HEADER ALLERGEN/IMMUNE SYSTEM 11-MAR-25 9NPH TITLE X-RAY CRYSTAL STRUCTURE OF RECOMBINANT CAN F 1 IN COMPLEX WITH HUMAN TITLE 2 IGE MAB 1J11 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 1J11 FAB LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 1J11 FAB HEAVY CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MAJOR ALLERGEN CAN F 1; COMPND 11 CHAIN: C; COMPND 12 SYNONYM: ALLERGEN DOG 1; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS; SOURCE 17 ORGANISM_COMMON: DOG; SOURCE 18 ORGANISM_TAXID: 9615; SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ALLERGEN-ANTIBODY COMPLEX, DOG ALLERGEN CAN F 1, ANTI CAN F 1 KEYWDS 2 ANTIBODY, HUMAN IGE BOUND TO CAN F 1, ALLERGEN-IMMUNE SYSTEM KEYWDS 3 COMPLEX, ALLERGEN EXPDTA X-RAY DIFFRACTION AUTHOR K.KHATRI,A.BALL,S.A.SMITH,M.D.CHAMPAN,A.POMES,M.CHRUSZCZ REVDAT 1 27-AUG-25 9NPH 0 JRNL AUTH K.KHATRI,A.BALL,J.GLESNER,C.LINN,L.D.VAILES,S.WUNSCHMANN, JRNL AUTH 2 S.A.GABEL,J.ZHANG,R.S.PEEBLES JR.,T.BOROWSKI,G.A.MUELLER, JRNL AUTH 3 M.D.CHAPMAN,S.A.SMITH,A.POMES,M.CHRUSZCZ JRNL TITL HUMAN IGE MONOCLONAL ANTIBODIES DEFINE TWO UNUSUAL EPITOPES JRNL TITL 2 TRAPPING DOG ALLERGEN CAN F 1 IN DIFFERENT CONFORMATIONS. JRNL REF PROTEIN SCI. V. 34 70269 2025 JRNL REFN ESSN 1469-896X JRNL PMID 40828364 JRNL DOI 10.1002/PRO.70269 REMARK 2 REMARK 2 RESOLUTION. 2.59 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0425 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.22 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 91.5 REMARK 3 NUMBER OF REFLECTIONS : 20507 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 1013 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.59 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1399 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.65 REMARK 3 BIN R VALUE (WORKING SET) : 0.2930 REMARK 3 BIN FREE R VALUE SET COUNT : 72 REMARK 3 BIN FREE R VALUE : 0.3550 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4373 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 109 REMARK 3 SOLVENT ATOMS : 60 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.96 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.17200 REMARK 3 B22 (A**2) : 0.17200 REMARK 3 B33 (A**2) : -0.55900 REMARK 3 B12 (A**2) : 0.08600 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 1.082 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.342 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.282 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.721 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4570 ; 0.009 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 4082 ; 0.002 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6246 ; 1.506 ; 1.804 REMARK 3 BOND ANGLES OTHERS (DEGREES): 9435 ; 0.953 ; 1.728 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 586 ; 7.577 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 16 ; 8.866 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 670 ;12.556 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 723 ; 0.071 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5310 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 978 ; 0.013 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 764 ; 0.221 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 87 ; 0.378 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2173 ; 0.178 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 142 ; 0.303 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2353 ; 3.532 ; 3.659 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2353 ; 3.532 ; 3.659 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2936 ; 5.708 ; 6.568 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2937 ; 5.707 ; 6.568 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2217 ; 4.542 ; 3.959 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2166 ; 4.212 ; 3.794 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3310 ; 6.907 ; 7.161 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3233 ; 6.473 ; 6.882 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 2 A 79 REMARK 3 ORIGIN FOR THE GROUP (A): 3.8920 -6.7590 -16.8850 REMARK 3 T TENSOR REMARK 3 T11: 0.1703 T22: 0.3703 REMARK 3 T33: 0.0311 T12: 0.1570 REMARK 3 T13: 0.0214 T23: 0.0000 REMARK 3 L TENSOR REMARK 3 L11: 1.5246 L22: 1.4562 REMARK 3 L33: 2.1068 L12: -0.9930 REMARK 3 L13: 0.0695 L23: 0.0449 REMARK 3 S TENSOR REMARK 3 S11: 0.1061 S12: 0.2031 S13: 0.0635 REMARK 3 S21: 0.0410 S22: -0.0234 S23: -0.1620 REMARK 3 S31: -0.0378 S32: 0.1665 S33: -0.0827 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 80 A 208 REMARK 3 ORIGIN FOR THE GROUP (A): -6.7850 -19.6230 -35.2050 REMARK 3 T TENSOR REMARK 3 T11: 0.2925 T22: 0.3915 REMARK 3 T33: 0.0534 T12: 0.2300 REMARK 3 T13: -0.1151 T23: -0.0661 REMARK 3 L TENSOR REMARK 3 L11: 0.7919 L22: 2.4278 REMARK 3 L33: 2.2873 L12: 1.1704 REMARK 3 L13: 0.1279 L23: 1.4335 REMARK 3 S TENSOR REMARK 3 S11: -0.2286 S12: 0.0307 S13: 0.1604 REMARK 3 S21: -0.3528 S22: 0.1509 S23: 0.2502 REMARK 3 S31: -0.1496 S32: 0.0580 S33: 0.0777 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -17.6170 0.4760 -15.1890 REMARK 3 T TENSOR REMARK 3 T11: 0.1465 T22: 0.3443 REMARK 3 T33: 0.0286 T12: 0.2036 REMARK 3 T13: -0.0255 T23: -0.0130 REMARK 3 L TENSOR REMARK 3 L11: 2.0952 L22: 2.1345 REMARK 3 L33: 1.0519 L12: -0.3702 REMARK 3 L13: 0.5664 L23: 1.0134 REMARK 3 S TENSOR REMARK 3 S11: 0.1607 S12: 0.1883 S13: -0.0422 REMARK 3 S21: -0.2114 S22: -0.1723 S23: 0.1606 REMARK 3 S31: -0.1157 S32: -0.1502 S33: 0.0115 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -19.3210 -34.1680 -39.7720 REMARK 3 T TENSOR REMARK 3 T11: 0.3208 T22: 0.4354 REMARK 3 T33: 0.2596 T12: 0.0428 REMARK 3 T13: 0.0476 T23: -0.1791 REMARK 3 L TENSOR REMARK 3 L11: 3.5474 L22: 0.8748 REMARK 3 L33: 0.9640 L12: -0.0622 REMARK 3 L13: -0.1927 L23: 0.2796 REMARK 3 S TENSOR REMARK 3 S11: -0.4063 S12: -0.3105 S13: -0.0092 REMARK 3 S21: 0.0890 S22: -0.0748 S23: 0.0727 REMARK 3 S31: 0.1885 S32: -0.4059 S33: 0.4811 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -5.8600 25.8150 -8.1650 REMARK 3 T TENSOR REMARK 3 T11: 0.1679 T22: 0.1959 REMARK 3 T33: 0.1754 T12: 0.1630 REMARK 3 T13: 0.0263 T23: 0.0408 REMARK 3 L TENSOR REMARK 3 L11: 2.1615 L22: 2.5750 REMARK 3 L33: 0.9250 L12: -1.1424 REMARK 3 L13: -0.4825 L23: 0.8924 REMARK 3 S TENSOR REMARK 3 S11: 0.1582 S12: 0.0062 S13: 0.4331 REMARK 3 S21: -0.0770 S22: -0.0391 S23: -0.2478 REMARK 3 S31: -0.1328 S32: -0.0838 S33: -0.1191 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -0.2840 29.2080 -2.6530 REMARK 3 T TENSOR REMARK 3 T11: 0.1658 T22: 0.2034 REMARK 3 T33: 0.1481 T12: 0.1220 REMARK 3 T13: 0.0279 T23: -0.0137 REMARK 3 L TENSOR REMARK 3 L11: 2.8563 L22: 3.0589 REMARK 3 L33: 3.7893 L12: 1.3755 REMARK 3 L13: -0.0158 L23: 0.3916 REMARK 3 S TENSOR REMARK 3 S11: 0.0231 S12: -0.1862 S13: 0.4909 REMARK 3 S21: 0.0423 S22: 0.0426 S23: -0.1284 REMARK 3 S31: -0.4901 S32: 0.1175 S33: -0.0656 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 9NPH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000293828. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-OCT-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20567 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.6 REMARK 200 DATA REDUNDANCY : 9.900 REMARK 200 R MERGE (I) : 0.12200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2 REMARK 200 DATA REDUNDANCY IN SHELL : 9.60 REMARK 200 R MERGE FOR SHELL (I) : 0.66000 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE MONOHYDRATE, 0.1 REMARK 280 M HEPES , 25% W/V PEG 3,350, PH 7.5, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K 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 82.34667 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 164.69333 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 164.69333 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 82.34667 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7530 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27420 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -155.0 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 213 REMARK 465 HIS B 235 REMARK 465 SER C 152 REMARK 465 PRO C 153 REMARK 465 GLY C 154 REMARK 465 GLY C 155 REMARK 465 GLN C 156 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 SER A 2 OG REMARK 470 GLN A 127 CG CD OE1 NE2 REMARK 470 LYS A 157 CG CD CE NZ REMARK 470 LYS A 167 CG CD CE NZ REMARK 470 LYS A 187 CG CD CE NZ REMARK 470 ARG A 190 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 211 CG CD OE1 OE2 REMARK 470 LYS B 43 CG CD CE NZ REMARK 470 LYS B 142 CG CD CE NZ REMARK 470 SER B 143 OG REMARK 470 THR B 144 OG1 CG2 REMARK 470 LYS B 223 CG CD CE NZ REMARK 470 LYS B 227 CG CD CE NZ REMARK 470 SER B 228 OG REMARK 470 HIS B 230 CG ND1 CD2 CE1 NE2 REMARK 470 HIS B 232 CG ND1 CD2 CE1 NE2 REMARK 470 HIS B 234 CG ND1 CD2 CE1 NE2 REMARK 470 GLN C 26 CG CD OE1 NE2 REMARK 470 GLU C 30 CG CD OE1 OE2 REMARK 470 LYS C 31 CG CD CE NZ REMARK 470 LYS C 69 CG CD CE NZ REMARK 470 GLU C 103 CG CD OE1 OE2 REMARK 470 LEU C 104 CG CD1 CD2 REMARK 470 HIS C 105 CG ND1 CD2 CE1 NE2 REMARK 470 ARG C 107 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 130 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 134 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 136 CG CD CE NZ REMARK 470 GLU C 141 CG CD OE1 OE2 REMARK 470 ILE C 142 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 ASP A 51 -49.29 69.67 REMARK 500 ASP A 92 -96.86 -98.11 REMARK 500 SER A 94 8.85 57.37 REMARK 500 ASP A 152 -9.84 65.85 REMARK 500 PRO A 155 161.07 -48.52 REMARK 500 ASN A 170 4.70 -65.23 REMARK 500 ALA B 92 168.92 177.78 REMARK 500 ARG B 106 114.45 -166.88 REMARK 500 PHE B 159 133.04 -173.78 REMARK 500 HIS B 231 -128.35 -115.36 REMARK 500 HIS B 233 -93.68 -113.88 REMARK 500 GLN C 26 -143.79 -119.88 REMARK 500 LEU C 104 -71.14 -108.72 REMARK 500 HIS C 105 59.82 -142.34 REMARK 500 GLU C 141 68.44 -100.56 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG B 106 0.07 SIDE CHAIN REMARK 500 ARG C 83 0.08 SIDE CHAIN REMARK 500 ARG C 93 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8VQF RELATED DB: PDB REMARK 900 RELATED ID: 8VQG RELATED DB: PDB DBREF 9NPH A 2 213 PDB 9NPH 9NPH 2 213 DBREF 9NPH B 1 235 PDB 9NPH 9NPH 1 235 DBREF 9NPH C 9 156 UNP O18873 ALL1_CANLF 27 174 SEQADV 9NPH GLY C 8 UNP O18873 EXPRESSION TAG SEQADV 9NPH SER C 100 UNP O18873 CYS 118 ENGINEERED MUTATION SEQRES 1 A 212 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 A 212 PRO GLY GLN THR ALA ASN ILE THR CYS SER GLY ASP LYS SEQRES 3 A 212 LEU GLY ASP LYS PHE THR SER TRP TYR GLN GLN ARG PRO SEQRES 4 A 212 GLY GLN SER PRO VAL LEU VAL ILE TYR GLN ASP ILE GLU SEQRES 5 A 212 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SEQRES 6 A 212 SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN SEQRES 7 A 212 ALA LEU ASP GLU ALA ASP TYR TYR CYS GLN ALA TRP ASP SEQRES 8 A 212 THR SER THR VAL VAL PHE GLY GLY GLY THR ARG LEU THR SEQRES 9 A 212 VAL LEU GLY GLN PRO LYS ALA ASN PRO THR VAL THR LEU SEQRES 10 A 212 PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA SEQRES 11 A 212 THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA SEQRES 12 A 212 VAL THR VAL ALA TRP LYS ALA ASP GLY SER PRO VAL LYS SEQRES 13 A 212 ALA GLY VAL GLU THR THR LYS PRO SER LYS GLN SER ASN SEQRES 14 A 212 ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO SEQRES 15 A 212 GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL SEQRES 16 A 212 THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO SEQRES 17 A 212 THR GLU CYS SER SEQRES 1 B 235 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 B 235 PRO GLY SER SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 B 235 PHE THR VAL ARG SER TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 B 235 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA LEU ILE LEU SEQRES 5 B 235 PHE ASP GLY THR THR LYS HIS TYR ALA ASP SER VAL LYS SEQRES 6 B 235 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASP THR SEQRES 7 B 235 LEU TYR LEU GLN MET THR SER LEU GLY ALA GLU ASP THR SEQRES 8 B 235 ALA MET TYR TYR CYS VAL ARG ASP PHE ASN GLN PHE VAL SEQRES 9 B 235 LYS ARG PHE VAL ASP GLY PRO ALA PHE ASP LEU TRP GLY SEQRES 10 B 235 GLN GLY THR ARG VAL THR VAL SER SER ALA SER THR LYS SEQRES 11 B 235 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 B 235 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 B 235 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 B 235 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 B 235 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 B 235 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 B 235 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 B 235 LYS LYS VAL GLU PRO LYS SER CYS HIS HIS HIS HIS HIS SEQRES 19 B 235 HIS SEQRES 1 C 149 GLY ASP THR VAL ALA VAL SER GLY LYS TRP TYR LEU LYS SEQRES 2 C 149 ALA MET THR ALA ASP GLN GLU VAL PRO GLU LYS PRO ASP SEQRES 3 C 149 SER VAL THR PRO MET ILE LEU LYS ALA GLN LYS GLY GLY SEQRES 4 C 149 ASN LEU GLU ALA LYS ILE THR MET LEU THR ASN GLY GLN SEQRES 5 C 149 CYS GLN ASN ILE THR VAL VAL LEU HIS LYS THR SER GLU SEQRES 6 C 149 PRO GLY LYS TYR THR ALA TYR GLU GLY GLN ARG VAL VAL SEQRES 7 C 149 PHE ILE GLN PRO SER PRO VAL ARG ASP HIS TYR ILE LEU SEQRES 8 C 149 TYR SER GLU GLY GLU LEU HIS GLY ARG GLN ILE ARG MET SEQRES 9 C 149 ALA LYS LEU LEU GLY ARG ASP PRO GLU GLN SER GLN GLU SEQRES 10 C 149 ALA LEU GLU ASP PHE ARG GLU PHE SER ARG ALA LYS GLY SEQRES 11 C 149 LEU ASN GLN GLU ILE LEU GLU LEU ALA GLN SER GLU THR SEQRES 12 C 149 CYS SER PRO GLY GLY GLN HET NAG A 301 14 HET EPE A 302 15 HET SO4 A 303 5 HET SO4 A 304 5 HET SO4 A 305 5 HET SO4 A 306 5 HET SO4 A 307 5 HET SO4 A 308 5 HET EPE B 301 15 HET SO4 B 302 5 HET SO4 B 303 5 HET SO4 B 304 5 HET SO4 B 305 5 HET SO4 B 306 5 HET SO4 B 307 5 HET SO4 C 201 5 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETNAM SO4 SULFATE ION 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 EPE HEPES FORMUL 4 NAG C8 H15 N O6 FORMUL 5 EPE 2(C8 H18 N2 O4 S) FORMUL 6 SO4 13(O4 S 2-) FORMUL 20 HOH *60(H2 O) HELIX 1 AA1 LYS A 27 LYS A 31 5 5 HELIX 2 AA2 GLN A 79 GLU A 83 5 5 HELIX 3 AA3 SER A 122 ALA A 128 1 7 HELIX 4 AA4 THR A 182 HIS A 189 1 8 HELIX 5 AA5 THR B 28 ARG B 30 5 3 HELIX 6 AA6 ASN B 74 LYS B 76 5 3 HELIX 7 AA7 GLY B 87 THR B 91 5 5 HELIX 8 AA8 SER B 200 THR B 204 5 5 HELIX 9 AA9 LYS B 214 ASN B 217 5 4 HELIX 10 AB1 SER C 122 LYS C 136 1 15 SHEET 1 AA1 5 SER A 10 VAL A 13 0 SHEET 2 AA1 5 THR A 102 VAL A 106 1 O THR A 105 N VAL A 11 SHEET 3 AA1 5 ALA A 84 TRP A 91 -1 N TYR A 86 O THR A 102 SHEET 4 AA1 5 SER A 34 GLN A 38 -1 N GLN A 38 O ASP A 85 SHEET 5 AA1 5 VAL A 45 ILE A 48 -1 O VAL A 45 N GLN A 37 SHEET 1 AA2 4 SER A 10 VAL A 13 0 SHEET 2 AA2 4 THR A 102 VAL A 106 1 O THR A 105 N VAL A 11 SHEET 3 AA2 4 ALA A 84 TRP A 91 -1 N TYR A 86 O THR A 102 SHEET 4 AA2 4 VAL A 96 PHE A 98 -1 O VAL A 97 N ALA A 90 SHEET 1 AA3 3 ALA A 19 SER A 24 0 SHEET 2 AA3 3 THR A 70 ILE A 75 -1 O ILE A 75 N ALA A 19 SHEET 3 AA3 3 PHE A 62 SER A 67 -1 N SER A 67 O THR A 70 SHEET 1 AA4 4 THR A 115 PHE A 119 0 SHEET 2 AA4 4 THR A 132 PHE A 140 -1 O VAL A 134 N PHE A 119 SHEET 3 AA4 4 TYR A 173 SER A 180 -1 O TYR A 173 N PHE A 140 SHEET 4 AA4 4 VAL A 160 THR A 162 -1 N GLU A 161 O TYR A 178 SHEET 1 AA5 4 THR A 115 PHE A 119 0 SHEET 2 AA5 4 THR A 132 PHE A 140 -1 O VAL A 134 N PHE A 119 SHEET 3 AA5 4 TYR A 173 SER A 180 -1 O TYR A 173 N PHE A 140 SHEET 4 AA5 4 SER A 166 LYS A 167 -1 N SER A 166 O ALA A 174 SHEET 1 AA6 4 SER A 154 VAL A 156 0 SHEET 2 AA6 4 THR A 146 ALA A 151 -1 N ALA A 151 O SER A 154 SHEET 3 AA6 4 TYR A 192 HIS A 198 -1 O GLN A 195 N ALA A 148 SHEET 4 AA6 4 SER A 201 VAL A 207 -1 O VAL A 207 N TYR A 192 SHEET 1 AA7 4 GLN B 3 SER B 7 0 SHEET 2 AA7 4 LEU B 18 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 3 AA7 4 THR B 78 MET B 83 -1 O LEU B 81 N LEU B 20 SHEET 4 AA7 4 PHE B 68 ASP B 73 -1 N ASP B 73 O THR B 78 SHEET 1 AA8 4 GLY B 10 VAL B 12 0 SHEET 2 AA8 4 THR B 120 VAL B 124 1 O THR B 123 N VAL B 12 SHEET 3 AA8 4 ALA B 92 PHE B 103 -1 N ALA B 92 O VAL B 122 SHEET 4 AA8 4 ARG B 106 PHE B 107 -1 O ARG B 106 N PHE B 103 SHEET 1 AA9 5 LYS B 58 TYR B 60 0 SHEET 2 AA9 5 GLU B 46 ILE B 51 -1 N LEU B 50 O HIS B 59 SHEET 3 AA9 5 TYR B 32 GLN B 39 -1 N ARG B 38 O GLU B 46 SHEET 4 AA9 5 ALA B 92 PHE B 103 -1 O TYR B 95 N VAL B 37 SHEET 5 AA9 5 PHE B 113 TRP B 116 -1 O LEU B 115 N ARG B 98 SHEET 1 AB1 4 SER B 133 LEU B 137 0 SHEET 2 AB1 4 THR B 148 TYR B 158 -1 O LYS B 156 N SER B 133 SHEET 3 AB1 4 TYR B 189 PRO B 198 -1 O VAL B 197 N ALA B 149 SHEET 4 AB1 4 VAL B 176 THR B 178 -1 N HIS B 177 O VAL B 194 SHEET 1 AB2 4 SER B 133 LEU B 137 0 SHEET 2 AB2 4 THR B 148 TYR B 158 -1 O LYS B 156 N SER B 133 SHEET 3 AB2 4 TYR B 189 PRO B 198 -1 O VAL B 197 N ALA B 149 SHEET 4 AB2 4 VAL B 182 LEU B 183 -1 N VAL B 182 O SER B 190 SHEET 1 AB3 3 THR B 164 TRP B 167 0 SHEET 2 AB3 3 TYR B 207 HIS B 213 -1 O ASN B 210 N SER B 166 SHEET 3 AB3 3 THR B 218 VAL B 224 -1 O VAL B 224 N TYR B 207 SHEET 1 AB4 6 LEU C 143 GLU C 144 0 SHEET 2 AB4 6 GLY C 15 ALA C 24 -1 N MET C 22 O LEU C 143 SHEET 3 AB4 6 MET C 38 ALA C 42 -1 O MET C 38 N TRP C 17 SHEET 4 AB4 6 LEU C 48 THR C 56 -1 O LYS C 51 N ILE C 39 SHEET 5 AB4 6 SER C 34 VAL C 35 -1 N SER C 34 O LEU C 55 SHEET 6 AB4 6 ALA C 146 GLN C 147 1 O ALA C 146 N VAL C 35 SHEET 1 AB510 LEU C 143 GLU C 144 0 SHEET 2 AB510 GLY C 15 ALA C 24 -1 N MET C 22 O LEU C 143 SHEET 3 AB510 MET C 111 GLY C 116 -1 O GLY C 116 N TYR C 18 SHEET 4 AB510 HIS C 95 GLY C 102 -1 N TYR C 96 O LEU C 115 SHEET 5 AB510 ARG C 83 PRO C 89 -1 N PHE C 86 O TYR C 99 SHEET 6 AB510 LYS C 75 ALA C 78 -1 N TYR C 76 O VAL C 85 SHEET 7 AB510 GLN C 59 LYS C 69 -1 N HIS C 68 O THR C 77 SHEET 8 AB510 LEU C 48 THR C 56 -1 N LEU C 48 O LEU C 67 SHEET 9 AB510 SER C 34 VAL C 35 -1 N SER C 34 O LEU C 55 SHEET 10 AB510 ALA C 146 GLN C 147 1 O ALA C 146 N VAL C 35 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.04 SSBOND 2 CYS A 135 CYS A 194 1555 1555 1.92 SSBOND 3 CYS A 212 CYS B 229 1555 1555 2.04 SSBOND 4 CYS B 22 CYS B 96 1555 1555 2.02 SSBOND 5 CYS B 153 CYS B 209 1555 1555 1.96 SSBOND 6 CYS C 60 CYS C 151 1555 1555 2.04 LINK ND2 ASN A 20 C1 NAG A 301 1555 1555 1.46 CISPEP 1 TYR A 141 PRO A 142 0 2.32 CISPEP 2 PHE B 159 PRO B 160 0 -13.85 CISPEP 3 GLU B 161 PRO B 162 0 10.82 CRYST1 69.511 69.511 247.040 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 0.014386 0.008306 0.000000 0.00000 SCALE2 0.000000 0.016612 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004048 0.00000