HEADER PROTEIN BINDING 03-NOV-24 9E7N TITLE PFS230 D13D14 IN COMPLEX WITH NANOBODY W2809 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAMETOCYTE SURFACE PROTEIN P230; COMPND 3 CHAIN: B, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY W2809; COMPND 7 CHAIN: C, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 3 ORGANISM_TAXID: 36329; SOURCE 4 GENE: PFS230, PF230, S230, PF3D7_0209000; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 9 ORGANISM_TAXID: 30538; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS 6-CYSTEINE PROTEIN, PLASMODIUM FALCIPARUM, MALARIA TRANSMISSION, KEYWDS 2 NANOBODY, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR L.L.TAN,M.H.DIETRICH,W.H.THAM REVDAT 1 30-JUL-25 9E7N 0 JRNL AUTH M.H.DIETRICH,L.J.CHAN,J.CHMIELEWSKI,L.L.TAN,A.ADAIR, JRNL AUTH 2 F.M.T.LYONS,M.GABRIELA,S.LOPATICKI,T.A.DITE,L.F.DAGLEY, JRNL AUTH 3 R.LONGLEY,I.MUELLER,A.GLUKHOVA,S.SHAKEEL,W.H.THAM JRNL TITL CRYO-EM STRUCTURE OF THE NATIVE PFS230 AND PFS48/45 JRNL TITL 2 FERTILISATION COMPLEX FROM PLASMODIUM FALCIPARUM JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.49 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.1_5286: ???) 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) : 2.49 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.17 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 39948 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 : 0.264 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1997 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 47.1700 - 6.0100 1.00 2997 158 0.2020 0.2077 REMARK 3 2 6.0000 - 4.7700 1.00 2802 148 0.1786 0.2300 REMARK 3 3 4.7700 - 4.1700 1.00 2758 145 0.1695 0.2274 REMARK 3 4 4.1700 - 3.7900 1.00 2719 143 0.2127 0.2224 REMARK 3 5 3.7900 - 3.5100 1.00 2724 144 0.2228 0.2756 REMARK 3 6 3.5100 - 3.3100 1.00 2699 141 0.2483 0.2994 REMARK 3 7 3.3100 - 3.1400 1.00 2689 141 0.2768 0.3471 REMARK 3 8 3.1400 - 3.0000 1.00 2685 142 0.3007 0.3685 REMARK 3 9 3.0000 - 2.8900 1.00 2672 140 0.2907 0.3349 REMARK 3 10 2.8900 - 2.7900 1.00 2681 141 0.2774 0.3120 REMARK 3 11 2.7900 - 2.7000 1.00 2645 139 0.2818 0.3617 REMARK 3 12 2.7000 - 2.6300 1.00 2666 141 0.2936 0.3427 REMARK 3 13 2.6200 - 2.5600 1.00 2644 139 0.3287 0.3581 REMARK 3 14 2.5600 - 2.4900 0.97 2570 135 0.3926 0.4395 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) : 0.410 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.030 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 68.30 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 : 0.004 6863 REMARK 3 ANGLE : 0.672 9318 REMARK 3 CHIRALITY : 0.049 1045 REMARK 3 PLANARITY : 0.005 1164 REMARK 3 DIHEDRAL : 14.943 2622 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 9E7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1000289738. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-SEP-24 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 : 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) : 0.953732 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 : 39958 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490 REMARK 200 RESOLUTION RANGE LOW (A) : 47.170 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 26.60 REMARK 200 R MERGE (I) : 0.10400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.15800 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 (%): 56.79 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12% (W/V) POLYETHYLENE GLYCOL (PEG) REMARK 280 8000, 4% (V/V) GLYCEROL 0.2 M SODIUM ACETATE, 0.1 M IMIDAZOLE PH REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 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 171.35150 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.95950 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.95950 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 257.02725 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.95950 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.95950 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 85.67575 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.95950 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.95950 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 257.02725 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.95950 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.95950 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 85.67575 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 171.35150 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: 3020 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19720 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F, E 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: 3210 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19810 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 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 2824 REMARK 465 ALA B 2825 REMARK 465 SER B 2826 REMARK 465 LYS B 2827 REMARK 465 LYS B 2828 REMARK 465 THR B 2829 REMARK 465 ILE B 2830 REMARK 465 GLY B 2831 REMARK 465 LYS B 2832 REMARK 465 ASP B 2833 REMARK 465 PRO B 3110 REMARK 465 GLU B 3111 REMARK 465 GLY A 2824 REMARK 465 ALA A 2825 REMARK 465 SER A 2826 REMARK 465 GLU A 3111 REMARK 465 HIS C 125 REMARK 465 HIS C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 HIS C 130 REMARK 465 SER D 124 REMARK 465 HIS D 125 REMARK 465 HIS D 126 REMARK 465 HIS D 127 REMARK 465 HIS D 128 REMARK 465 HIS D 129 REMARK 465 HIS D 130 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 LYS B2836 CD CE NZ REMARK 470 LYS B2959 CD CE NZ REMARK 470 LYS B3001 CG CD CE NZ REMARK 470 LYS B3031 CD CE NZ REMARK 470 LYS B3079 CE NZ REMARK 470 LYS A2827 CG CD CE NZ REMARK 470 LYS A2836 CD CE NZ REMARK 470 ARG A2927 CG CD NE CZ NH1 NH2 REMARK 470 LYS A2959 CD CE NZ REMARK 470 GLN A2960 OE1 NE2 REMARK 470 GLN A2962 CG CD OE1 NE2 REMARK 470 ILE A2964 CG1 CG2 CD1 REMARK 470 LYS A3031 CE NZ REMARK 470 LYS A3047 CD CE NZ REMARK 470 GLN C 1 CG CD OE1 NE2 REMARK 470 LEU C 11 CG CD1 CD2 REMARK 470 GLN C 13 CG CD OE1 NE2 REMARK 470 GLN D 1 CG CD OE1 NE2 REMARK 470 VAL D 2 CG1 CG2 REMARK 470 LEU D 11 CG CD1 CD2 REMARK 470 GLN D 13 CG CD OE1 NE2 REMARK 470 SER D 25 OG REMARK 470 LYS D 43 CE NZ REMARK 470 GLU D 44 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 ILE B2848 79.67 -113.41 REMARK 500 ILE B2849 -61.53 -136.88 REMARK 500 TRP B2872 -3.49 71.95 REMARK 500 ASN B2906 -78.90 -126.46 REMARK 500 ASN B2961 -116.33 60.57 REMARK 500 TYR B2980 -60.54 71.75 REMARK 500 ASP B3007 67.04 -151.62 REMARK 500 PRO B3032 -179.65 -69.68 REMARK 500 GLU B3044 52.50 -112.47 REMARK 500 LYS B3057 41.84 -101.71 REMARK 500 SER B3092 -165.90 -102.17 REMARK 500 THR A2829 -159.33 -129.93 REMARK 500 TRP A2872 -3.13 73.27 REMARK 500 HIS A2886 6.69 80.29 REMARK 500 ASN A2961 -103.45 52.56 REMARK 500 TYR A2980 -58.23 71.50 REMARK 500 TYR A2992 54.83 -118.67 REMARK 500 LYS A3057 57.96 -101.85 REMARK 500 ALA C 14 11.44 -68.90 REMARK 500 VAL C 48 -64.45 -109.45 REMARK 500 VAL D 48 -63.19 -103.38 REMARK 500 REMARK 500 REMARK: NULL DBREF 9E7N B 2827 3111 UNP P68874 P230_PLAF7 2827 3111 DBREF 9E7N A 2827 3111 UNP P68874 P230_PLAF7 2827 3111 DBREF 9E7N C 1 130 PDB 9E7N 9E7N 1 130 DBREF 9E7N D 1 130 PDB 9E7N 9E7N 1 130 SEQADV 9E7N GLY B 2824 UNP P68874 EXPRESSION TAG SEQADV 9E7N ALA B 2825 UNP P68874 EXPRESSION TAG SEQADV 9E7N SER B 2826 UNP P68874 EXPRESSION TAG SEQADV 9E7N GLY A 2824 UNP P68874 EXPRESSION TAG SEQADV 9E7N ALA A 2825 UNP P68874 EXPRESSION TAG SEQADV 9E7N SER A 2826 UNP P68874 EXPRESSION TAG SEQRES 1 B 288 GLY ALA SER LYS LYS THR ILE GLY LYS ASP ILE CYS LYS SEQRES 2 B 288 TYR ASP VAL THR THR LYS VAL ALA THR CYS GLU ILE ILE SEQRES 3 B 288 ASP THR ILE ASP SER SER VAL LEU LYS GLU HIS HIS THR SEQRES 4 B 288 VAL HIS TYR SER ILE THR LEU SER ARG TRP ASP LYS LEU SEQRES 5 B 288 ILE ILE LYS TYR PRO THR ASN GLU LYS THR HIS PHE GLU SEQRES 6 B 288 ASN PHE PHE VAL ASN PRO PHE ASN LEU LYS ASP LYS VAL SEQRES 7 B 288 LEU TYR ASN TYR ASN LYS PRO ILE ASN ILE GLU HIS ILE SEQRES 8 B 288 LEU PRO GLY ALA ILE THR THR ASP ILE TYR ASP THR ARG SEQRES 9 B 288 THR LYS ILE LYS GLN TYR ILE LEU ARG ILE PRO PRO TYR SEQRES 10 B 288 VAL HIS LYS ASP ILE HIS PHE SER LEU GLU PHE ASN ASN SEQRES 11 B 288 SER LEU SER LEU THR LYS GLN ASN GLN ASN ILE ILE TYR SEQRES 12 B 288 GLY ASN VAL ALA LYS ILE PHE ILE HIS ILE ASN GLN GLY SEQRES 13 B 288 TYR LYS GLU ILE HIS GLY CYS ASP PHE THR GLY LYS TYR SEQRES 14 B 288 SER HIS LEU PHE THR TYR SER LYS LYS PRO LEU PRO ASN SEQRES 15 B 288 ASP ASP ASP ILE CYS ASN VAL THR ILE GLY ASN ASN THR SEQRES 16 B 288 PHE SER GLY PHE ALA CYS LEU SER HIS PHE GLU LEU LYS SEQRES 17 B 288 PRO ASN ASN CYS PHE SER SER VAL TYR ASP TYR ASN GLU SEQRES 18 B 288 ALA ASN LYS VAL LYS LYS LEU PHE ASP LEU SER THR LYS SEQRES 19 B 288 VAL GLU LEU ASP HIS ILE LYS GLN ASN THR SER GLY TYR SEQRES 20 B 288 THR LEU SER TYR ILE ILE PHE ASN LYS GLU SER THR LYS SEQRES 21 B 288 LEU LYS PHE SER CYS THR CYS SER SER ASN TYR SER ASN SEQRES 22 B 288 TYR THR ILE ARG ILE THR PHE ASP PRO ASN TYR ILE ILE SEQRES 23 B 288 PRO GLU SEQRES 1 A 288 GLY ALA SER LYS LYS THR ILE GLY LYS ASP ILE CYS LYS SEQRES 2 A 288 TYR ASP VAL THR THR LYS VAL ALA THR CYS GLU ILE ILE SEQRES 3 A 288 ASP THR ILE ASP SER SER VAL LEU LYS GLU HIS HIS THR SEQRES 4 A 288 VAL HIS TYR SER ILE THR LEU SER ARG TRP ASP LYS LEU SEQRES 5 A 288 ILE ILE LYS TYR PRO THR ASN GLU LYS THR HIS PHE GLU SEQRES 6 A 288 ASN PHE PHE VAL ASN PRO PHE ASN LEU LYS ASP LYS VAL SEQRES 7 A 288 LEU TYR ASN TYR ASN LYS PRO ILE ASN ILE GLU HIS ILE SEQRES 8 A 288 LEU PRO GLY ALA ILE THR THR ASP ILE TYR ASP THR ARG SEQRES 9 A 288 THR LYS ILE LYS GLN TYR ILE LEU ARG ILE PRO PRO TYR SEQRES 10 A 288 VAL HIS LYS ASP ILE HIS PHE SER LEU GLU PHE ASN ASN SEQRES 11 A 288 SER LEU SER LEU THR LYS GLN ASN GLN ASN ILE ILE TYR SEQRES 12 A 288 GLY ASN VAL ALA LYS ILE PHE ILE HIS ILE ASN GLN GLY SEQRES 13 A 288 TYR LYS GLU ILE HIS GLY CYS ASP PHE THR GLY LYS TYR SEQRES 14 A 288 SER HIS LEU PHE THR TYR SER LYS LYS PRO LEU PRO ASN SEQRES 15 A 288 ASP ASP ASP ILE CYS ASN VAL THR ILE GLY ASN ASN THR SEQRES 16 A 288 PHE SER GLY PHE ALA CYS LEU SER HIS PHE GLU LEU LYS SEQRES 17 A 288 PRO ASN ASN CYS PHE SER SER VAL TYR ASP TYR ASN GLU SEQRES 18 A 288 ALA ASN LYS VAL LYS LYS LEU PHE ASP LEU SER THR LYS SEQRES 19 A 288 VAL GLU LEU ASP HIS ILE LYS GLN ASN THR SER GLY TYR SEQRES 20 A 288 THR LEU SER TYR ILE ILE PHE ASN LYS GLU SER THR LYS SEQRES 21 A 288 LEU LYS PHE SER CYS THR CYS SER SER ASN TYR SER ASN SEQRES 22 A 288 TYR THR ILE ARG ILE THR PHE ASP PRO ASN TYR ILE ILE SEQRES 23 A 288 PRO GLU SEQRES 1 C 130 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 130 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLU SEQRES 3 C 130 HIS THR PHE ARG ASP TYR ALA MET GLY TRP PHE ARG GLN SEQRES 4 C 130 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5 C 130 TRP SER GLY SER ILE LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 C 130 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ARG THR SEQRES 7 C 130 GLN TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 C 130 ALA VAL TYR TYR CYS ALA ALA ARG TRP PRO GLY GLY GLY SEQRES 9 C 130 MET TRP TYR GLU PRO PRO TYR ASP TYR TRP GLY GLN GLY SEQRES 10 C 130 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 D 130 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 130 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLU SEQRES 3 D 130 HIS THR PHE ARG ASP TYR ALA MET GLY TRP PHE ARG GLN SEQRES 4 D 130 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5 D 130 TRP SER GLY SER ILE LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 D 130 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ARG THR SEQRES 7 D 130 GLN TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 D 130 ALA VAL TYR TYR CYS ALA ALA ARG TRP PRO GLY GLY GLY SEQRES 9 D 130 MET TRP TYR GLU PRO PRO TYR ASP TYR TRP GLY GLN GLY SEQRES 10 D 130 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET MAN F 4 11 HET MAN F 5 11 HET NAG E 1 14 HET NAG E 2 14 HET NAG G 1 14 HET NAG G 2 14 HET GOL B3201 6 HET NAG B3202 14 HET NAG A3201 14 HET PEG A3202 7 HET GOL A3203 6 HET NAG A3204 14 HET NAG A3205 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 NAG 10(C8 H15 N O6) FORMUL 5 BMA C6 H12 O6 FORMUL 5 MAN 2(C6 H12 O6) FORMUL 8 GOL 2(C3 H8 O3) FORMUL 11 PEG C4 H10 O3 FORMUL 15 HOH *62(H2 O) HELIX 1 AA1 ILE B 2911 LEU B 2915 1 5 HELIX 2 AA2 ASN B 3043 ALA B 3045 5 3 HELIX 3 AA3 PHE B 3052 LEU B 3054 5 3 HELIX 4 AA4 ILE A 2848 ASP A 2853 1 6 HELIX 5 AA5 ASN A 2904 ASN A 2906 5 3 HELIX 6 AA6 ILE A 2911 LEU A 2915 1 5 HELIX 7 AA7 ASN A 3043 ALA A 3045 5 3 HELIX 8 AA8 PHE A 3052 LEU A 3054 5 3 HELIX 9 AA9 GLU C 26 TYR C 32 5 7 HELIX 10 AB1 LYS C 87 THR C 91 5 5 HELIX 11 AB2 GLU D 26 TYR D 32 5 7 HELIX 12 AB3 LYS D 87 THR D 91 5 5 SHEET 1 AA1 5 CYS B2835 ASP B2838 0 SHEET 2 AA1 5 VAL B2843 GLU B2847 -1 O VAL B2843 N ASP B2838 SHEET 3 AA1 5 LYS B2874 PRO B2880 1 O ILE B2876 N ALA B2844 SHEET 4 AA1 5 ILE B2930 ARG B2936 -1 O LYS B2931 N TYR B2879 SHEET 5 AA1 5 ILE B2919 ASP B2925 -1 N ILE B2919 O ARG B2936 SHEET 1 AA2 4 THR B2862 LEU B2869 0 SHEET 2 AA2 4 VAL B2969 ILE B2976 1 O PHE B2973 N TYR B2865 SHEET 3 AA2 4 ILE B2945 ASN B2952 -1 N PHE B2951 O ALA B2970 SHEET 4 AA2 4 PHE B2891 ASN B2893 -1 N ASN B2893 O GLU B2950 SHEET 1 AA3 5 THR B2862 LEU B2869 0 SHEET 2 AA3 5 VAL B2969 ILE B2976 1 O PHE B2973 N TYR B2865 SHEET 3 AA3 5 ILE B2945 ASN B2952 -1 N PHE B2951 O ALA B2970 SHEET 4 AA3 5 LYS B2900 TYR B2903 -1 N LEU B2902 O SER B2948 SHEET 5 AA3 5 LYS B2907 ASN B2910 -1 O ILE B2909 N VAL B2901 SHEET 1 AA4 2 LEU B2957 GLN B2960 0 SHEET 2 AA4 2 ASN B2963 TYR B2966 -1 O ILE B2965 N THR B2958 SHEET 1 AA5 6 VAL B3058 ILE B3063 0 SHEET 2 AA5 6 TYR B3070 PHE B3077 -1 O ILE B3076 N GLU B3059 SHEET 3 AA5 6 SER B3020 LEU B3025 -1 N CYS B3024 O THR B3071 SHEET 4 AA5 6 ILE B2983 ASP B2987 1 N CYS B2986 O GLY B3021 SHEET 5 AA5 6 PHE B2996 SER B2999 1 O TYR B2998 N ASP B2987 SHEET 6 AA5 6 GLY D 104 MET D 105 -1 O GLY D 104 N SER B2999 SHEET 1 AA6 4 ASP B3007 ILE B3014 0 SHEET 2 AA6 4 ASN B3096 PHE B3103 1 O THR B3098 N CYS B3010 SHEET 3 AA6 4 LEU B3084 SER B3091 -1 N CYS B3090 O TYR B3097 SHEET 4 AA6 4 GLU B3029 LYS B3031 -1 N LYS B3031 O THR B3089 SHEET 1 AA7 5 ASP B3007 ILE B3014 0 SHEET 2 AA7 5 ASN B3096 PHE B3103 1 O THR B3098 N CYS B3010 SHEET 3 AA7 5 LEU B3084 SER B3091 -1 N CYS B3090 O TYR B3097 SHEET 4 AA7 5 SER B3038 ASP B3041 -1 N TYR B3040 O SER B3087 SHEET 5 AA7 5 VAL B3048 LYS B3050 -1 O LYS B3049 N VAL B3039 SHEET 1 AA8 5 THR A2829 ASP A2833 0 SHEET 2 AA8 5 HIS A2860 LEU A2869 1 O HIS A2864 N GLY A2831 SHEET 3 AA8 5 VAL A2969 ILE A2976 1 O PHE A2973 N TYR A2865 SHEET 4 AA8 5 ILE A2945 ASN A2952 -1 N PHE A2947 O ILE A2974 SHEET 5 AA8 5 PHE A2891 ASN A2893 -1 N ASN A2893 O GLU A2950 SHEET 1 AA9 5 LYS A2836 ASP A2838 0 SHEET 2 AA9 5 VAL A2843 CYS A2846 -1 O VAL A2843 N ASP A2838 SHEET 3 AA9 5 LYS A2874 PRO A2880 1 O LYS A2874 N ALA A2844 SHEET 4 AA9 5 ILE A2930 ARG A2936 -1 O TYR A2933 N ILE A2877 SHEET 5 AA9 5 ILE A2919 ASP A2925 -1 N ILE A2923 O GLN A2932 SHEET 1 AB1 2 LYS A2900 LEU A2902 0 SHEET 2 AB1 2 PRO A2908 ASN A2910 -1 O ILE A2909 N VAL A2901 SHEET 1 AB2 2 LEU A2957 GLN A2960 0 SHEET 2 AB2 2 ASN A2963 TYR A2966 -1 O ASN A2963 N GLN A2960 SHEET 1 AB3 6 VAL A3058 ILE A3063 0 SHEET 2 AB3 6 TYR A3070 PHE A3077 -1 O TYR A3074 N ASP A3061 SHEET 3 AB3 6 SER A3020 LEU A3025 -1 N CYS A3024 O THR A3071 SHEET 4 AB3 6 ILE A2983 ASP A2987 1 N CYS A2986 O GLY A3021 SHEET 5 AB3 6 PHE A2996 SER A2999 1 O TYR A2998 N ASP A2987 SHEET 6 AB3 6 GLY C 104 MET C 105 -1 O GLY C 104 N SER A2999 SHEET 1 AB4 4 ASP A3007 ILE A3014 0 SHEET 2 AB4 4 ASN A3096 PHE A3103 1 O ARG A3100 N VAL A3012 SHEET 3 AB4 4 LEU A3084 SER A3091 -1 N PHE A3086 O ILE A3101 SHEET 4 AB4 4 GLU A3029 LYS A3031 -1 N GLU A3029 O SER A3091 SHEET 1 AB5 5 ASP A3007 ILE A3014 0 SHEET 2 AB5 5 ASN A3096 PHE A3103 1 O ARG A3100 N VAL A3012 SHEET 3 AB5 5 LEU A3084 SER A3091 -1 N PHE A3086 O ILE A3101 SHEET 4 AB5 5 SER A3038 ASP A3041 -1 N TYR A3040 O SER A3087 SHEET 5 AB5 5 VAL A3048 LYS A3050 -1 O LYS A3049 N VAL A3039 SHEET 1 AB6 4 GLU C 6 SER C 7 0 SHEET 2 AB6 4 LEU C 18 ALA C 23 -1 O SER C 21 N SER C 7 SHEET 3 AB6 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AB6 4 PHE C 68 ASP C 73 -1 N THR C 69 O GLN C 82 SHEET 1 AB7 6 GLY C 10 VAL C 12 0 SHEET 2 AB7 6 THR C 118 VAL C 122 1 O THR C 121 N GLY C 10 SHEET 3 AB7 6 ALA C 92 ARG C 99 -1 N TYR C 94 O THR C 118 SHEET 4 AB7 6 ALA C 33 GLN C 39 -1 N ALA C 33 O ARG C 99 SHEET 5 AB7 6 ARG C 45 ILE C 51 -1 O ALA C 49 N TRP C 36 SHEET 6 AB7 6 LYS C 58 TYR C 60 -1 O TYR C 59 N ALA C 50 SHEET 1 AB8 4 GLY C 10 VAL C 12 0 SHEET 2 AB8 4 THR C 118 VAL C 122 1 O THR C 121 N GLY C 10 SHEET 3 AB8 4 ALA C 92 ARG C 99 -1 N TYR C 94 O THR C 118 SHEET 4 AB8 4 TYR C 113 TRP C 114 -1 O TYR C 113 N ALA C 98 SHEET 1 AB9 4 GLN D 5 SER D 7 0 SHEET 2 AB9 4 LEU D 18 ALA D 23 -1 O ALA D 23 N GLN D 5 SHEET 3 AB9 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AB9 4 PHE D 68 ASP D 73 -1 N SER D 71 O TYR D 80 SHEET 1 AC1 6 LEU D 11 VAL D 12 0 SHEET 2 AC1 6 THR D 118 VAL D 122 1 O THR D 121 N VAL D 12 SHEET 3 AC1 6 ALA D 92 ARG D 99 -1 N TYR D 94 O THR D 118 SHEET 4 AC1 6 ALA D 33 GLN D 39 -1 N ALA D 33 O ARG D 99 SHEET 5 AC1 6 GLU D 46 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AC1 6 LYS D 58 TYR D 60 -1 O TYR D 59 N ALA D 50 SHEET 1 AC2 4 LEU D 11 VAL D 12 0 SHEET 2 AC2 4 THR D 118 VAL D 122 1 O THR D 121 N VAL D 12 SHEET 3 AC2 4 ALA D 92 ARG D 99 -1 N TYR D 94 O THR D 118 SHEET 4 AC2 4 TYR D 113 TRP D 114 -1 O TYR D 113 N ALA D 98 SSBOND 1 CYS B 2835 CYS B 2846 1555 1555 2.04 SSBOND 2 CYS B 2986 CYS B 3010 1555 1555 2.04 SSBOND 3 CYS B 3024 CYS B 3090 1555 1555 2.03 SSBOND 4 CYS B 3035 CYS B 3088 1555 1555 2.01 SSBOND 5 CYS A 2835 CYS A 2846 1555 1555 2.03 SSBOND 6 CYS A 2986 CYS A 3010 1555 1555 2.04 SSBOND 7 CYS A 3024 CYS A 3090 1555 1555 2.04 SSBOND 8 CYS A 3035 CYS A 3088 1555 1555 2.02 SSBOND 9 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 10 CYS D 22 CYS D 96 1555 1555 2.04 LINK ND2 ASN B2952 C1 NAG F 1 1555 1555 1.43 LINK ND2 ASN B3011 C1 NAG B3202 1555 1555 1.44 LINK ND2 ASN B3096 C1 NAG E 1 1555 1555 1.45 LINK ND2 ASN A2952 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN A3011 C1 NAG A3204 1555 1555 1.45 LINK ND2 ASN A3016 C1 NAG A3201 1555 1555 1.44 LINK ND2 ASN A3096 C1 NAG A3205 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.43 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44 LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.45 LINK O6 BMA F 3 C1 MAN F 5 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.46 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 CISPEP 1 ASN B 2893 PRO B 2894 0 3.63 CISPEP 2 LYS B 3031 PRO B 3032 0 -10.53 CISPEP 3 CYS B 3035 PHE B 3036 0 7.90 CISPEP 4 CYS B 3035 PHE B 3036 0 7.41 CISPEP 5 ASN A 2893 PRO A 2894 0 5.23 CISPEP 6 LYS A 3031 PRO A 3032 0 -7.10 CISPEP 7 CYS A 3035 PHE A 3036 0 6.57 CISPEP 8 CYS A 3035 PHE A 3036 0 5.12 CISPEP 9 PRO C 109 PRO C 110 0 7.61 CISPEP 10 PRO D 109 PRO D 110 0 7.28 CRYST1 79.919 79.919 342.703 90.00 90.00 90.00 P 43 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 0.012513 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012513 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002918 0.00000