HEADER IMMUNE SYSTEM 09-AUG-24 9GFL TITLE CRYSTAL STRUCTURE OF ASO BINDING FAB FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB FRAGMENT HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB FRAGMENT LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, FAB FRAGMENT, ASO, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR H.-E.HSIA,C.ZANINI,C.SIMONNEAU,J.FRAIDLING,T.KRAFT,K.MAYER,A.SOMMER, AUTHOR 2 A.INDLEKOFER,T.WIRTH,J.BENZ,G.GEORGES,L.M.LANGER,C.GASSNER, AUTHOR 3 V.LARRAILLET,M.MANSO,J.RAVN,K.HOFER,T.EMRICH,J.NIEWOEHNER, AUTHOR 4 F.SCHUMACHER,U.BRINKMANN REVDAT 1 20-AUG-25 9GFL 0 JRNL AUTH H.-E.HSIA,C.ZANINI,C.SIMONNEAU,J.FRAIDLING,T.KRAFT,K.MAYER, JRNL AUTH 2 A.SOMMER,A.INDLEKOFER,T.WIRTH,J.BENZ,G.GEORGES,L.M.LANGER, JRNL AUTH 3 C.GASSNER,V.LARRAILLET,M.MANSO,J.RAVN,K.HOFER,T.EMRICH, JRNL AUTH 4 J.NIEWOEHNER,F.SCHUMACHER,U.BRINKMANN JRNL TITL IMPROVED TARGETED DELIVERY OF ANTISENSE OLIGONUCLEOTIDE JRNL TITL 2 CONJUGATES WITH THE ANTIBODY MASK JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.8 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.90 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 53271 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.211 REMARK 3 R VALUE (WORKING SET) : 0.209 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2630 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.69 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.4513 REMARK 3 BIN FREE R VALUE : 0.5029 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 56 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3238 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 47 REMARK 3 SOLVENT ATOMS : 378 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.92 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.79870 REMARK 3 B22 (A**2) : -8.58150 REMARK 3 B33 (A**2) : 4.78280 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -2.71490 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.280 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.113 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.112 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.109 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.110 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3407 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4641 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1154 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 573 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3407 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 444 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 2948 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.05 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.34 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.31 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { H|* } REMARK 3 ORIGIN FOR THE GROUP (A): 10.1935 15.9519 2.9033 REMARK 3 T TENSOR REMARK 3 T11: -0.0731 T22: 0.0924 REMARK 3 T33: -0.0232 T12: -0.0039 REMARK 3 T13: -0.0131 T23: -0.0102 REMARK 3 L TENSOR REMARK 3 L11: 0.3118 L22: 0.3044 REMARK 3 L33: 0.6811 L12: 0.5036 REMARK 3 L13: -0.1404 L23: -0.2918 REMARK 3 S TENSOR REMARK 3 S11: -0.0965 S12: -0.1053 S13: 0.1201 REMARK 3 S21: -0.1053 S22: 0.0563 S23: -0.0461 REMARK 3 S31: 0.1201 S32: -0.0461 S33: 0.0402 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { L|* } REMARK 3 ORIGIN FOR THE GROUP (A): 25.4024 18.1354 12.5347 REMARK 3 T TENSOR REMARK 3 T11: -0.0727 T22: 0.1407 REMARK 3 T33: -0.0903 T12: -0.0197 REMARK 3 T13: 0.0227 T23: -0.0382 REMARK 3 L TENSOR REMARK 3 L11: 0.457 L22: 0.6612 REMARK 3 L33: 0.3668 L12: 0.395 REMARK 3 L13: -0.2449 L23: -0.4645 REMARK 3 S TENSOR REMARK 3 S11: 0.1107 S12: -0.0202 S13: -0.0195 REMARK 3 S21: -0.0202 S22: -0.0997 S23: 0.1459 REMARK 3 S31: -0.0195 S32: 0.1459 S33: -0.011 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9GFL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1292140925. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-AUG-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 : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.999859 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SADABS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53352 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680 REMARK 200 RESOLUTION RANGE LOW (A) : 63.380 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 3.430 REMARK 200 R MERGE (I) : 0.05500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.3200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.83000 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 (%): 50.53 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0, 20% PEG8000, VAPOR REMARK 280 DIFFUSION, SITTING DROP, 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 63.58550 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.80750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 63.58550 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.80750 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 H 534 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 SER H 129 REMARK 465 LYS H 130 REMARK 465 SER H 131 REMARK 465 THR H 132 REMARK 465 SER H 133 REMARK 465 GLY H 134 REMARK 465 SER H 216 REMARK 465 CYS H 217 REMARK 465 GLY H 218 REMARK 465 GLY H 219 REMARK 465 GLY H 220 REMARK 465 GLY H 221 REMARK 465 SER H 222 REMARK 465 GLU H 223 REMARK 465 PRO H 224 REMARK 465 GLU H 225 REMARK 465 ALA H 226 REMARK 465 CYS L 219 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 ASP H 145 65.48 64.81 REMARK 500 MET L 56 -39.63 68.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA H 305 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ARG H 65 O REMARK 620 2 ALA H 68 O 90.6 REMARK 620 N 1 DBREF 9GFL H 1 226 PDB 9GFL 9GFL 1 226 DBREF 9GFL L 1 219 PDB 9GFL 9GFL 1 219 SEQRES 1 H 226 PCA VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 H 226 PRO GLY THR SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 226 TYR ALA PHE THR ASN TYR LEU ILE GLU TRP ILE LYS GLN SEQRES 4 H 226 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY VAL ILE ASN SEQRES 5 H 226 PRO GLY SER GLY GLY THR ASN TYR ASN GLU LYS PHE ARG SEQRES 6 H 226 VAL LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 226 ALA TYR MET GLN LEU SER SER LEU THR SER ASP ASP SER SEQRES 8 H 226 ALA VAL TYR PHE CYS ALA ARG GLY GLY GLY TYR TYR TRP SEQRES 9 H 226 GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA SER THR SEQRES 10 H 226 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 H 226 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12 H 226 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13 H 226 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 H 226 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 H 226 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 H 226 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 H 226 ASP LYS LYS VAL GLU PRO LYS SER CYS GLY GLY GLY GLY SEQRES 18 H 226 SER GLU PRO GLU ALA SEQRES 1 L 219 ASP ILE VAL MET THR GLN ALA ALA PRO SER VAL PRO VAL SEQRES 2 L 219 THR PRO GLY GLU SER VAL SER ILE SER CYS ARG SER SER SEQRES 3 L 219 LYS SER LEU LEU HIS SER ASN GLY ASN THR TYR LEU PHE SEQRES 4 L 219 TRP PHE LEU GLN ARG PRO GLY GLN SER PRO GLN VAL LEU SEQRES 5 L 219 ILE TYR ARG MET SER ASN LEU ALA SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ALA PHE THR LEU SEQRES 7 L 219 ARG ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 219 TYR CYS MET GLN HIS LEU GLU TYR PRO TYR THR PHE GLY SEQRES 9 L 219 SER GLY THR ARG LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET PCA H 1 8 HET EDO H 301 4 HET EDO H 302 4 HET EDO H 303 4 HET EPE H 304 15 HET NA H 305 1 HET EPE L 301 15 HET EDO L 302 4 HETNAM PCA PYROGLUTAMIC ACID HETNAM EDO 1,2-ETHANEDIOL HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETNAM NA SODIUM ION HETSYN EDO ETHYLENE GLYCOL HETSYN EPE HEPES FORMUL 1 PCA C5 H7 N O3 FORMUL 3 EDO 4(C2 H6 O2) FORMUL 6 EPE 2(C8 H18 N2 O4 S) FORMUL 7 NA NA 1+ FORMUL 10 HOH *378(H2 O) HELIX 1 AA1 ALA H 28 TYR H 32 5 5 HELIX 2 AA2 GLU H 62 ARG H 65 5 4 HELIX 3 AA3 THR H 87 SER H 91 5 5 HELIX 4 AA4 SER H 157 ALA H 159 5 3 HELIX 5 AA5 SER H 188 LEU H 190 5 3 HELIX 6 AA6 LYS H 202 ASN H 205 5 4 HELIX 7 AA7 GLU L 84 VAL L 88 5 5 HELIX 8 AA8 SER L 126 SER L 132 1 7 HELIX 9 AA9 LYS L 188 GLU L 192 1 5 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O MET H 81 N VAL H 20 SHEET 4 AA1 4 ALA H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA2 6 GLU H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 108 VAL H 112 1 O THR H 111 N GLU H 10 SHEET 3 AA2 6 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 110 SHEET 4 AA2 6 ILE H 34 GLN H 39 -1 N GLU H 35 O ALA H 97 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O ASN H 59 N VAL H 50 SHEET 1 AA3 4 SER H 121 LEU H 125 0 SHEET 2 AA3 4 THR H 136 TYR H 146 -1 O LEU H 142 N PHE H 123 SHEET 3 AA3 4 TYR H 177 PRO H 186 -1 O VAL H 185 N ALA H 137 SHEET 4 AA3 4 VAL H 164 THR H 166 -1 N HIS H 165 O VAL H 182 SHEET 1 AA4 4 SER H 121 LEU H 125 0 SHEET 2 AA4 4 THR H 136 TYR H 146 -1 O LEU H 142 N PHE H 123 SHEET 3 AA4 4 TYR H 177 PRO H 186 -1 O VAL H 185 N ALA H 137 SHEET 4 AA4 4 VAL H 170 LEU H 171 -1 N VAL H 170 O SER H 178 SHEET 1 AA5 3 THR H 152 TRP H 155 0 SHEET 2 AA5 3 ILE H 196 HIS H 201 -1 O ASN H 198 N SER H 154 SHEET 3 AA5 3 THR H 206 LYS H 211 -1 O VAL H 208 N VAL H 199 SHEET 1 AA6 4 MET L 4 THR L 5 0 SHEET 2 AA6 4 VAL L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA6 4 ALA L 75 ILE L 80 -1 O PHE L 76 N CYS L 23 SHEET 4 AA6 4 PHE L 67 GLY L 71 -1 N SER L 68 O ARG L 79 SHEET 1 AA7 6 SER L 10 VAL L 13 0 SHEET 2 AA7 6 THR L 107 ILE L 111 1 O GLU L 110 N VAL L 11 SHEET 3 AA7 6 GLY L 89 GLN L 95 -1 N GLY L 89 O LEU L 109 SHEET 4 AA7 6 LEU L 38 GLN L 43 -1 N PHE L 41 O TYR L 92 SHEET 5 AA7 6 GLN L 50 TYR L 54 -1 O GLN L 50 N LEU L 42 SHEET 6 AA7 6 ASN L 58 LEU L 59 -1 O ASN L 58 N TYR L 54 SHEET 1 AA8 4 SER L 10 VAL L 13 0 SHEET 2 AA8 4 THR L 107 ILE L 111 1 O GLU L 110 N VAL L 11 SHEET 3 AA8 4 GLY L 89 GLN L 95 -1 N GLY L 89 O LEU L 109 SHEET 4 AA8 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AA9 4 SER L 119 PHE L 123 0 SHEET 2 AA9 4 THR L 134 PHE L 144 -1 O LEU L 140 N PHE L 121 SHEET 3 AA9 4 TYR L 178 SER L 187 -1 O LEU L 180 N LEU L 141 SHEET 4 AA9 4 SER L 164 VAL L 168 -1 N SER L 167 O SER L 181 SHEET 1 AB1 4 ALA L 158 LEU L 159 0 SHEET 2 AB1 4 LYS L 150 VAL L 155 -1 N VAL L 155 O ALA L 158 SHEET 3 AB1 4 VAL L 196 THR L 202 -1 O GLU L 200 N GLN L 152 SHEET 4 AB1 4 VAL L 210 ASN L 215 -1 O VAL L 210 N VAL L 201 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 141 CYS H 197 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 93 1555 1555 2.09 SSBOND 4 CYS L 139 CYS L 199 1555 1555 2.06 LINK C PCA H 1 N VAL H 2 1555 1555 1.34 LINK O ARG H 65 NA NA H 305 1555 1555 2.32 LINK O ALA H 68 NA NA H 305 1555 1555 2.84 CISPEP 1 PHE H 147 PRO H 148 0 -0.57 CISPEP 2 GLU H 149 PRO H 150 0 -1.14 CISPEP 3 TYR L 99 PRO L 100 0 -6.95 CISPEP 4 TYR L 145 PRO L 146 0 1.14 CRYST1 127.171 59.615 62.692 90.00 94.62 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 0.007863 0.000000 0.000635 0.00000 SCALE2 0.000000 0.016774 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016003 0.00000