 0.93 7148 129 0.3448 0.3247 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) : 0.210 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.660 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 : 0.007 7236 REMARK 3 ANGLE : 0.969 9874 REMARK 3 CHIRALITY : 0.063 1108 REMARK 3 PLANARITY : 0.011 1258 REMARK 3 DIHEDRAL : 14.023 2542 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 9CQA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000285967. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-APR-22 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 : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033167 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 : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110905 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740 REMARK 200 RESOLUTION RANGE LOW (A) : 47.320 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : 13.20 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77 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 (%): 47.79 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS (PH 6.5), 0.2M AMMONIUM REMARK 280 SULFATE, AND 24.5% PEG 3350, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 295.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 38.20900 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.59050 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.37650 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 87.59050 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.20900 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.37650 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5690 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21410 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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 350 REMARK 350 BIOMOLECULE: 2 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: 5290 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21310 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G, 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 SER E 138 REMARK 465 SER E 139 REMARK 465 LYS E 140 REMARK 465 SER E 141 REMARK 465 THR E 142 REMARK 465 SER E 143 REMARK 465 GLY E 144 REMARK 465 LYS E 225 REMARK 465 SER E 226 REMARK 465 CYS E 227 REMARK 465 ALA E 228 REMARK 465 SER E 229 REMARK 465 LEU E 230 REMARK 465 VAL E 231 REMARK 465 PRO E 232 REMARK 465 ARG E 233 REMARK 465 GLY E 234 REMARK 465 SER E 235 REMARK 465 GLY E 236 REMARK 465 TRP E 237 REMARK 465 SER E 238 REMARK 465 HIS E 239 REMARK 465 PRO E 240 REMARK 465 GLN E 241 REMARK 465 PHE E 242 REMARK 465 GLU E 243 REMARK 465 LYS E 244 REMARK 465 GLY E 245 REMARK 465 GLY E 246 REMARK 465 GLY E 247 REMARK 465 SER E 248 REMARK 465 GLY E 249 REMARK 465 GLY E 250 REMARK 465 GLY E 251 REMARK 465 SER E 252 REMARK 465 GLY E 253 REMARK 465 GLY E 254 REMARK 465 GLY E 255 REMARK 465 SER E 256 REMARK 465 TRP E 257 REMARK 465 SER E 258 REMARK 465 HIS E 259 REMARK 465 PRO E 260 REMARK 465 GLN E 261 REMARK 465 PHE E 262 REMARK 465 GLU E 263 REMARK 465 LYS E 264 REMARK 465 GLU F 214 REMARK 465 CYS F 215 REMARK 465 SER D 138 REMARK 465 SER D 139 REMARK 465 LYS D 140 REMARK 465 SER D 141 REMARK 465 THR D 142 REMARK 465 SER D 143 REMARK 465 GLY D 144 REMARK 465 LYS D 225 REMARK 465 SER D 226 REMARK 465 CYS D 227 REMARK 465 ALA D 228 REMARK 465 SER D 229 REMARK 465 LEU D 230 REMARK 465 VAL D 231 REMARK 465 PRO D 232 REMARK 465 ARG D 233 REMARK 465 GLY D 234 REMARK 465 SER D 235 REMARK 465 GLY D 236 REMARK 465 TRP D 237 REMARK 465 SER D 238 REMARK 465 HIS D 239 REMARK 465 PRO D 240 REMARK 465 GLN D 241 REMARK 465 PHE D 242 REMARK 465 GLU D 243 REMARK 465 LYS D 244 REMARK 465 GLY D 245 REMARK 465 GLY D 246 REMARK 465 GLY D 247 REMARK 465 SER D 248 REMARK 465 GLY D 249 REMARK 465 GLY D 250 REMARK 465 GLY D 251 REMARK 465 SER D 252 REMARK 465 GLY D 253 REMARK 465 GLY D 254 REMARK 465 GLY D 255 REMARK 465 SER D 256 REMARK 465 TRP D 257 REMARK 465 SER D 258 REMARK 465 HIS D 259 REMARK 465 PRO D 260 REMARK 465 GLN D 261 REMARK 465 PHE D 262 REMARK 465 GLU D 263 REMARK 465 LYS D 264 REMARK 465 GLU G 214 REMARK 465 CYS G 215 REMARK 465 MET A 155 REMARK 465 GLY A 156 REMARK 465 SER A 157 REMARK 465 LYS A 158 REMARK 465 PRO A 159 REMARK 465 ASN A 160 REMARK 465 ILE A 189 REMARK 465 PRO A 190 REMARK 465 ASN A 191 REMARK 465 LYS A 192 REMARK 465 LYS A 193 REMARK 465 PRO A 194 REMARK 465 GLY A 195 REMARK 465 LYS A 196 REMARK 465 LYS A 197 REMARK 465 HIS A 198 REMARK 465 HIS A 199 REMARK 465 HIS A 200 REMARK 465 HIS A 201 REMARK 465 HIS A 202 REMARK 465 HIS A 203 REMARK 465 MET B 155 REMARK 465 GLY B 156 REMARK 465 SER B 157 REMARK 465 LYS B 158 REMARK 465 PRO B 159 REMARK 465 ASN B 160 REMARK 465 ILE B 189 REMARK 465 PRO B 190 REMARK 465 ASN B 191 REMARK 465 LYS B 192 REMARK 465 LYS B 193 REMARK 465 PRO B 194 REMARK 465 GLY B 195 REMARK 465 LYS B 196 REMARK 465 LYS B 197 REMARK 465 HIS B 198 REMARK 465 HIS B 199 REMARK 465 HIS B 200 REMARK 465 HIS B 201 REMARK 465 HIS B 202 REMARK 465 HIS B 203 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 ASP E 155 68.18 62.52 REMARK 500 THR F 50 -41.54 68.76 REMARK 500 SER F 66 94.12 -167.03 REMARK 500 ALA F 83 170.96 179.91 REMARK 500 ASP D 155 62.44 62.80 REMARK 500 THR G 50 -43.55 70.85 REMARK 500 SER A 177 -119.58 53.15 REMARK 500 SER B 177 -120.01 53.81 REMARK 500 REMARK 500 REMARK: NULL DBREF 9CQA E 1 264 PDB 9CQA 9CQA 1 264 DBREF 9CQA F 1 215 PDB 9CQA 9CQA 1 215 DBREF 9CQA D 1 264 PDB 9CQA 9CQA 1 264 DBREF 9CQA G 1 215 PDB 9CQA 9CQA 1 215 DBREF 9CQA A 157 197 UNP P03423 GLYC_HRSVA 157 197 DBREF 9CQA B 157 197 UNP P03423 GLYC_HRSVA 157 197 SEQADV 9CQA MET A 155 UNP P03423 INITIATING METHIONINE SEQADV 9CQA GLY A 156 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS A 198 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS A 199 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS A 200 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS A 201 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS A 202 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS A 203 UNP P03423 EXPRESSION TAG SEQADV 9CQA MET B 155 UNP P03423 INITIATING METHIONINE SEQADV 9CQA GLY B 156 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS B 198 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS B 199 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS B 200 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS B 201 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS B 202 UNP P03423 EXPRESSION TAG SEQADV 9CQA HIS B 203 UNP P03423 EXPRESSION TAG SEQRES 1 E 264 GLN VAL HIS LEU VAL GLN SER GLY VAL GLU VAL LYS LYS SEQRES 2 E 264 PRO GLY ALA SER VAL ARG VAL SER CYS LYS ALA SER GLY SEQRES 3 E 264 TYR THR PHE ALA THR TYR GLY ILE THR TRP VAL ARG GLN SEQRES 4 E 264 ALA PRO GLY ARG GLY LEU GLU TRP VAL GLY TRP ILE THR SEQRES 5 E 264 PRO TYR ASN ASP ARG THR SER TYR ALA GLN ILE PHE HIS SEQRES 6 E 264 GLY ARG VAL THR MET THR THR ASP THR SER THR ASN THR SEQRES 7 E 264 ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP THR SEQRES 8 E 264 ALA MET TYR TYR CYS ALA ARG ASN HIS CYS ASN PHE TYR SEQRES 9 E 264 HIS ASP PHE TRP SER GLY LEU ASP TYR TRP GLY GLN GLY SEQRES 10 E 264 THR LEU VAL SER VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 E 264 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 E 264 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 E 264 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 E 264 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 E 264 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 E 264 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 E 264 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 E 264 VAL GLU PRO LYS SER CYS ALA SER LEU VAL PRO ARG GLY SEQRES 19 E 264 SER GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SEQRES 20 E 264 SER GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO SEQRES 21 E 264 GLN PHE GLU LYS SEQRES 1 F 215 SER PHE GLU LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 F 215 PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY ASP ALA SEQRES 3 F 215 LEU PRO LYS GLN TYR VAL TYR TRP TYR GLN GLN LYS PRO SEQRES 4 F 215 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS THR THR GLU SEQRES 5 F 215 ARG PRO SER GLY ILE PRO GLU ARG PHE SER ASP SER SER SEQRES 6 F 215 SER GLY THR THR VAL THR LEU THR ILE SER ALA ALA GLN SEQRES 7 F 215 ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER VAL ASP SEQRES 8 F 215 SER SER GLY THR TYR VAL PHE GLY ILE GLY THR LYS VAL SEQRES 9 F 215 THR VAL LEU GLY ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 F 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 F 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 F 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 F 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 F 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 F 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 F 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 F 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 264 GLN VAL HIS LEU VAL GLN SER GLY VAL GLU VAL LYS LYS SEQRES 2 D 264 PRO GLY ALA SER VAL ARG VAL SER CYS LYS ALA SER GLY SEQRES 3 D 264 TYR THR PHE ALA THR TYR GLY ILE THR TRP VAL ARG GLN SEQRES 4 D 264 ALA PRO GLY ARG GLY LEU GLU TRP VAL GLY TRP ILE THR SEQRES 5 D 264 PRO TYR ASN ASP ARG THR SER TYR ALA GLN ILE PHE HIS SEQRES 6 D 264 GLY ARG VAL THR MET THR THR ASP THR SER THR ASN THR SEQRES 7 D 264 ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP THR SEQRES 8 D 264 ALA MET TYR TYR CYS ALA ARG ASN HIS CYS ASN PHE TYR SEQRES 9 D 264 HIS ASP PHE TRP SER GLY LEU ASP TYR TRP GLY GLN GLY SEQRES 10 D 264 THR LEU VAL SER VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 D 264 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 D 264 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 D 264 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 D 264 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 D 264 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 D 264 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 D 264 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 D 264 VAL GLU PRO LYS SER CYS ALA SER LEU VAL PRO ARG GLY SEQRES 19 D 264 SER GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY SEQRES 20 D 264 SER GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO SEQRES 21 D 264 GLN PHE GLU LYS SEQRES 1 G 215 SER PHE GLU LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 G 215 PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY ASP ALA SEQRES 3 G 215 LEU PRO LYS GLN TYR VAL TYR TRP TYR GLN GLN LYS PRO SEQRES 4 G 215 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS THR THR GLU SEQRES 5 G 215 ARG PRO SER GLY ILE PRO GLU ARG PHE SER ASP SER SER SEQRES 6 G 215 SER GLY THR THR VAL THR LEU THR ILE SER ALA ALA GLN SEQRES 7 G 215 ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER VAL ASP SEQRES 8 G 215 SER SER GLY THR TYR VAL PHE GLY ILE GLY THR LYS VAL SEQRES 9 G 215 THR VAL LEU GLY ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 G 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 G 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 G 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 G 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 G 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 G 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 G 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 G 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 49 MET GLY SER LYS PRO ASN ASN ASP PHE HIS PHE GLU VAL SEQRES 2 A 49 PHE ASN PHE VAL PRO CYS SER ILE CYS SER ASN ASN PRO SEQRES 3 A 49 THR CYS TRP ALA ILE CYS LYS ARG ILE PRO ASN LYS LYS SEQRES 4 A 49 PRO GLY LYS LYS HIS HIS HIS HIS HIS HIS SEQRES 1 B 49 MET GLY SER LYS PRO ASN ASN ASP PHE HIS PHE GLU VAL SEQRES 2 B 49 PHE ASN PHE VAL PRO CYS SER ILE CYS SER ASN ASN PRO SEQRES 3 B 49 THR CYS TRP ALA ILE CYS LYS ARG ILE PRO ASN LYS LYS SEQRES 4 B 49 PRO GLY LYS LYS HIS HIS HIS HIS HIS HIS HET SO4 E 301 5 HET SO4 G 301 5 HET SO4 A 301 5 HET SO4 B 301 5 HETNAM SO4 SULFATE ION FORMUL 7 SO4 4(O4 S 2-) FORMUL 11 HOH *393(H2 O) HELIX 1 AA1 THR E 28 TYR E 32 5 5 HELIX 2 AA2 GLN E 62 HIS E 65 5 4 HELIX 3 AA3 ARG E 87 THR E 91 5 5 HELIX 4 AA4 SER E 167 ALA E 169 5 3 HELIX 5 AA5 SER E 198 GLY E 201 5 4 HELIX 6 AA6 LYS E 212 ASN E 215 5 4 HELIX 7 AA7 GLN F 78 GLU F 82 5 5 HELIX 8 AA8 SER F 122 SER F 128 1 7 HELIX 9 AA9 LYS F 184 LYS F 189 1 6 HELIX 10 AB1 THR D 28 TYR D 32 5 5 HELIX 11 AB2 GLN D 62 HIS D 65 5 4 HELIX 12 AB3 ARG D 87 THR D 91 5 5 HELIX 13 AB4 SER D 167 ALA D 169 5 3 HELIX 14 AB5 SER D 198 LEU D 200 5 3 HELIX 15 AB6 LYS D 212 ASN D 215 5 4 HELIX 16 AB7 GLN G 78 GLU G 82 5 5 HELIX 17 AB8 SER G 122 SER G 128 1 7 HELIX 18 AB9 LYS G 184 GLU G 188 1 5 HELIX 19 AC1 PRO A 172 CYS A 176 5 5 HELIX 20 AC2 ASN A 179 CYS A 186 1 8 HELIX 21 AC3 PRO B 172 CYS B 176 5 5 HELIX 22 AC4 ASN B 179 CYS B 186 1 8 SHEET 1 AA1 4 HIS E 3 GLN E 6 0 SHEET 2 AA1 4 VAL E 18 SER E 25 -1 O LYS E 23 N VAL E 5 SHEET 3 AA1 4 THR E 78 LEU E 83 -1 O ALA E 79 N CYS E 22 SHEET 4 AA1 4 VAL E 68 ASP E 73 -1 N ASP E 73 O THR E 78 SHEET 1 AA2 6 GLU E 10 LYS E 12 0 SHEET 2 AA2 6 THR E 118 VAL E 122 1 O SER E 121 N LYS E 12 SHEET 3 AA2 6 ALA E 92 ASN E 99 -1 N TYR E 94 O THR E 118 SHEET 4 AA2 6 GLY E 33 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AA2 6 GLU E 46 THR E 52 -1 O GLU E 46 N ARG E 38 SHEET 6 AA2 6 ARG E 57 TYR E 60 -1 O ARG E 57 N THR E 52 SHEET 1 AA3 2 CYS E 101 ASN E 102 0 SHEET 2 AA3 2 PHE E 107 TRP E 108 -1 O PHE E 107 N ASN E 102 SHEET 1 AA4 4 SER E 131 LEU E 135 0 SHEET 2 AA4 4 THR E 146 TYR E 156 -1 O GLY E 150 N LEU E 135 SHEET 3 AA4 4 TYR E 187 PRO E 196 -1 O VAL E 195 N ALA E 147 SHEET 4 AA4 4 VAL E 174 THR E 176 -1 N HIS E 175 O VAL E 192 SHEET 1 AA5 4 SER E 131 LEU E 135 0 SHEET 2 AA5 4 THR E 146 TYR E 156 -1 O GLY E 150 N LEU E 135 SHEET 3 AA5 4 TYR E 187 PRO E 196 -1 O VAL E 195 N ALA E 147 SHEET 4 AA5 4 VAL E 180 LEU E 181 -1 N VAL E 180 O SER E 188 SHEET 1 AA6 3 THR E 162 TRP E 165 0 SHEET 2 AA6 3 ILE E 206 HIS E 211 -1 O ASN E 208 N SER E 164 SHEET 3 AA6 3 THR E 216 LYS E 221 -1 O VAL E 218 N VAL E 209 SHEET 1 AA7 5 SER F 9 VAL F 12 0 SHEET 2 AA7 5 THR F 102 VAL F 106 1 O THR F 105 N VAL F 12 SHEET 3 AA7 5 ALA F 83 VAL F 90 -1 N ALA F 83 O VAL F 104 SHEET 4 AA7 5 TYR F 33 GLN F 37 -1 N GLN F 37 O ASP F 84 SHEET 5 AA7 5 VAL F 44 ILE F 47 -1 O VAL F 46 N TRP F 34 SHEET 1 AA8 4 SER F 9 VAL F 12 0 SHEET 2 AA8 4 THR F 102 VAL F 106 1 O THR F 105 N VAL F 12 SHEET 3 AA8 4 ALA F 83 VAL F 90 -1 N ALA F 83 O VAL F 104 SHEET 4 AA8 4 TYR F 96 PHE F 98 -1 O VAL F 97 N SER F 89 SHEET 1 AA9 3 ALA F 18 SER F 23 0 SHEET 2 AA9 3 THR F 69 ILE F 74 -1 O LEU F 72 N ILE F 20 SHEET 3 AA9 3 PHE F 61 SER F 66 -1 N SER F 62 O THR F 73 SHEET 1 AB1 4 SER F 115 PHE F 119 0 SHEET 2 AB1 4 THR F 130 PHE F 140 -1 O LEU F 136 N PHE F 117 SHEET 3 AB1 4 TYR F 174 SER F 183 -1 O LEU F 182 N ALA F 131 SHEET 4 AB1 4 SER F 160 VAL F 164 -1 N SER F 163 O SER F 177 SHEET 1 AB2 4 ALA F 154 LEU F 155 0 SHEET 2 AB2 4 LYS F 146 VAL F 151 -1 N VAL F 151 O ALA F 154 SHEET 3 AB2 4 VAL F 192 THR F 198 -1 O GLU F 196 N GLN F 148 SHEET 4 AB2 4 VAL F 206 ASN F 211 -1 O VAL F 206 N VAL F 197 SHEET 1 AB3 4 HIS D 3 GLN D 6 0 SHEET 2 AB3 4 VAL D 18 SER D 25 -1 O LYS D 23 N VAL D 5 SHEET 3 AB3 4 THR D 78 LEU D 83 -1 O MET D 81 N VAL D 20 SHEET 4 AB3 4 VAL D 68 ASP D 73 -1 N ASP D 73 O THR D 78 SHEET 1 AB4 6 GLU D 10 LYS D 12 0 SHEET 2 AB4 6 THR D 118 VAL D 122 1 O SER D 121 N LYS D 12 SHEET 3 AB4 6 ALA D 92 ASN D 99 -1 N TYR D 94 O THR D 118 SHEET 4 AB4 6 GLY D 33 GLN D 39 -1 N VAL D 37 O TYR D 95 SHEET 5 AB4 6 GLU D 46 THR D 52 -1 O GLU D 46 N ARG D 38 SHEET 6 AB4 6 ARG D 57 TYR D 60 -1 O ARG D 57 N THR D 52 SHEET 1 AB5 2 CYS D 101 ASN D 102 0 SHEET 2 AB5 2 PHE D 107 TRP D 108 -1 O PHE D 107 N ASN D 102 SHEET 1 AB6 4 SER D 131 LEU D 135 0 SHEET 2 AB6 4 THR D 146 TYR D 156 -1 O LEU D 152 N PHE D 133 SHEET 3 AB6 4 TYR D 187 PRO D 196 -1 O VAL D 195 N ALA D 147 SHEET 4 AB6 4 VAL D 174 THR D 176 -1 N HIS D 175 O VAL D 192 SHEET 1 AB7 4 SER D 131 LEU D 135 0 SHEET 2 AB7 4 THR D 146 TYR D 156 -1 O LEU D 152 N PHE D 133 SHEET 3 AB7 4 TYR D 187 PRO D 196 -1 O VAL D 195 N ALA D 147 SHEET 4 AB7 4 VAL D 180 LEU D 181 -1 N VAL D 180 O SER D 188 SHEET 1 AB8 3 THR D 162 TRP D 165 0 SHEET 2 AB8 3 ILE D 206 HIS D 211 -1 O ASN D 208 N SER D 164 SHEET 3 AB8 3 THR D 216 LYS D 221 -1 O VAL D 218 N VAL D 209 SHEET 1 AB9 5 SER G 9 VAL G 12 0 SHEET 2 AB9 5 THR G 102 VAL G 106 1 O THR G 105 N VAL G 12 SHEET 3 AB9 5 ALA G 83 VAL G 90 -1 N ALA G 83 O VAL G 104 SHEET 4 AB9 5 TYR G 33 GLN G 37 -1 N GLN G 37 O ASP G 84 SHEET 5 AB9 5 VAL G 44 ILE G 47 -1 O VAL G 46 N TRP G 34 SHEET 1 AC1 4 SER G 9 VAL G 12 0 SHEET 2 AC1 4 THR G 102 VAL G 106 1 O THR G 105 N VAL G 12 SHEET 3 AC1 4 ALA G 83 VAL G 90 -1 N ALA G 83 O VAL G 104 SHEET 4 AC1 4 TYR G 96 PHE G 98 -1 O VAL G 97 N SER G 89 SHEET 1 AC2 3 ALA G 18 SER G 23 0 SHEET 2 AC2 3 THR G 69 ILE G 74 -1 O LEU G 72 N ILE G 20 SHEET 3 AC2 3 PHE G 61 SER G 66 -1 N SER G 62 O THR G 73 SHEET 1 AC3 4 SER G 115 PHE G 119 0 SHEET 2 AC3 4 THR G 130 PHE G 140 -1 O LEU G 136 N PHE G 117 SHEET 3 AC3 4 TYR G 174 SER G 183 -1 O LEU G 180 N VAL G 133 SHEET 4 AC3 4 SER G 160 VAL G 164 -1 N SER G 163 O SER G 177 SHEET 1 AC4 3 ALA G 145 VAL G 151 0 SHEET 2 AC4 3 VAL G 192 HIS G 199 -1 O GLU G 196 N GLN G 148 SHEET 3 AC4 3 VAL G 206 ASN G 211 -1 O VAL G 206 N VAL G 197 SSBOND 1 CYS E 22 CYS E 96 1555 1555 2.08 SSBOND 2 CYS E 151 CYS E 207 1555 1555 2.04 SSBOND 3 CYS F 22 CYS F 87 1555 1555 2.09 SSBOND 4 CYS F 135 CYS F 195 1555 1555 2.07 SSBOND 5 CYS D 22 CYS D 96 1555 1555 2.08 SSBOND 6 CYS D 151 CYS D 207 1555 1555 2.03 SSBOND 7 CYS G 22 CYS G 87 1555 1555 2.09 SSBOND 8 CYS G 135 CYS G 195 1555 1555 2.06 SSBOND 9 CYS A 173 CYS A 186 1555 1555 2.04 SSBOND 10 CYS A 176 CYS A 182 1555 1555 2.06 SSBOND 11 CYS B 173 CYS B 186 1555 1555 2.04 SSBOND 12 CYS B 176 CYS B 182 1555 1555 2.06 CISPEP 1 PHE E 157 PRO E 158 0 -5.10 CISPEP 2 GLU E 159 PRO E 160 0 -2.29 CISPEP 3 TYR F 141 PRO F 142 0 0.68 CISPEP 4 PHE D 157 PRO D 158 0 -8.15 CISPEP 5 GLU D 159 PRO D 160 0 -0.47 CISPEP 6 TYR G 141 PRO G 142 0 4.76 CRYST1 76.418 80.753 175.181 90.00 90.00 90.00 P 21 21 21 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 0.013086 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012383 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005708 0.00000