HEADER IMMUNE SYSTEM 09-DEC-24 9HML TITLE KIR2DL1 BOUND TO RIFIN PFKE01_040007400 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RIFIN PFKE01_040007400; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: KIR2DL PROTEIN; COMPND 7 CHAIN: B; COMPND 8 SYNONYM: KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: NANOBODY NB1; COMPND 12 CHAIN: C; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM; SOURCE 3 ORGANISM_TAXID: 5833; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 GENE: KIR2DL1, 3DL2; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 15 ORGANISM_TAXID: 562; SOURCE 16 EXPRESSION_SYSTEM: LAMA GLAMA; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9844 KEYWDS RIFIN, KIR2DL1, IMMUNE RECEPTOR, MALARIA, INFECTED-ERYTHROCYTE, KEYWDS 2 PLASMODIUM FALCIPARUM, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.G.CHAMBERLAIN,M.K.HIGGINS REVDAT 1 09-APR-25 9HML 0 JRNL AUTH S.G.CHAMBERLAIN,M.K.HIGGINS JRNL TITL RIFINS DISPLAYED ON MALARIA-INFECTED ERYTHROCYTES BIND BOTH JRNL TITL 2 KIR2DL1 AND KIR2DS1 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.17 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.4 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.05 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 31974 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.221 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1592 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.19 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.05 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3611 REMARK 3 BIN FREE R VALUE : 0.3847 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 31 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3184 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 38 REMARK 3 SOLVENT ATOMS : 158 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.29 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.63160 REMARK 3 B22 (A**2) : 0.63160 REMARK 3 B33 (A**2) : -1.26320 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.320 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.209 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.164 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.205 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.163 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3302 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4481 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1119 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 559 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3302 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 439 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 2563 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 0.96 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.48 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.62 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): -2.304 -29.5041 -27.5657 REMARK 3 T TENSOR REMARK 3 T11: -0.1481 T22: 0.0659 REMARK 3 T33: -0.075 T12: 0.1031 REMARK 3 T13: 0.0757 T23: 0.0312 REMARK 3 L TENSOR REMARK 3 L11: 3.471 L22: 0.6794 REMARK 3 L33: 5.6251 L12: 0.7651 REMARK 3 L13: 0.0609 L23: -0.1042 REMARK 3 S TENSOR REMARK 3 S11: 0.2415 S12: -0.2391 S13: -0.0541 REMARK 3 S21: -0.2391 S22: -0.0063 S23: -0.1978 REMARK 3 S31: -0.0541 S32: -0.1978 S33: -0.2352 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): 1.7518 -36.9004 1.5692 REMARK 3 T TENSOR REMARK 3 T11: -0.2126 T22: 0.0875 REMARK 3 T33: 0.0241 T12: 0.1237 REMARK 3 T13: -0.0693 T23: -0.0834 REMARK 3 L TENSOR REMARK 3 L11: 1.5952 L22: 1.6338 REMARK 3 L33: 2.7836 L12: 0.226 REMARK 3 L13: -2.1925 L23: -1.011 REMARK 3 S TENSOR REMARK 3 S11: -0.0822 S12: -0.081 S13: 0.1914 REMARK 3 S21: -0.081 S22: 0.1751 S23: 0.8535 REMARK 3 S31: 0.1914 S32: 0.8535 S33: -0.0929 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { C|* } REMARK 3 ORIGIN FOR THE GROUP (A): -23.8406 -42.5832 14.7588 REMARK 3 T TENSOR REMARK 3 T11: -0.0424 T22: -0.1154 REMARK 3 T33: -0.0378 T12: 0.1023 REMARK 3 T13: 0.0284 T23: 0.0632 REMARK 3 L TENSOR REMARK 3 L11: 1.9125 L22: 1.7021 REMARK 3 L33: 2.9502 L12: 0.1775 REMARK 3 L13: -1.2373 L23: 0.2975 REMARK 3 S TENSOR REMARK 3 S11: -0.2731 S12: 0.3173 S13: 0.3527 REMARK 3 S21: 0.3173 S22: 0.1843 S23: 0.0408 REMARK 3 S31: 0.3527 S32: 0.0408 S33: 0.0887 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9HML COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292143804. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-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 : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.976246 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32044 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170 REMARK 200 RESOLUTION RANGE LOW (A) : 84.150 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 20.30 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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 (%): 58.79 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM MALONATE PH 4.6, 14% PEG REMARK 280 3,350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 36.40067 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 72.80133 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 72.80133 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 36.40067 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 -1 REMARK 465 SER A 0 REMARK 465 ALA A 1 REMARK 465 LYS A 2 REMARK 465 GLY A 3 REMARK 465 ALA A 4 REMARK 465 ALA A 5 REMARK 465 ALA A 6 REMARK 465 CYS A 7 REMARK 465 GLU A 8 REMARK 465 ALA A 123 REMARK 465 CYS A 124 REMARK 465 LYS A 125 REMARK 465 LYS A 126 REMARK 465 ALA A 127 REMARK 465 THR A 128 REMARK 465 GLU A 129 REMARK 465 GLY A 130 REMARK 465 THR A 131 REMARK 465 GLY A 132 REMARK 465 GLY A 133 REMARK 465 SER A 134 REMARK 465 GLU A 135 REMARK 465 PRO A 136 REMARK 465 GLU A 137 REMARK 465 ALA A 138 REMARK 465 THR B 25 REMARK 465 GLY B 26 REMARK 465 GLN B 134 REMARK 465 PRO B 135 REMARK 465 GLY B 136 REMARK 465 PRO B 137 REMARK 465 THR B 138 REMARK 465 VAL B 139 REMARK 465 LEU B 140 REMARK 465 PRO B 189 REMARK 465 ALA B 190 REMARK 465 THR B 191 REMARK 465 HIS B 192 REMARK 465 GLY B 193 REMARK 465 GLY B 220 REMARK 465 THR B 221 REMARK 465 LYS B 222 REMARK 465 HIS B 223 REMARK 465 HIS B 224 REMARK 465 HIS B 225 REMARK 465 HIS B 226 REMARK 465 HIS B 227 REMARK 465 HIS B 228 REMARK 465 GLY C 120 REMARK 465 HIS C 121 REMARK 465 HIS C 122 REMARK 465 HIS C 123 REMARK 465 HIS C 124 REMARK 465 HIS C 125 REMARK 465 HIS C 126 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 PHE A 84 -69.14 -148.16 REMARK 500 ARG B 89 100.20 -163.10 REMARK 500 VAL B 104 -65.17 -91.46 REMARK 500 SER C 25 72.81 -119.25 REMARK 500 REMARK 500 REMARK: NULL DBREF 9HML A -1 138 PDB 9HML 9HML -1 138 DBREF1 9HML B 27 219 UNP A0A191URJ7_HUMAN DBREF2 9HML B A0A191URJ7 27 219 DBREF 9HML C 1 126 PDB 9HML 9HML 1 126 SEQADV 9HML THR B 25 UNP A0A191URJ EXPRESSION TAG SEQADV 9HML GLY B 26 UNP A0A191URJ EXPRESSION TAG SEQADV 9HML GLY B 220 UNP A0A191URJ EXPRESSION TAG SEQADV 9HML THR B 221 UNP A0A191URJ EXPRESSION TAG SEQADV 9HML LYS B 222 UNP A0A191URJ EXPRESSION TAG SEQADV 9HML HIS B 223 UNP A0A191URJ EXPRESSION TAG SEQADV 9HML HIS B 224 UNP A0A191URJ EXPRESSION TAG SEQADV 9HML HIS B 225 UNP A0A191URJ EXPRESSION TAG SEQADV 9HML HIS B 226 UNP A0A191URJ EXPRESSION TAG SEQADV 9HML HIS B 227 UNP A0A191URJ EXPRESSION TAG SEQADV 9HML HIS B 228 UNP A0A191URJ EXPRESSION TAG SEQRES 1 A 140 GLY SER ALA LYS GLY ALA ALA ALA CYS GLU ALA ALA ARG SEQRES 2 A 140 ILE PRO ALA ALA ILE ASP ALA VAL ILE LYS GLY ILE VAL SEQRES 3 A 140 THR LYS PHE GLY VAL SER THR GLU SER VAL GLN GLY LEU SEQRES 4 A 140 LYS SER LEU PHE THR ALA ASN THR TYR ASN ASP VAL THR SEQRES 5 A 140 LYS ILE ALA ARG ALA ILE ASN GLU GLN TYR ASN PRO SER SEQRES 6 A 140 SER CYS LEU THR GLY GLY SER GLY ALA ASP ASN SER ILE SEQRES 7 A 140 CYS PRO TRP ALA MET GLU ASN PHE PHE ALA ALA ARG LYS SEQRES 8 A 140 ILE PRO GLY PHE ILE GLN ARG GLU ALA VAL SER MET ASN SEQRES 9 A 140 ASP VAL ILE GLU LYS THR VAL LYS THR ILE VAL SER ASP SEQRES 10 A 140 ALA PRO LYS THR ALA GLU THR ALA CYS LYS LYS ALA THR SEQRES 11 A 140 GLU GLY THR GLY GLY SER GLU PRO GLU ALA SEQRES 1 B 204 THR GLY ARG LYS PRO SER LEU LEU ALA HIS PRO GLY PRO SEQRES 2 B 204 LEU VAL LYS SER GLU GLU THR VAL ILE LEU GLN CYS TRP SEQRES 3 B 204 SER ASP VAL MET PHE GLU HIS PHE LEU LEU HIS ARG GLU SEQRES 4 B 204 GLY MET PHE ASN ASP THR LEU ARG LEU ILE GLY GLU HIS SEQRES 5 B 204 HIS ASP GLY VAL SER LYS ALA ASN PHE SER ILE SER ARG SEQRES 6 B 204 MET THR GLN ASP LEU ALA GLY THR TYR ARG CYS TYR GLY SEQRES 7 B 204 SER VAL THR HIS SER PRO TYR GLN VAL SER ALA PRO SER SEQRES 8 B 204 ASP PRO LEU ASP ILE VAL ILE ILE GLY LEU TYR GLU LYS SEQRES 9 B 204 PRO SER LEU SER ALA GLN PRO GLY PRO THR VAL LEU ALA SEQRES 10 B 204 GLY GLU ASN VAL THR LEU SER CYS SER SER ARG SER SER SEQRES 11 B 204 TYR ASP MET TYR HIS LEU SER ARG GLU GLY GLU ALA HIS SEQRES 12 B 204 GLU ARG ARG LEU PRO ALA GLY PRO LYS VAL ASN GLY THR SEQRES 13 B 204 PHE GLN ALA ASP PHE PRO LEU GLY PRO ALA THR HIS GLY SEQRES 14 B 204 GLY THR TYR ARG CYS PHE GLY SER PHE HIS ASP SER PRO SEQRES 15 B 204 TYR GLU TRP SER LYS SER SER ASP PRO LEU LEU VAL SER SEQRES 16 B 204 GLY THR LYS HIS HIS HIS HIS HIS HIS SEQRES 1 C 126 GLN ARG GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 126 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 126 ARG SER PHE SER ASP TYR THR MET GLY TRP PHE ARG GLN SEQRES 4 C 126 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5 C 126 TRP SER GLY GLY SER THR TYR ALA ASP SER VAL LYS GLY SEQRES 6 C 126 ARG PHE ILE ILE SER ARG ASP ASN VAL LYS ASN THR VAL SEQRES 7 C 126 TYR LEU GLN MET ASN SER LEU GLU PRO GLU ASP THR ALA SEQRES 8 C 126 VAL TYR TYR CYS ALA ALA GLU ARG THR GLY TRP SER SER SEQRES 9 C 126 GLU TYR ASP TYR TRP GLY LYS GLY THR PRO VAL THR VAL SEQRES 10 C 126 SER SER GLY HIS HIS HIS HIS HIS HIS HET NAG D 1 14 HET FUC D 2 10 HET NAG B 400 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE 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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 4 NAG 2(C8 H15 N O6) FORMUL 4 FUC C6 H12 O5 FORMUL 6 HOH *158(H2 O) HELIX 1 AA1 ALA A 10 GLY A 28 1 19 HELIX 2 AA2 SER A 30 GLY A 36 1 7 HELIX 3 AA3 ASP A 48 ASN A 61 1 14 HELIX 4 AA4 PRO A 62 LEU A 66 5 5 HELIX 5 AA5 ILE A 76 PHE A 84 1 9 HELIX 6 AA6 MET A 101 THR A 122 1 22 HELIX 7 AA7 THR B 91 LEU B 94 5 4 HELIX 8 AA8 SER C 28 TYR C 32 5 5 HELIX 9 AA9 GLU C 86 THR C 90 5 5 SHEET 1 AA1 6 ALA A 98 SER A 100 0 SHEET 2 AA1 6 ASP B 68 ILE B 73 -1 O ARG B 71 N VAL A 99 SHEET 3 AA1 6 HIS B 57 GLY B 64 -1 N PHE B 58 O LEU B 72 SHEET 4 AA1 6 GLY B 96 THR B 105 -1 O TYR B 101 N LEU B 59 SHEET 5 AA1 6 LEU B 118 ILE B 123 -1 O ILE B 120 N GLY B 96 SHEET 6 AA1 6 LEU B 38 LYS B 40 1 N VAL B 39 O VAL B 121 SHEET 1 AA2 5 ALA A 98 SER A 100 0 SHEET 2 AA2 5 ASP B 68 ILE B 73 -1 O ARG B 71 N VAL A 99 SHEET 3 AA2 5 HIS B 57 GLY B 64 -1 N PHE B 58 O LEU B 72 SHEET 4 AA2 5 GLY B 96 THR B 105 -1 O TYR B 101 N LEU B 59 SHEET 5 AA2 5 GLN B 110 VAL B 111 -1 O GLN B 110 N VAL B 104 SHEET 1 AA3 4 SER B 30 HIS B 34 0 SHEET 2 AA3 4 VAL B 45 SER B 51 -1 O TRP B 50 N SER B 30 SHEET 3 AA3 4 VAL B 80 ILE B 87 -1 O ILE B 87 N VAL B 45 SHEET 4 AA3 4 GLU B 75 HIS B 77 -1 N GLU B 75 O LYS B 82 SHEET 1 AA4 4 SER B 130 SER B 132 0 SHEET 2 AA4 4 VAL B 145 SER B 151 -1 O SER B 150 N SER B 130 SHEET 3 AA4 4 PHE B 181 GLY B 188 -1 O PHE B 185 N LEU B 147 SHEET 4 AA4 4 GLY B 174 PRO B 175 -1 N GLY B 174 O GLN B 182 SHEET 1 AA5 4 ARG B 169 PRO B 172 0 SHEET 2 AA5 4 MET B 157 ARG B 162 -1 N TYR B 158 O LEU B 171 SHEET 3 AA5 4 THR B 195 PHE B 202 -1 O PHE B 199 N HIS B 159 SHEET 4 AA5 4 SER B 205 TRP B 209 -1 O SER B 205 N PHE B 202 SHEET 1 AA6 4 ARG B 169 PRO B 172 0 SHEET 2 AA6 4 MET B 157 ARG B 162 -1 N TYR B 158 O LEU B 171 SHEET 3 AA6 4 THR B 195 PHE B 202 -1 O PHE B 199 N HIS B 159 SHEET 4 AA6 4 LEU B 216 LEU B 217 -1 O LEU B 216 N TYR B 196 SHEET 1 AA7 4 LEU C 4 SER C 7 0 SHEET 2 AA7 4 LEU C 18 ALA C 24 -1 O SER C 21 N SER C 7 SHEET 3 AA7 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AA7 4 PHE C 67 ASP C 72 -1 N SER C 70 O TYR C 79 SHEET 1 AA8 6 GLY C 10 VAL C 12 0 SHEET 2 AA8 6 THR C 113 VAL C 117 1 O THR C 116 N GLY C 10 SHEET 3 AA8 6 ALA C 91 GLU C 98 -1 N TYR C 93 O THR C 113 SHEET 4 AA8 6 THR C 33 GLN C 39 -1 N PHE C 37 O TYR C 94 SHEET 5 AA8 6 GLU C 46 ILE C 51 -1 O ALA C 49 N TRP C 36 SHEET 6 AA8 6 SER C 57 TYR C 59 -1 O THR C 58 N ALA C 50 SHEET 1 AA9 4 GLY C 10 VAL C 12 0 SHEET 2 AA9 4 THR C 113 VAL C 117 1 O THR C 116 N GLY C 10 SHEET 3 AA9 4 ALA C 91 GLU C 98 -1 N TYR C 93 O THR C 113 SHEET 4 AA9 4 TYR C 106 TRP C 109 -1 O TYR C 108 N ALA C 97 SSBOND 1 CYS A 65 CYS A 77 1555 1555 2.04 SSBOND 2 CYS B 49 CYS B 100 1555 1555 2.03 SSBOND 3 CYS B 149 CYS B 198 1555 1555 2.04 SSBOND 4 CYS C 22 CYS C 95 1555 1555 2.03 LINK ND2 ASN B 67 C1 NAG D 1 1555 1555 1.43 LINK ND2 ASN B 84 C1 NAG B 400 1555 1555 1.43 LINK O6 NAG D 1 C1 FUC D 2 1555 1555 1.43 CISPEP 1 HIS B 34 PRO B 35 0 -0.40 CRYST1 97.171 97.171 109.202 90.00 90.00 120.00 P 31 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 0.010291 0.005942 0.000000 0.00000 SCALE2 0.000000 0.011883 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009157 0.00000