HEADER PROTEIN BINDING 03-NOV-24 9E7P TITLE PFS230 D13D14 IN COMPLEX WITH NANOBODY W2812 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NANOBODY W2812; 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 9E7P 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. 3.22 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) : 3.22 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.60 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 11747 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.289 REMARK 3 R VALUE (WORKING SET) : 0.286 REMARK 3 FREE R VALUE : 0.320 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.010 REMARK 3 FREE R VALUE TEST SET COUNT : 1058 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 47.6000 - 6.4400 1.00 1441 143 0.2449 0.2780 REMARK 3 2 6.4400 - 5.1100 1.00 1360 135 0.2808 0.3104 REMARK 3 3 5.1100 - 4.4600 1.00 1338 132 0.2551 0.3057 REMARK 3 4 4.4600 - 4.0600 1.00 1317 130 0.2742 0.2853 REMARK 3 5 4.0600 - 3.7700 1.00 1315 130 0.3588 0.4160 REMARK 3 6 3.7700 - 3.5400 1.00 1317 130 0.3552 0.3704 REMARK 3 7 3.5400 - 3.3700 1.00 1293 128 0.3678 0.4408 REMARK 3 8 3.3700 - 3.2200 1.00 1308 130 0.4100 0.4107 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) : 0.560 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.970 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 95.46 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 : 0.003 3226 REMARK 3 ANGLE : 0.602 4412 REMARK 3 CHIRALITY : 0.048 507 REMARK 3 PLANARITY : 0.004 567 REMARK 3 DIHEDRAL : 16.080 1143 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 9E7P 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_1000289744. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-DEC-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 : 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) : 0.953728 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 : 11793 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.220 REMARK 200 RESOLUTION RANGE LOW (A) : 47.600 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 13.30 REMARK 200 R MERGE (I) : 0.07700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.22 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.41 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.79600 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 (%): 65.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 5% (W/V) PEG8000, 5% (W/V) PEG10000, REMARK 280 5% (W/V) PEG 6000, 0.15M AMMONIUM ACETATE, 0.1 M SODIUM CITRATE REMARK 280 PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K 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 37.87000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 67.32350 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 67.32350 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 18.93500 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 67.32350 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 67.32350 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.80500 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 67.32350 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 67.32350 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 18.93500 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 67.32350 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 67.32350 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.80500 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 37.87000 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: 2380 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18410 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 126 REMARK 465 SER A 127 REMARK 465 HIS A 128 REMARK 465 HIS A 129 REMARK 465 HIS A 130 REMARK 465 HIS A 131 REMARK 465 HIS A 132 REMARK 465 HIS A 133 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 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 LEU A 11 CG CD1 CD2 REMARK 470 MET A 34 CG SD CE REMARK 470 GLN A 41 CG CD OE1 NE2 REMARK 470 LYS A 76 CD CE NZ REMARK 470 LYS A 87 CG CD CE NZ REMARK 470 LYS A 89 CG CD CE NZ REMARK 470 LYS B2832 CG CD CE NZ REMARK 470 ASP B2833 CG OD1 OD2 REMARK 470 LYS B2836 CD CE NZ REMARK 470 LYS B2842 CG CD CE NZ REMARK 470 LYS B2907 CG CD CE NZ REMARK 470 ARG B2927 CG CD NE CZ NH1 NH2 REMARK 470 LYS B2929 CG CD CE NZ REMARK 470 LYS B2943 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 LEU B3003 CG CD1 CD2 REMARK 470 GLU B3029 CG CD OE1 OE2 REMARK 470 LYS B3031 CE NZ REMARK 470 VAL B3039 CG1 CG2 REMARK 470 ASN B3046 CG OD1 ND2 REMARK 470 LYS B3047 CG CD CE NZ REMARK 470 LYS B3049 CG CD CE NZ REMARK 470 LYS B3050 CG CD CE NZ REMARK 470 LEU B3051 CG CD1 CD2 REMARK 470 PHE B3052 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU B3054 CG CD1 CD2 REMARK 470 LYS B3057 CG CD CE NZ REMARK 470 LYS B3064 CG CD CE NZ REMARK 470 ASN B3078 CG OD1 ND2 REMARK 470 LYS B3079 CG CD CE NZ REMARK 470 SER B3081 OG REMARK 470 LYS B3083 CG CD CE NZ REMARK 470 LEU B3084 CG CD1 CD2 REMARK 470 LYS B3085 CD CE NZ REMARK 470 TYR B3094 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG B3100 CG CD NE CZ NH1 NH2 REMARK 470 ASP B3104 CG OD1 OD2 REMARK 470 ASN B3106 CG OD1 ND2 REMARK 470 ILE B3108 CG1 CG2 CD1 REMARK 470 ILE B3109 CG1 CG2 CD1 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 GLN A 39 99.54 -163.22 REMARK 500 THR A 91 105.65 -59.91 REMARK 500 ILE B2849 -64.94 -124.54 REMARK 500 SER B2870 -167.17 -118.61 REMARK 500 HIS B2886 -2.65 72.37 REMARK 500 ASN B2889 40.57 -93.09 REMARK 500 ASN B2906 -80.31 -132.83 REMARK 500 ASN B2961 -130.40 56.49 REMARK 500 TYR B2980 -62.22 73.14 REMARK 500 TYR B2992 42.66 -93.59 REMARK 500 PHE B3036 -36.94 70.87 REMARK 500 GLU B3044 39.14 -81.67 REMARK 500 REMARK 500 REMARK: NULL DBREF 9E7P A 1 133 PDB 9E7P 9E7P 1 133 DBREF 9E7P B 2827 3111 UNP P68874 P230_PLAF7 2827 3111 SEQADV 9E7P GLY B 2824 UNP P68874 EXPRESSION TAG SEQADV 9E7P ALA B 2825 UNP P68874 EXPRESSION TAG SEQADV 9E7P SER B 2826 UNP P68874 EXPRESSION TAG SEQRES 1 A 133 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 133 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 133 ARG THR PHE SER SER TYR MET MET ALA TRP PHE ARG GLN SEQRES 4 A 133 SER GLN GLY ASN GLU ARG GLU LEU VAL ALA GLY LEU THR SEQRES 5 A 133 ARG SER GLY VAL SER ALA TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 133 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 A 133 VAL TYR LEU GLN MET ASN SER LEU LYS PRO LYS ASP THR SEQRES 8 A 133 ALA VAL TYR TYR CYS ALA ALA ALA SER THR THR TYR ILE SEQRES 9 A 133 ASN HIS ILE TYR THR ASN PRO SER ASN TYR PRO HIS TRP SEQRES 10 A 133 GLY PRO GLY THR GLN VAL THR VAL SER SER HIS HIS HIS SEQRES 11 A 133 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 C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET CIT A 201 13 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM CIT CITRIC ACID 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 FORMUL 3 NAG 2(C8 H15 N O6) FORMUL 3 BMA C6 H12 O6 FORMUL 4 CIT C6 H8 O7 HELIX 1 AA1 THR A 28 SER A 30 5 3 HELIX 2 AA2 LYS A 87 THR A 91 5 5 HELIX 3 AA3 ASN A 110 TYR A 114 5 5 HELIX 4 AA4 ILE B 2849 ASP B 2853 5 5 HELIX 5 AA5 ILE B 2911 LEU B 2915 1 5 HELIX 6 AA6 LYS B 3050 SER B 3055 1 6 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 SER A 17 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA1 4 THR A 78 ASN A 84 -1 O MET A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82 SHEET 1 AA2 5 ALA A 58 TYR A 60 0 SHEET 2 AA2 5 GLU A 46 LEU A 51 -1 N GLY A 50 O TYR A 59 SHEET 3 AA2 5 TYR A 32 ARG A 38 -1 N ARG A 38 O GLU A 46 SHEET 4 AA2 5 ALA A 92 SER A 100 -1 O ALA A 97 N ALA A 35 SHEET 5 AA2 5 HIS A 116 TRP A 117 -1 O HIS A 116 N ALA A 98 SHEET 1 AA3 5 ALA A 58 TYR A 60 0 SHEET 2 AA3 5 GLU A 46 LEU A 51 -1 N GLY A 50 O TYR A 59 SHEET 3 AA3 5 TYR A 32 ARG A 38 -1 N ARG A 38 O GLU A 46 SHEET 4 AA3 5 ALA A 92 SER A 100 -1 O ALA A 97 N ALA A 35 SHEET 5 AA3 5 THR A 121 VAL A 123 -1 O VAL A 123 N ALA A 92 SHEET 1 AA4 3 HIS A 106 TYR A 108 0 SHEET 2 AA4 3 ASN B2963 TYR B2966 -1 O ILE B2964 N ILE A 107 SHEET 3 AA4 3 LEU B2957 GLN B2960 -1 N THR B2958 O ILE B2965 SHEET 1 AA5 5 CYS B2835 ASP B2838 0 SHEET 2 AA5 5 VAL B2843 GLU B2847 -1 O THR B2845 N LYS B2836 SHEET 3 AA5 5 LYS B2874 PRO B2880 1 O LYS B2874 N ALA B2844 SHEET 4 AA5 5 ILE B2930 ARG B2936 -1 O LEU B2935 N LEU B2875 SHEET 5 AA5 5 ILE B2919 ASP B2925 -1 N ILE B2919 O ARG B2936 SHEET 1 AA6 4 THR B2862 LEU B2869 0 SHEET 2 AA6 4 VAL B2969 ILE B2976 1 O HIS B2975 N LEU B2869 SHEET 3 AA6 4 ILE B2945 ASN B2952 -1 N PHE B2947 O ILE B2974 SHEET 4 AA6 4 PHE B2891 ASN B2893 -1 N ASN B2893 O GLU B2950 SHEET 1 AA7 5 THR B2862 LEU B2869 0 SHEET 2 AA7 5 VAL B2969 ILE B2976 1 O HIS B2975 N LEU B2869 SHEET 3 AA7 5 ILE B2945 ASN B2952 -1 N PHE B2947 O ILE B2974 SHEET 4 AA7 5 LYS B2900 TYR B2903 -1 N LEU B2902 O SER B2948 SHEET 5 AA7 5 LYS B2907 ASN B2910 -1 O ILE B2909 N VAL B2901 SHEET 1 AA8 5 PHE B2996 SER B2999 0 SHEET 2 AA8 5 ILE B2983 ASP B2987 1 O ILE B2983 N THR B2997 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 ILE B3063 O LEU B3072 SHEET 1 AA9 4 ILE B3009 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 LEU B3084 O PHE B3103 SHEET 4 AA9 4 GLU B3029 LYS B3031 -1 N GLU B3029 O SER B3091 SHEET 1 AB1 2 TYR B3040 ASP B3041 0 SHEET 2 AB1 2 LYS B3047 VAL B3048 -1 O LYS B3047 N ASP B3041 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS B 2835 CYS B 2846 1555 1555 2.03 SSBOND 3 CYS B 2986 CYS B 3010 1555 1555 2.03 SSBOND 4 CYS B 3024 CYS B 3090 1555 1555 2.03 SSBOND 5 CYS B 3035 CYS B 3088 1555 1555 2.03 LINK ND2 ASN B2952 C1 NAG C 1 1555 1555 1.45 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.46 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45 CISPEP 1 ASN B 2893 PRO B 2894 0 1.44 CISPEP 2 LYS B 3031 PRO B 3032 0 -1.60 CRYST1 134.647 134.647 75.740 90.00 90.00 90.00 P 41 21 2 8 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 0.007427 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007427 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013203 0.00000