HEADER IMMUNE SYSTEM 23-JAN-24 8VS7 TITLE CRYSTAL STRUCTURE OF ADI-19425 FAB IN COMPLEX WITH ANTI-IDIOTYPIC 2C1 TITLE 2 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 2C1 LIGHT CHAIN; COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 2C1 HEAVY CHAIN; COMPND 7 CHAIN: A; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ADI-19425 HEAVY CHAIN; COMPND 11 CHAIN: H; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: ADI-19425 LIGHT CHAIN; COMPND 15 CHAIN: L; COMPND 16 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: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 30 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 32 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS RSV, ANTIBODY, ANTI-IDIOTYPE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR G.KHER,L.J.HOMAD,A.T.MCGUIRE,M.PANCERA REVDAT 1 18-SEP-24 8VS7 0 JRNL AUTH S.SCHARFFENBERGER,A.T.MCGUIRE JRNL TITL A NOVEL RSV VACCINE CANDIDATE DERIVED FROM ANTI-IDIOTYPIC JRNL TITL 2 ANTIBODIES TARGETS PUTATIVE NEUTRALIZING B-CELLS IN BULK JRNL TITL 3 PBMCS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.41 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) : 2.41 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.96 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 3 NUMBER OF REFLECTIONS : 42768 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.203 REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.730 REMARK 3 FREE R VALUE TEST SET COUNT : 2025 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 45.9600 - 5.8000 0.98 3057 125 0.1917 0.1993 REMARK 3 2 5.8000 - 4.6100 0.99 2962 135 0.1706 0.1810 REMARK 3 3 4.6100 - 4.0300 1.00 2979 146 0.1617 0.2165 REMARK 3 4 4.0300 - 3.6600 0.99 2946 137 0.1894 0.2684 REMARK 3 5 3.6600 - 3.4000 0.99 2907 151 0.1846 0.2327 REMARK 3 6 3.4000 - 3.2000 0.99 2919 146 0.1973 0.2518 REMARK 3 7 3.2000 - 3.0400 1.00 2942 149 0.2192 0.3059 REMARK 3 8 3.0400 - 2.9000 0.99 2915 158 0.2164 0.2915 REMARK 3 9 2.9000 - 2.7900 0.99 2880 151 0.2273 0.3073 REMARK 3 10 2.7900 - 2.7000 0.99 2921 153 0.2293 0.2947 REMARK 3 11 2.7000 - 2.6100 0.99 2910 144 0.2377 0.3108 REMARK 3 12 2.6100 - 2.5400 0.99 2900 153 0.2483 0.2768 REMARK 3 13 2.5400 - 2.4700 0.99 2906 145 0.2502 0.3433 REMARK 3 14 2.4700 - 2.4100 0.89 2599 132 0.2672 0.3316 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) : 0.290 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.780 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 : 0.004 6649 REMARK 3 ANGLE : 0.684 9058 REMARK 3 CHIRALITY : 0.045 1024 REMARK 3 PLANARITY : 0.005 1151 REMARK 3 DIHEDRAL : 16.296 2332 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 8VS7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1000275976. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-JUL-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 : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42821 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 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 (%) : 99.2 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : 0.22300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.40 REMARK 200 R MERGE FOR SHELL (I) : 0.82200 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.19 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M IMIDAZOLE PH 6.5, 12% PEG 3350, REMARK 280 30% MPD AND 0.2M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K 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 33.46500 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, H, L 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 CYS B 214 REMARK 465 GLY A 55 REMARK 465 GLY A 56 REMARK 465 PHE A 57 REMARK 465 ALA A 58 REMARK 465 TYR A 59 REMARK 465 THR A 60 REMARK 465 GLN A 61 REMARK 465 LYS A 62 REMARK 465 LYS A 129 REMARK 465 SER A 130 REMARK 465 LYS A 214 REMARK 465 SER A 215 REMARK 465 CYS A 216 REMARK 465 ASP A 217 REMARK 465 LYS A 218 REMARK 465 THR A 219 REMARK 465 GLY A 220 REMARK 465 SER A 221 REMARK 465 GLY A 222 REMARK 465 SER A 223 REMARK 465 GLY A 224 REMARK 465 HIS A 225 REMARK 465 HIS A 226 REMARK 465 HIS A 227 REMARK 465 HIS A 228 REMARK 465 HIS A 229 REMARK 465 HIS A 230 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR L 209 REMARK 465 GLU L 210 REMARK 465 CYS L 211 REMARK 465 SER L 212 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 123 CG CD OE1 OE2 REMARK 470 GLU B 143 CG CD OE1 OE2 REMARK 470 GLU B 213 CG CD OE1 OE2 REMARK 470 GLN H 105 CG CD OE1 NE2 REMARK 470 LYS H 201 CG CD CE NZ REMARK 470 ARG H 210 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 108 CG CD OE1 NE2 REMARK 470 LYS L 149 CG CD CE NZ REMARK 470 GLU L 183 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 NH1 ARG B 142 O HOH B 401 2.03 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 ASN B 30 -108.08 49.21 REMARK 500 ALA B 51 -36.59 80.87 REMARK 500 HIS B 91 50.70 -115.95 REMARK 500 ASN B 138 74.62 55.46 REMARK 500 LYS A 64 -70.18 -57.06 REMARK 500 ARG A 82A -145.08 -81.18 REMARK 500 SER A 82B 95.63 -49.25 REMARK 500 SER A 127 -148.53 -136.83 REMARK 500 ASP A 144 62.48 65.89 REMARK 500 THR H 28 95.83 -68.36 REMARK 500 LYS H 43 -167.02 -119.20 REMARK 500 SER H 99 72.21 -104.40 REMARK 500 SER H 100B 133.77 77.48 REMARK 500 PHE H 146 136.77 -174.78 REMARK 500 ASN L 27B -94.49 -130.78 REMARK 500 ASN L 51 -47.04 75.10 REMARK 500 SER L 52 13.98 -145.64 REMARK 500 ALA L 84 -174.98 170.78 REMARK 500 SER L 90 -155.20 -155.60 REMARK 500 SER L 95A -0.67 75.57 REMARK 500 ASP L 138 38.61 70.15 REMARK 500 PRO L 141 -168.47 -69.99 REMARK 500 ASP L 151 -102.57 57.59 REMARK 500 REMARK 500 REMARK: NULL DBREF 8VS7 B 1 214 PDB 8VS7 8VS7 1 214 DBREF 8VS7 A 1 230 PDB 8VS7 8VS7 1 230 DBREF 8VS7 H 1 218 PDB 8VS7 8VS7 1 218 DBREF 8VS7 L 1 212 PDB 8VS7 8VS7 1 212 SEQRES 1 B 214 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 B 214 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA ASN SEQRES 3 B 214 HIS ASP VAL ASN ILE ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 B 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL SEQRES 7 B 214 GLN ALA GLU ASP LEU ALA VAL TYR TYR CYS GLN GLN HIS SEQRES 8 B 214 TYR ASP THR PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS SEQRES 1 A 238 PCA VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 A 238 PRO GLY ALA SER VAL THR LEU SER CYS LYS ALA SER GLY SEQRES 3 A 238 TYR ILE PHE THR ASP TYR GLU ILE HIS TRP LEU LYS GLN SEQRES 4 A 238 THR PRO VAL HIS GLY LEU GLU TRP ILE GLY THR SER ASP SEQRES 5 A 238 PRO GLU THR GLY GLY PHE ALA TYR THR GLN LYS PHE LYS SEQRES 6 A 238 GLY LYS ALA ILE LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 A 238 ALA TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 A 238 ALA VAL TYR TYR CYS THR ARG ARG PRO TYR TYR GLY SER SEQRES 9 A 238 GLY ALA TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 A 238 THR VAL SER ALA ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 A 238 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 A 238 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 A 238 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 A 238 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 A 238 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 A 238 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 A 238 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 A 238 LYS SER CYS ASP LYS THR GLY SER GLY SER GLY HIS HIS SEQRES 19 A 238 HIS HIS HIS HIS SEQRES 1 H 227 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 227 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 227 PHE THR PHE SER SER TYR SER MET ASN TRP VAL ARG GLN SEQRES 4 H 227 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5 H 227 SER SER SER SER TYR ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 227 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 227 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 227 ALA VAL TYR TYR CYS ALA ARG LEU GLY TYR CYS SER GLY SEQRES 9 H 227 GLY SER CYS HIS PHE ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 H 227 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 227 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 227 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 227 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 227 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 227 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 227 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 227 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 H 227 PRO LYS SER CYS ASP LYS SEQRES 1 L 218 PCA PRO VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 218 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3 L 218 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4 L 218 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5 L 218 ASN SER ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 218 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 L 218 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 L 218 SER TYR ASP SER SER LEU SER GLY PHE TYR VAL PHE GLY SEQRES 9 L 218 THR GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA SEQRES 10 L 218 ALA PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU SEQRES 11 L 218 LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER SEQRES 12 L 218 ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA SEQRES 13 L 218 ASP SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR SEQRES 14 L 218 PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER SEQRES 15 L 218 TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SEQRES 16 L 218 SER TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL SEQRES 17 L 218 GLU LYS THR VAL ALA PRO THR GLU CYS SER HET PCA A 1 16 HET PCA L 1 8 HET EDO B 301 10 HET EDO B 302 10 HET EDO B 303 10 HET SO4 B 304 5 HET SO4 B 305 5 HET EDO A 301 10 HET EDO A 302 10 HETNAM PCA PYROGLUTAMIC ACID HETNAM EDO 1,2-ETHANEDIOL HETNAM SO4 SULFATE ION HETSYN EDO ETHYLENE GLYCOL FORMUL 2 PCA 2(C5 H7 N O3) FORMUL 5 EDO 5(C2 H6 O2) FORMUL 8 SO4 2(O4 S 2-) FORMUL 12 HOH *166(H2 O) HELIX 1 AA1 GLN B 79 LEU B 83 5 5 HELIX 2 AA2 SER B 121 LYS B 126 1 6 HELIX 3 AA3 LYS B 183 GLU B 187 1 5 HELIX 4 AA4 ILE A 28 TYR A 32 5 5 HELIX 5 AA5 THR A 83 SER A 87 5 5 HELIX 6 AA6 SER A 156 ALA A 158 5 3 HELIX 7 AA7 SER A 187 LEU A 189 5 3 HELIX 8 AA8 LYS A 201 ASN A 204 5 4 HELIX 9 AA9 THR H 28 TYR H 32 5 5 HELIX 10 AB1 ASP H 61 LYS H 64 5 4 HELIX 11 AB2 ARG H 83 THR H 87 5 5 HELIX 12 AB3 SER H 156 ALA H 158 5 3 HELIX 13 AB4 SER H 187 GLY H 190 5 4 HELIX 14 AB5 LYS H 201 ASN H 204 5 4 HELIX 15 AB6 ASN L 27B GLY L 30 5 5 HELIX 16 AB7 GLN L 79 GLU L 83 5 5 HELIX 17 AB8 SER L 93 GLY L 95B 5 5 HELIX 18 AB9 SER L 121 ALA L 127 1 7 HELIX 19 AC1 THR L 181 HIS L 188 1 8 SHEET 1 AA1 4 MET B 4 THR B 5 0 SHEET 2 AA1 4 VAL B 19 ALA B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AA1 4 ASP B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AA1 4 PHE B 62 SER B 67 -1 N THR B 63 O THR B 74 SHEET 1 AA2 6 PHE B 10 SER B 14 0 SHEET 2 AA2 6 THR B 102 LYS B 107 1 O LYS B 107 N THR B 13 SHEET 3 AA2 6 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA2 6 VAL B 33 GLN B 38 -1 N ALA B 34 O GLN B 89 SHEET 5 AA2 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA2 6 TYR B 53 ARG B 54 -1 O TYR B 53 N TYR B 49 SHEET 1 AA3 4 PHE B 10 SER B 14 0 SHEET 2 AA3 4 THR B 102 LYS B 107 1 O LYS B 107 N THR B 13 SHEET 3 AA3 4 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA3 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AA4 4 SER B 114 PHE B 118 0 SHEET 2 AA4 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AA4 4 TYR B 173 SER B 182 -1 O TYR B 173 N PHE B 139 SHEET 4 AA4 4 SER B 159 VAL B 163 -1 N SER B 162 O SER B 176 SHEET 1 AA5 4 ALA B 153 LEU B 154 0 SHEET 2 AA5 4 ALA B 144 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AA5 4 VAL B 191 HIS B 198 -1 O GLU B 195 N GLN B 147 SHEET 4 AA5 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SHEET 1 AA6 4 GLN A 3 GLN A 6 0 SHEET 2 AA6 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AA6 4 THR A 77 LEU A 82 -1 O LEU A 82 N VAL A 18 SHEET 4 AA6 4 ALA A 67 ASP A 72 -1 N THR A 70 O TYR A 79 SHEET 1 AA7 5 GLU A 10 VAL A 12 0 SHEET 2 AA7 5 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA7 5 ALA A 88 ARG A 94 -1 N ALA A 88 O VAL A 109 SHEET 4 AA7 5 ILE A 34 THR A 40 -1 N HIS A 35 O THR A 93 SHEET 5 AA7 5 GLY A 44 SER A 51 -1 O ILE A 48 N TRP A 36 SHEET 1 AA8 4 GLU A 10 VAL A 12 0 SHEET 2 AA8 4 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA8 4 ALA A 88 ARG A 94 -1 N ALA A 88 O VAL A 109 SHEET 4 AA8 4 TYR A 102 TRP A 103 -1 O TYR A 102 N ARG A 94 SHEET 1 AA9 4 SER A 120 LEU A 124 0 SHEET 2 AA9 4 THR A 135 TYR A 145 -1 O GLY A 139 N LEU A 124 SHEET 3 AA9 4 TYR A 176 PRO A 185 -1 O TYR A 176 N TYR A 145 SHEET 4 AA9 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AB1 4 SER A 120 LEU A 124 0 SHEET 2 AB1 4 THR A 135 TYR A 145 -1 O GLY A 139 N LEU A 124 SHEET 3 AB1 4 TYR A 176 PRO A 185 -1 O TYR A 176 N TYR A 145 SHEET 4 AB1 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AB2 3 THR A 151 TRP A 154 0 SHEET 2 AB2 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AB2 3 THR A 205 ARG A 210 -1 O THR A 205 N HIS A 200 SHEET 1 AB3 4 GLN H 3 SER H 7 0 SHEET 2 AB3 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AB3 4 SER H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AB3 4 PHE H 67 ASP H 72 -1 N ASP H 72 O SER H 77 SHEET 1 AB4 6 LEU H 11 VAL H 12 0 SHEET 2 AB4 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB4 6 ALA H 88 LEU H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AB4 6 SER H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AB4 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AB4 6 ILE H 57 TYR H 59 -1 O TYR H 58 N SER H 50 SHEET 1 AB5 4 LEU H 11 VAL H 12 0 SHEET 2 AB5 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB5 4 ALA H 88 LEU H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AB5 4 PHE H 100E TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AB6 4 SER H 120 SER H 127 0 SHEET 2 AB6 4 THR H 135 TYR H 145 -1 O ALA H 137 N SER H 127 SHEET 3 AB6 4 TYR H 176 PRO H 185 -1 O VAL H 182 N LEU H 138 SHEET 4 AB6 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB7 4 SER H 120 SER H 127 0 SHEET 2 AB7 4 THR H 135 TYR H 145 -1 O ALA H 137 N SER H 127 SHEET 3 AB7 4 TYR H 176 PRO H 185 -1 O VAL H 182 N LEU H 138 SHEET 4 AB7 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB8 3 THR H 151 TRP H 154 0 SHEET 2 AB8 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AB8 3 THR H 205 VAL H 211 -1 O VAL H 211 N TYR H 194 SHEET 1 AB9 5 SER L 9 GLY L 13 0 SHEET 2 AB9 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AB9 5 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AB9 5 HIS L 34 GLN L 38 -1 N HIS L 34 O GLN L 89 SHEET 5 AB9 5 LYS L 45 ILE L 48 -1 O ILE L 48 N TRP L 35 SHEET 1 AC1 4 SER L 9 GLY L 13 0 SHEET 2 AC1 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AC1 4 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AC1 4 PHE L 95C PHE L 98 -1 O PHE L 95C N ASP L 92 SHEET 1 AC2 3 VAL L 19 THR L 24 0 SHEET 2 AC2 3 SER L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 3 AC2 3 PHE L 62 SER L 67 -1 N SER L 67 O SER L 70 SHEET 1 AC3 4 SER L 114 PHE L 118 0 SHEET 2 AC3 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AC3 4 TYR L 172 LEU L 180 -1 O ALA L 174 N ILE L 136 SHEET 4 AC3 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177 SHEET 1 AC4 4 SER L 114 PHE L 118 0 SHEET 2 AC4 4 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AC4 4 TYR L 172 LEU L 180 -1 O ALA L 174 N ILE L 136 SHEET 4 AC4 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AC5 4 SER L 153 PRO L 154 0 SHEET 2 AC5 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153 SHEET 3 AC5 4 TYR L 191 HIS L 197 -1 O THR L 196 N THR L 145 SHEET 4 AC5 4 SER L 200 VAL L 206 -1 O SER L 200 N HIS L 197 SSBOND 1 CYS B 23 CYS B 88 1555 1555 2.05 SSBOND 2 CYS B 134 CYS B 194 1555 1555 2.06 SSBOND 3 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 4 CYS A 140 CYS A 196 1555 1555 2.05 SSBOND 5 CYS H 22 CYS H 92 1555 1555 2.05 SSBOND 6 CYS H 98 CYS H 100C 1555 1555 2.05 SSBOND 7 CYS H 140 CYS H 196 1555 1555 2.04 SSBOND 8 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 9 CYS L 134 CYS L 193 1555 1555 2.04 LINK C APCA A 1 N AVAL A 2 1555 1555 1.33 LINK C BPCA A 1 N BVAL A 2 1555 1555 1.33 LINK C PCA L 1 N PRO L 2 1555 1555 1.34 CISPEP 1 THR B 94 PRO B 95 0 1.80 CISPEP 2 TYR B 140 PRO B 141 0 4.32 CISPEP 3 PHE A 146 PRO A 147 0 -0.91 CISPEP 4 GLU A 148 PRO A 149 0 1.43 CISPEP 5 PHE H 146 PRO H 147 0 -2.52 CISPEP 6 GLU H 148 PRO H 149 0 3.56 CISPEP 7 TYR L 140 PRO L 141 0 -0.83 CRYST1 66.802 66.930 130.191 90.00 103.74 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 0.014970 0.000000 0.003659 0.00000 SCALE2 0.000000 0.014941 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007907 0.00000