HEADER PROTEIN BINDING 03-NOV-24 9E7O TITLE PFS230 D13D14 IN COMPLEX WITH NANOBODY W2810 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NANOBODY W2810; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GAMETOCYTE SURFACE PROTEIN P230; 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 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 8 ORGANISM_TAXID: 36329; SOURCE 9 GENE: PFS230, PF230, S230, PF3D7_0209000; SOURCE 10 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS 6-CYSTEINE PROTEIN, PLASMODIUM FALCIPARUM, MALARIA TRANSMISSION, KEYWDS 2 NANOBODY, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR M.H.DIETRICH,L.L.TAN,W.H.THAM REVDAT 1 30-JUL-25 9E7O 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. 1.93 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) : 1.93 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.92 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 35377 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.216 REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 1767 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 39.9200 - 4.5400 1.00 2667 141 0.1785 0.2039 REMARK 3 2 4.5300 - 3.6000 1.00 2605 137 0.1831 0.2039 REMARK 3 3 3.6000 - 3.1500 1.00 2581 136 0.2103 0.2380 REMARK 3 4 3.1500 - 2.8600 1.00 2605 137 0.2338 0.2958 REMARK 3 5 2.8600 - 2.6500 1.00 2582 136 0.2399 0.3184 REMARK 3 6 2.6500 - 2.5000 1.00 2571 135 0.2415 0.3251 REMARK 3 7 2.5000 - 2.3700 1.00 2582 136 0.2442 0.2809 REMARK 3 8 2.3700 - 2.2700 1.00 2565 135 0.2383 0.3183 REMARK 3 9 2.2700 - 2.1800 1.00 2561 135 0.2529 0.3135 REMARK 3 10 2.1800 - 2.1100 1.00 2592 136 0.2670 0.3416 REMARK 3 11 2.1100 - 2.0400 1.00 2589 137 0.2719 0.3308 REMARK 3 12 2.0400 - 1.9800 1.00 2543 132 0.2928 0.3406 REMARK 3 13 1.9800 - 1.9300 1.00 2567 134 0.3528 0.4036 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) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.800 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 43.98 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 : 0.009 3288 REMARK 3 ANGLE : 1.028 4475 REMARK 3 CHIRALITY : 0.064 504 REMARK 3 PLANARITY : 0.007 570 REMARK 3 DIHEDRAL : 17.008 1208 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 9E7O 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_1000289740. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-MAR-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) : 0.953647 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 : 35422 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930 REMARK 200 RESOLUTION RANGE LOW (A) : 39.920 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : 0.04800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.8300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.64200 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 (%): 51.27 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM MALONATE DIBASIC REMARK 280 MONOHYDRATE PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293K 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 67.74700 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.41200 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.74700 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.41200 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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, D 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 HOH A 303 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 A 26 REMARK 465 ARG A 27 REMARK 465 SER A 120 REMARK 465 SER A 121 REMARK 465 HIS A 122 REMARK 465 HIS A 123 REMARK 465 HIS A 124 REMARK 465 HIS A 125 REMARK 465 HIS A 126 REMARK 465 HIS A 127 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 GLU B 3111 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 VAL A 12 CG1 CG2 REMARK 470 GLN A 13 CG CD OE1 NE2 REMARK 470 LYS A 65 CD CE NZ REMARK 470 LYS A 87 CE NZ REMARK 470 GLU A 89 CG CD OE1 OE2 REMARK 470 LYS B2832 CD CE NZ REMARK 470 LYS B2836 CG CD CE NZ REMARK 470 LYS B2842 CE NZ REMARK 470 LYS B2907 CG CD CE NZ REMARK 470 LYS B2981 CG CD CE NZ REMARK 470 LYS B3000 CG CD CE NZ REMARK 470 LYS B3001 CG CD CE NZ REMARK 470 ASN B3005 CG OD1 ND2 REMARK 470 LYS B3031 CE NZ REMARK 470 LYS B3049 CE NZ REMARK 470 LYS B3050 CD CE NZ REMARK 470 PHE B3052 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B3057 CG CD CE NZ REMARK 470 LYS B3064 CD CE NZ REMARK 470 LYS B3079 CG CD CE NZ REMARK 470 LYS B3083 CG CD CE NZ REMARK 470 LYS B3085 CD CE NZ REMARK 470 ILE B3108 CG1 CG2 CD1 REMARK 470 ILE B3109 CG1 CG2 CD1 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 O GLY B 2979 O HOH B 3301 2.07 REMARK 500 O CYS B 2846 O HOH B 3302 2.17 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 ALA A 14 107.05 -49.30 REMARK 500 TRP B2872 -6.83 70.58 REMARK 500 ASN B2906 -52.59 -133.08 REMARK 500 ASN B2906 -51.27 -133.81 REMARK 500 TYR B2980 -69.75 75.91 REMARK 500 GLU B3044 51.76 -152.98 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG B 3202 DBREF 9E7O A 1 127 PDB 9E7O 9E7O 1 127 DBREF 9E7O B 2827 3111 UNP P68874 P230_PLAF7 2827 3111 SEQADV 9E7O GLY B 2824 UNP P68874 EXPRESSION TAG SEQADV 9E7O ALA B 2825 UNP P68874 EXPRESSION TAG SEQADV 9E7O SER B 2826 UNP P68874 EXPRESSION TAG SEQRES 1 A 127 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 127 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 127 ARG THR PHE SER SER TYR ALA MET GLY TRP PHE HIS GLN SEQRES 4 A 127 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA SER ILE SER SEQRES 5 A 127 TRP SER GLY GLY SER ILE ARG TYR ALA ASP SER VAL LYS SEQRES 6 A 127 GLY ARG PHE THR VAL SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 A 127 ALA TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 A 127 GLY VAL TYR TYR CYS ALA ALA GLY PRO TYR SER SER ASP SEQRES 9 A 127 TYR GLY GLY PHE GLY SER TRP GLY GLN GLY THR GLN VAL SEQRES 10 A 127 THR VAL SER SER HIS HIS HIS HIS HIS HIS 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 HET NAG D 1 14 HET NAG D 2 14 HET EDO A 201 4 HET EDO A 202 4 HET EDO A 203 4 HET EDO B3201 4 HET NAG B3202 14 HET NAG B3203 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM EDO 1,2-ETHANEDIOL 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 EDO ETHYLENE GLYCOL FORMUL 3 NAG 4(C8 H15 N O6) FORMUL 4 EDO 4(C2 H6 O2) FORMUL 10 HOH *128(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASN A 74 LYS A 76 5 3 HELIX 3 AA3 LYS A 87 THR A 91 5 5 HELIX 4 AA4 ASP A 104 PHE A 108 5 5 HELIX 5 AA5 ILE B 2848 ASP B 2853 1 6 HELIX 6 AA6 ILE B 2911 LEU B 2915 1 5 HELIX 7 AA7 ASN B 3043 ALA B 3045 5 3 HELIX 8 AA8 LEU B 3051 SER B 3055 1 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N GLN A 5 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 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AA2 5 ILE A 58 TYR A 60 0 SHEET 2 AA2 5 GLU A 46 ILE A 51 -1 N SER A 50 O ARG A 59 SHEET 3 AA2 5 ALA A 33 GLN A 39 -1 N TRP A 36 O VAL A 48 SHEET 4 AA2 5 GLY A 92 GLY A 99 -1 O VAL A 93 N GLN A 39 SHEET 5 AA2 5 SER A 110 TRP A 111 -1 O SER A 110 N ALA A 98 SHEET 1 AA3 5 ILE A 58 TYR A 60 0 SHEET 2 AA3 5 GLU A 46 ILE A 51 -1 N SER A 50 O ARG A 59 SHEET 3 AA3 5 ALA A 33 GLN A 39 -1 N TRP A 36 O VAL A 48 SHEET 4 AA3 5 GLY A 92 GLY A 99 -1 O VAL A 93 N GLN A 39 SHEET 5 AA3 5 THR A 115 VAL A 117 -1 O VAL A 117 N GLY A 92 SHEET 1 AA4 5 ILE B2830 ILE B2834 0 SHEET 2 AA4 5 THR B2862 LEU B2869 1 O HIS B2864 N GLY B2831 SHEET 3 AA4 5 VAL B2969 ILE B2976 1 O PHE B2973 N TYR B2865 SHEET 4 AA4 5 ILE B2945 ASN B2952 -1 N PHE B2947 O ILE B2974 SHEET 5 AA4 5 PHE B2891 ASN B2893 -1 N PHE B2891 O ASN B2952 SHEET 1 AA5 6 ILE B2830 ILE B2834 0 SHEET 2 AA5 6 THR B2862 LEU B2869 1 O HIS B2864 N GLY B2831 SHEET 3 AA5 6 VAL B2969 ILE B2976 1 O PHE B2973 N TYR B2865 SHEET 4 AA5 6 ILE B2945 ASN B2952 -1 N PHE B2947 O ILE B2974 SHEET 5 AA5 6 LYS B2900 TYR B2903 -1 N LEU B2902 O SER B2948 SHEET 6 AA5 6 LYS B2907 ASN B2910 -1 O LYS B2907 N TYR B2903 SHEET 1 AA6 5 LYS B2836 ASP B2838 0 SHEET 2 AA6 5 VAL B2843 GLU B2847 -1 O VAL B2843 N ASP B2838 SHEET 3 AA6 5 LYS B2874 PRO B2880 1 O LYS B2874 N ALA B2844 SHEET 4 AA6 5 ILE B2930 ARG B2936 -1 O LYS B2931 N TYR B2879 SHEET 5 AA6 5 ILE B2919 TYR B2924 -1 N ILE B2919 O ARG B2936 SHEET 1 AA7 2 LEU B2957 GLN B2960 0 SHEET 2 AA7 2 ASN B2963 TYR B2966 -1 O ILE B2965 N THR B2958 SHEET 1 AA8 5 PHE B2996 SER B2999 0 SHEET 2 AA8 5 ILE B2983 ASP B2987 1 N ASP B2987 O TYR B2998 SHEET 3 AA8 5 PHE B3019 LEU B3025 1 O GLY B3021 N CYS B2986 SHEET 4 AA8 5 TYR B3070 PHE B3077 -1 O THR B3071 N CYS B3024 SHEET 5 AA8 5 VAL B3058 ILE B3063 -1 N GLU B3059 O ILE B3076 SHEET 1 AA9 4 ASP B3007 ILE B3014 0 SHEET 2 AA9 4 ASN B3096 PHE B3103 1 O THR B3098 N CYS B3010 SHEET 3 AA9 4 LEU B3084 SER B3091 -1 N CYS B3088 O ILE B3099 SHEET 4 AA9 4 GLU B3029 LYS B3031 -1 N LYS B3031 O THR B3089 SHEET 1 AB1 5 ASP B3007 ILE B3014 0 SHEET 2 AB1 5 ASN B3096 PHE B3103 1 O THR B3098 N CYS B3010 SHEET 3 AB1 5 LEU B3084 SER B3091 -1 N CYS B3088 O ILE B3099 SHEET 4 AB1 5 SER B3038 ASP B3041 -1 N TYR B3040 O SER B3087 SHEET 5 AB1 5 VAL B3048 LYS B3050 -1 O LYS B3049 N VAL B3039 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.10 SSBOND 2 CYS B 2835 CYS B 2846 1555 1555 2.03 SSBOND 3 CYS B 2986 CYS B 3010 1555 1555 2.05 SSBOND 4 CYS B 3024 CYS B 3090 1555 1555 2.04 SSBOND 5 CYS B 3035 CYS B 3088 1555 1555 2.00 LINK ND2 ASN B2952 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN B3096 C1 NAG B3203 1555 1555 1.45 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 CISPEP 1 ASN B 2893 PRO B 2894 0 6.49 CISPEP 2 LYS B 3031 PRO B 3032 0 -9.47 CISPEP 3 CYS B 3035 PHE B 3036 0 7.29 CISPEP 4 CYS B 3035 PHE B 3036 0 5.83 CRYST1 135.494 62.824 56.481 90.00 98.92 90.00 C 1 2 1 4 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 0.007380 0.000000 0.001158 0.00000 SCALE2 0.000000 0.015917 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017922 0.00000