HEADER IMMUNE SYSTEM 27-JUN-24 9FVK TITLE CRYSTAL STRUCTURE OF AMYLOIDOGENIC LIGHT CHAIN AL-55 IN OPEN TITLE 2 CONFORMATION. COMPND MOL_ID: 1; COMPND 2 MOLECULE: AL55; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS LIGHT CHAIN, AMYLOIDOSIS, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR I.POLSINELLI,S.PURI,L.BROGGINI,A.GADDA,U.PETRALIA,S.RICAGNO REVDAT 1 09-JUL-25 9FVK 0 JRNL AUTH S.PURI,I.POLSINELLI,S.RICAGNO JRNL TITL TO BE PUBLISHED JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.64 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) : 2.64 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.64 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 25173 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.195 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 1280 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 5.4900 - 4.3600 1.00 2681 150 0.1517 0.1780 REMARK 3 2 4.3600 - 3.8100 1.00 2630 157 0.1653 0.1872 REMARK 3 3 3.8100 - 3.4600 1.00 2624 168 0.1903 0.2601 REMARK 3 4 3.4600 - 3.2100 1.00 2649 125 0.2198 0.2774 REMARK 3 5 3.2100 - 3.0200 1.00 2633 119 0.2401 0.2833 REMARK 3 6 3.0200 - 2.8700 1.00 2625 138 0.2453 0.2597 REMARK 3 7 2.8700 - 2.7500 1.00 2628 140 0.2728 0.3417 REMARK 3 8 2.7500 - 2.6400 1.00 2613 139 0.3201 0.3744 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) : 0.381 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.122 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 54.64 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.37 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 : 0.002 5072 REMARK 3 ANGLE : 0.573 6925 REMARK 3 CHIRALITY : 0.043 773 REMARK 3 PLANARITY : 0.004 895 REMARK 3 DIHEDRAL : 6.755 700 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 9FVK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1292139739. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-APR-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 : MASSIF-3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677 REMARK 200 MONOCHROMATOR : M REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25185 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.640 REMARK 200 RESOLUTION RANGE LOW (A) : 45.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 13.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.2700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.64 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.73 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.97 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MIB (SODIUM MALONATE DIBASIC REMARK 280 MONOHYDRATE, IMIDAZOLE, BORIC ACID) PH 5.0, AND 25 % W/V PEG REMARK 280 1500, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 36.01500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.01500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 55.90850 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 104.19050 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 55.90850 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 104.19050 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.01500 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 55.90850 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 104.19050 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 36.01500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 55.90850 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 104.19050 REMARK 290 SMTRY3 8 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2710 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21700 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21510 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C 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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 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 SER A 217 REMARK 465 SER B 217 REMARK 465 SER C 217 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 OD1 ASP B 85 O HOH B 401 2.00 REMARK 500 O ASP C 156 O HOH C 401 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH B 414 O HOH B 428 3555 1.88 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 LYS A 16 -168.05 -100.72 REMARK 500 SER A 26 -3.60 69.43 REMARK 500 ASN A 52 -54.97 74.10 REMARK 500 SER A 93 -148.45 -144.71 REMARK 500 ASP A 95 -159.51 -87.42 REMARK 500 LEU A 111 109.20 -56.13 REMARK 500 PRO A 146 -178.85 -69.43 REMARK 500 SER A 157 -46.68 111.11 REMARK 500 GLU A 203 -121.49 60.21 REMARK 500 SER B 26 -5.58 68.44 REMARK 500 ASN B 52 -48.47 73.87 REMARK 500 ASP B 53 3.51 -150.36 REMARK 500 SER B 93 -148.56 -147.39 REMARK 500 ASP B 156 -90.69 56.89 REMARK 500 PHE C 2 128.45 -172.83 REMARK 500 PRO C 41 93.49 -60.55 REMARK 500 ALA C 44 94.43 63.40 REMARK 500 ASN C 52 -49.25 68.94 REMARK 500 ASP C 53 -0.97 -141.04 REMARK 500 ALA C 87 -169.92 -166.86 REMARK 500 SER C 93 -149.86 -137.24 REMARK 500 ASP C 156 -86.40 56.81 REMARK 500 SER C 192 30.63 -88.55 REMARK 500 GLU C 203 72.06 62.37 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 B 303 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 86 OE2 REMARK 620 2 PO4 C 301 O2 134.2 REMARK 620 3 PO4 C 301 O4 124.0 51.4 REMARK 620 N 1 2 DBREF 9FVK A 1 217 PDB 9FVK 9FVK 1 217 DBREF 9FVK B 1 217 PDB 9FVK 9FVK 1 217 DBREF 9FVK C 1 217 PDB 9FVK 9FVK 1 217 SEQRES 1 A 217 ASN PHE MET LEU THR GLN PRO HIS SER VAL SER GLU SER SEQRES 2 A 217 PRO GLY LYS THR LEU THR ILE SER CYS THR GLY SER SER SEQRES 3 A 217 ALA SER ILE ALA SER HIS TYR VAL GLN TRP TYR GLN GLN SEQRES 4 A 217 ARG PRO GLY GLY ALA PRO THR THR LEU ILE TYR GLU ASN SEQRES 5 A 217 ASP GLN ARG PRO SER GLU VAL PRO ASP ARG PHE SER GLY SEQRES 6 A 217 SER ILE ASP SER SER SER ASN SER ALA SER LEU THR ILE SEQRES 7 A 217 SER GLY LEU LYS THR GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 A 217 GLN SER TYR ASP GLY ASN ASN HIS TRP VAL PHE GLY GLY SEQRES 9 A 217 GLY THR LYS LEU THR VAL LEU SER GLN PRO LYS ALA ALA SEQRES 10 A 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 A 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 A 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 A 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 A 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 A 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER SEQRES 16 A 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 A 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 B 217 ASN PHE MET LEU THR GLN PRO HIS SER VAL SER GLU SER SEQRES 2 B 217 PRO GLY LYS THR LEU THR ILE SER CYS THR GLY SER SER SEQRES 3 B 217 ALA SER ILE ALA SER HIS TYR VAL GLN TRP TYR GLN GLN SEQRES 4 B 217 ARG PRO GLY GLY ALA PRO THR THR LEU ILE TYR GLU ASN SEQRES 5 B 217 ASP GLN ARG PRO SER GLU VAL PRO ASP ARG PHE SER GLY SEQRES 6 B 217 SER ILE ASP SER SER SER ASN SER ALA SER LEU THR ILE SEQRES 7 B 217 SER GLY LEU LYS THR GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 B 217 GLN SER TYR ASP GLY ASN ASN HIS TRP VAL PHE GLY GLY SEQRES 9 B 217 GLY THR LYS LEU THR VAL LEU SER GLN PRO LYS ALA ALA SEQRES 10 B 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 B 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 B 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 B 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 B 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 B 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER SEQRES 16 B 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 B 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 C 217 ASN PHE MET LEU THR GLN PRO HIS SER VAL SER GLU SER SEQRES 2 C 217 PRO GLY LYS THR LEU THR ILE SER CYS THR GLY SER SER SEQRES 3 C 217 ALA SER ILE ALA SER HIS TYR VAL GLN TRP TYR GLN GLN SEQRES 4 C 217 ARG PRO GLY GLY ALA PRO THR THR LEU ILE TYR GLU ASN SEQRES 5 C 217 ASP GLN ARG PRO SER GLU VAL PRO ASP ARG PHE SER GLY SEQRES 6 C 217 SER ILE ASP SER SER SER ASN SER ALA SER LEU THR ILE SEQRES 7 C 217 SER GLY LEU LYS THR GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 C 217 GLN SER TYR ASP GLY ASN ASN HIS TRP VAL PHE GLY GLY SEQRES 9 C 217 GLY THR LYS LEU THR VAL LEU SER GLN PRO LYS ALA ALA SEQRES 10 C 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 C 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 C 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 C 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 C 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 C 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER SEQRES 16 C 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 C 217 LYS THR VAL ALA PRO THR GLU CYS SER HET PEG A 301 7 HET PO4 A 302 5 HET PGE B 301 10 HET EDO B 302 4 HET NA B 303 1 HET PO4 C 301 5 HET PO4 C 302 5 HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM PO4 PHOSPHATE ION HETNAM PGE TRIETHYLENE GLYCOL HETNAM EDO 1,2-ETHANEDIOL HETNAM NA SODIUM ION HETSYN EDO ETHYLENE GLYCOL FORMUL 4 PEG C4 H10 O3 FORMUL 5 PO4 3(O4 P 3-) FORMUL 6 PGE C6 H14 O4 FORMUL 7 EDO C2 H6 O2 FORMUL 8 NA NA 1+ FORMUL 11 HOH *100(H2 O) HELIX 1 AA1 SER A 28 HIS A 32 5 5 HELIX 2 AA2 LYS A 82 GLU A 86 5 5 HELIX 3 AA3 SER A 126 ALA A 132 1 7 HELIX 4 AA4 THR A 186 SER A 192 1 7 HELIX 5 AA5 SER B 28 HIS B 32 5 5 HELIX 6 AA6 LYS B 82 GLU B 86 5 5 HELIX 7 AA7 SER B 126 GLN B 131 1 6 HELIX 8 AA8 THR B 186 HIS B 193 1 8 HELIX 9 AA9 SER C 28 HIS C 32 5 5 HELIX 10 AB1 LYS C 82 GLU C 86 5 5 HELIX 11 AB2 SER C 126 GLN C 131 1 6 HELIX 12 AB3 THR C 186 SER C 192 1 7 SHEET 1 AA1 4 MET A 3 THR A 5 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O THR A 23 N THR A 5 SHEET 3 AA1 4 SER A 73 ILE A 78 -1 O LEU A 76 N ILE A 20 SHEET 4 AA1 4 PHE A 63 ASP A 68 -1 N ASP A 68 O SER A 73 SHEET 1 AA2 5 SER A 9 GLU A 12 0 SHEET 2 AA2 5 THR A 106 VAL A 110 1 O THR A 109 N VAL A 10 SHEET 3 AA2 5 ASP A 88 TYR A 94 -1 N TYR A 89 O THR A 106 SHEET 4 AA2 5 GLN A 35 GLN A 39 -1 N GLN A 39 O ASP A 88 SHEET 5 AA2 5 THR A 46 ILE A 49 -1 O LEU A 48 N TRP A 36 SHEET 1 AA3 4 SER A 9 GLU A 12 0 SHEET 2 AA3 4 THR A 106 VAL A 110 1 O THR A 109 N VAL A 10 SHEET 3 AA3 4 ASP A 88 TYR A 94 -1 N TYR A 89 O THR A 106 SHEET 4 AA3 4 TRP A 100 PHE A 102 -1 O VAL A 101 N SER A 93 SHEET 1 AA4 4 SER A 119 PHE A 123 0 SHEET 2 AA4 4 ALA A 135 PHE A 144 -1 O LEU A 140 N THR A 121 SHEET 3 AA4 4 TYR A 177 LEU A 185 -1 O SER A 181 N CYS A 139 SHEET 4 AA4 4 VAL A 164 THR A 166 -1 N GLU A 165 O TYR A 182 SHEET 1 AA5 4 SER A 119 PHE A 123 0 SHEET 2 AA5 4 ALA A 135 PHE A 144 -1 O LEU A 140 N THR A 121 SHEET 3 AA5 4 TYR A 177 LEU A 185 -1 O SER A 181 N CYS A 139 SHEET 4 AA5 4 SER A 170 LYS A 171 -1 N SER A 170 O ALA A 178 SHEET 1 AA6 4 SER A 158 VAL A 160 0 SHEET 2 AA6 4 THR A 150 ALA A 155 -1 N ALA A 155 O SER A 158 SHEET 3 AA6 4 TYR A 196 HIS A 202 -1 O GLN A 199 N ALA A 152 SHEET 4 AA6 4 SER A 205 VAL A 211 -1 O SER A 205 N HIS A 202 SHEET 1 AA7 4 MET B 3 THR B 5 0 SHEET 2 AA7 4 LEU B 18 SER B 25 -1 O THR B 23 N THR B 5 SHEET 3 AA7 4 SER B 73 ILE B 78 -1 O LEU B 76 N ILE B 20 SHEET 4 AA7 4 PHE B 63 ASP B 68 -1 N SER B 64 O THR B 77 SHEET 1 AA8 5 SER B 9 GLU B 12 0 SHEET 2 AA8 5 THR B 106 VAL B 110 1 O LYS B 107 N VAL B 10 SHEET 3 AA8 5 ASP B 88 TYR B 94 -1 N TYR B 89 O THR B 106 SHEET 4 AA8 5 GLN B 35 GLN B 39 -1 N GLN B 39 O ASP B 88 SHEET 5 AA8 5 THR B 46 ILE B 49 -1 O ILE B 49 N TRP B 36 SHEET 1 AA9 4 SER B 9 GLU B 12 0 SHEET 2 AA9 4 THR B 106 VAL B 110 1 O LYS B 107 N VAL B 10 SHEET 3 AA9 4 ASP B 88 TYR B 94 -1 N TYR B 89 O THR B 106 SHEET 4 AA9 4 TRP B 100 PHE B 102 -1 O VAL B 101 N SER B 93 SHEET 1 AB1 4 SER B 119 PHE B 123 0 SHEET 2 AB1 4 ALA B 135 PHE B 144 -1 O LEU B 140 N THR B 121 SHEET 3 AB1 4 TYR B 177 LEU B 185 -1 O SER B 181 N CYS B 139 SHEET 4 AB1 4 VAL B 164 THR B 166 -1 N GLU B 165 O TYR B 182 SHEET 1 AB2 4 SER B 119 PHE B 123 0 SHEET 2 AB2 4 ALA B 135 PHE B 144 -1 O LEU B 140 N THR B 121 SHEET 3 AB2 4 TYR B 177 LEU B 185 -1 O SER B 181 N CYS B 139 SHEET 4 AB2 4 SER B 170 LYS B 171 -1 N SER B 170 O ALA B 178 SHEET 1 AB3 4 SER B 158 VAL B 160 0 SHEET 2 AB3 4 THR B 150 ALA B 155 -1 N ALA B 155 O SER B 158 SHEET 3 AB3 4 TYR B 196 HIS B 202 -1 O GLN B 199 N ALA B 152 SHEET 4 AB3 4 SER B 205 VAL B 211 -1 O SER B 205 N HIS B 202 SHEET 1 AB4 4 MET C 3 THR C 5 0 SHEET 2 AB4 4 LEU C 18 SER C 25 -1 O SER C 25 N MET C 3 SHEET 3 AB4 4 SER C 73 ILE C 78 -1 O ILE C 78 N LEU C 18 SHEET 4 AB4 4 PHE C 63 ASP C 68 -1 N ASP C 68 O SER C 73 SHEET 1 AB5 5 SER C 9 GLU C 12 0 SHEET 2 AB5 5 THR C 106 VAL C 110 1 O LYS C 107 N VAL C 10 SHEET 3 AB5 5 ALA C 87 TYR C 94 -1 N ALA C 87 O LEU C 108 SHEET 4 AB5 5 GLN C 35 GLN C 39 -1 N GLN C 39 O ASP C 88 SHEET 5 AB5 5 THR C 46 ILE C 49 -1 O ILE C 49 N TRP C 36 SHEET 1 AB6 4 SER C 9 GLU C 12 0 SHEET 2 AB6 4 THR C 106 VAL C 110 1 O LYS C 107 N VAL C 10 SHEET 3 AB6 4 ALA C 87 TYR C 94 -1 N ALA C 87 O LEU C 108 SHEET 4 AB6 4 TRP C 100 PHE C 102 -1 O VAL C 101 N SER C 93 SHEET 1 AB7 4 SER C 119 PHE C 123 0 SHEET 2 AB7 4 ALA C 135 PHE C 144 -1 O LEU C 140 N THR C 121 SHEET 3 AB7 4 TYR C 177 LEU C 185 -1 O SER C 181 N CYS C 139 SHEET 4 AB7 4 VAL C 164 THR C 166 -1 N GLU C 165 O TYR C 182 SHEET 1 AB8 4 SER C 119 PHE C 123 0 SHEET 2 AB8 4 ALA C 135 PHE C 144 -1 O LEU C 140 N THR C 121 SHEET 3 AB8 4 TYR C 177 LEU C 185 -1 O SER C 181 N CYS C 139 SHEET 4 AB8 4 SER C 170 LYS C 171 -1 N SER C 170 O ALA C 178 SHEET 1 AB9 4 SER C 158 VAL C 160 0 SHEET 2 AB9 4 THR C 150 ALA C 155 -1 N ALA C 155 O SER C 158 SHEET 3 AB9 4 TYR C 196 HIS C 202 -1 O SER C 197 N LYS C 154 SHEET 4 AB9 4 SER C 205 VAL C 211 -1 O VAL C 207 N VAL C 200 SSBOND 1 CYS A 22 CYS A 91 1555 1555 2.03 SSBOND 2 CYS A 139 CYS A 198 1555 1555 2.03 SSBOND 3 CYS A 216 CYS B 216 1555 1555 2.03 SSBOND 4 CYS B 22 CYS B 91 1555 1555 2.03 SSBOND 5 CYS B 139 CYS B 198 1555 1555 2.03 SSBOND 6 CYS C 22 CYS C 91 1555 1555 2.03 SSBOND 7 CYS C 139 CYS C 198 1555 1555 2.03 SSBOND 8 CYS C 216 CYS C 216 1555 4555 2.74 LINK OE2 GLU B 86 NA NA B 303 1555 1555 2.88 LINK NA NA B 303 O2 PO4 C 301 1555 1555 2.82 LINK NA NA B 303 O4 PO4 C 301 1555 1555 2.87 CISPEP 1 TYR A 145 PRO A 146 0 -0.62 CISPEP 2 TYR B 145 PRO B 146 0 -2.49 CISPEP 3 TYR C 145 PRO C 146 0 1.80 CRYST1 111.817 208.381 72.030 90.00 90.00 90.00 C 2 2 21 24 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 0.008943 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004799 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013883 0.00000