HEADER IMMUNE SYSTEM 10-FEB-25 9LUY TITLE SINGLE-CHAIN FV ANTIBODY OF G2 FUSED WITH ANTIGEN PEPTIDE FROM CHICKEN TITLE 2 CHROMOSOME 6 C10ORF76 HOMOLOG COMPND MOL_ID: 1; COMPND 2 MOLECULE: SINGLE-CHAIN FV ANTIBODY OF G2 FUSED WITH ANTIGEN PEPTIDE COMPND 3 FROM CHICKEN CHROMOSOME 6 C10ORF76 HOMOLOG; COMPND 4 CHAIN: A; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: THE FUSION PROTEIN COMPOSED OF AN EXPRESSION TAG COMPND 7 (RESIDUES 1-2), A FRAGMENT FROM CHICKEN CHROMOSOME 6 C10ORF76 HOMOLOG COMPND 8 (RESIDUES 3-22), A LINKER (RESIDUES 23-30), THE LIGHT CHAIN (RESIDUES COMPND 9 31-140), A SECOND LINKER (RESIDUES 141-155), AND THE HEAVY CHAIN COMPND 10 (RESIDUES 156-273). SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS, MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 9031, 10090; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIGEN BINDING, AFFINITY MATURATION, SOMATIC HYPERMUTATION, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.HANAZONO,S.YABUNO,T.HAYASHI,N.NUMOTO,N.ITO,M.ODA REVDAT 1 11-JUN-25 9LUY 0 JRNL AUTH Y.HANAZONO,S.YABUNO,T.HAYASHI,N.NUMOTO,Y.O.KAMATARI,N.ITO, JRNL AUTH 2 M.ODA JRNL TITL ANTIGEN RECOGNITION MECHANISM OF G2 ANTIBODY POSSESSING JRNL TITL 2 MULTI-SPECIFICITY REVEALED BY CRYSTAL STRUCTURES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.62 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 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) : 1.62 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.14 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 28833 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.168 REMARK 3 R VALUE (WORKING SET) : 0.167 REMARK 3 FREE R VALUE : 0.188 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1441 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 31.1400 - 3.4900 0.98 2755 146 0.1440 0.1481 REMARK 3 2 3.4900 - 2.7700 0.99 2739 143 0.1554 0.1717 REMARK 3 3 2.7700 - 2.4200 1.00 2746 145 0.1699 0.1775 REMARK 3 4 2.4200 - 2.2000 1.00 2734 144 0.1601 0.2059 REMARK 3 5 2.2000 - 2.0400 1.00 2737 144 0.1729 0.1947 REMARK 3 6 2.0400 - 1.9200 1.00 2750 143 0.1754 0.2069 REMARK 3 7 1.9200 - 1.8200 1.00 2725 144 0.1824 0.2380 REMARK 3 8 1.8200 - 1.7500 1.00 2717 143 0.2220 0.2722 REMARK 3 9 1.7500 - 1.6800 1.00 2731 144 0.2322 0.3122 REMARK 3 10 1.6800 - 1.6200 1.00 2758 145 0.2433 0.2690 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) : 0.157 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.897 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 18.29 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.66 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 1932 REMARK 3 ANGLE : 1.060 2619 REMARK 3 CHIRALITY : 0.064 284 REMARK 3 PLANARITY : 0.007 336 REMARK 3 DIHEDRAL : 14.167 708 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 179 THROUGH 238 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.2639 -7.3813 3.6099 REMARK 3 T TENSOR REMARK 3 T11: 0.0945 T22: 0.0846 REMARK 3 T33: 0.1383 T12: -0.0173 REMARK 3 T13: -0.0140 T23: 0.0053 REMARK 3 L TENSOR REMARK 3 L11: 3.2281 L22: 2.9761 REMARK 3 L33: 3.2006 L12: 0.0975 REMARK 3 L13: -1.3038 L23: 0.5137 REMARK 3 S TENSOR REMARK 3 S11: 0.1189 S12: -0.1228 S13: 0.0712 REMARK 3 S21: 0.0822 S22: -0.0501 S23: 0.1565 REMARK 3 S31: 0.0035 S32: 0.0500 S33: -0.0471 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 239 THROUGH 273 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.2955 -4.6830 6.2028 REMARK 3 T TENSOR REMARK 3 T11: 0.1167 T22: 0.1076 REMARK 3 T33: 0.2038 T12: 0.0098 REMARK 3 T13: 0.0150 T23: -0.0559 REMARK 3 L TENSOR REMARK 3 L11: 6.0980 L22: 3.9725 REMARK 3 L33: 2.4172 L12: 2.3712 REMARK 3 L13: 0.4518 L23: 0.0941 REMARK 3 S TENSOR REMARK 3 S11: -0.0514 S12: -0.0304 S13: 0.3735 REMARK 3 S21: -0.1117 S22: -0.0010 S23: 0.5981 REMARK 3 S31: 0.0315 S32: -0.1598 S33: 0.0100 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.4131 -3.7936 7.9490 REMARK 3 T TENSOR REMARK 3 T11: 0.1297 T22: 0.1997 REMARK 3 T33: 0.2045 T12: -0.0135 REMARK 3 T13: -0.0455 T23: 0.0169 REMARK 3 L TENSOR REMARK 3 L11: 4.1208 L22: 5.2690 REMARK 3 L33: 1.7303 L12: -2.4756 REMARK 3 L13: 0.7704 L23: 1.9827 REMARK 3 S TENSOR REMARK 3 S11: -0.0320 S12: 0.0137 S13: -0.1613 REMARK 3 S21: 0.1500 S22: 0.1119 S23: -0.2909 REMARK 3 S31: -0.0291 S32: 0.6277 S33: -0.0169 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 34 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.7194 13.6825 13.3808 REMARK 3 T TENSOR REMARK 3 T11: 0.1366 T22: 0.1448 REMARK 3 T33: 0.1252 T12: -0.0237 REMARK 3 T13: -0.0108 T23: -0.0341 REMARK 3 L TENSOR REMARK 3 L11: 1.8365 L22: 3.5839 REMARK 3 L33: 2.2105 L12: -0.5916 REMARK 3 L13: -0.3822 L23: -0.4950 REMARK 3 S TENSOR REMARK 3 S11: -0.0394 S12: -0.1366 S13: -0.0207 REMARK 3 S21: 0.3292 S22: -0.0398 S23: 0.0374 REMARK 3 S31: -0.0548 S32: -0.0342 S33: 0.0658 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 178 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.0772 -2.0855 9.1100 REMARK 3 T TENSOR REMARK 3 T11: 0.1868 T22: 0.1492 REMARK 3 T33: 0.2224 T12: -0.0179 REMARK 3 T13: 0.0226 T23: 0.0200 REMARK 3 L TENSOR REMARK 3 L11: 1.2589 L22: 1.1013 REMARK 3 L33: 0.8778 L12: 0.2380 REMARK 3 L13: -0.0695 L23: 0.9045 REMARK 3 S TENSOR REMARK 3 S11: 0.0793 S12: -0.1147 S13: -0.0409 REMARK 3 S21: 0.1778 S22: -0.1702 S23: 0.2272 REMARK 3 S31: 0.0424 S32: -0.1187 S33: 0.0847 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 9LUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1300056389. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-DEC-24 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 : PHOTON FACTORY REMARK 200 BEAMLINE : BL-5A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28848 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : 0.05100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 0.71200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 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: 6PGX REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.01 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES MONOHYDRATE PH 6.5, 12% W/V REMARK 280 POLYETHYLENE GLYCOL 20,000, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.02700 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.69500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.02700 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.69500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 464 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 492 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 593 LIES ON A SPECIAL POSITION. 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 MET A 1 REMARK 465 GLU A 18 REMARK 465 ASP A 19 REMARK 465 GLN A 20 REMARK 465 VAL A 21 REMARK 465 LEU A 22 REMARK 465 LEU A 23 REMARK 465 GLU A 24 REMARK 465 VAL A 25 REMARK 465 LEU A 26 REMARK 465 PHE A 27 REMARK 465 GLN A 28 REMARK 465 GLY A 29 REMARK 465 PRO A 30 REMARK 465 GLY A 141 REMARK 465 GLY A 142 REMARK 465 GLY A 143 REMARK 465 GLY A 144 REMARK 465 SER A 145 REMARK 465 GLY A 146 REMARK 465 GLY A 147 REMARK 465 GLY A 148 REMARK 465 GLY A 149 REMARK 465 SER A 150 REMARK 465 GLY A 151 REMARK 465 GLY A 152 REMARK 465 GLY A 153 REMARK 465 GLY A 154 REMARK 465 SER A 155 REMARK 465 GLU A 156 REMARK 465 VAL A 157 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 TYR A 66 60.97 -102.34 REMARK 500 ALA A 85 -43.77 75.18 REMARK 500 ASP A 128 -148.76 52.72 REMARK 500 ALA A 204 148.78 -170.10 REMARK 500 REMARK 500 REMARK: NULL DBREF 9LUY A 1 22 PDB 9LUY 9LUY 1 22 DBREF 9LUY A 23 273 PDB 9LUY 9LUY 23 273 SEQRES 1 A 273 MET GLY LYS ILE GLU SER TYR ALA ALA VAL ASN HIS ILE SEQRES 2 A 273 SER GLN LEU SER GLU ASP GLN VAL LEU LEU GLU VAL LEU SEQRES 3 A 273 PHE GLN GLY PRO ASP ILE VAL LEU THR GLN SER PRO ALA SEQRES 4 A 273 SER LEU ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER SEQRES 5 A 273 CYS LYS ALA SER GLN THR LEU ASP TYR ASP GLY GLY THR SEQRES 6 A 273 TYR MET ASN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO SEQRES 7 A 273 LYS LEU LEU ILE PHE ALA ALA SER ASN LEU GLU SER GLY SEQRES 8 A 273 ILE PRO ALA ARG PHE SER GLY SER GLY SER GLY THR ASP SEQRES 9 A 273 PHE THR LEU ASN ILE HIS PRO VAL GLU GLU GLU ASP ALA SEQRES 10 A 273 ALA THR TYR TYR CYS GLN GLN SER ARG GLU ASP LEU THR SEQRES 11 A 273 PHE GLY ALA GLY THR LYS LEU ASP LEU LYS GLY GLY GLY SEQRES 12 A 273 GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLU SEQRES 13 A 273 VAL MET LEU VAL GLU SER GLY GLY VAL LEU VAL LYS PRO SEQRES 14 A 273 GLY GLY SER LEU LYS LEU SER CYS SER ALA SER GLY PHE SEQRES 15 A 273 THR PHE SER ARG TYR ALA MET SER TRP VAL ARG GLN THR SEQRES 16 A 273 PRO GLU LYS ARG LEU GLU TRP VAL ALA SER ILE SER SER SEQRES 17 A 273 GLY GLY SER TYR THR PHE TYR PRO ASP SER VAL LYS GLY SEQRES 18 A 273 ARG PHE THR ILE SER ARG ASN ASN ALA LYS ASN PHE LEU SEQRES 19 A 273 TYR LEU LYS MET SER SER LEU ARG SER GLU ASP THR ALA SEQRES 20 A 273 MET TYR TYR CYS ALA ARG SER GLY ASN ASP TYR ALA VAL SEQRES 21 A 273 ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER HET GOL A 301 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 GOL C3 H8 O3 FORMUL 3 HOH *209(H2 O) HELIX 1 AA1 ALA A 9 ILE A 13 5 5 HELIX 2 AA2 GLU A 113 ALA A 117 5 5 HELIX 3 AA3 THR A 183 TYR A 187 5 5 HELIX 4 AA4 ARG A 242 THR A 246 5 5 HELIX 5 AA5 ASN A 256 TYR A 258 5 3 SHEET 1 AA1 4 LEU A 34 SER A 37 0 SHEET 2 AA1 4 ALA A 49 ALA A 55 -1 O LYS A 54 N THR A 35 SHEET 3 AA1 4 ASP A 104 ILE A 109 -1 O LEU A 107 N ILE A 51 SHEET 4 AA1 4 PHE A 96 SER A 101 -1 N SER A 97 O ASN A 108 SHEET 1 AA2 6 SER A 40 VAL A 43 0 SHEET 2 AA2 6 THR A 135 LEU A 139 1 O LYS A 136 N LEU A 41 SHEET 3 AA2 6 ALA A 118 GLN A 124 -1 N ALA A 118 O LEU A 137 SHEET 4 AA2 6 MET A 67 GLN A 72 -1 N ASN A 68 O GLN A 123 SHEET 5 AA2 6 LYS A 79 PHE A 83 -1 O LEU A 81 N TRP A 69 SHEET 6 AA2 6 ASN A 87 LEU A 88 -1 O ASN A 87 N PHE A 83 SHEET 1 AA3 4 SER A 40 VAL A 43 0 SHEET 2 AA3 4 THR A 135 LEU A 139 1 O LYS A 136 N LEU A 41 SHEET 3 AA3 4 ALA A 118 GLN A 124 -1 N ALA A 118 O LEU A 137 SHEET 4 AA3 4 THR A 130 PHE A 131 -1 O THR A 130 N GLN A 124 SHEET 1 AA4 2 ASP A 60 TYR A 61 0 SHEET 2 AA4 2 GLY A 64 THR A 65 -1 O GLY A 64 N TYR A 61 SHEET 1 AA5 6 VAL A 165 VAL A 167 0 SHEET 2 AA5 6 THR A 267 VAL A 271 1 O THR A 270 N VAL A 167 SHEET 3 AA5 6 ALA A 247 SER A 254 -1 N TYR A 249 O THR A 267 SHEET 4 AA5 6 MET A 189 GLN A 194 -1 N VAL A 192 O TYR A 250 SHEET 5 AA5 6 LEU A 200 ILE A 206 -1 O GLU A 201 N ARG A 193 SHEET 6 AA5 6 THR A 213 PHE A 214 -1 O PHE A 214 N SER A 205 SHEET 1 AA6 4 VAL A 165 VAL A 167 0 SHEET 2 AA6 4 THR A 267 VAL A 271 1 O THR A 270 N VAL A 167 SHEET 3 AA6 4 ALA A 247 SER A 254 -1 N TYR A 249 O THR A 267 SHEET 4 AA6 4 VAL A 260 TRP A 263 -1 O TYR A 262 N ARG A 253 SHEET 1 AA7 3 LEU A 173 SER A 178 0 SHEET 2 AA7 3 PHE A 233 MET A 238 -1 O MET A 238 N LEU A 173 SHEET 3 AA7 3 PHE A 223 ASN A 228 -1 N THR A 224 O LYS A 237 SSBOND 1 CYS A 53 CYS A 122 1555 1555 2.08 SSBOND 2 CYS A 177 CYS A 251 1555 1555 2.04 CISPEP 1 SER A 37 PRO A 38 0 -2.08 CISPEP 2 HIS A 110 PRO A 111 0 -7.14 CRYST1 76.054 71.390 43.352 90.00 100.91 90.00 C 1 2 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 0.013149 0.000000 0.002534 0.00000 SCALE2 0.000000 0.014008 0.000000 0.00000 SCALE3 0.000000 0.000000 0.023491 0.00000