HEADER DE NOVO PROTEIN 07-MAY-24 9F91 TITLE CRYSTAL STRUCTURE OF A DESIGNED RESPIRATORY SYNCYTIAL VIRUS IMMUNOGEN TITLE 2 IN COMPLEX WITH RSV90 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: RSV90 FAB HEAVY CHAIN; COMPND 3 CHAIN: E, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RSV90 FAB LIGHT CHAIN; COMPND 7 CHAIN: F, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: DESIGNED SINGLE EPITOPE RESPIRATORY SYNCYTIAL VIRUS COMPND 11 IMMUNOGEN IN COMPLEX WITH RSV90 FAB; COMPND 12 CHAIN: I, J; COMPND 13 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; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 13 ORGANISM_TAXID: 32630; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DESIGNED IMMUNOGEN, SPECIFIC BINDING, RSV F PROTEIN, DE NOVO PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.M.CASTRO,B.E.CORREIA REVDAT 1 21-MAY-25 9F91 0 JRNL AUTH K.M.CASTRO,J.L.WATSON,J.WANG,J.SOUTHERN,R.AYARDULABI, JRNL AUTH 2 S.GEORGEON,S.ROSSET,D.BAKER,B.E.CORREIA JRNL TITL ACCURATE SINGLE DOMAIN SCAFFOLDING OF THREE NON-OVERLAPPING JRNL TITL 2 PROTEIN EPITOPES USING DEEP LEARNING JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.43 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 2.43 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.83 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 52204 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.253 REMARK 3 R VALUE (WORKING SET) : 0.251 REMARK 3 FREE R VALUE : 0.287 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 2632 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 73.8300 - 6.4800 0.99 2798 159 0.1848 0.2153 REMARK 3 2 6.4800 - 5.1400 0.99 2664 136 0.2091 0.2565 REMARK 3 3 5.1400 - 4.4900 1.00 2649 144 0.1846 0.1991 REMARK 3 4 4.4900 - 4.0800 1.00 2630 139 0.2048 0.2335 REMARK 3 5 4.0800 - 3.7900 1.00 2609 133 0.2355 0.2729 REMARK 3 6 3.7900 - 3.5700 1.00 2623 146 0.2623 0.3078 REMARK 3 7 3.5700 - 3.3900 1.00 2623 136 0.2693 0.3329 REMARK 3 8 3.3900 - 3.2400 1.00 2555 152 0.2806 0.3311 REMARK 3 9 3.2400 - 3.1200 0.99 2598 134 0.2928 0.3312 REMARK 3 10 3.1200 - 3.0100 1.00 2578 144 0.3057 0.3326 REMARK 3 11 3.0100 - 2.9100 1.00 2583 137 0.3219 0.3955 REMARK 3 12 2.9100 - 2.8300 1.00 2611 131 0.3307 0.3438 REMARK 3 13 2.8300 - 2.7600 1.00 2578 150 0.3294 0.3832 REMARK 3 14 2.7600 - 2.6900 1.00 2596 142 0.3361 0.3890 REMARK 3 15 2.6900 - 2.6300 1.00 2576 116 0.3510 0.3829 REMARK 3 16 2.6300 - 2.5700 1.00 2594 129 0.3735 0.4184 REMARK 3 17 2.5700 - 2.5200 1.00 2559 149 0.3739 0.4305 REMARK 3 18 2.5200 - 2.4700 1.00 2571 134 0.4048 0.4666 REMARK 3 19 2.4700 - 2.4300 1.00 2589 121 0.4211 0.4535 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) : 0.417 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.564 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 52.45 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.76 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 : 0.017 7830 REMARK 3 ANGLE : 0.753 10655 REMARK 3 CHIRALITY : 0.045 1226 REMARK 3 PLANARITY : 0.009 1361 REMARK 3 DIHEDRAL : 12.269 2767 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 9F91 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1292137980. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-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 : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 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 : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AUTOPROC REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52204 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.430 REMARK 200 RESOLUTION RANGE LOW (A) : 73.830 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 6.360 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.5800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.52 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.21 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5 AND 20 % (V/V) PEG REMARK 280 SMEAR HIGH, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 56.69500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 68.82500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.69500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 68.82500 REMARK 290 SMTRY3 4 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, I 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, J 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 GLU E -2 REMARK 465 THR E -1 REMARK 465 GLY E 0 REMARK 465 SER E 142 REMARK 465 GLU F 0 REMARK 465 GLU F 125 REMARK 465 GLN F 126 REMARK 465 LEU F 127 REMARK 465 LYS F 128 REMARK 465 CYS F 216 REMARK 465 GLU A -2 REMARK 465 THR A -1 REMARK 465 GLY A 0 REMARK 465 GLY A 145 REMARK 465 GLU B 0 REMARK 465 MET I -17 REMARK 465 GLY I -16 REMARK 465 TRP I -15 REMARK 465 HIS I -14 REMARK 465 HIS I -13 REMARK 465 HIS I -12 REMARK 465 HIS I -11 REMARK 465 HIS I -10 REMARK 465 HIS I -9 REMARK 465 GLU I -8 REMARK 465 ASN I -7 REMARK 465 LEU I -6 REMARK 465 TYR I -5 REMARK 465 PHE I -4 REMARK 465 GLN I -3 REMARK 465 GLY I -2 REMARK 465 ALA I -1 REMARK 465 SER I 0 REMARK 465 MET I 1 REMARK 465 GLU I 2 REMARK 465 GLU I 73 REMARK 465 ALA I 74 REMARK 465 GLU I 75 REMARK 465 ARG I 76 REMARK 465 LYS I 77 REMARK 465 GLU I 78 REMARK 465 LYS I 79 REMARK 465 MET J -17 REMARK 465 GLY J -16 REMARK 465 TRP J -15 REMARK 465 HIS J -14 REMARK 465 HIS J -13 REMARK 465 HIS J -12 REMARK 465 HIS J -11 REMARK 465 HIS J -10 REMARK 465 HIS J -9 REMARK 465 GLU J -8 REMARK 465 ASN J -7 REMARK 465 LEU J -6 REMARK 465 TYR J -5 REMARK 465 PHE J -4 REMARK 465 GLN J -3 REMARK 465 GLY J -2 REMARK 465 ALA J -1 REMARK 465 SER J 0 REMARK 465 MET J 1 REMARK 465 GLU J 2 REMARK 465 HIS J 72 REMARK 465 GLU J 73 REMARK 465 ALA J 74 REMARK 465 GLU J 75 REMARK 465 ARG J 76 REMARK 465 LYS J 77 REMARK 465 GLU J 78 REMARK 465 LYS J 79 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 ARG E 117 CZ NH1 NH2 REMARK 470 LYS E 141 CG CD CE NZ REMARK 470 ASP F 124 CG OD1 OD2 REMARK 470 GLU F 145 CD OE1 OE2 REMARK 470 LYS F 185 CG CD CE NZ REMARK 470 GLU F 215 CG CD OE1 OE2 REMARK 470 ARG A 76 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 141 CG CD CE NZ REMARK 470 LYS B 128 CE NZ REMARK 470 GLU B 215 CG CD OE1 OE2 REMARK 470 CYS B 216 SG REMARK 470 LYS I 28 CG CD CE NZ REMARK 470 ARG I 30 CG CD NE CZ NH1 NH2 REMARK 470 LYS I 43 CG CD CE NZ REMARK 470 GLU I 55 CG CD OE1 OE2 REMARK 470 GLU I 71 CG CD OE1 OE2 REMARK 470 HIS I 72 CG ND1 CD2 CE1 NE2 REMARK 470 GLU J 26 CG CD OE1 OE2 REMARK 470 LYS J 28 CG CD CE NZ REMARK 470 ARG J 30 CG CD NE CZ NH1 NH2 REMARK 470 LYS J 43 CG CD CE NZ REMARK 470 GLU J 55 CG CD OE1 OE2 REMARK 470 GLU J 71 CG CD OE1 OE2 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 ARG E 15 -1.77 72.91 REMARK 500 ARG E 16 -159.43 -95.13 REMARK 500 ASP E 156 74.65 56.95 REMARK 500 ILE F 32 -123.03 51.93 REMARK 500 ALA F 86 -167.00 -164.27 REMARK 500 ARG A 15 -15.97 71.73 REMARK 500 ASN A 77 54.09 39.47 REMARK 500 LYS A 155 -70.41 -80.90 REMARK 500 THR A 172 -39.20 -133.73 REMARK 500 ILE B 32 -108.75 52.11 REMARK 500 ASN B 140 75.01 52.79 REMARK 500 LEU I 27 -70.10 -66.78 REMARK 500 LEU J 27 49.65 -82.50 REMARK 500 LYS J 28 -48.44 65.34 REMARK 500 ARG J 30 130.23 -170.51 REMARK 500 REMARK 500 REMARK: NULL DBREF 9F91 E -2 225 PDB 9F91 9F91 -2 225 DBREF 9F91 F 0 216 PDB 9F91 9F91 0 216 DBREF 9F91 A -2 225 PDB 9F91 9F91 -2 225 DBREF 9F91 B 0 216 PDB 9F91 9F91 0 216 DBREF 9F91 I -17 79 PDB 9F91 9F91 -17 79 DBREF 9F91 J -17 79 PDB 9F91 9F91 -17 79 SEQRES 1 E 228 GLU THR GLY GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 E 228 LEU VAL GLN PRO ARG ARG SER LEU ARG LEU SER CYS ALA SEQRES 3 E 228 ALA SER GLY PHE THR PHE ASP ASP TYR THR ILE HIS TRP SEQRES 4 E 228 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SEQRES 5 E 228 GLY ILE THR TRP ASN SER GLY TYR ILE GLY TYR ALA ASP SEQRES 6 E 228 SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA SEQRES 7 E 228 ARG ASN SER LEU TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 E 228 GLU ASP THR ALA LEU TYR TYR CYS VAL ARG ASP ALA TYR SEQRES 9 E 228 VAL SER GLY SER ASP TYR TYR TYR TYR GLY LEU ASP VAL SEQRES 10 E 228 TRP GLY ARG GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 11 E 228 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 E 228 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 E 228 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 E 228 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 E 228 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 E 228 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 E 228 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 E 228 VAL ASP LYS LYS VAL GLU PRO SEQRES 1 F 217 GLU THR GLY GLU ILE VAL MET THR SER SER PRO ALA THR SEQRES 2 F 217 LEU SER VAL SER PRO GLY GLU ARG VAL THR LEU PHE CYS SEQRES 3 F 217 ARG ALA SER GLN SER VAL ILE SER ASN LEU ALA TRP TYR SEQRES 4 F 217 GLN GLN LYS SER GLY GLN ALA PRO ARG LEU LEU ILE TYR SEQRES 5 F 217 GLY ALA SER THR ARG ALA THR GLY ILE PRO SER ARG PHE SEQRES 6 F 217 SER GLY SER GLY SER GLY THR GLU PHE THR LEU THR ILE SEQRES 7 F 217 SER SER LEU GLN SER GLU ASP PHE ALA VAL TYR PHE CYS SEQRES 8 F 217 GLN GLN TYR ASN ASN TRP PRO LEU THR PHE GLY GLY GLY SEQRES 9 F 217 THR GLN VAL ASN VAL GLN ARG THR VAL ALA ALA PRO SER SEQRES 10 F 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 F 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 F 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 F 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 F 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 F 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 F 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 F 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 228 GLU THR GLY GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 A 228 LEU VAL GLN PRO ARG ARG SER LEU ARG LEU SER CYS ALA SEQRES 3 A 228 ALA SER GLY PHE THR PHE ASP ASP TYR THR ILE HIS TRP SEQRES 4 A 228 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SEQRES 5 A 228 GLY ILE THR TRP ASN SER GLY TYR ILE GLY TYR ALA ASP SEQRES 6 A 228 SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA SEQRES 7 A 228 ARG ASN SER LEU TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 A 228 GLU ASP THR ALA LEU TYR TYR CYS VAL ARG ASP ALA TYR SEQRES 9 A 228 VAL SER GLY SER ASP TYR TYR TYR TYR GLY LEU ASP VAL SEQRES 10 A 228 TRP GLY ARG GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 11 A 228 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 A 228 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 A 228 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 A 228 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 A 228 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 A 228 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 A 228 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 A 228 VAL ASP LYS LYS VAL GLU PRO SEQRES 1 B 217 GLU THR GLY GLU ILE VAL MET THR SER SER PRO ALA THR SEQRES 2 B 217 LEU SER VAL SER PRO GLY GLU ARG VAL THR LEU PHE CYS SEQRES 3 B 217 ARG ALA SER GLN SER VAL ILE SER ASN LEU ALA TRP TYR SEQRES 4 B 217 GLN GLN LYS SER GLY GLN ALA PRO ARG LEU LEU ILE TYR SEQRES 5 B 217 GLY ALA SER THR ARG ALA THR GLY ILE PRO SER ARG PHE SEQRES 6 B 217 SER GLY SER GLY SER GLY THR GLU PHE THR LEU THR ILE SEQRES 7 B 217 SER SER LEU GLN SER GLU ASP PHE ALA VAL TYR PHE CYS SEQRES 8 B 217 GLN GLN TYR ASN ASN TRP PRO LEU THR PHE GLY GLY GLY SEQRES 9 B 217 THR GLN VAL ASN VAL GLN ARG THR VAL ALA ALA PRO SER SEQRES 10 B 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 B 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 B 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 B 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 B 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 B 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 B 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 B 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 I 97 MET GLY TRP HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR SEQRES 2 I 97 PHE GLN GLY ALA SER MET GLU THR GLU GLU GLU ILE ILE SEQRES 3 I 97 GLU LYS VAL LYS SER ALA LEU LEU SER THR ASN LYS ALA SEQRES 4 I 97 VAL ILE SER VAL GLU LEU LYS GLY ARG THR ILE PRO LEU SEQRES 5 I 97 TYR VAL GLU ILE THR LYS GLU GLY LYS LEU HIS LEU THR SEQRES 6 I 97 ALA GLU GLY ALA THR GLU GLU GLU LYS GLU ILE ILE LYS SEQRES 7 I 97 GLU ALA GLN LYS ALA PHE GLN GLU GLU ILE GLU HIS GLU SEQRES 8 I 97 ALA GLU ARG LYS GLU LYS SEQRES 1 J 97 MET GLY TRP HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR SEQRES 2 J 97 PHE GLN GLY ALA SER MET GLU THR GLU GLU GLU ILE ILE SEQRES 3 J 97 GLU LYS VAL LYS SER ALA LEU LEU SER THR ASN LYS ALA SEQRES 4 J 97 VAL ILE SER VAL GLU LEU LYS GLY ARG THR ILE PRO LEU SEQRES 5 J 97 TYR VAL GLU ILE THR LYS GLU GLY LYS LEU HIS LEU THR SEQRES 6 J 97 ALA GLU GLY ALA THR GLU GLU GLU LYS GLU ILE ILE LYS SEQRES 7 J 97 GLU ALA GLN LYS ALA PHE GLN GLU GLU ILE GLU HIS GLU SEQRES 8 J 97 ALA GLU ARG LYS GLU LYS FORMUL 7 HOH *43(H2 O) HELIX 1 AA1 THR E 28 TYR E 32 5 5 HELIX 2 AA2 ARG E 87 THR E 91 5 5 HELIX 3 AA3 SER E 199 THR E 203 5 5 HELIX 4 AA4 LYS E 213 ASN E 216 5 4 HELIX 5 AA5 GLN F 81 PHE F 85 5 5 HELIX 6 AA6 SER F 184 GLU F 189 1 6 HELIX 7 AA7 THR A 28 TYR A 32 5 5 HELIX 8 AA8 ASN A 74 ARG A 76 5 3 HELIX 9 AA9 ARG A 87 THR A 91 5 5 HELIX 10 AB1 SER A 199 THR A 203 5 5 HELIX 11 AB2 LYS A 213 ASN A 216 5 4 HELIX 12 AB3 GLN B 81 PHE B 85 5 5 HELIX 13 AB4 SER B 123 GLY B 130 1 8 HELIX 14 AB5 LYS B 185 GLU B 189 1 5 HELIX 15 AB6 GLU I 4 LEU I 15 1 12 HELIX 16 AB7 THR I 52 HIS I 72 1 21 HELIX 17 AB8 GLU J 4 LEU J 15 1 12 HELIX 18 AB9 THR J 52 GLU J 69 1 18 SHEET 1 AA1 4 GLN E 3 SER E 7 0 SHEET 2 AA1 4 LEU E 18 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AA1 4 SER E 78 MET E 83 -1 O MET E 83 N LEU E 18 SHEET 4 AA1 4 PHE E 68 ASP E 73 -1 N THR E 69 O GLN E 82 SHEET 1 AA2 6 LEU E 11 VAL E 12 0 SHEET 2 AA2 6 THR E 119 VAL E 123 1 O THR E 122 N VAL E 12 SHEET 3 AA2 6 ALA E 92 ASP E 99 -1 N TYR E 94 O THR E 119 SHEET 4 AA2 6 ILE E 34 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AA2 6 LEU E 45 ILE E 51 -1 O SER E 49 N TRP E 36 SHEET 6 AA2 6 ILE E 58 TYR E 60 -1 O GLY E 59 N GLY E 50 SHEET 1 AA3 4 LEU E 11 VAL E 12 0 SHEET 2 AA3 4 THR E 119 VAL E 123 1 O THR E 122 N VAL E 12 SHEET 3 AA3 4 ALA E 92 ASP E 99 -1 N TYR E 94 O THR E 119 SHEET 4 AA3 4 LEU E 112 TRP E 115 -1 O VAL E 114 N ARG E 98 SHEET 1 AA4 4 SER E 132 LEU E 136 0 SHEET 2 AA4 4 THR E 147 TYR E 157 -1 O GLY E 151 N LEU E 136 SHEET 3 AA4 4 TYR E 188 PRO E 197 -1 O VAL E 196 N ALA E 148 SHEET 4 AA4 4 VAL E 175 THR E 177 -1 N HIS E 176 O VAL E 193 SHEET 1 AA5 4 SER E 132 LEU E 136 0 SHEET 2 AA5 4 THR E 147 TYR E 157 -1 O GLY E 151 N LEU E 136 SHEET 3 AA5 4 TYR E 188 PRO E 197 -1 O VAL E 196 N ALA E 148 SHEET 4 AA5 4 VAL E 181 LEU E 182 -1 N VAL E 181 O SER E 189 SHEET 1 AA6 3 THR E 163 TRP E 166 0 SHEET 2 AA6 3 TYR E 206 HIS E 212 -1 O ASN E 209 N SER E 165 SHEET 3 AA6 3 THR E 217 VAL E 223 -1 O THR E 217 N HIS E 212 SHEET 1 AA7 4 MET F 6 SER F 9 0 SHEET 2 AA7 4 VAL F 21 ALA F 27 -1 O PHE F 24 N SER F 9 SHEET 3 AA7 4 GLU F 72 ILE F 77 -1 O ILE F 77 N VAL F 21 SHEET 4 AA7 4 PHE F 64 GLY F 68 -1 N SER F 65 O THR F 76 SHEET 1 AA8 5 THR F 12 VAL F 15 0 SHEET 2 AA8 5 THR F 104 VAL F 108 1 O ASN F 107 N LEU F 13 SHEET 3 AA8 5 VAL F 87 GLN F 92 -1 N TYR F 88 O THR F 104 SHEET 4 AA8 5 LEU F 35 GLN F 40 -1 N ALA F 36 O GLN F 91 SHEET 5 AA8 5 ARG F 47 ILE F 50 -1 O LEU F 49 N TRP F 37 SHEET 1 AA9 4 THR F 12 VAL F 15 0 SHEET 2 AA9 4 THR F 104 VAL F 108 1 O ASN F 107 N LEU F 13 SHEET 3 AA9 4 VAL F 87 GLN F 92 -1 N TYR F 88 O THR F 104 SHEET 4 AA9 4 THR F 99 PHE F 100 -1 O THR F 99 N GLN F 92 SHEET 1 AB1 4 SER F 116 PHE F 120 0 SHEET 2 AB1 4 SER F 133 PHE F 141 -1 O LEU F 137 N PHE F 118 SHEET 3 AB1 4 TYR F 175 THR F 182 -1 O LEU F 181 N VAL F 134 SHEET 4 AB1 4 SER F 161 VAL F 165 -1 N GLN F 162 O THR F 180 SHEET 1 AB2 4 ALA F 155 LEU F 156 0 SHEET 2 AB2 4 LYS F 147 VAL F 152 -1 N VAL F 152 O ALA F 155 SHEET 3 AB2 4 VAL F 193 THR F 199 -1 O GLU F 197 N GLN F 149 SHEET 4 AB2 4 VAL F 207 ASN F 212 -1 O LYS F 209 N CYS F 196 SHEET 1 AB3 4 GLN A 3 SER A 7 0 SHEET 2 AB3 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AB3 4 SER A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AB3 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AB4 6 LEU A 11 VAL A 12 0 SHEET 2 AB4 6 THR A 119 VAL A 123 1 O THR A 122 N VAL A 12 SHEET 3 AB4 6 ALA A 92 ASP A 99 -1 N TYR A 94 O THR A 119 SHEET 4 AB4 6 ILE A 34 GLN A 39 -1 N HIS A 35 O VAL A 97 SHEET 5 AB4 6 LEU A 45 ILE A 51 -1 O VAL A 48 N TRP A 36 SHEET 6 AB4 6 ILE A 58 TYR A 60 -1 O GLY A 59 N GLY A 50 SHEET 1 AB5 4 LEU A 11 VAL A 12 0 SHEET 2 AB5 4 THR A 119 VAL A 123 1 O THR A 122 N VAL A 12 SHEET 3 AB5 4 ALA A 92 ASP A 99 -1 N TYR A 94 O THR A 119 SHEET 4 AB5 4 LEU A 112 TRP A 115 -1 O VAL A 114 N ARG A 98 SHEET 1 AB6 4 VAL A 133 LEU A 136 0 SHEET 2 AB6 4 THR A 147 TYR A 157 -1 O LEU A 153 N PHE A 134 SHEET 3 AB6 4 TYR A 188 PRO A 197 -1 O VAL A 196 N ALA A 148 SHEET 4 AB6 4 VAL A 175 THR A 177 -1 N HIS A 176 O VAL A 193 SHEET 1 AB7 4 VAL A 133 LEU A 136 0 SHEET 2 AB7 4 THR A 147 TYR A 157 -1 O LEU A 153 N PHE A 134 SHEET 3 AB7 4 TYR A 188 PRO A 197 -1 O VAL A 196 N ALA A 148 SHEET 4 AB7 4 VAL A 181 LEU A 182 -1 N VAL A 181 O SER A 189 SHEET 1 AB8 3 THR A 163 TRP A 166 0 SHEET 2 AB8 3 TYR A 206 HIS A 212 -1 O ASN A 209 N SER A 165 SHEET 3 AB8 3 THR A 217 VAL A 223 -1 O LYS A 221 N CYS A 208 SHEET 1 AB9 4 MET B 6 SER B 9 0 SHEET 2 AB9 4 VAL B 21 ALA B 27 -1 O PHE B 24 N SER B 9 SHEET 3 AB9 4 GLU B 72 ILE B 77 -1 O LEU B 75 N LEU B 23 SHEET 4 AB9 4 PHE B 64 SER B 69 -1 N SER B 65 O THR B 76 SHEET 1 AC1 5 THR B 12 VAL B 15 0 SHEET 2 AC1 5 THR B 104 VAL B 108 1 O ASN B 107 N LEU B 13 SHEET 3 AC1 5 VAL B 87 GLN B 92 -1 N TYR B 88 O THR B 104 SHEET 4 AC1 5 LEU B 35 GLN B 40 -1 N GLN B 40 O VAL B 87 SHEET 5 AC1 5 ARG B 47 ILE B 50 -1 O LEU B 49 N TRP B 37 SHEET 1 AC2 4 THR B 12 VAL B 15 0 SHEET 2 AC2 4 THR B 104 VAL B 108 1 O ASN B 107 N LEU B 13 SHEET 3 AC2 4 VAL B 87 GLN B 92 -1 N TYR B 88 O THR B 104 SHEET 4 AC2 4 THR B 99 PHE B 100 -1 O THR B 99 N GLN B 92 SHEET 1 AC3 4 SER B 116 PHE B 120 0 SHEET 2 AC3 4 THR B 131 PHE B 141 -1 O LEU B 137 N PHE B 118 SHEET 3 AC3 4 TYR B 175 SER B 184 -1 O LEU B 181 N VAL B 134 SHEET 4 AC3 4 SER B 161 VAL B 165 -1 N GLN B 162 O THR B 180 SHEET 1 AC4 4 ALA B 155 LEU B 156 0 SHEET 2 AC4 4 LYS B 147 VAL B 152 -1 N VAL B 152 O ALA B 155 SHEET 3 AC4 4 VAL B 193 THR B 199 -1 O ALA B 195 N LYS B 151 SHEET 4 AC4 4 VAL B 207 ASN B 212 -1 O VAL B 207 N VAL B 198 SHEET 1 AC5 3 LYS I 20 GLU I 26 0 SHEET 2 AC5 3 THR I 31 ILE I 38 -1 O ILE I 32 N VAL I 25 SHEET 3 AC5 3 LEU I 44 ALA I 48 -1 O THR I 47 N TYR I 35 SHEET 1 AC6 2 LYS J 20 GLU J 26 0 SHEET 2 AC6 2 THR J 31 GLU J 37 -1 O ILE J 32 N VAL J 25 SSBOND 1 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 2 CYS E 152 CYS E 208 1555 1555 2.03 SSBOND 3 CYS F 25 CYS F 90 1555 1555 2.04 SSBOND 4 CYS F 136 CYS F 196 1555 1555 2.03 SSBOND 5 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 6 CYS A 152 CYS A 208 1555 1555 2.03 SSBOND 7 CYS B 25 CYS B 90 1555 1555 2.04 SSBOND 8 CYS B 136 CYS B 196 1555 1555 2.03 CISPEP 1 PHE E 158 PRO E 159 0 -2.38 CISPEP 2 GLU E 160 PRO E 161 0 -0.74 CISPEP 3 SER F 9 PRO F 10 0 -4.34 CISPEP 4 TRP F 96 PRO F 97 0 2.54 CISPEP 5 TYR F 142 PRO F 143 0 0.58 CISPEP 6 PHE A 158 PRO A 159 0 -3.94 CISPEP 7 GLU A 160 PRO A 161 0 -1.21 CISPEP 8 SER B 9 PRO B 10 0 -2.12 CISPEP 9 TRP B 96 PRO B 97 0 5.19 CISPEP 10 TYR B 142 PRO B 143 0 0.11 CRYST1 113.390 137.650 87.470 90.00 90.00 90.00 P 21 21 2 8 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 0.008819 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007265 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011432 0.00000