HEADER ALLERGEN/IMMUNE SYSTEM 18-JAN-24 8VQF TITLE X-RAY CRYSTAL STRUCTURE OF NATURAL CAN F 1 IN COMPLEX WITH HUMAN IGE TITLE 2 1J11 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGE 1J11 LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGE 1J11 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 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 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 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.KHATRI,A.BALL,C.M.RICHARDSON,S.A.SMITH,M.D.CHAMPAN,A.POMES, AUTHOR 2 M.CHRUSZCZ REVDAT 1 22-JAN-25 8VQF 0 JRNL AUTH K.KHATRI,A.BALL,S.A.SMITH,M.D.CHAMPAN,A.POMES,M.CHRUSZCZ JRNL TITL X-RAY CRYSTAL STRUCTURE OF NATURAL CAN F 1 IN COMPLEX WITH JRNL TITL 2 HUMAN IGE 1J11 FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.11 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0419 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) : 3.11 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.96 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 22377 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) : 0.248 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.211 REMARK 3 FREE R VALUE TEST SET COUNT : 1166 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) : 3.11 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1470 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.02 REMARK 3 BIN R VALUE (WORKING SET) : 0.4300 REMARK 3 BIN FREE R VALUE SET COUNT : 75 REMARK 3 BIN FREE R VALUE : 0.4330 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4324 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 88 REMARK 3 SOLVENT ATOMS : 3 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 182.0 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.54000 REMARK 3 B22 (A**2) : 1.54000 REMARK 3 B33 (A**2) : -4.99600 REMARK 3 B12 (A**2) : 0.77000 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): 0.877 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.388 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.407 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 58.527 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.911 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4504 ; 0.004 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 4050 ; 0.002 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6158 ; 0.938 ; 1.806 REMARK 3 BOND ANGLES OTHERS (DEGREES): 9357 ; 1.049 ; 1.730 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 576 ; 6.086 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 17 ; 2.430 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 671 ;10.581 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 714 ; 0.039 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5251 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 971 ; 0.012 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 813 ; 0.195 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 41 ; 0.231 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2196 ; 0.171 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 129 ; 0.130 ; 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): 2316 ; 4.665 ;13.382 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2316 ; 4.665 ;13.382 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2888 ; 7.937 ;24.050 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2889 ; 7.936 ;24.052 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2188 ; 7.133 ;14.398 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2141 ; 7.194 ;13.785 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3270 ;11.425 ;26.294 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3199 ;11.526 ;25.228 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 : 8 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 106 REMARK 3 ORIGIN FOR THE GROUP (A): -83.4224 22.6422 21.3494 REMARK 3 T TENSOR REMARK 3 T11: 0.9021 T22: 0.3381 REMARK 3 T33: 0.3968 T12: -0.1409 REMARK 3 T13: 0.0766 T23: 0.0357 REMARK 3 L TENSOR REMARK 3 L11: 6.1454 L22: 0.3364 REMARK 3 L33: 3.6343 L12: 1.3868 REMARK 3 L13: -0.5579 L23: 0.0498 REMARK 3 S TENSOR REMARK 3 S11: 0.0653 S12: -0.4067 S13: 0.2122 REMARK 3 S21: 0.0140 S22: -0.1100 S23: 0.1092 REMARK 3 S31: 0.2640 S32: 0.2773 S33: 0.0447 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 107 A 211 REMARK 3 ORIGIN FOR THE GROUP (A): -92.0177 -7.0565 15.9446 REMARK 3 T TENSOR REMARK 3 T11: 1.7678 T22: 0.0870 REMARK 3 T33: 0.0238 T12: -0.0591 REMARK 3 T13: 0.0700 T23: 0.0011 REMARK 3 L TENSOR REMARK 3 L11: 3.0126 L22: 6.7030 REMARK 3 L33: 1.1710 L12: -2.3241 REMARK 3 L13: -1.7260 L23: 1.2131 REMARK 3 S TENSOR REMARK 3 S11: 0.2702 S12: -0.0997 S13: 0.1329 REMARK 3 S21: 0.6708 S22: -0.2237 S23: 0.0332 REMARK 3 S31: 0.3518 S32: 0.0748 S33: -0.0465 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): -68.5839 19.0553 6.0688 REMARK 3 T TENSOR REMARK 3 T11: 0.9174 T22: 0.5544 REMARK 3 T33: 0.3001 T12: 0.0594 REMARK 3 T13: 0.1543 T23: 0.0535 REMARK 3 L TENSOR REMARK 3 L11: 1.9598 L22: 2.5653 REMARK 3 L33: 3.4058 L12: 1.3715 REMARK 3 L13: -1.8580 L23: 0.0860 REMARK 3 S TENSOR REMARK 3 S11: -0.3809 S12: -0.2071 S13: -0.0896 REMARK 3 S21: -0.3925 S22: 0.0567 S23: 0.1612 REMARK 3 S31: 0.3916 S32: 0.8400 S33: 0.3242 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): -94.6982 -8.4835 -0.4173 REMARK 3 T TENSOR REMARK 3 T11: 1.3453 T22: 0.1908 REMARK 3 T33: 0.1634 T12: 0.0659 REMARK 3 T13: 0.1117 T23: -0.1520 REMARK 3 L TENSOR REMARK 3 L11: 6.5325 L22: 2.2468 REMARK 3 L33: 4.8808 L12: 3.3456 REMARK 3 L13: 0.1580 L23: 1.5813 REMARK 3 S TENSOR REMARK 3 S11: 0.0933 S12: 0.0829 S13: -0.3622 REMARK 3 S21: 0.0379 S22: -0.1665 S23: -0.0758 REMARK 3 S31: -0.8358 S32: -0.4409 S33: 0.0732 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): -54.9861 43.0014 19.5259 REMARK 3 T TENSOR REMARK 3 T11: 0.4379 T22: 1.2039 REMARK 3 T33: 0.1976 T12: -0.3410 REMARK 3 T13: 0.1155 T23: 0.0139 REMARK 3 L TENSOR REMARK 3 L11: 4.3016 L22: 5.0920 REMARK 3 L33: 0.3553 L12: 4.6775 REMARK 3 L13: -1.0894 L23: -1.1749 REMARK 3 S TENSOR REMARK 3 S11: 0.0654 S12: -0.0426 S13: 0.3979 REMARK 3 S21: 0.0435 S22: 0.0101 S23: 0.4112 REMARK 3 S31: 0.0221 S32: 0.2448 S33: -0.0755 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): -52.1297 34.0867 18.9479 REMARK 3 T TENSOR REMARK 3 T11: 0.6210 T22: 0.8219 REMARK 3 T33: 0.3877 T12: -0.0870 REMARK 3 T13: 0.0424 T23: -0.0084 REMARK 3 L TENSOR REMARK 3 L11: 10.7860 L22: 0.3404 REMARK 3 L33: 4.2243 L12: 1.4578 REMARK 3 L13: -3.8639 L23: 0.0876 REMARK 3 S TENSOR REMARK 3 S11: -0.2521 S12: -0.2381 S13: -0.3785 REMARK 3 S21: 0.0537 S22: 0.1412 S23: -0.0004 REMARK 3 S31: 0.6048 S32: 0.6643 S33: 0.1109 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -54.0597 44.7288 23.5393 REMARK 3 T TENSOR REMARK 3 T11: 0.3297 T22: 0.8825 REMARK 3 T33: 0.3225 T12: -0.3770 REMARK 3 T13: 0.0067 T23: 0.0819 REMARK 3 L TENSOR REMARK 3 L11: 0.6948 L22: 3.0958 REMARK 3 L33: 6.2082 L12: 1.2847 REMARK 3 L13: -0.5723 L23: 0.9181 REMARK 3 S TENSOR REMARK 3 S11: 0.0165 S12: -0.0179 S13: 0.1490 REMARK 3 S21: 0.0035 S22: 0.0856 S23: 0.1813 REMARK 3 S31: -0.1024 S32: 0.3351 S33: -0.1021 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -47.1966 50.7313 16.2935 REMARK 3 T TENSOR REMARK 3 T11: 0.3724 T22: 0.9074 REMARK 3 T33: 0.2115 T12: -0.3083 REMARK 3 T13: 0.0242 T23: 0.1676 REMARK 3 L TENSOR REMARK 3 L11: 1.6806 L22: 7.4023 REMARK 3 L33: 4.5386 L12: 0.3703 REMARK 3 L13: 1.5837 L23: 1.2676 REMARK 3 S TENSOR REMARK 3 S11: -0.2672 S12: 0.3063 S13: 0.4693 REMARK 3 S21: -0.2771 S22: -0.1741 S23: 0.1158 REMARK 3 S31: -0.2721 S32: 0.7388 S33: 0.4413 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 8VQF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1000280681. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-OCT-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5-8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22392 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 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 (%) : 99.9 REMARK 200 DATA REDUNDANCY : 10.00 REMARK 200 R MERGE (I) : 0.16000 REMARK 200 R SYM (I) : 0.16000 REMARK 200 FOR THE DATA SET : 20.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 11.00 REMARK 200 R MERGE FOR SHELL (I) : 1.07900 REMARK 200 R SYM FOR SHELL (I) : 1.07900 REMARK 200 FOR SHELL : 2.100 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: PDB ENTRY 7MLH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 73.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 0.1 M TRIS, PH REMARK 280 8, VAPOR DIFFUSION, SITTING 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 29.80500 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 59.61000 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 59.61000 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 29.80500 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 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 CYS A 212 REMARK 465 SER A 213 REMARK 465 SER B 141 REMARK 465 LYS B 142 REMARK 465 SER B 143 REMARK 465 THR B 144 REMARK 465 SER B 145 REMARK 465 GLY B 146 REMARK 465 HIS B 230 REMARK 465 HIS B 231 REMARK 465 HIS B 232 REMARK 465 HIS B 233 REMARK 465 HIS B 234 REMARK 465 HIS B 235 REMARK 465 GLN C 1 REMARK 465 ASP C 2 REMARK 465 THR C 3 REMARK 465 PRO C 4 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 LYS A 27 CG CD CE NZ REMARK 470 GLU A 60 CG CD OE1 OE2 REMARK 470 LYS A 111 CG CD CE NZ REMARK 470 LYS A 164 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 GLN B 1 CG CD OE1 NE2 REMARK 470 LYS B 43 CG CD CE NZ REMARK 470 LYS B 76 CG CD CE NZ REMARK 470 LEU B 202 CG CD1 CD2 REMARK 470 LYS B 223 CG CD CE NZ REMARK 470 LYS B 227 CG CD CE NZ REMARK 470 GLN C 26 CG CD OE1 NE2 REMARK 470 LYS C 31 CG CD CE NZ REMARK 470 ASN C 57 CG OD1 ND2 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 GLU C 120 CG CD OE1 OE2 REMARK 470 ARG C 130 CG CD NE CZ NH1 NH2 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 -52.61 76.11 REMARK 500 ASN A 129 38.66 74.75 REMARK 500 VAL B 48 -62.36 -106.10 REMARK 500 ARG B 106 92.82 -166.80 REMARK 500 SER B 125 138.38 -172.01 REMARK 500 THR B 129 107.18 -48.91 REMARK 500 ASP B 157 67.86 68.60 REMARK 500 THR B 204 -63.79 -122.56 REMARK 500 ASN B 217 62.44 63.19 REMARK 500 MET C 22 84.52 -169.19 REMARK 500 GLN C 140 -156.20 -107.79 REMARK 500 REMARK 500 REMARK: NULL DBREF 8VQF A 2 213 PDB 8VQF 8VQF 2 213 DBREF 8VQF B 1 235 PDB 8VQF 8VQF 1 235 DBREF 8VQF C 1 156 UNP O18873 ALL1_CANLF 19 174 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 156 GLN ASP THR PRO ALA LEU GLY LYS ASP THR VAL ALA VAL SEQRES 2 C 156 SER GLY LYS TRP TYR LEU LYS ALA MET THR ALA ASP GLN SEQRES 3 C 156 GLU VAL PRO GLU LYS PRO ASP SER VAL THR PRO MET ILE SEQRES 4 C 156 LEU LYS ALA GLN LYS GLY GLY ASN LEU GLU ALA LYS ILE SEQRES 5 C 156 THR MET LEU THR ASN GLY GLN CYS GLN ASN ILE THR VAL SEQRES 6 C 156 VAL LEU HIS LYS THR SER GLU PRO GLY LYS TYR THR ALA SEQRES 7 C 156 TYR GLU GLY GLN ARG VAL VAL PHE ILE GLN PRO SER PRO SEQRES 8 C 156 VAL ARG ASP HIS TYR ILE LEU TYR CYS GLU GLY GLU LEU SEQRES 9 C 156 HIS GLY ARG GLN ILE ARG MET ALA LYS LEU LEU GLY ARG SEQRES 10 C 156 ASP PRO GLU GLN SER GLN GLU ALA LEU GLU ASP PHE ARG SEQRES 11 C 156 GLU PHE SER ARG ALA LYS GLY LEU ASN GLN GLU ILE LEU SEQRES 12 C 156 GLU LEU ALA GLN SER GLU THR CYS SER PRO GLY GLY GLN HET NAG A 301 14 HET SO4 A 302 5 HET SO4 A 303 5 HET SO4 A 304 5 HET SO4 A 305 5 HET SO4 A 306 5 HET SO4 B 301 5 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 NAG C 201 14 HET SO4 C 202 5 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 4 NAG 2(C8 H15 N O6) FORMUL 5 SO4 12(O4 S 2-) FORMUL 18 HOH *3(H2 O) HELIX 1 AA1 GLN A 79 GLU A 83 5 5 HELIX 2 AA2 SER A 122 ALA A 128 1 7 HELIX 3 AA3 THR A 182 SER A 188 1 7 HELIX 4 AA4 SER B 169 ALA B 171 5 3 HELIX 5 AA5 SER B 199 GLN B 205 1 7 HELIX 6 AA6 LYS B 214 ASN B 217 5 4 HELIX 7 AA7 GLY C 7 VAL C 13 1 7 HELIX 8 AA8 SER C 122 GLY C 137 1 16 SHEET 1 AA1 5 SER A 10 VAL A 13 0 SHEET 2 AA1 5 THR A 102 VAL A 106 1 O ARG A 103 N VAL A 11 SHEET 3 AA1 5 ALA A 84 ASP A 92 -1 N ALA A 84 O LEU A 104 SHEET 4 AA1 5 THR A 33 GLN A 38 -1 N TYR A 36 O TYR A 87 SHEET 5 AA1 5 VAL A 45 ILE A 48 -1 O ILE A 48 N TRP A 35 SHEET 1 AA2 4 SER A 10 VAL A 13 0 SHEET 2 AA2 4 THR A 102 VAL A 106 1 O ARG A 103 N VAL A 11 SHEET 3 AA2 4 ALA A 84 ASP A 92 -1 N ALA A 84 O LEU A 104 SHEET 4 AA2 4 THR A 95 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 LEU A 73 N ILE A 21 SHEET 3 AA3 3 PHE A 62 SER A 65 -1 N SER A 63 O THR A 74 SHEET 1 AA4 4 THR A 115 PHE A 119 0 SHEET 2 AA4 4 ALA A 131 PHE A 140 -1 O SER A 138 N THR A 115 SHEET 3 AA4 4 TYR A 173 LEU A 181 -1 O SER A 177 N CYS A 135 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 ALA A 131 PHE A 140 -1 O SER A 138 N THR A 115 SHEET 3 AA5 4 TYR A 173 LEU A 181 -1 O SER A 177 N CYS A 135 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 203 N VAL A 196 SHEET 1 AA7 4 LEU B 4 SER B 7 0 SHEET 2 AA7 4 ARG B 19 VAL B 24 -1 O ALA B 23 N VAL B 5 SHEET 3 AA7 4 THR B 78 MET B 83 -1 O LEU B 79 N CYS B 22 SHEET 4 AA7 4 PHE B 68 ASP B 73 -1 N SER B 71 O TYR B 80 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 TYR B 94 O THR B 120 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 LEU B 45 ILE B 51 -1 N LEU B 50 O HIS B 59 SHEET 3 AA9 5 TYR B 32 GLN B 39 -1 N TRP B 36 O ALA B 49 SHEET 4 AA9 5 ALA B 92 PHE B 103 -1 O VAL B 97 N HIS B 35 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 LEU B 154 N PHE B 135 SHEET 3 AB1 4 TYR B 189 PRO B 198 -1 O LEU B 191 N VAL B 155 SHEET 4 AB1 4 VAL B 176 THR B 178 -1 N HIS B 177 O VAL B 194 SHEET 1 AB2 3 THR B 164 TRP B 167 0 SHEET 2 AB2 3 ILE B 208 HIS B 213 -1 O ASN B 212 N THR B 164 SHEET 3 AB2 3 THR B 218 LYS B 223 -1 O VAL B 220 N VAL B 211 SHEET 1 AB311 ALA C 146 GLN C 147 0 SHEET 2 AB311 SER C 34 VAL C 35 1 N VAL C 35 O ALA C 146 SHEET 3 AB311 LEU C 48 THR C 56 -1 O LEU C 55 N SER C 34 SHEET 4 AB311 GLN C 59 LYS C 69 -1 O LEU C 67 N LEU C 48 SHEET 5 AB311 LYS C 75 ALA C 78 -1 O THR C 77 N HIS C 68 SHEET 6 AB311 ARG C 83 PRO C 89 -1 O VAL C 85 N TYR C 76 SHEET 7 AB311 HIS C 95 CYS C 100 -1 O ILE C 97 N GLN C 88 SHEET 8 AB311 MET C 111 GLY C 116 -1 O LEU C 115 N TYR C 96 SHEET 9 AB311 GLY C 15 ALA C 24 -1 N TYR C 18 O GLY C 116 SHEET 10 AB311 MET C 38 ALA C 42 -1 O MET C 38 N TRP C 17 SHEET 11 AB311 LEU C 48 THR C 56 -1 O GLU C 49 N LYS C 41 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.05 SSBOND 2 CYS A 135 CYS A 194 1555 1555 2.04 SSBOND 3 CYS B 22 CYS B 96 1555 1555 2.05 SSBOND 4 CYS B 153 CYS B 209 1555 1555 2.03 SSBOND 5 CYS C 60 CYS C 151 1555 1555 2.04 LINK ND2 ASN A 20 C1 NAG A 301 1555 1555 1.47 LINK ND2 ASN C 62 C1 NAG C 201 1555 1555 1.51 CISPEP 1 TYR A 141 PRO A 142 0 5.08 CRYST1 154.758 154.758 89.415 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 0.006462 0.003731 0.000000 0.00000 SCALE2 0.000000 0.007461 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011184 0.00000