HEADER IMMUNE SYSTEM 17-JAN-24 8XWZ TITLE NON-CRYSTALLINE PROXIMAL TUBULOPATHY AND CRYSTALLINE CAST NEPHROPATHY- TITLE 2 CAUSING BENCE-JONES PROTEIN PT-CN: AN ENTIRE IMMUNOGLOBULIN KAPPA TITLE 3 LIGHT CHAIN DIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: BENCE-JONES PROTEIN KAPPA LIGHT CHAIN PT-CN; COMPND 3 CHAIN: A, B; COMPND 4 OTHER_DETAILS: DDBJ:LC795522 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606 KEYWDS BENCE-JONES PROTEIN, IMMUNOGLOBULIN, KAPPA LIGHT CHAIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.EZAWA,R.OTOMO,K.NOZAWA,S.KYOYA,K.NOGUCHI,M.YOHDA,M.ODAKA, AUTHOR 2 H.MATSUMURA REVDAT 1 22-JAN-25 8XWZ 0 JRNL AUTH T.EZAWA,R.OTOMO,Y.KARIYA,K.NOZAWA,S.KYOYA,C.FURUTANI, JRNL AUTH 2 K.NOGUCHI,M.YOHDA,M.ODAKA,H.MATSUMURA,A.SAITO,M.SAITO,F.ABE, JRNL AUTH 3 Y.FUJIOKA,A.KITADATE,H.WAKUI,N.TAKAHASHI JRNL TITL MULTIPLE MYELOMA-ASSOCIATED NON-CRYSTALLINE PROXIMAL JRNL TITL 2 TUBULOPATHY AND CRYSTALLINE CAST NEPHROPATHY: BIOCHEMICAL JRNL TITL 3 AND STRUCTURAL FEATURES OF DISEASE-CAUSING MONOCLONAL KAPPA JRNL TITL 4 LIGHT CHAINS. JRNL REF FASEB J. V. 39 70296 2025 JRNL REFN ESSN 1530-6860 JRNL PMID 39781602 JRNL DOI 10.1096/FJ.202402104R REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.16_3549 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 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.29 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.920 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 21310 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.207 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 1079 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 44.2900 - 4.6000 1.00 2713 152 0.2134 0.2395 REMARK 3 2 4.6000 - 3.6500 1.00 2569 135 0.1654 0.2237 REMARK 3 3 3.6500 - 3.1900 1.00 2495 151 0.1846 0.2613 REMARK 3 4 3.1900 - 2.9000 1.00 2548 104 0.2094 0.2596 REMARK 3 5 2.9000 - 2.6900 1.00 2480 142 0.2265 0.2873 REMARK 3 6 2.6900 - 2.5300 1.00 2462 151 0.2429 0.3298 REMARK 3 7 2.5300 - 2.4000 1.00 2488 125 0.2587 0.2891 REMARK 3 8 2.4000 - 2.3000 1.00 2476 119 0.2828 0.3393 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.294 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.489 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 45.92 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.02 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 3612 REMARK 3 ANGLE : 0.559 4757 REMARK 3 CHIRALITY : 0.040 518 REMARK 3 PLANARITY : 0.003 586 REMARK 3 DIHEDRAL : 7.008 2849 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): -11.1898 31.9476 -13.3653 REMARK 3 T TENSOR REMARK 3 T11: 0.2805 T22: 0.3007 REMARK 3 T33: 0.2278 T12: -0.0128 REMARK 3 T13: -0.0710 T23: -0.0304 REMARK 3 L TENSOR REMARK 3 L11: 1.6271 L22: 1.5154 REMARK 3 L33: 0.8645 L12: -0.6892 REMARK 3 L13: -1.0705 L23: 0.7236 REMARK 3 S TENSOR REMARK 3 S11: -0.0336 S12: -0.0534 S13: 0.0333 REMARK 3 S21: 0.0061 S22: 0.0027 S23: 0.0695 REMARK 3 S31: -0.1460 S32: 0.0899 S33: 0.0349 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 8XWZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1300044375. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-NOV-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-1A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.04 REMARK 200 MONOCHROMATOR : CRYO-COOLED CHANNEL-CUT SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21369 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 47.080 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 13.20 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 11.30 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 1B6D REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 8% MPD, 10% PEG6000, PH REMARK 280 6.5, COUNTER-DIFFUSION, TEMPERATURE 283K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 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 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 70.62500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 40.21100 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 40.21100 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.31250 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 40.21100 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 40.21100 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 105.93750 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 40.21100 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.21100 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 35.31250 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 40.21100 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.21100 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 105.93750 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.62500 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 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 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 P PO4 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 212 REMARK 465 GLU B 213 REMARK 465 CYS B 214 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 SER A 30 -129.64 56.82 REMARK 500 ALA A 51 -25.45 70.07 REMARK 500 ASN A 138 71.96 58.92 REMARK 500 LYS A 190 -62.87 -121.68 REMARK 500 SER B 30 -120.68 57.90 REMARK 500 ALA B 51 -40.43 73.60 REMARK 500 ASN B 138 74.54 54.40 REMARK 500 LYS B 190 -77.65 -114.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 465 DISTANCE = 6.39 ANGSTROMS REMARK 525 HOH A 466 DISTANCE = 6.46 ANGSTROMS REMARK 525 HOH A 467 DISTANCE = 8.36 ANGSTROMS REMARK 525 HOH A 468 DISTANCE = 8.38 ANGSTROMS REMARK 525 HOH A 469 DISTANCE = 8.92 ANGSTROMS REMARK 525 HOH B 450 DISTANCE = 6.22 ANGSTROMS DBREF 8XWZ A 1 214 PDB 8XWZ 8XWZ 1 214 DBREF 8XWZ B 1 214 PDB 8XWZ 8XWZ 1 214 SEQRES 1 A 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 A 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 A 214 GLN THR ILE SER ASN PHE LEU ASN TRP TYR GLN GLN LYS SEQRES 4 A 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 A 214 THR LEU GLN SER GLY VAL PRO SER GLY PHE SER GLY SER SEQRES 6 A 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 A 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN THR SEQRES 8 A 214 TYR SER THR PRO TYR THR PHE GLY LEU GLY THR LYS LEU SEQRES 9 A 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 A 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 A 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 A 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 A 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 A 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 A 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 A 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 A 214 PHE ASN ARG GLY GLU CYS SEQRES 1 B 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 214 GLN THR ILE SER ASN PHE LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 B 214 THR LEU GLN SER GLY VAL PRO SER GLY PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN THR SEQRES 8 B 214 TYR SER THR PRO TYR THR PHE GLY LEU GLY THR LYS LEU SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS HET PO4 A 301 5 HET PO4 A 302 5 HET ETX A 303 6 HET PGE A 304 10 HET GOL A 305 6 HET EDO A 306 4 HET EDO A 307 4 HET EDO A 308 4 HET EDO A 309 4 HET EDO A 310 4 HET EDO A 311 4 HET EDO A 312 4 HET EDO A 313 4 HET EDO A 314 4 HET EDO A 315 4 HET EDO A 316 4 HET EDO A 317 4 HET EDO A 318 4 HET EDO A 319 4 HET EDO A 320 4 HET EDO A 321 4 HET EDO A 322 4 HET EDO A 323 4 HET EDO A 324 4 HET EDO A 325 4 HET EDO A 326 4 HET EDO A 327 4 HET EDO A 328 4 HET EDO A 329 4 HET EDO A 330 4 HET EDO A 331 4 HET EDO A 332 4 HET EDO A 333 4 HET EDO A 334 4 HET EDO A 335 4 HET EDO A 336 4 HET EDO A 337 4 HET PO4 B 301 5 HET PO4 B 302 5 HET PEG B 303 7 HET PEG B 304 7 HET GOL B 305 6 HET EDO B 306 4 HET EDO B 307 4 HET EDO B 308 4 HET EDO B 309 4 HET EDO B 310 4 HET EDO B 311 4 HET EDO B 312 4 HET EDO B 313 4 HET EDO B 314 4 HET EDO B 315 4 HET EDO B 316 4 HET EDO B 317 4 HET EDO B 318 4 HET EDO B 319 4 HET EDO B 320 4 HET EDO B 321 4 HET EDO B 322 4 HET EDO B 323 4 HET EDO B 324 4 HET EDO B 325 4 HET EDO B 326 4 HET EDO B 327 4 HET EDO B 328 4 HET EDO B 329 4 HET EDO B 330 4 HET EDO B 331 4 HET EDO B 332 4 HET EDO B 333 4 HET EDO B 334 4 HET EDO B 335 4 HET EDO B 336 4 HET EDO B 337 4 HET EDO B 338 4 HET EDO B 339 4 HET EDO B 340 4 HET EDO B 341 4 HET EDO B 342 4 HETNAM PO4 PHOSPHATE ION HETNAM ETX 2-ETHOXYETHANOL HETNAM PGE TRIETHYLENE GLYCOL HETNAM GOL GLYCEROL HETNAM EDO 1,2-ETHANEDIOL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 3 PO4 4(O4 P 3-) FORMUL 5 ETX C4 H10 O2 FORMUL 6 PGE C6 H14 O4 FORMUL 7 GOL 2(C3 H8 O3) FORMUL 8 EDO 69(C2 H6 O2) FORMUL 42 PEG 2(C4 H10 O3) FORMUL 82 HOH *119(H2 O) HELIX 1 AA1 SER A 121 LYS A 126 1 6 HELIX 2 AA2 LYS A 183 LYS A 188 1 6 HELIX 3 AA3 GLN B 79 PHE B 83 5 5 HELIX 4 AA4 SER B 121 LYS B 126 1 6 HELIX 5 AA5 LYS B 183 LYS B 188 1 6 SHEET 1 AA1 4 MET A 4 SER A 7 0 SHEET 2 AA1 4 VAL A 19 ALA A 25 -1 O THR A 22 N SER A 7 SHEET 3 AA1 4 ASP A 70 ILE A 75 -1 O LEU A 73 N ILE A 21 SHEET 4 AA1 4 PHE A 62 GLY A 66 -1 N SER A 63 O THR A 74 SHEET 1 AA2 6 SER A 10 ALA A 13 0 SHEET 2 AA2 6 THR A 102 ILE A 106 1 O GLU A 105 N LEU A 11 SHEET 3 AA2 6 THR A 85 GLN A 90 -1 N TYR A 86 O THR A 102 SHEET 4 AA2 6 LEU A 33 GLN A 38 -1 N GLN A 38 O THR A 85 SHEET 5 AA2 6 LYS A 45 TYR A 49 -1 O LYS A 45 N GLN A 37 SHEET 6 AA2 6 THR A 53 LEU A 54 -1 O THR A 53 N TYR A 49 SHEET 1 AA3 4 SER A 114 PHE A 118 0 SHEET 2 AA3 4 THR A 129 PHE A 139 -1 O VAL A 133 N PHE A 118 SHEET 3 AA3 4 TYR A 173 SER A 182 -1 O LEU A 175 N LEU A 136 SHEET 4 AA3 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178 SHEET 1 AA4 3 LYS A 145 VAL A 150 0 SHEET 2 AA4 3 VAL A 191 THR A 197 -1 O GLU A 195 N GLN A 147 SHEET 3 AA4 3 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196 SHEET 1 AA5 4 MET B 4 SER B 7 0 SHEET 2 AA5 4 VAL B 19 ALA B 25 -1 O THR B 22 N SER B 7 SHEET 3 AA5 4 ASP B 70 ILE B 75 -1 O ILE B 75 N VAL B 19 SHEET 4 AA5 4 PHE B 62 GLY B 66 -1 N SER B 63 O THR B 74 SHEET 1 AA6 6 SER B 10 ALA B 13 0 SHEET 2 AA6 6 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AA6 6 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA6 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AA6 6 LYS B 45 TYR B 49 -1 O LYS B 45 N GLN B 37 SHEET 6 AA6 6 THR B 53 LEU B 54 -1 O THR B 53 N TYR B 49 SHEET 1 AA7 4 SER B 114 PHE B 118 0 SHEET 2 AA7 4 THR B 129 PHE B 139 -1 O VAL B 133 N PHE B 118 SHEET 3 AA7 4 TYR B 173 SER B 182 -1 O TYR B 173 N PHE B 139 SHEET 4 AA7 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 SHEET 1 AA8 4 ALA B 153 LEU B 154 0 SHEET 2 AA8 4 ALA B 144 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AA8 4 VAL B 191 HIS B 198 -1 O GLU B 195 N GLN B 147 SHEET 4 AA8 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.04 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.04 CISPEP 1 SER A 7 PRO A 8 0 -5.19 CISPEP 2 THR A 94 PRO A 95 0 -0.08 CISPEP 3 TYR A 140 PRO A 141 0 2.30 CISPEP 4 SER B 7 PRO B 8 0 -2.87 CISPEP 5 THR B 94 PRO B 95 0 -1.85 CISPEP 6 TYR B 140 PRO B 141 0 1.45 CRYST1 80.422 80.422 141.250 90.00 90.00 90.00 P 41 21 2 16 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 0.012434 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012434 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007080 0.00000