HEADER VIRAL PROTEIN/IMMUNE SYSTEM 19-JUL-24 9CQB TITLE ANTIBODY 1G8 BOUND TO THE CENTRAL CONSERVED DOMAIN OF RSV G COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 1G8 LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB 1G8 HEAVY CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MATURE SECRETED GLYCOPROTEIN G; COMPND 11 CHAIN: D; 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.J.JUAREZ,M.J.DUBOIS REVDAT 1 19-FEB-25 9CQB 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. 2.50 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.37 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 27195 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.229 REMARK 3 R VALUE (WORKING SET) : 0.226 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.380 REMARK 3 FREE R VALUE TEST SET COUNT : 2007 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 58.3700 - 6.0200 1.00 1981 165 0.1826 0.2305 REMARK 3 2 6.0200 - 4.7800 1.00 1860 147 0.1786 0.1882 REMARK 3 3 4.7800 - 4.1800 1.00 1817 144 0.1689 0.1987 REMARK 3 4 4.1800 - 3.8000 1.00 1821 145 0.2048 0.2342 REMARK 3 5 3.8000 - 3.5200 1.00 1807 144 0.2296 0.2771 REMARK 3 6 3.5200 - 3.3200 1.00 1792 142 0.2365 0.3114 REMARK 3 7 3.3200 - 3.1500 1.00 1783 142 0.2573 0.2988 REMARK 3 8 3.1500 - 3.0100 1.00 1770 142 0.2661 0.3087 REMARK 3 9 3.0100 - 2.9000 1.00 1774 142 0.2891 0.3534 REMARK 3 10 2.9000 - 2.8000 1.00 1747 138 0.2976 0.3255 REMARK 3 11 2.8000 - 2.7100 1.00 1769 140 0.3233 0.3557 REMARK 3 12 2.7100 - 2.6300 1.00 1773 143 0.3240 0.3353 REMARK 3 13 2.6300 - 2.5600 1.00 1760 136 0.3506 0.3824 REMARK 3 14 2.5600 - 2.5000 1.00 1734 137 0.3699 0.4198 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) : 0.454 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.111 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 51.91 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.41 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 : 0.009 3666 REMARK 3 ANGLE : 1.091 4995 REMARK 3 CHIRALITY : 0.059 567 REMARK 3 PLANARITY : 0.008 636 REMARK 3 DIHEDRAL : 16.710 1312 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 9CQB 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_1000286035. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-OCT-23 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 : ALS REMARK 200 BEAMLINE : 5.0.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : .97 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27297 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 286.350 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 18.90 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54 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 (%): 61.84 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: .15M SODIUM THIOCYANATE AND 16% PEG REMARK 280 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 95.44867 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 190.89733 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 190.89733 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 95.44867 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5320 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20650 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D 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 THR B 144 REMARK 465 SER B 145 REMARK 465 GLY B 146 REMARK 465 CYS B 229 REMARK 465 ALA B 230 REMARK 465 SER B 231 REMARK 465 LEU B 232 REMARK 465 VAL B 233 REMARK 465 PRO B 234 REMARK 465 ARG B 235 REMARK 465 GLY B 236 REMARK 465 SER B 237 REMARK 465 GLY B 238 REMARK 465 TRP B 239 REMARK 465 SER B 240 REMARK 465 HIS B 241 REMARK 465 PRO B 242 REMARK 465 GLN B 243 REMARK 465 PHE B 244 REMARK 465 GLU B 245 REMARK 465 LYS B 246 REMARK 465 GLY B 247 REMARK 465 GLY B 248 REMARK 465 GLY B 249 REMARK 465 SER B 250 REMARK 465 GLY B 251 REMARK 465 GLY B 252 REMARK 465 GLY B 253 REMARK 465 SER B 254 REMARK 465 GLY B 255 REMARK 465 GLY B 256 REMARK 465 GLY B 257 REMARK 465 SER B 258 REMARK 465 TRP B 259 REMARK 465 SER B 260 REMARK 465 HIS B 261 REMARK 465 PRO B 262 REMARK 465 GLN B 263 REMARK 465 PHE B 264 REMARK 465 GLU B 265 REMARK 465 LYS B 266 REMARK 465 MET D 155 REMARK 465 GLY D 156 REMARK 465 SER D 157 REMARK 465 LYS D 158 REMARK 465 PRO D 159 REMARK 465 ASN D 160 REMARK 465 ASN D 161 REMARK 465 ASN D 191 REMARK 465 LYS D 192 REMARK 465 LYS D 193 REMARK 465 PRO D 194 REMARK 465 GLY D 195 REMARK 465 LYS D 196 REMARK 465 LYS D 197 REMARK 465 HIS D 198 REMARK 465 HIS D 199 REMARK 465 HIS D 200 REMARK 465 HIS D 201 REMARK 465 HIS D 202 REMARK 465 HIS D 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 ARG A 27 -169.65 -110.57 REMARK 500 ALA A 51 -16.31 74.26 REMARK 500 SER A 52 -8.24 -146.24 REMARK 500 TYR A 91 49.69 -148.81 REMARK 500 ASP A 153 57.47 33.09 REMARK 500 SER B 15 -10.30 67.37 REMARK 500 GLN B 33 45.58 -103.13 REMARK 500 SER B 64 2.65 -65.86 REMARK 500 ALA B 90 4.59 -68.58 REMARK 500 TRP B 110 -179.95 -171.96 REMARK 500 ASP B 112 122.95 -171.11 REMARK 500 ALA B 125 3.17 -67.09 REMARK 500 THR B 173 -31.76 -132.93 REMARK 500 HIS B 213 78.75 -110.64 REMARK 500 ASN B 217 44.71 37.74 REMARK 500 SER D 177 -117.64 46.44 REMARK 500 REMARK 500 REMARK: NULL DBREF 9CQB A 1 216 PDB 9CQB 9CQB 1 216 DBREF 9CQB B 1 266 PDB 9CQB 9CQB 1 266 DBREF 9CQB D 157 197 UNP P03423 GLYC_HRSVA 157 197 SEQADV 9CQB MET D 155 UNP P03423 INITIATING METHIONINE SEQADV 9CQB GLY D 156 UNP P03423 EXPRESSION TAG SEQADV 9CQB HIS D 198 UNP P03423 EXPRESSION TAG SEQADV 9CQB HIS D 199 UNP P03423 EXPRESSION TAG SEQADV 9CQB HIS D 200 UNP P03423 EXPRESSION TAG SEQADV 9CQB HIS D 201 UNP P03423 EXPRESSION TAG SEQADV 9CQB HIS D 202 UNP P03423 EXPRESSION TAG SEQADV 9CQB HIS D 203 UNP P03423 EXPRESSION TAG SEQRES 1 A 216 GLU ILE VAL VAL THR GLN SER PRO VAL THR LEU SER VAL SEQRES 2 A 216 SER PRO GLY GLU SER ALA ALA LEU SER CYS ARG ALA SER SEQRES 3 A 216 ARG SER VAL GLY SER ARG LEU ALA TRP TYR GLN GLN LYS SEQRES 4 A 216 PRO GLY GLN PRO PRO ARG LEU LEU ILE PHE ALA ALA SER SEQRES 5 A 216 THR ARG GLU SER GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 A 216 GLY SER GLY THR ASP PHE THR LEU ILE ILE SER GLY LEU SEQRES 7 A 216 GLN SER GLU ASP TYR ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 A 216 LYS GLU TRP PRO LEU PHE THR PHE GLY PRO GLY THR THR SEQRES 9 A 216 VAL ASP SER LYS ARG ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 A 216 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 A 216 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 A 216 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 A 216 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 A 216 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 A 216 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 A 216 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 A 216 LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 266 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 B 266 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 B 266 ASP SER ILE THR SER GLY GLN TYR TYR TRP ALA TRP ILE SEQRES 4 B 266 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY SER SEQRES 5 B 266 ILE HIS TYR SER GLY SER THR TYR GLN ASN PRO SER LEU SEQRES 6 B 266 LYS SER ARG LEU THR ILE SER VAL ASP THR SER ARG ASP SEQRES 7 B 266 GLN ILE SER MET LYS LEU SER SER VAL THR VAL ALA GLU SEQRES 8 B 266 SER ALA VAL TYR TYR CYS ALA LYS GLN GLN LEU SER LEU SEQRES 9 B 266 SER PRO VAL GLU ASN TRP PHE ASP PRO TRP GLY GLN GLY SEQRES 10 B 266 THR LEU VAL THR VAL SER SER ALA SER ALA SER THR LYS SEQRES 11 B 266 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 B 266 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 B 266 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 B 266 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 B 266 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 B 266 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 B 266 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 B 266 LYS LYS VAL GLU PRO LYS SER CYS ALA SER LEU VAL PRO SEQRES 19 B 266 ARG GLY SER GLY TRP SER HIS PRO GLN PHE GLU LYS GLY SEQRES 20 B 266 GLY GLY SER GLY GLY GLY SER GLY GLY GLY SER TRP SER SEQRES 21 B 266 HIS PRO GLN PHE GLU LYS SEQRES 1 D 49 MET GLY SER LYS PRO ASN ASN ASP PHE HIS PHE GLU VAL SEQRES 2 D 49 PHE ASN PHE VAL PRO CYS SER ILE CYS SER ASN ASN PRO SEQRES 3 D 49 THR CYS TRP ALA ILE CYS LYS ARG ILE PRO ASN LYS LYS SEQRES 4 D 49 PRO GLY LYS LYS HIS HIS HIS HIS HIS HIS FORMUL 4 HOH *16(H2 O) HELIX 1 AA1 GLN A 79 TYR A 83 5 5 HELIX 2 AA2 SER A 123 SER A 129 1 7 HELIX 3 AA3 LYS A 185 GLU A 189 1 5 HELIX 4 AA4 PRO B 63 LYS B 66 5 4 HELIX 5 AA5 THR B 88 SER B 92 5 5 HELIX 6 AA6 SER B 169 ALA B 171 5 3 HELIX 7 AA7 SER B 200 LEU B 202 5 3 HELIX 8 AA8 LYS B 214 ASN B 217 5 4 HELIX 9 AA9 HIS D 164 PHE D 168 5 5 HELIX 10 AB1 PRO D 172 CYS D 176 5 5 HELIX 11 AB2 ASN D 179 CYS D 186 1 8 SHEET 1 AA1 4 VAL A 4 SER A 7 0 SHEET 2 AA1 4 SER A 18 ALA A 25 -1 O SER A 22 N SER A 7 SHEET 3 AA1 4 ASP A 70 SER A 76 -1 O LEU A 73 N LEU A 21 SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N SER A 63 O ILE A 74 SHEET 1 AA2 6 THR A 10 VAL A 13 0 SHEET 2 AA2 6 THR A 103 SER A 107 1 O THR A 104 N LEU A 11 SHEET 3 AA2 6 VAL A 85 GLN A 90 -1 N TYR A 86 O THR A 103 SHEET 4 AA2 6 LEU A 33 GLN A 38 -1 N TYR A 36 O TYR A 87 SHEET 5 AA2 6 ARG A 45 PHE A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 AA2 6 THR A 53 ARG A 54 -1 O THR A 53 N PHE A 49 SHEET 1 AA3 4 THR A 10 VAL A 13 0 SHEET 2 AA3 4 THR A 103 SER A 107 1 O THR A 104 N LEU A 11 SHEET 3 AA3 4 VAL A 85 GLN A 90 -1 N TYR A 86 O THR A 103 SHEET 4 AA3 4 THR A 98 PHE A 99 -1 O THR A 98 N GLN A 90 SHEET 1 AA4 4 SER A 116 PHE A 120 0 SHEET 2 AA4 4 THR A 131 PHE A 141 -1 O VAL A 135 N PHE A 120 SHEET 3 AA4 4 TYR A 175 SER A 184 -1 O LEU A 177 N LEU A 138 SHEET 4 AA4 4 SER A 161 VAL A 165 -1 N GLN A 162 O THR A 180 SHEET 1 AA5 4 ALA A 155 LEU A 156 0 SHEET 2 AA5 4 LYS A 147 VAL A 152 -1 N VAL A 152 O ALA A 155 SHEET 3 AA5 4 VAL A 193 THR A 199 -1 O GLU A 197 N GLN A 149 SHEET 4 AA5 4 VAL A 207 ASN A 212 -1 O VAL A 207 N VAL A 198 SHEET 1 AA6 4 GLN B 3 SER B 7 0 SHEET 2 AA6 4 LEU B 18 SER B 25 -1 O THR B 21 N SER B 7 SHEET 3 AA6 4 GLN B 79 LEU B 84 -1 O ILE B 80 N CYS B 22 SHEET 4 AA6 4 LEU B 69 ASP B 74 -1 N ASP B 74 O GLN B 79 SHEET 1 AA7 6 LEU B 11 VAL B 12 0 SHEET 2 AA7 6 THR B 118 VAL B 122 1 O THR B 121 N VAL B 12 SHEET 3 AA7 6 ALA B 93 SER B 103 -1 N ALA B 93 O VAL B 120 SHEET 4 AA7 6 TYR B 35 GLN B 41 -1 N ILE B 39 O TYR B 96 SHEET 5 AA7 6 GLU B 48 ILE B 53 -1 O ILE B 53 N TRP B 36 SHEET 6 AA7 6 THR B 59 GLN B 61 -1 O TYR B 60 N SER B 52 SHEET 1 AA8 4 LEU B 11 VAL B 12 0 SHEET 2 AA8 4 THR B 118 VAL B 122 1 O THR B 121 N VAL B 12 SHEET 3 AA8 4 ALA B 93 SER B 103 -1 N ALA B 93 O VAL B 120 SHEET 4 AA8 4 GLU B 108 TRP B 114 -1 O ASP B 112 N LYS B 99 SHEET 1 AA9 4 SER B 133 LEU B 137 0 SHEET 2 AA9 4 THR B 148 TYR B 158 -1 O GLY B 152 N LEU B 137 SHEET 3 AA9 4 TYR B 189 PRO B 198 -1 O VAL B 197 N ALA B 149 SHEET 4 AA9 4 VAL B 176 THR B 178 -1 N HIS B 177 O VAL B 194 SHEET 1 AB1 4 SER B 133 LEU B 137 0 SHEET 2 AB1 4 THR B 148 TYR B 158 -1 O GLY B 152 N LEU B 137 SHEET 3 AB1 4 TYR B 189 PRO B 198 -1 O VAL B 197 N ALA B 149 SHEET 4 AB1 4 VAL B 182 LEU B 183 -1 N VAL B 182 O SER B 190 SHEET 1 AB2 3 THR B 164 TRP B 167 0 SHEET 2 AB2 3 TYR B 207 HIS B 213 -1 O ASN B 210 N SER B 166 SHEET 3 AB2 3 THR B 218 VAL B 224 -1 O THR B 218 N HIS B 213 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.05 SSBOND 2 CYS A 136 CYS A 196 1555 1555 2.04 SSBOND 3 CYS B 22 CYS B 97 1555 1555 2.04 SSBOND 4 CYS B 153 CYS B 209 1555 1555 2.05 SSBOND 5 CYS D 173 CYS D 186 1555 1555 2.01 SSBOND 6 CYS D 176 CYS D 182 1555 1555 2.03 CISPEP 1 SER A 7 PRO A 8 0 -8.75 CISPEP 2 TRP A 94 PRO A 95 0 -0.48 CISPEP 3 TYR A 142 PRO A 143 0 -0.43 CISPEP 4 ASP B 112 PRO B 113 0 -1.18 CISPEP 5 PHE B 159 PRO B 160 0 -2.17 CISPEP 6 GLU B 161 PRO B 162 0 -0.87 CRYST1 67.394 67.394 286.346 90.00 90.00 120.00 P 31 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 0.014838 0.008567 0.000000 0.00000 SCALE2 0.000000 0.017134 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003492 0.00000