HEADER IMMUNE SYSTEM 08-AUG-22 8AON TITLE OXIDOREDUCTASE FRAGMENT OF HUMAN QSOX1 IN COMPLEX WITH A FAB FRAGMENT TITLE 2 OF A HUMANIZED ANTI-QSOX1 ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: OXIDOREDUCTASE FRAGMENT OF HUMAN QSOX1; COMPND 3 CHAIN: B00A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEAVY CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LIGHT CHAIN; COMPND 11 CHAIN: C; COMPND 12 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: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HEK293-F; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: HEK293-F KEYWDS ANTIBODY, HUMANIZED, FAB, QSOX1, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR L.KHMELNITSKY,D.FASS JRNL AUTH A.TENNENHOUSE,L.KHMELNITSKY,N.YESHAYA,A.NORONHA,M.LINDZEN, JRNL AUTH 2 R.KHALAILA,I.ZARETSKY,Y.FRIDMANN SIRKIS,Y.GALON-WOLFENSON, JRNL AUTH 3 J.ABRAMSON,Y.YARDEN,D.FASS,S.J.FLEISHMAN JRNL TITL RELIABLE ENERGY-BASED ANTIBODY HUMANIZATION AND JRNL TITL 2 STABILIZATION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20_4459 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.36 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.250 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 77284 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.204 REMARK 3 R VALUE (WORKING SET) : 0.198 REMARK 3 FREE R VALUE : 0.259 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 7728 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 49.3600 - 6.5200 0.99 2295 259 0.1494 0.2004 REMARK 3 2 6.5200 - 5.1800 0.99 2313 256 0.1612 0.1847 REMARK 3 3 5.1800 - 4.5200 0.99 2309 255 0.1353 0.2022 REMARK 3 4 4.5200 - 4.1100 0.99 2327 251 0.1497 0.2032 REMARK 3 5 4.1100 - 3.8200 0.99 2305 254 0.1623 0.1906 REMARK 3 6 3.8200 - 3.5900 0.99 2328 262 0.1791 0.2303 REMARK 3 7 3.5900 - 3.4100 0.99 2290 257 0.2001 0.3114 REMARK 3 8 3.4100 - 3.2600 0.99 2306 255 0.2124 0.3031 REMARK 3 9 3.2600 - 3.1400 0.99 2313 260 0.2141 0.3023 REMARK 3 10 3.1400 - 3.0300 1.00 2318 254 0.2348 0.2947 REMARK 3 11 3.0300 - 2.9300 1.00 2330 261 0.2281 0.2932 REMARK 3 12 2.9300 - 2.8500 1.00 2333 257 0.2385 0.3065 REMARK 3 13 2.8500 - 2.7800 1.00 2304 255 0.2294 0.3522 REMARK 3 14 2.7700 - 2.7100 1.00 2306 254 0.2360 0.3192 REMARK 3 15 2.7100 - 2.6500 1.00 2339 262 0.2358 0.2872 REMARK 3 16 2.6500 - 2.5900 1.00 2356 265 0.2374 0.3299 REMARK 3 17 2.5900 - 2.5400 1.00 2264 251 0.2435 0.3150 REMARK 3 18 2.5400 - 2.4900 1.00 2356 263 0.2388 0.3245 REMARK 3 19 2.4900 - 2.4500 1.00 2275 255 0.2450 0.2994 REMARK 3 20 2.4500 - 2.4000 1.00 2347 264 0.2496 0.3053 REMARK 3 21 2.4000 - 2.3700 1.00 2334 257 0.2749 0.2883 REMARK 3 22 2.3700 - 2.3300 1.00 2326 261 0.2668 0.3844 REMARK 3 23 2.3300 - 2.2900 1.00 2301 254 0.2838 0.3291 REMARK 3 24 2.2900 - 2.2600 1.00 2368 264 0.2903 0.3751 REMARK 3 25 2.2600 - 2.2300 1.00 2312 253 0.2941 0.3352 REMARK 3 26 2.2300 - 2.2000 1.00 2352 262 0.2990 0.3573 REMARK 3 27 2.2000 - 2.1800 1.00 2270 252 0.3165 0.3224 REMARK 3 28 2.1800 - 2.1500 1.00 2349 261 0.3197 0.3783 REMARK 3 29 2.1500 - 2.1200 1.00 2373 260 0.3438 0.4113 REMARK 3 30 2.1200 - 2.1000 1.00 2257 254 0.3690 0.4318 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) : 0.343 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.475 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 46.08 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.26 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 5196 REMARK 3 ANGLE : 0.908 7096 REMARK 3 CHIRALITY : 0.055 798 REMARK 3 PLANARITY : 0.008 920 REMARK 3 DIHEDRAL : 7.295 740 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 8AON COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292124727. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-FEB-22 REMARK 200 TEMPERATURE (KELVIN) : 77 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID30B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102949 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 49.360 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : 0.10500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.82 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: 4IJ3 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.76 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM PHOSPHATE DIBASIC, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K 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 49.36050 REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28490 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B00A, B, C 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 B 29 REMARK 465 SER B 30 REMARK 465 HIS B 31 REMARK 465 MET B 32 REMARK 465 SER B 33 REMARK 465 ALA B 34 REMARK 465 LEU B 269 REMARK 465 THR B 270 REMARK 465 ARG B 271 REMARK 465 GLU B 272 REMARK 465 LYS B 134 REMARK 465 SER B 135 REMARK 465 THR B 136 REMARK 465 SER B 137 REMARK 465 GLY B 138 REMARK 465 ASP B 222 REMARK 465 LYS B 223 REMARK 465 THR B 224 REMARK 465 HIS B 225 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU B 104 CG CD OE1 OE2 REMARK 470 HIS B 158 CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 172 CG CD CE NZ REMARK 470 GLU B 174 CG CD OE1 OE2 REMARK 470 LYS B 211 CG CD CE NZ REMARK 470 PHE B 258 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN B 1 CG CD OE1 NE2 REMARK 470 ARG B 56 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 71 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 86 CG CD CE NZ REMARK 470 LYS C 45 CG CD CE NZ REMARK 470 LYS C 145 CG CD CE NZ REMARK 470 GLN C 147 CG CD OE1 NE2 REMARK 470 LYS C 149 CG CD CE NZ REMARK 470 LEU C 154 CG CD1 CD2 REMARK 470 LYS C 169 CG CD CE NZ REMARK 470 LYS C 188 CG CD CE NZ REMARK 470 LYS C 190 CG CD CE NZ REMARK 470 GLU C 195 CG CD OE1 OE2 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 LYS0A 228 O HOH0A 401 2.05 REMARK 500 OD2 ASP B 98 O HOH B 301 2.12 REMARK 500 OE2 GLU0A 169 O HOH0A 402 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH0A 401 O HOH B 321 2345 2.14 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 ASN0A 114 68.97 61.67 REMARK 500 SER B 74 -45.72 -138.34 REMARK 500 SER B 132 -168.52 -104.67 REMARK 500 ASP B 149 70.16 64.50 REMARK 500 SER C 30 -125.32 57.01 REMARK 500 ALA C 51 -46.85 83.73 REMARK 500 LYS C 169 -60.69 -102.59 REMARK 500 ALA C 184 -70.14 -60.97 REMARK 500 LYS C 190 -71.50 -115.04 REMARK 500 PRO C 204 106.51 -54.96 REMARK 500 ARG C 211 105.10 -58.34 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4IJ3 RELATED DB: PDB REMARK 900 4IJ3 CONTAINS THE SAME PROTEIN IN COMPLEX WITH A DIFFERENT FAB REMARK 900 RELATED ID: 5D96 RELATED DB: PDB REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH A DIFFERENT FAB DBREF 8AON0A 33 272 UNP A8K4C2 A8K4C2_HUMAN 33 272 DBREF 8AON B 1 225 PDB 8AON 8AON 1 225 DBREF 8AON C 1 214 PDB 8AON 8AON 1 214 SEQADV 8AON GLY0A 29 UNP A8K4C2 EXPRESSION TAG SEQADV 8AON SER0A 30 UNP A8K4C2 EXPRESSION TAG SEQADV 8AON HIS0A 31 UNP A8K4C2 EXPRESSION TAG SEQADV 8AON MET0A 32 UNP A8K4C2 EXPRESSION TAG SEQRES 10A 244 GLY SER HIS MET SER ALA LEU TYR SER PRO SER ASP PRO SEQRES 20A 244 LEU THR LEU LEU GLN ALA ASP THR VAL ARG GLY ALA VAL SEQRES 30A 244 LEU GLY SER ARG SER ALA TRP ALA VAL GLU PHE PHE ALA SEQRES 40A 244 SER TRP CYS GLY HIS CYS ILE ALA PHE ALA PRO THR TRP SEQRES 50A 244 LYS ALA LEU ALA GLU ASP VAL LYS ALA TRP ARG PRO ALA SEQRES 60A 244 LEU TYR LEU ALA ALA LEU ASP CYS ALA GLU GLU THR ASN SEQRES 70A 244 SER ALA VAL CYS ARG ASP PHE ASN ILE PRO GLY PHE PRO SEQRES 80A 244 THR VAL ARG PHE PHE LYS ALA PHE THR LYS ASN GLY SER SEQRES 90A 244 GLY ALA VAL PHE PRO VAL ALA GLY ALA ASP VAL GLN THR SEQRES 100A 244 LEU ARG GLU ARG LEU ILE ASP ALA LEU GLU SER HIS HIS SEQRES 110A 244 ASP THR TRP PRO PRO ALA CYS PRO PRO LEU GLU PRO ALA SEQRES 120A 244 LYS LEU GLU GLU ILE ASP GLY PHE PHE ALA ARG ASN ASN SEQRES 130A 244 GLU GLU TYR LEU ALA LEU ILE PHE GLU LYS GLY GLY SER SEQRES 140A 244 TYR LEU ALA ARG GLU VAL ALA LEU ASP LEU SER GLN HIS SEQRES 150A 244 LYS GLY VAL ALA VAL ARG ARG VAL LEU ASN THR GLU ALA SEQRES 160A 244 ASN VAL VAL ARG LYS PHE GLY VAL THR ASP PHE PRO SER SEQRES 170A 244 CYS TYR LEU LEU PHE ARG ASN GLY SER VAL SER ARG VAL SEQRES 180A 244 PRO VAL LEU MET GLU SER ARG SER PHE TYR THR ALA TYR SEQRES 190A 244 LEU GLN ARG LEU SER GLY LEU THR ARG GLU SEQRES 1 B 225 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 225 PRO GLY ARG SER LEU ARG LEU SER CYS THR VAL SER GLY SEQRES 3 B 225 PHE SER LEU THR GLY TYR GLY VAL ASN TRP PHE ARG GLN SEQRES 4 B 225 ALA PRO GLY LYS GLY LEU GLU TRP LEU GLY MET ILE TRP SEQRES 5 B 225 GLY ASP GLY ARG THR ASP TYR THR ALA SER VAL LYS GLY SEQRES 6 B 225 ARG PHE THR ILE SER ARG ASP GLY SER LYS SER ILE ALA SEQRES 7 B 225 TYR LEU GLN MET ASN SER LEU LYS THR GLU ASP THR ALA SEQRES 8 B 225 VAL TYR TYR CYS ALA SER ASP TYR TYR GLY SER GLY SER SEQRES 9 B 225 PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 B 225 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 B 225 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 B 225 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 B 225 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 B 225 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 B 225 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 B 225 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 B 225 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 18 B 225 ASP LYS THR HIS SEQRES 1 C 214 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 C 214 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS ALA SER SEQRES 3 C 214 GLN ASP VAL SER THR ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 C 214 PRO GLY GLN PRO PRO LYS LEU LEU ILE HIS SER ALA SER SEQRES 5 C 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE SER GLY SER SEQRES 6 C 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 C 214 GLN ALA GLU ASP VAL ALA VAL TYR TYR CYS GLN GLN HIS SEQRES 8 C 214 TYR SER ILE PRO LEU THR PHE GLY GLN GLY THR ARG LEU SEQRES 9 C 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 C 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 C 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 C 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 C 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 C 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 C 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 C 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 C 214 PHE ASN ARG GLY GLU CYS HET GOL 0A 301 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 GOL C3 H8 O3 FORMUL 5 HOH *211(H2 O) HELIX 1 AA1 THR0A 49 LEU0A 55 1 7 HELIX 2 AA2 CYS0A 70 VAL0A 87 1 18 HELIX 3 AA3 LYS0A 88 ARG0A 91 5 4 HELIX 4 AA4 GLU0A 103 THR0A 105 5 3 HELIX 5 AA5 ASN0A 106 ASN0A 114 1 9 HELIX 6 AA6 ASP0A 142 GLU0A 155 1 14 HELIX 7 AA7 LYS0A 172 GLY0A 178 1 7 HELIX 8 AA8 GLY0A 178 ASN0A 183 1 6 HELIX 9 AA9 TYR0A 198 LEU0A 207 1 10 HELIX 10 AB1 GLU0A 222 PHE0A 229 1 8 HELIX 11 AB2 SER0A 255 ARG0A 265 1 11 HELIX 12 AB3 LYS B 86 THR B 90 5 5 HELIX 13 AB4 SER B 161 ALA B 163 5 3 HELIX 14 AB5 SER B 192 LEU B 194 5 3 HELIX 15 AB6 LYS B 206 ASN B 209 5 4 HELIX 16 AB7 GLN C 79 VAL C 83 5 5 HELIX 17 AB8 SER C 121 SER C 127 1 7 HELIX 18 AB9 LYS C 183 HIS C 189 1 7 SHEET 1 AA1 5 THR0A 43 LEU0A 44 0 SHEET 2 AA1 5 LEU0A 94 ASP0A 100 1 O LEU0A 96 N THR0A 43 SHEET 3 AA1 5 ALA0A 60 PHE0A 66 1 N ALA0A 62 O ALA0A 97 SHEET 4 AA1 5 THR0A 120 PHE0A 124 -1 O PHE0A 124 N TRP0A 61 SHEET 5 AA1 5 ALA0A 134 PHE0A 136 -1 O ALA0A 134 N PHE0A 123 SHEET 1 AA2 4 VAL0A 213 LEU0A 219 0 SHEET 2 AA2 4 TYR0A 187 GLU0A 193 1 N ALA0A 189 O ALA0A 214 SHEET 3 AA2 4 SER0A 236 PHE0A 241 -1 O TYR0A 238 N LEU0A 190 SHEET 4 AA2 4 VAL0A 246 ARG0A 248 -1 O SER0A 247 N LEU0A 239 SHEET 1 AA3 4 GLN B 3 SER B 7 0 SHEET 2 AA3 4 LEU B 18 SER B 25 -1 O SER B 25 N GLN B 3 SHEET 3 AA3 4 ILE B 77 MET B 82 -1 O ALA B 78 N CYS B 22 SHEET 4 AA3 4 PHE B 67 ARG B 71 -1 N SER B 70 O TYR B 79 SHEET 1 AA4 6 LEU B 11 VAL B 12 0 SHEET 2 AA4 6 THR B 112 VAL B 116 1 O THR B 115 N VAL B 12 SHEET 3 AA4 6 ALA B 91 ASP B 98 -1 N TYR B 93 O THR B 112 SHEET 4 AA4 6 VAL B 34 GLN B 39 -1 N PHE B 37 O TYR B 94 SHEET 5 AA4 6 GLU B 46 ILE B 51 -1 O GLY B 49 N TRP B 36 SHEET 6 AA4 6 THR B 57 TYR B 59 -1 O ASP B 58 N MET B 50 SHEET 1 AA5 4 LEU B 11 VAL B 12 0 SHEET 2 AA5 4 THR B 112 VAL B 116 1 O THR B 115 N VAL B 12 SHEET 3 AA5 4 ALA B 91 ASP B 98 -1 N TYR B 93 O THR B 112 SHEET 4 AA5 4 PHE B 105 TRP B 108 -1 O TYR B 107 N SER B 97 SHEET 1 AA6 4 SER B 125 LEU B 129 0 SHEET 2 AA6 4 THR B 140 TYR B 150 -1 O LEU B 146 N PHE B 127 SHEET 3 AA6 4 TYR B 181 PRO B 190 -1 O LEU B 183 N VAL B 147 SHEET 4 AA6 4 VAL B 168 THR B 170 -1 N HIS B 169 O VAL B 186 SHEET 1 AA7 4 SER B 125 LEU B 129 0 SHEET 2 AA7 4 THR B 140 TYR B 150 -1 O LEU B 146 N PHE B 127 SHEET 3 AA7 4 TYR B 181 PRO B 190 -1 O LEU B 183 N VAL B 147 SHEET 4 AA7 4 VAL B 174 LEU B 175 -1 N VAL B 174 O SER B 182 SHEET 1 AA8 3 THR B 156 TRP B 159 0 SHEET 2 AA8 3 TYR B 199 HIS B 205 -1 O ASN B 202 N SER B 158 SHEET 3 AA8 3 THR B 210 VAL B 216 -1 O VAL B 216 N TYR B 199 SHEET 1 AA9 4 MET C 4 SER C 7 0 SHEET 2 AA9 4 ALA C 19 ALA C 25 -1 O LYS C 24 N THR C 5 SHEET 3 AA9 4 ASP C 70 ILE C 75 -1 O ILE C 75 N ALA C 19 SHEET 4 AA9 4 PHE C 62 SER C 67 -1 N SER C 63 O THR C 74 SHEET 1 AB1 6 SER C 10 SER C 14 0 SHEET 2 AB1 6 THR C 102 LYS C 107 1 O LYS C 107 N VAL C 13 SHEET 3 AB1 6 ALA C 84 GLN C 90 -1 N ALA C 84 O LEU C 104 SHEET 4 AB1 6 VAL C 33 GLN C 38 -1 N ALA C 34 O GLN C 89 SHEET 5 AB1 6 LYS C 45 HIS C 49 -1 O LEU C 47 N TRP C 35 SHEET 6 AB1 6 TYR C 53 ARG C 54 -1 O TYR C 53 N HIS C 49 SHEET 1 AB2 4 SER C 10 SER C 14 0 SHEET 2 AB2 4 THR C 102 LYS C 107 1 O LYS C 107 N VAL C 13 SHEET 3 AB2 4 ALA C 84 GLN C 90 -1 N ALA C 84 O LEU C 104 SHEET 4 AB2 4 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90 SHEET 1 AB3 4 SER C 114 PHE C 118 0 SHEET 2 AB3 4 THR C 129 PHE C 139 -1 O LEU C 135 N PHE C 116 SHEET 3 AB3 4 TYR C 173 SER C 182 -1 O LEU C 179 N VAL C 132 SHEET 4 AB3 4 SER C 159 VAL C 163 -1 N SER C 162 O SER C 176 SHEET 1 AB4 4 ALA C 153 GLN C 155 0 SHEET 2 AB4 4 LYS C 145 VAL C 150 -1 N TRP C 148 O GLN C 155 SHEET 3 AB4 4 VAL C 191 THR C 197 -1 O GLU C 195 N GLN C 147 SHEET 4 AB4 4 VAL C 205 ASN C 210 -1 O PHE C 209 N TYR C 192 SSBOND 1 CYS0A 70 CYS0A 73 1555 1555 2.10 SSBOND 2 CYS0A 101 CYS0A 110 1555 1555 2.03 SSBOND 3 CYS B 22 CYS B 95 1555 1555 2.04 SSBOND 4 CYS B 145 CYS B 201 1555 1555 2.04 SSBOND 5 CYS B 221 CYS C 214 1555 1555 2.03 SSBOND 6 CYS C 23 CYS C 88 1555 1555 2.10 SSBOND 7 CYS C 134 CYS C 194 1555 1555 2.05 CISPEP 1 ARG0A 91 PRO0A 92 0 4.05 CISPEP 2 PHE0A 118 PRO0A 119 0 -3.76 CISPEP 3 PHE0A 234 PRO0A 235 0 0.89 CISPEP 4 PHE B 151 PRO B 152 0 -2.64 CISPEP 5 GLU B 153 PRO B 154 0 -5.09 CISPEP 6 SER C 7 PRO C 8 0 -1.32 CISPEP 7 ILE C 94 PRO C 95 0 -1.82 CISPEP 8 TYR C 140 PRO C 141 0 3.85 CRYST1 56.168 98.721 63.090 90.00 101.19 90.00 P 1 21 1 2 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 0.017804 0.000000 0.003522 0.00000 SCALE2 0.000000 0.010130 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016158 0.00000