HEADER DE NOVO PROTEIN 07-MAY-24 9F90 TITLE CRYSTAL STRUCTURE OF A DESIGNED THREE-MOTIF RESPIRATORY SYNCYTIAL TITLE 2 VIRUS IMMUNOGEN IN COMPLEX WITH MOTAVIZUMAB FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: MOTAVIZUMAB FAB LIGHT CHAIN; COMPND 3 CHAIN: B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MOTAVIZUMAB FAB HEAVY CHAIN; COMPND 7 CHAIN: A, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: RSVF-MULTI-EPITOPE DESIGNED SCAFFOLD; COMPND 11 CHAIN: H, G; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; 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 9F90 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. 2.91 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) : 2.91 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 28679 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.226 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.262 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920 REMARK 3 FREE R VALUE TEST SET COUNT : 1411 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 61.5000 - 6.2600 0.99 2816 139 0.2065 0.2270 REMARK 3 2 6.2600 - 4.9700 1.00 2743 144 0.1994 0.2108 REMARK 3 3 4.9700 - 4.3400 1.00 2756 137 0.1684 0.2334 REMARK 3 4 4.3400 - 3.9500 1.00 2719 136 0.1967 0.2527 REMARK 3 5 3.9400 - 3.6600 1.00 2701 151 0.2238 0.2523 REMARK 3 6 3.6600 - 3.4500 1.00 2733 144 0.2322 0.2731 REMARK 3 7 3.4500 - 3.2700 1.00 2697 142 0.2508 0.3015 REMARK 3 8 3.2700 - 3.1300 1.00 2699 137 0.2936 0.3325 REMARK 3 9 3.1300 - 3.0100 1.00 2712 136 0.3089 0.3339 REMARK 3 10 3.0100 - 2.9100 1.00 2692 145 0.3240 0.3649 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) : 0.361 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.906 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 45.57 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.42 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 8428 REMARK 3 ANGLE : 1.081 11473 REMARK 3 CHIRALITY : 0.064 1327 REMARK 3 PLANARITY : 0.008 1452 REMARK 3 DIHEDRAL : 15.606 2994 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 9F90 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_1292138394. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-SEP-23 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 : 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) : 0.873129 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AUTOPROC REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28710 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.907 REMARK 200 RESOLUTION RANGE LOW (A) : 89.350 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 3.030 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.1400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.91 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.01 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 (%): 53.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM THIOCYANATE, 0.1 M REMARK 280 SODIUM CACODYLATE PH 6.5, AND 10 % (V/V) PEG 1000, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291.15K 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 92.03600 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.42950 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.03600 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.42950 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: B, A, H 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: C, D, G 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 K K A 301 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 GLY B 213 REMARK 465 GLU B 214 REMARK 465 SER A 127 REMARK 465 SER A 128 REMARK 465 LYS A 129 REMARK 465 SER A 130 REMARK 465 THR A 131 REMARK 465 SER A 132 REMARK 465 GLY A 133 REMARK 465 GLY A 134 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 GLY C 212 REMARK 465 GLY C 213 REMARK 465 GLU C 214 REMARK 465 SER D 127 REMARK 465 SER D 128 REMARK 465 LYS D 129 REMARK 465 SER D 130 REMARK 465 THR D 131 REMARK 465 SER D 132 REMARK 465 GLY D 133 REMARK 465 GLY D 134 REMARK 465 LYS D 214 REMARK 465 SER D 215 REMARK 465 CYS D 216 REMARK 465 ASP D 217 REMARK 465 LYS D 218 REMARK 465 MET H -17 REMARK 465 GLY H -16 REMARK 465 TRP H -15 REMARK 465 HIS H -14 REMARK 465 HIS H -13 REMARK 465 HIS H -12 REMARK 465 HIS H -11 REMARK 465 HIS H -10 REMARK 465 HIS H -9 REMARK 465 GLU H -8 REMARK 465 ASN H -7 REMARK 465 LEU H -6 REMARK 465 TYR H -5 REMARK 465 PHE H -4 REMARK 465 GLN H -3 REMARK 465 GLY H -2 REMARK 465 ALA H -1 REMARK 465 MET G -17 REMARK 465 GLY G -16 REMARK 465 TRP G -15 REMARK 465 HIS G -14 REMARK 465 HIS G -13 REMARK 465 HIS G -12 REMARK 465 HIS G -11 REMARK 465 HIS G -10 REMARK 465 HIS G -9 REMARK 465 GLU G -8 REMARK 465 ASN G -7 REMARK 465 LEU G -6 REMARK 465 TYR G -5 REMARK 465 PHE G -4 REMARK 465 GLN G -3 REMARK 465 GLY G -2 REMARK 465 ALA G -1 REMARK 465 SER G 0 REMARK 465 ALA G 33 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 143 CG CD OE1 OE2 REMARK 470 ARG A 5 NE CZ NH1 NH2 REMARK 470 LYS A 13 NZ REMARK 470 LYS A 64 CG CD CE NZ REMARK 470 ARG C 142 CZ NH1 NH2 REMARK 470 ARG D 5 NE CZ NH1 NH2 REMARK 470 LYS D 64 CG CD CE NZ REMARK 470 LYS D 81 CG CD CE NZ REMARK 470 GLU H 24 CG CD OE1 OE2 REMARK 470 LYS H 32 CE NZ REMARK 470 GLU H 41 CG CD OE1 OE2 REMARK 470 LYS H 44 CE NZ REMARK 470 PHE H 50 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP H 53 CG OD1 OD2 REMARK 470 GLU H 58 CD OE1 OE2 REMARK 470 LYS H 64 CG CD CE NZ REMARK 470 ASN H 65 CG OD1 ND2 REMARK 470 ILE H 107 CG1 CG2 CD1 REMARK 470 GLU H 109 CD OE1 OE2 REMARK 470 LYS H 116 CG CD CE NZ REMARK 470 MET G 1 CG SD CE REMARK 470 LYS G 18 CG CD CE NZ REMARK 470 GLU G 21 CD OE1 OE2 REMARK 470 LYS G 22 CD CE NZ REMARK 470 ILE G 23 CG1 CG2 CD1 REMARK 470 GLU G 24 CD OE1 OE2 REMARK 470 LYS G 28 CG CD CE NZ REMARK 470 ASN G 31 CG OD1 ND2 REMARK 470 LYS G 32 CG CD CE NZ REMARK 470 LYS G 40 CD CE NZ REMARK 470 LYS G 44 CE NZ REMARK 470 LYS G 52 CG CD CE NZ REMARK 470 ASP G 53 CG OD1 OD2 REMARK 470 VAL G 55 CG1 CG2 REMARK 470 GLU G 58 CG CD OE1 OE2 REMARK 470 ARG G 60 CG CD NE CZ NH1 NH2 REMARK 470 ASP G 63 CG OD1 OD2 REMARK 470 LYS G 64 CG CD CE NZ REMARK 470 ASN G 65 CG OD1 ND2 REMARK 470 LYS G 70 CG CD CE NZ REMARK 470 LYS G 75 CE NZ REMARK 470 GLU G 76 CG CD OE1 OE2 REMARK 470 LYS G 116 CG CD CE NZ 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 LEU B 47 -62.81 -101.01 REMARK 500 THR B 51 -48.04 68.56 REMARK 500 SER B 52 30.94 -142.39 REMARK 500 ALA B 84 -174.23 -173.15 REMARK 500 ASN B 137 -150.23 54.73 REMARK 500 THR A 15 -6.03 70.54 REMARK 500 PRO A 61 -5.37 -58.67 REMARK 500 ASP A 144 72.75 47.76 REMARK 500 LEU C 47 -62.60 -93.99 REMARK 500 THR C 51 -42.95 68.55 REMARK 500 SER C 52 24.12 -146.88 REMARK 500 ALA C 84 -171.46 -172.66 REMARK 500 PRO C 141 -164.73 -78.18 REMARK 500 ASP D 65 -15.23 71.47 REMARK 500 PRO D 84 -34.10 -38.66 REMARK 500 LYS D 143 -64.82 -97.68 REMARK 500 ASP H 9 -121.18 53.17 REMARK 500 ASP H 63 -137.56 -93.54 REMARK 500 ASP G 9 -145.31 57.46 REMARK 500 LYS G 64 -128.08 56.01 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 K A 301 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 LYS A 71 O REMARK 620 2 LYS A 71 O 0.0 REMARK 620 N 1 DBREF 9F90 B 1 214 PDB 9F90 9F90 1 214 DBREF 9F90 A 1 218 PDB 9F90 9F90 1 218 DBREF 9F90 C 1 214 PDB 9F90 9F90 1 214 DBREF 9F90 D 1 218 PDB 9F90 9F90 1 218 DBREF 9F90 H -17 116 PDB 9F90 9F90 -17 116 DBREF 9F90 G -17 116 PDB 9F90 9F90 -17 116 SEQRES 1 B 213 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 B 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS SER ALA SER SEQRES 3 B 213 SER ARG VAL GLY TYR MET HIS TRP TYR GLN GLN LYS PRO SEQRES 4 B 213 GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP THR SER LYS SEQRES 5 B 213 LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 B 213 SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU GLN SEQRES 7 B 213 PRO ASP ASP PHE ALA THR TYR TYR CYS PHE GLN GLY SER SEQRES 8 B 213 GLY TYR PRO PHE THR PHE GLY GLY GLY THR LYS VAL GLU SEQRES 9 B 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 B 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 B 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 B 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 B 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 B 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 B 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 B 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 B 213 ASN ARG GLY GLY GLU SEQRES 1 A 225 GLN VAL THR LEU ARG GLU SER GLY PRO ALA LEU VAL LYS SEQRES 2 A 225 PRO THR GLN THR LEU THR LEU THR CYS THR PHE SER GLY SEQRES 3 A 225 PHE SER LEU SER THR ALA GLY MET SER VAL GLY TRP ILE SEQRES 4 A 225 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA ASP SEQRES 5 A 225 ILE TRP TRP ASP ASP LYS LYS HIS TYR ASN PRO SER LEU SEQRES 6 A 225 LYS ASP ARG LEU THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 A 225 GLN VAL VAL LEU LYS VAL THR ASN MET ASP PRO ALA ASP SEQRES 8 A 225 THR ALA THR TYR TYR CYS ALA ARG ASP MET ILE PHE ASN SEQRES 9 A 225 PHE TYR PHE ASP VAL TRP GLY GLN GLY THR THR VAL THR SEQRES 10 A 225 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 A 225 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 A 225 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 A 225 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 A 225 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 A 225 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 A 225 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 A 225 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 A 225 SER CYS ASP LYS SEQRES 1 C 213 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 C 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS SER ALA SER SEQRES 3 C 213 SER ARG VAL GLY TYR MET HIS TRP TYR GLN GLN LYS PRO SEQRES 4 C 213 GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP THR SER LYS SEQRES 5 C 213 LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 C 213 SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU GLN SEQRES 7 C 213 PRO ASP ASP PHE ALA THR TYR TYR CYS PHE GLN GLY SER SEQRES 8 C 213 GLY TYR PRO PHE THR PHE GLY GLY GLY THR LYS VAL GLU SEQRES 9 C 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 C 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 C 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 C 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 C 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 C 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 C 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 C 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 C 213 ASN ARG GLY GLY GLU SEQRES 1 D 225 GLN VAL THR LEU ARG GLU SER GLY PRO ALA LEU VAL LYS SEQRES 2 D 225 PRO THR GLN THR LEU THR LEU THR CYS THR PHE SER GLY SEQRES 3 D 225 PHE SER LEU SER THR ALA GLY MET SER VAL GLY TRP ILE SEQRES 4 D 225 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA ASP SEQRES 5 D 225 ILE TRP TRP ASP ASP LYS LYS HIS TYR ASN PRO SER LEU SEQRES 6 D 225 LYS ASP ARG LEU THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 D 225 GLN VAL VAL LEU LYS VAL THR ASN MET ASP PRO ALA ASP SEQRES 8 D 225 THR ALA THR TYR TYR CYS ALA ARG ASP MET ILE PHE ASN SEQRES 9 D 225 PHE TYR PHE ASP VAL TRP GLY GLN GLY THR THR VAL THR SEQRES 10 D 225 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 D 225 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 D 225 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 D 225 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 D 225 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 D 225 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 D 225 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 D 225 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 D 225 SER CYS ASP LYS SEQRES 1 H 134 MET GLY TRP HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR SEQRES 2 H 134 PHE GLN GLY ALA SER MET LYS TYR MET LEU VAL LYS ALA SEQRES 3 H 134 ASP ASP TYR TYR PHE LEU LEU PRO PRO LYS ASP VAL GLU SEQRES 4 H 134 LYS ILE GLU SER ALA LEU LYS SER THR ASN LYS ALA VAL SEQRES 5 H 134 VAL SER PHE PHE ASP LYS GLU ASN ASN LYS THR TYR GLU SEQRES 6 H 134 PHE THR PHE ASN LYS ASP LEU VAL VAL THR GLU VAL ARG SEQRES 7 H 134 GLU THR ASP LYS ASN ARG GLY ILE ILE LYS THR PHE SER SEQRES 8 H 134 VAL LYS GLU VAL LYS PHE PHE ASP ASN LYS GLU GLU LEU SEQRES 9 H 134 LEU GLU TYR ILE ASN ASP LEU PRO ILE SER ASN ASP ASP SEQRES 10 H 134 LYS LYS LEU LEU SER ASN ASN ILE ASP GLU PHE LEU VAL SEQRES 11 H 134 VAL LYS ALA LYS SEQRES 1 G 134 MET GLY TRP HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR SEQRES 2 G 134 PHE GLN GLY ALA SER MET LYS TYR MET LEU VAL LYS ALA SEQRES 3 G 134 ASP ASP TYR TYR PHE LEU LEU PRO PRO LYS ASP VAL GLU SEQRES 4 G 134 LYS ILE GLU SER ALA LEU LYS SER THR ASN LYS ALA VAL SEQRES 5 G 134 VAL SER PHE PHE ASP LYS GLU ASN ASN LYS THR TYR GLU SEQRES 6 G 134 PHE THR PHE ASN LYS ASP LEU VAL VAL THR GLU VAL ARG SEQRES 7 G 134 GLU THR ASP LYS ASN ARG GLY ILE ILE LYS THR PHE SER SEQRES 8 G 134 VAL LYS GLU VAL LYS PHE PHE ASP ASN LYS GLU GLU LEU SEQRES 9 G 134 LEU GLU TYR ILE ASN ASP LEU PRO ILE SER ASN ASP ASP SEQRES 10 G 134 LYS LYS LEU LEU SER ASN ASN ILE ASP GLU PHE LEU VAL SEQRES 11 G 134 VAL LYS ALA LYS HET K B 301 1 HET K A 301 1 HET K C 301 1 HET K H 201 1 HETNAM K POTASSIUM ION FORMUL 7 K 4(K 1+) FORMUL 11 HOH *45(H2 O) HELIX 1 AA1 GLN B 79 PHE B 83 5 5 HELIX 2 AA2 SER B 121 SER B 127 1 7 HELIX 3 AA3 LYS B 183 GLU B 187 1 5 HELIX 4 AA4 ASP A 83 THR A 87 5 5 HELIX 5 AA5 PRO A 185 LEU A 189 5 5 HELIX 6 AA6 LYS A 201 ASN A 204 5 4 HELIX 7 AA7 GLN C 79 PHE C 83 5 5 HELIX 8 AA8 SER C 121 SER C 127 1 7 HELIX 9 AA9 LYS C 183 LYS C 188 1 6 HELIX 10 AB1 ASP D 83 THR D 87 5 5 HELIX 11 AB2 SER D 156 ALA D 158 5 3 HELIX 12 AB3 LYS D 201 ASN D 204 5 4 HELIX 13 AB4 PRO H 16 THR H 30 1 15 HELIX 14 AB5 ASN H 82 LEU H 93 1 12 HELIX 15 AB6 SER H 96 ASN H 106 1 11 HELIX 16 AB7 PRO G 16 THR G 30 1 15 HELIX 17 AB8 ASN G 82 ASN G 91 1 10 HELIX 18 AB9 SER G 96 ASN G 106 1 11 SHEET 1 AA1 3 MET B 4 SER B 7 0 SHEET 2 AA1 3 VAL B 19 VAL B 30 -1 O THR B 22 N SER B 7 SHEET 3 AA1 3 PHE B 62 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 1 AA212 LYS B 53 LEU B 54 0 SHEET 2 AA212 LYS B 45 TYR B 49 -1 N TYR B 49 O LYS B 53 SHEET 3 AA212 HIS B 34 GLN B 38 -1 N TRP B 35 O ILE B 48 SHEET 4 AA212 ALA B 84 GLN B 90 -1 O PHE B 89 N HIS B 34 SHEET 5 AA212 THR B 102 LYS B 107 -1 O VAL B 104 N ALA B 84 SHEET 6 AA212 THR B 10 SER B 14 1 N LEU B 11 O GLU B 105 SHEET 7 AA212 THR C 10 SER C 14 -1 O THR C 10 N SER B 12 SHEET 8 AA212 THR C 102 LYS C 107 1 O GLU C 105 N LEU C 11 SHEET 9 AA212 ALA C 84 GLN C 90 -1 N TYR C 86 O THR C 102 SHEET 10 AA212 HIS C 34 GLN C 38 -1 N TYR C 36 O TYR C 87 SHEET 11 AA212 LYS C 45 TYR C 49 -1 O ILE C 48 N TRP C 35 SHEET 12 AA212 LYS C 53 LEU C 54 -1 O LYS C 53 N TYR C 49 SHEET 1 AA3 8 THR B 97 PHE B 98 0 SHEET 2 AA3 8 ALA B 84 GLN B 90 -1 N GLN B 90 O THR B 97 SHEET 3 AA3 8 THR B 102 LYS B 107 -1 O VAL B 104 N ALA B 84 SHEET 4 AA3 8 THR B 10 SER B 14 1 N LEU B 11 O GLU B 105 SHEET 5 AA3 8 THR C 10 SER C 14 -1 O THR C 10 N SER B 12 SHEET 6 AA3 8 THR C 102 LYS C 107 1 O GLU C 105 N LEU C 11 SHEET 7 AA3 8 ALA C 84 GLN C 90 -1 N TYR C 86 O THR C 102 SHEET 8 AA3 8 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90 SHEET 1 AA4 4 PHE B 116 PHE B 118 0 SHEET 2 AA4 4 THR B 129 LEU B 135 -1 O VAL B 133 N PHE B 118 SHEET 3 AA4 4 LEU B 175 SER B 182 -1 O LEU B 181 N ALA B 130 SHEET 4 AA4 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 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 THR A 3 SER A 7 0 SHEET 2 AA6 4 LEU A 18 SER A 25 -1 O THR A 23 N ARG A 5 SHEET 3 AA6 4 GLN A 77 VAL A 82 -1 O VAL A 78 N CYS A 22 SHEET 4 AA6 4 LEU A 67 ASP A 72 -1 N THR A 68 O LYS A 81 SHEET 1 AA7 6 LEU A 11 VAL A 12 0 SHEET 2 AA7 6 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA7 6 ALA A 88 MET A 96 -1 N TYR A 90 O THR A 107 SHEET 4 AA7 6 MET A 34 GLN A 39 -1 N ILE A 37 O TYR A 91 SHEET 5 AA7 6 GLU A 46 TRP A 52 -1 O LEU A 48 N TRP A 36 SHEET 6 AA7 6 LYS A 57 TYR A 59 -1 O HIS A 58 N ASP A 50 SHEET 1 AA8 4 LEU A 11 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 MET A 96 -1 N TYR A 90 O THR A 107 SHEET 4 AA8 4 ASN A 99 TRP A 103 -1 O VAL A 102 N ARG A 94 SHEET 1 AA9 4 SER A 120 LEU A 124 0 SHEET 2 AA9 4 ALA A 136 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA9 4 TYR A 176 VAL A 184 -1 O TYR A 176 N TYR A 145 SHEET 4 AA9 4 HIS A 164 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 ALA A 136 TYR A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AB1 4 TYR A 176 VAL A 184 -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 TYR A 194 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AB2 3 THR A 205 VAL A 211 -1 O VAL A 211 N TYR A 194 SHEET 1 AB3 3 MET C 4 SER C 7 0 SHEET 2 AB3 3 VAL C 19 VAL C 30 -1 O THR C 22 N SER C 7 SHEET 3 AB3 3 PHE C 62 ILE C 75 -1 O THR C 69 N ALA C 25 SHEET 1 AB4 4 VAL C 115 PHE C 118 0 SHEET 2 AB4 4 THR C 129 PHE C 139 -1 O VAL C 133 N PHE C 118 SHEET 3 AB4 4 TYR C 173 SER C 182 -1 O LEU C 179 N VAL C 132 SHEET 4 AB4 4 SER C 159 VAL C 163 -1 N GLN C 160 O THR C 178 SHEET 1 AB5 4 ALA C 153 LEU C 154 0 SHEET 2 AB5 4 ALA C 144 VAL C 150 -1 N VAL C 150 O ALA C 153 SHEET 3 AB5 4 VAL C 191 HIS C 198 -1 O GLU C 195 N GLN C 147 SHEET 4 AB5 4 VAL C 205 ASN C 210 -1 O VAL C 205 N VAL C 196 SHEET 1 AB6 4 THR D 3 SER D 7 0 SHEET 2 AB6 4 LEU D 18 SER D 25 -1 O THR D 21 N SER D 7 SHEET 3 AB6 4 GLN D 77 VAL D 82 -1 O VAL D 78 N CYS D 22 SHEET 4 AB6 4 LEU D 67 ASP D 72 -1 N THR D 68 O LYS D 81 SHEET 1 AB7 6 LEU D 11 VAL D 12 0 SHEET 2 AB7 6 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AB7 6 ALA D 88 MET D 96 -1 N TYR D 90 O THR D 107 SHEET 4 AB7 6 MET D 34 GLN D 39 -1 N ILE D 37 O TYR D 91 SHEET 5 AB7 6 GLU D 46 TRP D 52 -1 O ALA D 49 N TRP D 36 SHEET 6 AB7 6 LYS D 57 TYR D 59 -1 O HIS D 58 N ASP D 50 SHEET 1 AB8 4 VAL D 121 LEU D 124 0 SHEET 2 AB8 4 ALA D 136 TYR D 145 -1 O GLY D 139 N LEU D 124 SHEET 3 AB8 4 TYR D 176 VAL D 184 -1 O VAL D 184 N ALA D 136 SHEET 4 AB8 4 VAL D 163 THR D 165 -1 N HIS D 164 O VAL D 181 SHEET 1 AB9 4 VAL D 121 LEU D 124 0 SHEET 2 AB9 4 ALA D 136 TYR D 145 -1 O GLY D 139 N LEU D 124 SHEET 3 AB9 4 TYR D 176 VAL D 184 -1 O VAL D 184 N ALA D 136 SHEET 4 AB9 4 VAL D 169 LEU D 170 -1 N VAL D 169 O SER D 177 SHEET 1 AC1 3 THR D 151 TRP D 154 0 SHEET 2 AC1 3 TYR D 194 HIS D 200 -1 O ASN D 197 N SER D 153 SHEET 3 AC1 3 THR D 205 VAL D 211 -1 O VAL D 211 N TYR D 194 SHEET 1 AC2 4 VAL H 74 PHE H 80 0 SHEET 2 AC2 4 TYR H 3 ALA H 8 -1 N TYR H 3 O PHE H 80 SHEET 3 AC2 4 TYR H 11 LEU H 15 -1 O PHE H 13 N VAL H 6 SHEET 4 AC2 4 LEU H 111 LYS H 114 -1 O VAL H 113 N TYR H 12 SHEET 1 AC3 4 ALA H 33 ASP H 39 0 SHEET 2 AC3 4 LYS H 44 PHE H 50 -1 O PHE H 48 N VAL H 35 SHEET 3 AC3 4 VAL H 56 THR H 62 -1 O THR H 57 N THR H 49 SHEET 4 AC3 4 ILE H 68 PHE H 72 -1 O LYS H 70 N GLU H 61 SHEET 1 AC4 4 VAL G 74 PHE G 80 0 SHEET 2 AC4 4 TYR G 3 ALA G 8 -1 N LYS G 7 O LYS G 75 SHEET 3 AC4 4 TYR G 11 LEU G 15 -1 O LEU G 15 N MET G 4 SHEET 4 AC4 4 LEU G 111 LYS G 114 -1 O VAL G 113 N TYR G 12 SHEET 1 AC5 4 VAL G 35 ASP G 39 0 SHEET 2 AC5 4 LYS G 44 PHE G 50 -1 O TYR G 46 N PHE G 37 SHEET 3 AC5 4 VAL G 56 THR G 62 -1 O GLU G 58 N THR G 49 SHEET 4 AC5 4 LYS G 70 PHE G 72 -1 O PHE G 72 N VAL G 59 SSBOND 1 CYS B 23 CYS B 88 1555 1555 2.05 SSBOND 2 CYS B 134 CYS B 194 1555 1555 2.03 SSBOND 3 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 4 CYS A 140 CYS A 196 1555 1555 2.02 SSBOND 5 CYS C 23 CYS C 88 1555 1555 2.04 SSBOND 6 CYS C 134 CYS C 194 1555 1555 2.03 SSBOND 7 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 8 CYS D 140 CYS D 196 1555 1555 2.02 LINK O LYS A 71 K K A 301 1555 1555 3.30 LINK O LYS A 71 K K A 301 1555 2556 3.30 CISPEP 1 SER B 7 PRO B 8 0 2.36 CISPEP 2 TYR B 94 PRO B 95 0 6.24 CISPEP 3 TYR B 140 PRO B 141 0 3.77 CISPEP 4 PHE A 146 PRO A 147 0 -3.98 CISPEP 5 GLU A 148 PRO A 149 0 8.18 CISPEP 6 SER C 7 PRO C 8 0 3.67 CISPEP 7 TYR C 94 PRO C 95 0 3.62 CISPEP 8 TYR C 140 PRO C 141 0 3.00 CISPEP 9 PHE D 146 PRO D 147 0 -12.57 CISPEP 10 GLU D 148 PRO D 149 0 5.53 CRYST1 184.072 66.859 109.410 90.00 103.87 90.00 C 1 2 1 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 0.005433 0.000000 0.001341 0.00000 SCALE2 0.000000 0.014957 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009414 0.00000