HEADER PROTEIN BINDING 18-SEP-25 9YC3 TITLE CRYSTAL STRUCTURE OF MALARIA TRANSMISSION-BLOCKING ANTIGEN PFHAP2 TITLE 2 DOMAIN 3 IN COMPLEX WITH NANOBODY WNB 334 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NANOBODY WNB 334; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MALE GAMETE FUSION FACTOR HAP2; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 3 ORGANISM_TAXID: 30538; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: WK6; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM; SOURCE 9 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM; SOURCE 10 ORGANISM_TAXID: 5833; SOURCE 11 GENE: PF3D7_1014200; SOURCE 12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: SF21 KEYWDS TRANSMISSION-BLOCKING, NANOBODY, FUSOGEN, MALARIA, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR F.M.T.LYONS,P.PYMM,M.H.DIETRICH,W.H.THAM REVDAT 1 31-DEC-25 9YC3 0 JRNL AUTH F.M.T.LYONS,L.J.CHAN,J.CHMIELEWSKI,M.GABRIELA,R.CHAN, JRNL AUTH 2 A.ADAIR,J.TONG,P.PYMM,K.ZEGLINSKI,G.QUENTIN,M.H.DIETRICH, JRNL AUTH 3 W.H.THAM JRNL TITL CRYSTAL STRUCTURE AND NANOBODIES AGAINST DOMAIN 3 OF THE JRNL TITL 2 MALARIA PARASITE FUSOGEN PLASMODIUM FALCIPARUM HAP2 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.2_5419: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.79 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 8334 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.225 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.253 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 417 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 38.7900 - 4.0400 1.00 2720 144 0.2003 0.2249 REMARK 3 2 4.0400 - 3.2100 1.00 2602 137 0.2379 0.2948 REMARK 3 3 3.2100 - 2.8000 1.00 2595 136 0.2900 0.3005 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) : 0.380 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.400 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 1818 REMARK 3 ANGLE : 0.597 2480 REMARK 3 CHIRALITY : 0.045 293 REMARK 3 PLANARITY : 0.003 322 REMARK 3 DIHEDRAL : 16.807 610 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): -8.7178 32.2960 5.7311 REMARK 3 T TENSOR REMARK 3 T11: 0.5228 T22: 0.5014 REMARK 3 T33: 0.5454 T12: -0.1794 REMARK 3 T13: 0.0078 T23: -0.0882 REMARK 3 L TENSOR REMARK 3 L11: 3.3655 L22: 1.6945 REMARK 3 L33: 1.9079 L12: -2.2220 REMARK 3 L13: -1.8742 L23: 0.9235 REMARK 3 S TENSOR REMARK 3 S11: -0.1450 S12: 0.7307 S13: -0.2093 REMARK 3 S21: 0.3900 S22: -0.1981 S23: 0.1382 REMARK 3 S31: 0.2363 S32: -0.5522 S33: 0.1903 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 9YC3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-25. REMARK 100 THE DEPOSITION ID IS D_1000299985. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-OCT-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.953740 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8345 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 38.790 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 11.00 REMARK 200 R MERGE (I) : 0.15700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.9500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.35100 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 (%): 53.52 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.7, 27% W/V PEG 3350, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.80800 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.90400 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.90400 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 63.80800 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1280 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 11450 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 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 HIS A 131 REMARK 465 HIS A 132 REMARK 465 HIS A 133 REMARK 465 HIS A 134 REMARK 465 HIS A 135 REMARK 465 ALA B 498 REMARK 465 ASP B 499 REMARK 465 PRO B 500 REMARK 465 VAL B 501 REMARK 465 GLU B 617 REMARK 465 THR B 618 REMARK 465 ILE B 619 REMARK 465 ASN B 620 REMARK 465 SER B 621 REMARK 465 GLY B 622 REMARK 465 ARG B 623 REMARK 465 GLU B 624 REMARK 465 ASN B 625 REMARK 465 LEU B 626 REMARK 465 TYR B 627 REMARK 465 PHE B 628 REMARK 465 GLN B 629 REMARK 465 GLY B 630 REMARK 465 HIS B 631 REMARK 465 HIS B 632 REMARK 465 HIS B 633 REMARK 465 HIS B 634 REMARK 465 HIS B 635 REMARK 465 HIS B 636 REMARK 465 HIS B 637 REMARK 465 HIS B 638 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 GLN A 1 CG CD OE1 NE2 REMARK 470 LYS A 43 CG CD CE NZ REMARK 470 LYS A 102 CD CE NZ REMARK 470 GLN A 121 CG CD OE1 NE2 REMARK 470 TYR B 503 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS B 513 CE NZ REMARK 470 ASP B 514 CG OD1 OD2 REMARK 470 SER B 517 OG REMARK 470 THR B 520 OG1 CG2 REMARK 470 SER B 522 OG REMARK 470 LYS B 523 CG CD CE NZ REMARK 470 LYS B 536 CD CE NZ REMARK 470 ILE B 538 CG1 CG2 CD1 REMARK 470 SER B 564 OG REMARK 470 LYS B 565 CG CD CE NZ REMARK 470 ILE B 566 CG1 CG2 CD1 REMARK 470 HIS B 569 CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 583 CG CD CE NZ REMARK 470 ILE B 586 CG1 CG2 CD1 REMARK 470 LYS B 588 CG CD CE NZ REMARK 470 LYS B 589 CG CD CE NZ REMARK 470 ASP B 602 CG OD1 OD2 REMARK 470 ARG B 604 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 608 CE NZ REMARK 470 LYS B 616 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 LYS B 523 6.84 -65.19 REMARK 500 CYS B 525 50.27 -147.74 REMARK 500 LYS B 536 41.55 -90.92 REMARK 500 THR B 537 -53.09 -129.45 REMARK 500 SER B 564 -98.39 -114.73 REMARK 500 REMARK 500 REMARK: NULL DBREF 9YC3 A 1 135 PDB 9YC3 9YC3 1 135 DBREF 9YC3 B 500 620 UNP Q8IJQ3 Q8IJQ3_PLAF7 500 620 SEQADV 9YC3 ALA B 498 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 ASP B 499 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 SER B 621 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 GLY B 622 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 ARG B 623 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 GLU B 624 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 ASN B 625 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 LEU B 626 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 TYR B 627 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 PHE B 628 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 GLN B 629 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 GLY B 630 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 HIS B 631 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 HIS B 632 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 HIS B 633 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 HIS B 634 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 HIS B 635 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 HIS B 636 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 HIS B 637 UNP Q8IJQ3 EXPRESSION TAG SEQADV 9YC3 HIS B 638 UNP Q8IJQ3 EXPRESSION TAG SEQRES 1 A 135 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 135 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 135 PHE THR LEU ASP ASP TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 A 135 ASP PRO GLY LYS GLY ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 A 135 LEU SER ASP GLY SER THR TYR TYR ALA ASP ALA VAL THR SEQRES 6 A 135 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASP THR SEQRES 7 A 135 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 A 135 ALA VAL TYR TYR CYS ALA ALA LEU SER GLN LYS GLN MET SEQRES 9 A 135 THR THR VAL GLN ALA MET CYS ALA VAL PRO ILE ALA ASN SEQRES 10 A 135 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 11 A 135 HIS HIS HIS HIS HIS SEQRES 1 B 141 ALA ASP PRO VAL SER TYR GLY THR ILE THR HIS ILE THR SEQRES 2 B 141 ILE PRO LYS ASP CYS SER SER ASN GLN THR ASN SER LYS SEQRES 3 B 141 GLU CYS ILE LEU VAL VAL HIS THR TRP ASN ASN ASN LYS SEQRES 4 B 141 THR ILE GLY ALA ASN PHE SER CYS HIS VAL LEU CYS VAL SEQRES 5 B 141 ASP LYS SER THR GLN GLN VAL ALA THR HIS ILE SER PRO SEQRES 6 B 141 ILE SER LYS ILE ASN ALA HIS ILE ASP ALA ASN LYS ASN SEQRES 7 B 141 TYR ALA PHE TYR PHE ILE ILE LYS PHE LEU ILE ASN LYS SEQRES 8 B 141 LYS ILE THR SER ASN CYS THR ALA ILE LEU LYS ASP ALA SEQRES 9 B 141 ASP GLY ARG GLU CYS SER LYS LEU SER PHE ASN LEU THR SEQRES 10 B 141 SER LYS GLU THR ILE ASN SER GLY ARG GLU ASN LEU TYR SEQRES 11 B 141 PHE GLN GLY HIS HIS HIS HIS HIS HIS HIS HIS FORMUL 3 HOH *6(H2 O) HELIX 1 AA1 THR A 28 ASP A 30 5 3 HELIX 2 AA2 LYS A 87 THR A 91 5 5 HELIX 3 AA3 THR A 106 VAL A 113 1 8 HELIX 4 AA4 ASN B 521 GLU B 524 5 4 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ARG A 72 -1 N THR A 69 O GLN A 82 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 123 VAL A 127 1 O THR A 126 N GLY A 10 SHEET 3 AA2 6 ALA A 92 SER A 100 -1 N TYR A 94 O THR A 123 SHEET 4 AA2 6 TYR A 32 GLN A 39 -1 N PHE A 37 O TYR A 95 SHEET 5 AA2 6 GLU A 46 SER A 52 -1 O SER A 49 N TRP A 36 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O TYR A 59 N CYS A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 123 VAL A 127 1 O THR A 126 N GLY A 10 SHEET 3 AA3 4 ALA A 92 SER A 100 -1 N TYR A 94 O THR A 123 SHEET 4 AA3 4 TYR A 118 TRP A 119 -1 O TYR A 118 N ALA A 98 SHEET 1 AA4 7 ILE A 115 ALA A 116 0 SHEET 2 AA4 7 GLY B 504 THR B 510 1 O ILE B 509 N ALA A 116 SHEET 3 AA4 7 ILE B 526 ASN B 533 -1 O HIS B 530 N HIS B 508 SHEET 4 AA4 7 ASN B 575 PHE B 584 -1 O PHE B 578 N VAL B 529 SHEET 5 AA4 7 VAL B 556 PRO B 562 -1 N HIS B 559 O LYS B 583 SHEET 6 AA4 7 ASN B 541 ASP B 550 -1 N CYS B 548 O ALA B 557 SHEET 7 AA4 7 ASN B 567 HIS B 569 -1 O ALA B 568 N PHE B 542 SHEET 1 AA5 8 ILE A 115 ALA A 116 0 SHEET 2 AA5 8 GLY B 504 THR B 510 1 O ILE B 509 N ALA A 116 SHEET 3 AA5 8 ILE B 526 ASN B 533 -1 O HIS B 530 N HIS B 508 SHEET 4 AA5 8 ASN B 575 PHE B 584 -1 O PHE B 578 N VAL B 529 SHEET 5 AA5 8 VAL B 556 PRO B 562 -1 N HIS B 559 O LYS B 583 SHEET 6 AA5 8 ASN B 541 ASP B 550 -1 N CYS B 548 O ALA B 557 SHEET 7 AA5 8 SER B 592 LYS B 599 -1 O ILE B 597 N HIS B 545 SHEET 8 AA5 8 GLU B 605 ASN B 612 -1 O PHE B 611 N CYS B 594 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS A 50 CYS A 111 1555 1555 2.03 SSBOND 3 CYS B 515 CYS B 525 1555 1555 2.03 SSBOND 4 CYS B 548 CYS B 594 1555 1555 2.03 CRYST1 76.474 76.474 95.712 90.00 90.00 120.00 P 32 2 1 6 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 0.013076 0.007550 0.000000 0.00000 SCALE2 0.000000 0.015099 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010448 0.00000