HEADER IMMUNE SYSTEM 26-AUG-22 8GPK TITLE CRYSTAL STRUCTURE OF HUMAN ANTI-HIV-1 BROADLY NEUTRALIZING ANTIBODY F6 TITLE 2 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: F6 FAB HEAVY CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: F6 FAB LIGHT CHAIN; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIBODY, FAB, HIV-1, ENV BINDING, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.NIU,B.YANG JRNL AUTH J.NIU,B.YANG JRNL TITL STRUCTURE AND IMMUNE RECOGNITION OF ENV TIMERS FROM TWO ASIA JRNL TITL 2 PREVALENT HIV-1 CIRCULATING RECOMBINANT FORMS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.34 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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) : 3.34 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.71 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 29265 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.246 REMARK 3 R VALUE (WORKING SET) : 0.242 REMARK 3 FREE R VALUE : 0.281 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2955 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 19.7100 - 8.9300 0.98 1264 141 0.2302 0.2669 REMARK 3 2 8.9300 - 7.2000 0.98 1269 138 0.2282 0.2472 REMARK 3 3 7.2000 - 6.3300 1.00 1301 140 0.2544 0.2715 REMARK 3 4 6.3200 - 5.7600 0.99 1257 141 0.2556 0.2815 REMARK 3 5 5.7600 - 5.3600 0.98 1261 149 0.2393 0.3030 REMARK 3 6 5.3600 - 5.0500 1.00 1296 130 0.2139 0.2626 REMARK 3 7 5.0500 - 4.8000 1.00 1254 151 0.2131 0.2322 REMARK 3 8 4.8000 - 4.5900 1.00 1285 162 0.2039 0.2391 REMARK 3 9 4.5900 - 4.4200 1.00 1255 139 0.2057 0.2736 REMARK 3 10 4.4200 - 4.2700 0.98 1299 135 0.2247 0.2717 REMARK 3 11 4.2700 - 4.1400 0.99 1249 156 0.2289 0.2804 REMARK 3 12 4.1400 - 4.0200 1.00 1319 148 0.2271 0.2991 REMARK 3 13 4.0200 - 3.9100 1.00 1263 150 0.2603 0.2887 REMARK 3 14 3.9100 - 3.8200 1.00 1304 115 0.2517 0.3176 REMARK 3 15 3.8200 - 3.7300 1.00 1272 162 0.2571 0.2711 REMARK 3 16 3.7300 - 3.6500 1.00 1276 126 0.2747 0.2791 REMARK 3 17 3.6500 - 3.5800 1.00 1288 169 0.2659 0.3645 REMARK 3 18 3.5800 - 3.5100 0.98 1254 126 0.2911 0.3037 REMARK 3 19 3.5100 - 3.4500 1.00 1284 130 0.3033 0.2961 REMARK 3 20 3.4500 - 3.3900 0.97 1243 156 0.2985 0.3186 REMARK 3 21 3.3900 - 3.3400 0.63 817 91 0.3573 0.3527 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.420 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.280 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 63.58 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 5875 REMARK 3 ANGLE : 0.741 7964 REMARK 3 CHIRALITY : 0.046 900 REMARK 3 PLANARITY : 0.006 1007 REMARK 3 DIHEDRAL : 5.360 810 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): -14.4640 15.8549 -22.6410 REMARK 3 T TENSOR REMARK 3 T11: 0.8583 T22: 0.5322 REMARK 3 T33: 0.6138 T12: -0.0120 REMARK 3 T13: -0.2451 T23: 0.0023 REMARK 3 L TENSOR REMARK 3 L11: 0.9815 L22: -0.1365 REMARK 3 L33: 0.0630 L12: 0.0137 REMARK 3 L13: -0.4615 L23: 0.0509 REMARK 3 S TENSOR REMARK 3 S11: -0.0207 S12: -0.0809 S13: 0.0980 REMARK 3 S21: -0.0402 S22: 0.0598 S23: 0.0405 REMARK 3 S31: 0.1013 S32: 0.0140 S33: -0.0501 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 8GPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ. REMARK 100 THE DEPOSITION ID IS D_1300031831. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-NOV-20 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 : SSRF REMARK 200 BEAMLINE : BL19U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.987 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 : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29265 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 19.710 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.1100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.50 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: NULL REMARK 200 STARTING MODEL: 5BMF REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CITRATE, 20% PEG 3,350., REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K 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 31.13550 REMARK 290 SMTRY3 2 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3500 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20100 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2170 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15400 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 LYS A 225 REMARK 465 SER A 226 REMARK 465 CYS A 227 REMARK 465 ASP A 228 REMARK 465 LYS A 229 REMARK 465 THR A 230 REMARK 465 HIS A 231 REMARK 465 THR A 232 REMARK 465 GLU B 218 REMARK 465 CYS B 219 REMARK 465 GLY B 220 REMARK 465 SER C 131 REMARK 465 VAL C 132 REMARK 465 PHE C 133 REMARK 465 PRO C 134 REMARK 465 LEU C 135 REMARK 465 ALA C 136 REMARK 465 PRO C 137 REMARK 465 SER C 138 REMARK 465 SER C 139 REMARK 465 LYS C 140 REMARK 465 SER C 141 REMARK 465 THR C 142 REMARK 465 SER C 143 REMARK 465 GLY C 144 REMARK 465 GLY C 145 REMARK 465 THR C 146 REMARK 465 ALA C 147 REMARK 465 ALA C 148 REMARK 465 LEU C 149 REMARK 465 GLY C 150 REMARK 465 ASN C 166 REMARK 465 SER C 167 REMARK 465 GLY C 168 REMARK 465 ALA C 169 REMARK 465 LEU C 170 REMARK 465 THR C 171 REMARK 465 VAL C 193 REMARK 465 THR C 194 REMARK 465 VAL C 195 REMARK 465 PRO C 196 REMARK 465 SER C 197 REMARK 465 SER C 198 REMARK 465 SER C 199 REMARK 465 LEU C 200 REMARK 465 GLY C 201 REMARK 465 THR C 202 REMARK 465 GLN C 203 REMARK 465 THR C 204 REMARK 465 TYR C 205 REMARK 465 ILE C 206 REMARK 465 LYS C 217 REMARK 465 VAL C 218 REMARK 465 ASP C 219 REMARK 465 LYS C 220 REMARK 465 LYS C 221 REMARK 465 VAL C 222 REMARK 465 GLU C 223 REMARK 465 PRO C 224 REMARK 465 LYS C 225 REMARK 465 SER C 226 REMARK 465 CYS C 227 REMARK 465 ASP C 228 REMARK 465 LYS C 229 REMARK 465 THR C 230 REMARK 465 HIS C 231 REMARK 465 THR C 232 REMARK 465 THR D 114 REMARK 465 VAL D 115 REMARK 465 ALA D 116 REMARK 465 ALA D 117 REMARK 465 PRO D 118 REMARK 465 SER D 119 REMARK 465 VAL D 120 REMARK 465 PHE D 121 REMARK 465 ILE D 122 REMARK 465 PHE D 123 REMARK 465 PRO D 124 REMARK 465 PRO D 125 REMARK 465 SER D 126 REMARK 465 ASP D 127 REMARK 465 SER D 128 REMARK 465 GLN D 129 REMARK 465 LEU D 130 REMARK 465 LYS D 131 REMARK 465 SER D 132 REMARK 465 GLY D 133 REMARK 465 THR D 134 REMARK 465 ALA D 135 REMARK 465 SER D 136 REMARK 465 VAL D 137 REMARK 465 VAL D 138 REMARK 465 CYS D 139 REMARK 465 LEU D 140 REMARK 465 LEU D 141 REMARK 465 ASN D 142 REMARK 465 ASN D 143 REMARK 465 PHE D 144 REMARK 465 TYR D 145 REMARK 465 PRO D 146 REMARK 465 ARG D 147 REMARK 465 GLU D 148 REMARK 465 ALA D 149 REMARK 465 LYS D 150 REMARK 465 VAL D 151 REMARK 465 GLN D 152 REMARK 465 TRP D 153 REMARK 465 LYS D 154 REMARK 465 VAL D 155 REMARK 465 ASP D 156 REMARK 465 ASN D 157 REMARK 465 ALA D 158 REMARK 465 LEU D 159 REMARK 465 GLN D 160 REMARK 465 SER D 161 REMARK 465 THR D 177 REMARK 465 TYR D 178 REMARK 465 SER D 179 REMARK 465 LEU D 180 REMARK 465 SER D 181 REMARK 465 SER D 182 REMARK 465 THR D 183 REMARK 465 LEU D 184 REMARK 465 THR D 185 REMARK 465 LEU D 186 REMARK 465 SER D 187 REMARK 465 LYS D 188 REMARK 465 ALA D 189 REMARK 465 ASP D 190 REMARK 465 TYR D 191 REMARK 465 GLU D 192 REMARK 465 LYS D 193 REMARK 465 HIS D 194 REMARK 465 LYS D 195 REMARK 465 VAL D 196 REMARK 465 TYR D 197 REMARK 465 ALA D 198 REMARK 465 CYS D 199 REMARK 465 GLU D 200 REMARK 465 VAL D 201 REMARK 465 THR D 202 REMARK 465 HIS D 203 REMARK 465 GLN D 204 REMARK 465 GLY D 205 REMARK 465 LEU D 206 REMARK 465 SER D 207 REMARK 465 SER D 208 REMARK 465 PRO D 209 REMARK 465 VAL D 210 REMARK 465 THR D 211 REMARK 465 LYS D 212 REMARK 465 SER D 213 REMARK 465 PHE D 214 REMARK 465 ASN D 215 REMARK 465 ARG D 216 REMARK 465 GLY D 217 REMARK 465 GLU D 218 REMARK 465 CYS D 219 REMARK 465 GLY D 220 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 SER A 15 -1.87 77.23 REMARK 500 ASP A 104 -8.27 70.23 REMARK 500 LEU B 52 -66.42 -106.04 REMARK 500 ASN B 143 72.16 54.06 REMARK 500 SER B 173 1.63 -66.57 REMARK 500 LYS B 195 -67.12 -103.61 REMARK 500 SER D 20 81.28 -150.20 REMARK 500 LEU D 29 78.29 -101.74 REMARK 500 ASN D 31 -169.98 -110.45 REMARK 500 SER D 57 -22.75 -141.80 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-34190 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-34192 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-34193 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-34194 RELATED DB: EMDB DBREF 8GPK A 1 232 PDB 8GPK 8GPK 1 232 DBREF 8GPK B 1 220 PDB 8GPK 8GPK 1 220 DBREF 8GPK C 1 232 PDB 8GPK 8GPK 1 232 DBREF 8GPK D 1 220 PDB 8GPK 8GPK 1 220 SEQRES 1 A 232 GLN VAL GLN LEU GLN GLN TRP GLY THR GLY LEU LEU LYS SEQRES 2 A 232 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL TYR GLY SEQRES 3 A 232 VAL SER LEU ARG GLY TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 A 232 SER PRO LYS LYS GLY LEU GLU TRP ILE GLY GLU ILE ASP SEQRES 5 A 232 GLU ILE GLY ARG THR LYS TYR SER GLN SER LEU ARG SER SEQRES 6 A 232 ARG ALA THR LEU SER ILE ASP THR SER LYS LYS GLN PHE SEQRES 7 A 232 SER LEU ARG LEU THR SER VAL THR ALA ALA ASP MET ALA SEQRES 8 A 232 THR TYR TYR CYS ALA ARG TRP ARG LEU MET MET VAL ASP SEQRES 9 A 232 GLU VAL THR ARG HIS GLY MET ASP VAL TRP SER GLN GLY SEQRES 10 A 232 THR MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 A 232 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 A 232 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 A 232 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 A 232 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 A 232 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 A 232 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 A 232 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 A 232 VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 B 220 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU SER VAL SEQRES 2 B 220 ALA PRO GLY GLU ALA ALA SER ILE SER CYS ARG SER THR SEQRES 3 B 220 GLN SER LEU LEU ASN ARG ASN GLY ASP ASN TYR LEU GLU SEQRES 4 B 220 TRP TYR LEU ARG ARG PRO GLY ARG SER PRO GLN LEU LEU SEQRES 5 B 220 ILE TYR LEU GLY SER GLU ARG ALA LEU GLY VAL PRO ASP SEQRES 6 B 220 ARG PHE SER GLY SER GLY SER GLY ARG ASP PHE THR LEU SEQRES 7 B 220 LYS ILE SER ARG VAL GLU ALA GLN ASP VAL GLY THR TYR SEQRES 8 B 220 TYR CYS LEU GLN THR ARG GLN GLY ALA PHE THR PHE GLY SEQRES 9 B 220 GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 B 220 PRO SER VAL PHE ILE PHE PRO PRO SER ASP SER GLN LEU SEQRES 11 B 220 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 B 220 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 B 220 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 B 220 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 B 220 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 B 220 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 B 220 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS GLY SEQRES 1 C 232 GLN VAL GLN LEU GLN GLN TRP GLY THR GLY LEU LEU LYS SEQRES 2 C 232 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL TYR GLY SEQRES 3 C 232 VAL SER LEU ARG GLY TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 C 232 SER PRO LYS LYS GLY LEU GLU TRP ILE GLY GLU ILE ASP SEQRES 5 C 232 GLU ILE GLY ARG THR LYS TYR SER GLN SER LEU ARG SER SEQRES 6 C 232 ARG ALA THR LEU SER ILE ASP THR SER LYS LYS GLN PHE SEQRES 7 C 232 SER LEU ARG LEU THR SER VAL THR ALA ALA ASP MET ALA SEQRES 8 C 232 THR TYR TYR CYS ALA ARG TRP ARG LEU MET MET VAL ASP SEQRES 9 C 232 GLU VAL THR ARG HIS GLY MET ASP VAL TRP SER GLN GLY SEQRES 10 C 232 THR MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 C 232 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 C 232 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 C 232 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 C 232 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 C 232 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 C 232 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 C 232 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 C 232 VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 D 220 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU SER VAL SEQRES 2 D 220 ALA PRO GLY GLU ALA ALA SER ILE SER CYS ARG SER THR SEQRES 3 D 220 GLN SER LEU LEU ASN ARG ASN GLY ASP ASN TYR LEU GLU SEQRES 4 D 220 TRP TYR LEU ARG ARG PRO GLY ARG SER PRO GLN LEU LEU SEQRES 5 D 220 ILE TYR LEU GLY SER GLU ARG ALA LEU GLY VAL PRO ASP SEQRES 6 D 220 ARG PHE SER GLY SER GLY SER GLY ARG ASP PHE THR LEU SEQRES 7 D 220 LYS ILE SER ARG VAL GLU ALA GLN ASP VAL GLY THR TYR SEQRES 8 D 220 TYR CYS LEU GLN THR ARG GLN GLY ALA PHE THR PHE GLY SEQRES 9 D 220 GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 D 220 PRO SER VAL PHE ILE PHE PRO PRO SER ASP SER GLN LEU SEQRES 11 D 220 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 D 220 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 D 220 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 D 220 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 D 220 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 D 220 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 D 220 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS GLY HELIX 1 AA1 SER A 60 SER A 65 1 6 HELIX 2 AA2 SER A 198 LEU A 200 5 3 HELIX 3 AA3 LYS A 212 ASN A 215 5 4 HELIX 4 AA4 GLU B 84 VAL B 88 5 5 HELIX 5 AA5 SER B 126 GLY B 133 1 8 HELIX 6 AA6 LYS B 188 HIS B 194 1 7 HELIX 7 AA7 THR C 86 MET C 90 5 5 HELIX 8 AA8 GLU D 84 VAL D 88 5 5 SHEET 1 AA1 4 GLN A 3 GLY A 8 0 SHEET 2 AA1 4 LEU A 18 TYR A 25 -1 O TYR A 25 N GLN A 3 SHEET 3 AA1 4 GLN A 77 LEU A 82 -1 O LEU A 82 N LEU A 18 SHEET 4 AA1 4 ALA A 67 ASP A 72 -1 N SER A 70 O SER A 79 SHEET 1 AA2 7 LEU A 11 LEU A 12 0 SHEET 2 AA2 7 TRP A 34 SER A 40 0 SHEET 3 AA2 7 GLY A 44 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 4 AA2 7 THR A 57 TYR A 59 -1 O LYS A 58 N GLU A 50 SHEET 5 AA2 7 ALA A 91 MET A 102 -1 O THR A 92 N GLN A 39 SHEET 6 AA2 7 VAL A 106 TRP A 114 -1 O HIS A 109 N ARG A 99 SHEET 7 AA2 7 THR A 118 VAL A 122 -1 O VAL A 120 N ALA A 91 SHEET 1 AA3 5 VAL A 132 LEU A 135 0 SHEET 2 AA3 5 THR A 146 TYR A 156 -1 O GLY A 150 N LEU A 135 SHEET 3 AA3 5 VAL A 174 THR A 176 0 SHEET 4 AA3 5 VAL A 180 LEU A 181 0 SHEET 5 AA3 5 TYR A 187 PRO A 196 -1 O SER A 188 N VAL A 180 SHEET 1 AA4 3 THR A 162 TRP A 165 0 SHEET 2 AA4 3 ILE A 206 HIS A 211 -1 O ASN A 208 N SER A 164 SHEET 3 AA4 3 THR A 216 LYS A 221 -1 O THR A 216 N HIS A 211 SHEET 1 AA5 4 MET B 4 GLN B 6 0 SHEET 2 AA5 4 ALA B 19 SER B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA5 4 ASP B 75 ILE B 80 -1 O PHE B 76 N CYS B 23 SHEET 4 AA5 4 PHE B 67 SER B 72 -1 N SER B 68 O LYS B 79 SHEET 1 AA6 6 SER B 10 VAL B 13 0 SHEET 2 AA6 6 THR B 107 ILE B 111 1 O GLU B 110 N LEU B 11 SHEET 3 AA6 6 GLY B 89 GLN B 95 -1 N GLY B 89 O LEU B 109 SHEET 4 AA6 6 LEU B 38 ARG B 43 -1 N ARG B 43 O THR B 90 SHEET 5 AA6 6 PRO B 49 TYR B 54 -1 O LEU B 52 N TRP B 40 SHEET 6 AA6 6 GLU B 58 ARG B 59 -1 O GLU B 58 N TYR B 54 SHEET 1 AA7 4 SER B 119 PHE B 123 0 SHEET 2 AA7 4 THR B 134 PHE B 144 -1 O LEU B 140 N PHE B 121 SHEET 3 AA7 4 TYR B 178 SER B 187 -1 O LEU B 180 N LEU B 141 SHEET 4 AA7 4 SER B 164 VAL B 168 -1 N SER B 167 O SER B 181 SHEET 1 AA8 4 ALA B 158 GLN B 160 0 SHEET 2 AA8 4 LYS B 150 VAL B 155 -1 N TRP B 153 O GLN B 160 SHEET 3 AA8 4 TYR B 197 THR B 202 -1 O GLU B 200 N GLN B 152 SHEET 4 AA8 4 VAL B 210 PHE B 214 -1 O VAL B 210 N VAL B 201 SHEET 1 AA9 4 GLN C 3 GLY C 8 0 SHEET 2 AA9 4 LEU C 18 TYR C 25 -1 O TYR C 25 N GLN C 3 SHEET 3 AA9 4 GLN C 77 LEU C 82 -1 O LEU C 82 N LEU C 18 SHEET 4 AA9 4 ALA C 67 ASP C 72 -1 N ASP C 72 O GLN C 77 SHEET 1 AB1 7 LEU C 11 LEU C 12 0 SHEET 2 AB1 7 TYR C 32 SER C 40 0 SHEET 3 AB1 7 GLY C 44 ILE C 51 -1 O ILE C 48 N TRP C 36 SHEET 4 AB1 7 THR C 57 TYR C 59 -1 O LYS C 58 N GLU C 50 SHEET 5 AB1 7 ALA C 91 MET C 102 -1 O TRP C 98 N TYR C 33 SHEET 6 AB1 7 VAL C 106 TRP C 114 -1 O HIS C 109 N ARG C 99 SHEET 7 AB1 7 THR C 118 VAL C 122 -1 O VAL C 120 N ALA C 91 SHEET 1 AB2 6 LEU C 152 TYR C 156 0 SHEET 2 AB2 6 THR C 162 TRP C 165 0 SHEET 3 AB2 6 GLY C 173 THR C 176 0 SHEET 4 AB2 6 VAL C 180 LEU C 181 0 SHEET 5 AB2 6 TYR C 187 VAL C 192 -1 O SER C 188 N VAL C 180 SHEET 6 AB2 6 ASN C 208 ASN C 210 -1 O ASN C 210 N THR C 162 SHEET 1 AB3 4 MET D 4 SER D 7 0 SHEET 2 AB3 4 ALA D 19 SER D 25 -1 O SER D 22 N SER D 7 SHEET 3 AB3 4 ASP D 75 ILE D 80 -1 O LEU D 78 N ILE D 21 SHEET 4 AB3 4 PHE D 67 SER D 72 -1 N SER D 68 O LYS D 79 SHEET 1 AB4 6 SER D 10 VAL D 13 0 SHEET 2 AB4 6 THR D 107 ILE D 111 1 O GLU D 110 N LEU D 11 SHEET 3 AB4 6 GLY D 89 GLN D 95 -1 N TYR D 91 O THR D 107 SHEET 4 AB4 6 LEU D 38 ARG D 43 -1 N TYR D 41 O TYR D 92 SHEET 5 AB4 6 PRO D 49 TYR D 54 -1 O GLN D 50 N LEU D 42 SHEET 6 AB4 6 GLU D 58 ARG D 59 -1 O GLU D 58 N TYR D 54 SSBOND 1 CYS A 22 CYS A 95 1555 1555 2.03 SSBOND 2 CYS A 151 CYS A 207 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 93 1555 1555 2.04 SSBOND 4 CYS B 139 CYS B 199 1555 1555 2.03 SSBOND 5 CYS C 22 CYS C 95 1555 1555 2.03 SSBOND 6 CYS C 151 CYS C 207 1555 1555 2.03 SSBOND 7 CYS D 23 CYS D 93 1555 1555 2.04 CISPEP 1 PHE A 157 PRO A 158 0 -9.29 CISPEP 2 TYR B 145 PRO B 146 0 -2.18 CISPEP 3 SER D 7 PRO D 8 0 -10.03 CRYST1 91.245 62.271 97.843 90.00 105.18 90.00 P 1 21 1 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 0.010960 0.000000 0.002973 0.00000 SCALE2 0.000000 0.016059 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010590 0.00000