HEADER ALLERGEN/IMMUNE SYSTEM 11-MAR-25 9NPI TITLE X-RAY CRYSTAL STRUCTURE OF RECOMBINANT CAN F 1 IN COMPLEX WITH HUMAN TITLE 2 IGE 12F3 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HUMAN IGE 12F3 HEAVY CHAIN; COMPND 3 CHAIN: C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HUMAN IGE 12F3 LIGHT 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: A; COMPND 12 SYNONYM: ALLERGEN DOG 1; COMPND 13 ENGINEERED: 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, CAN F 1 ANTIBODY, KEYWDS 2 IGE-CAN F 1 COMPLEX, ALLERGEN-ANTIBODY, ALLERGEN, ALLERGEN-IMMUNE KEYWDS 3 SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.KHATRI,A.BALL,S.A.SMITH,M.D.CHAMPAN,A.POMES,M.CHRUSZCZ REVDAT 1 27-AUG-25 9NPI 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. 1.85 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) : 1.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.13 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 3 NUMBER OF REFLECTIONS : 50932 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) : 0.179 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840 REMARK 3 FREE R VALUE TEST SET COUNT : 2465 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) : 1.85 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3359 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.16 REMARK 3 BIN R VALUE (WORKING SET) : 0.2530 REMARK 3 BIN FREE R VALUE SET COUNT : 169 REMARK 3 BIN FREE R VALUE : 0.2710 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4293 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 1 REMARK 3 SOLVENT ATOMS : 694 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.28 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.16000 REMARK 3 B22 (A**2) : 1.02000 REMARK 3 B33 (A**2) : -0.97900 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.51700 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.143 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.137 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.105 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.895 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4419 ; 0.008 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 4091 ; 0.002 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6020 ; 1.405 ; 1.814 REMARK 3 BOND ANGLES OTHERS (DEGREES): 9465 ; 0.762 ; 1.736 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 575 ; 7.089 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 20 ; 9.826 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 711 ;11.472 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 692 ; 0.068 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5194 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 974 ; 0.008 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 689 ; 0.197 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 45 ; 0.199 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2124 ; 0.172 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 489 ; 0.200 ; 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): 2285 ; 1.459 ; 1.667 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2285 ; 1.459 ; 1.667 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2850 ; 2.312 ; 2.974 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2851 ; 2.312 ; 2.975 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2134 ; 1.979 ; 1.863 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2135 ; 1.978 ; 1.864 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3165 ; 3.116 ; 3.311 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3166 ; 3.116 ; 3.312 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 : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -8.8618 -2.7959 35.3814 REMARK 3 T TENSOR REMARK 3 T11: 0.0289 T22: 0.1133 REMARK 3 T33: 0.0678 T12: 0.0121 REMARK 3 T13: 0.0160 T23: 0.0146 REMARK 3 L TENSOR REMARK 3 L11: 4.1810 L22: 2.0680 REMARK 3 L33: 1.2389 L12: -0.3798 REMARK 3 L13: 0.1008 L23: -0.0306 REMARK 3 S TENSOR REMARK 3 S11: 0.0173 S12: -0.2454 S13: -0.0611 REMARK 3 S21: 0.0054 S22: 0.0850 S23: 0.3419 REMARK 3 S31: -0.1674 S32: -0.2031 S33: -0.1023 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 0.3370 -4.1935 41.8540 REMARK 3 T TENSOR REMARK 3 T11: 0.0442 T22: 0.1262 REMARK 3 T33: 0.0109 T12: -0.0190 REMARK 3 T13: 0.0056 T23: 0.0094 REMARK 3 L TENSOR REMARK 3 L11: 3.1141 L22: 2.5063 REMARK 3 L33: 2.6823 L12: -0.0373 REMARK 3 L13: -0.3184 L23: -0.9798 REMARK 3 S TENSOR REMARK 3 S11: 0.0497 S12: -0.5355 S13: -0.0940 REMARK 3 S21: 0.1212 S22: 0.0070 S23: 0.0983 REMARK 3 S31: -0.0896 S32: -0.1112 S33: -0.0567 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): 11.6059 -3.2043 6.9648 REMARK 3 T TENSOR REMARK 3 T11: 0.0504 T22: 0.0254 REMARK 3 T33: 0.0512 T12: 0.0155 REMARK 3 T13: -0.0204 T23: -0.0076 REMARK 3 L TENSOR REMARK 3 L11: 0.4208 L22: 0.1772 REMARK 3 L33: 0.5360 L12: 0.1155 REMARK 3 L13: -0.0790 L23: 0.0395 REMARK 3 S TENSOR REMARK 3 S11: 0.0032 S12: -0.0072 S13: 0.0140 REMARK 3 S21: 0.0313 S22: 0.0048 S23: 0.0388 REMARK 3 S31: 0.0303 S32: -0.0895 S33: -0.0080 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): 35.1982 -6.8431 -12.6113 REMARK 3 T TENSOR REMARK 3 T11: 0.0610 T22: 0.0414 REMARK 3 T33: 0.0599 T12: 0.0171 REMARK 3 T13: -0.0149 T23: -0.0316 REMARK 3 L TENSOR REMARK 3 L11: 2.5883 L22: 0.6905 REMARK 3 L33: 0.8062 L12: 0.5563 REMARK 3 L13: 0.5914 L23: 0.3363 REMARK 3 S TENSOR REMARK 3 S11: -0.0544 S12: 0.2079 S13: -0.3210 REMARK 3 S21: 0.0150 S22: 0.1178 S23: -0.1216 REMARK 3 S31: 0.0879 S32: 0.1296 S33: -0.0634 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 1 C 118 REMARK 3 ORIGIN FOR THE GROUP (A): 23.7804 4.4329 23.2261 REMARK 3 T TENSOR REMARK 3 T11: 0.1027 T22: 0.0643 REMARK 3 T33: 0.0571 T12: -0.0031 REMARK 3 T13: -0.0251 T23: 0.0139 REMARK 3 L TENSOR REMARK 3 L11: 1.8437 L22: 0.7405 REMARK 3 L33: 1.5725 L12: 0.7033 REMARK 3 L13: 0.0578 L23: -0.7144 REMARK 3 S TENSOR REMARK 3 S11: 0.0796 S12: -0.0517 S13: 0.0365 REMARK 3 S21: 0.1488 S22: -0.1447 S23: -0.0614 REMARK 3 S31: -0.0908 S32: 0.1679 S33: 0.0651 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 119 C 224 REMARK 3 ORIGIN FOR THE GROUP (A): 35.1460 10.1333 -10.9426 REMARK 3 T TENSOR REMARK 3 T11: 0.0592 T22: 0.0076 REMARK 3 T33: 0.0442 T12: -0.0077 REMARK 3 T13: -0.0277 T23: -0.0033 REMARK 3 L TENSOR REMARK 3 L11: 1.1076 L22: 0.9239 REMARK 3 L33: 2.0654 L12: 0.3830 REMARK 3 L13: 0.0669 L23: -0.1944 REMARK 3 S TENSOR REMARK 3 S11: -0.0381 S12: 0.0319 S13: 0.0032 REMARK 3 S21: -0.1217 S22: 0.0460 S23: 0.0529 REMARK 3 S31: -0.0651 S32: 0.0323 S33: -0.0079 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 9NPI 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_1000293838. 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 : 6.5 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 : 50951 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850 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 (%) : 98.8 REMARK 200 DATA REDUNDANCY : 7.100 REMARK 200 R MERGE (I) : 0.10600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.1100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7 REMARK 200 DATA REDUNDANCY IN SHELL : 6.80 REMARK 200 R MERGE FOR SHELL (I) : 0.55000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 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 (%): 47.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM CHLORIDE, 20% W/V PEG REMARK 280 3,350, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.97500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6000 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25630 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, B, A 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 C 139 REMARK 465 THR C 140 REMARK 465 CYS C 225 REMARK 465 CYS B 215 REMARK 465 GLN A 1 REMARK 465 ASP A 2 REMARK 465 THR A 3 REMARK 465 PRO A 4 REMARK 465 ALA A 5 REMARK 465 LEU A 6 REMARK 465 GLY A 7 REMARK 465 LYS A 8 REMARK 465 ASP A 9 REMARK 465 THR A 10 REMARK 465 VAL A 28 REMARK 465 PRO A 29 REMARK 465 GLU A 30 REMARK 465 GLY A 102 REMARK 465 GLU A 103 REMARK 465 LEU A 104 REMARK 465 HIS A 105 REMARK 465 GLY A 106 REMARK 465 ARG A 107 REMARK 465 GLN A 108 REMARK 465 GLY A 154 REMARK 465 GLY A 155 REMARK 465 GLN A 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 C 138 CG CD CE NZ REMARK 470 LYS B 170 CG CD CE NZ REMARK 470 GLU B 214 CG CD OE1 OE2 REMARK 470 GLU A 27 CG CD OE1 OE2 REMARK 470 LYS A 31 CG CD CE NZ REMARK 470 LYS A 44 CG CD CE NZ REMARK 470 LYS A 69 CG CD CE NZ REMARK 470 GLU A 80 CG CD OE1 OE2 REMARK 470 ARG A 83 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 109 CG1 CG2 CD1 REMARK 470 GLU A 141 CG CD OE1 OE2 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 C 43 -163.45 -112.30 REMARK 500 ASP C 153 53.86 71.32 REMARK 500 LEU B 13 -157.82 -140.95 REMARK 500 SER B 30 -122.84 53.95 REMARK 500 SER B 30 -125.57 58.16 REMARK 500 ALA B 51 -35.16 74.34 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 C 31 0.10 SIDE CHAIN REMARK 500 ARG B 54 0.14 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C 588 DISTANCE = 5.81 ANGSTROMS REMARK 525 HOH C 589 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH C 590 DISTANCE = 6.57 ANGSTROMS REMARK 525 HOH C 591 DISTANCE = 10.26 ANGSTROMS REMARK 525 HOH B 742 DISTANCE = 6.09 ANGSTROMS REMARK 525 HOH B 743 DISTANCE = 6.66 ANGSTROMS REMARK 525 HOH B 744 DISTANCE = 7.77 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8VQF RELATED DB: PDB REMARK 900 RELATED ID: 8VQG RELATED DB: PDB DBREF 9NPI C 1 225 PDB 9NPI 9NPI 1 225 DBREF 9NPI B 1 215 PDB 9NPI 9NPI 1 215 DBREF 9NPI A 1 156 UNP O18873 ALL1_CANLF 19 174 SEQRES 1 C 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL GLN LYS SEQRES 2 C 225 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 C 225 GLY THR PHE SER ARG TYR PRO LEU ILE TRP VAL ARG GLN SEQRES 4 C 225 THR PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE PHE SEQRES 5 C 225 PRO VAL ILE GLY ARG THR ASN TYR ALA GLU LYS PHE GLN SEQRES 6 C 225 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 C 225 ALA TYR MET GLU LEU ASN SER LEU THR SER GLU ASP THR SEQRES 8 C 225 ALA VAL TYR TYR CYS ALA ARG LEU ASP THR TYR GLU ILE SEQRES 9 C 225 LEU GLY TYR GLY THR ASP VAL TRP GLY GLN GLY THR THR SEQRES 10 C 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 C 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 C 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 C 225 PRO LYS SER CYS SEQRES 1 B 215 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 B 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 B 215 GLU SER VAL SER SER SER VAL ALA TRP TYR GLN GLN LYS SEQRES 4 B 215 PHE GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 B 215 ASN ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 B 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 215 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN LEU ARG SEQRES 8 B 215 SER ASN TRP PRO PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 B 215 VAL GLN ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 156 GLN ASP THR PRO ALA LEU GLY LYS ASP THR VAL ALA VAL SEQRES 2 A 156 SER GLY LYS TRP TYR LEU LYS ALA MET THR ALA ASP GLN SEQRES 3 A 156 GLU VAL PRO GLU LYS PRO ASP SER VAL THR PRO MET ILE SEQRES 4 A 156 LEU LYS ALA GLN LYS GLY GLY ASN LEU GLU ALA LYS ILE SEQRES 5 A 156 THR MET LEU THR ASN GLY GLN CYS GLN ASN ILE THR VAL SEQRES 6 A 156 VAL LEU HIS LYS THR SER GLU PRO GLY LYS TYR THR ALA SEQRES 7 A 156 TYR GLU GLY GLN ARG VAL VAL PHE ILE GLN PRO SER PRO SEQRES 8 A 156 VAL ARG ASP HIS TYR ILE LEU TYR CYS GLU GLY GLU LEU SEQRES 9 A 156 HIS GLY ARG GLN ILE ARG MET ALA LYS LEU LEU GLY ARG SEQRES 10 A 156 ASP PRO GLU GLN SER GLN GLU ALA LEU GLU ASP PHE ARG SEQRES 11 A 156 GLU PHE SER ARG ALA LYS GLY LEU ASN GLN GLU ILE LEU SEQRES 12 A 156 GLU LEU ALA GLN SER GLU THR CYS SER PRO GLY GLY GLN HET CL B 301 1 HETNAM CL CHLORIDE ION FORMUL 4 CL CL 1- FORMUL 5 HOH *694(H2 O) HELIX 1 AA1 GLU C 62 GLN C 65 5 4 HELIX 2 AA2 GLU C 74 THR C 76 5 3 HELIX 3 AA3 THR C 87 THR C 91 5 5 HELIX 4 AA4 SER C 165 ALA C 167 5 3 HELIX 5 AA5 SER C 196 LEU C 198 5 3 HELIX 6 AA6 LYS C 210 ASN C 213 5 4 HELIX 7 AA7 GLU B 79 PHE B 83 5 5 HELIX 8 AA8 SER B 122 SER B 128 1 7 HELIX 9 AA9 LYS B 184 GLU B 188 1 5 HELIX 10 AB1 SER A 122 LYS A 136 1 15 SHEET 1 AA1 4 GLN C 3 GLN C 6 0 SHEET 2 AA1 4 VAL C 18 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AA1 4 THR C 78 LEU C 83 -1 O MET C 81 N VAL C 20 SHEET 4 AA1 4 VAL C 68 ASP C 73 -1 N ASP C 73 O THR C 78 SHEET 1 AA2 6 GLU C 10 GLN C 12 0 SHEET 2 AA2 6 THR C 116 VAL C 120 1 O THR C 117 N GLU C 10 SHEET 3 AA2 6 ALA C 92 ARG C 98 -1 N ALA C 92 O VAL C 118 SHEET 4 AA2 6 LEU C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AA2 6 LEU C 45 PHE C 52 -1 O MET C 48 N TRP C 36 SHEET 6 AA2 6 ARG C 57 TYR C 60 -1 O ASN C 59 N GLY C 50 SHEET 1 AA3 4 GLU C 10 GLN C 12 0 SHEET 2 AA3 4 THR C 116 VAL C 120 1 O THR C 117 N GLU C 10 SHEET 3 AA3 4 ALA C 92 ARG C 98 -1 N ALA C 92 O VAL C 118 SHEET 4 AA3 4 VAL C 111 TRP C 112 -1 O VAL C 111 N ARG C 98 SHEET 1 AA4 4 SER C 129 LEU C 133 0 SHEET 2 AA4 4 THR C 144 TYR C 154 -1 O GLY C 148 N LEU C 133 SHEET 3 AA4 4 TYR C 185 PRO C 194 -1 O LEU C 187 N VAL C 151 SHEET 4 AA4 4 VAL C 172 THR C 174 -1 N HIS C 173 O VAL C 190 SHEET 1 AA5 4 SER C 129 LEU C 133 0 SHEET 2 AA5 4 THR C 144 TYR C 154 -1 O GLY C 148 N LEU C 133 SHEET 3 AA5 4 TYR C 185 PRO C 194 -1 O LEU C 187 N VAL C 151 SHEET 4 AA5 4 VAL C 178 LEU C 179 -1 N VAL C 178 O SER C 186 SHEET 1 AA6 3 THR C 160 TRP C 163 0 SHEET 2 AA6 3 ILE C 204 HIS C 209 -1 O ASN C 206 N SER C 162 SHEET 3 AA6 3 THR C 214 LYS C 219 -1 O VAL C 216 N VAL C 207 SHEET 1 AA7 4 LEU B 4 THR B 5 0 SHEET 2 AA7 4 ALA B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA7 4 ASP B 70 ILE B 75 -1 O LEU B 73 N LEU B 21 SHEET 4 AA7 4 PHE B 62 SER B 65 -1 N SER B 63 O THR B 74 SHEET 1 AA8 6 THR B 10 LEU B 13 0 SHEET 2 AA8 6 THR B 103 ILE B 107 1 O LYS B 104 N LEU B 11 SHEET 3 AA8 6 ALA B 84 LEU B 90 -1 N ALA B 84 O VAL B 105 SHEET 4 AA8 6 VAL B 33 GLN B 38 -1 N ALA B 34 O GLN B 89 SHEET 5 AA8 6 ARG B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA8 6 ASN B 53 ARG B 54 -1 O ASN B 53 N TYR B 49 SHEET 1 AA9 4 SER B 115 PHE B 119 0 SHEET 2 AA9 4 THR B 130 PHE B 140 -1 O LEU B 136 N PHE B 117 SHEET 3 AA9 4 TYR B 174 SER B 183 -1 O LEU B 182 N ALA B 131 SHEET 4 AA9 4 SER B 160 VAL B 164 -1 N SER B 163 O SER B 177 SHEET 1 AB1 4 ALA B 154 LEU B 155 0 SHEET 2 AB1 4 LYS B 146 VAL B 151 -1 N VAL B 151 O ALA B 154 SHEET 3 AB1 4 VAL B 192 THR B 198 -1 O GLU B 196 N GLN B 148 SHEET 4 AB1 4 VAL B 206 ASN B 211 -1 O VAL B 206 N VAL B 197 SHEET 1 AB2 5 SER A 34 VAL A 35 0 SHEET 2 AB2 5 LEU A 48 THR A 56 -1 O LEU A 55 N SER A 34 SHEET 3 AB2 5 MET A 38 ALA A 42 -1 N LYS A 41 O GLU A 49 SHEET 4 AB2 5 VAL A 13 ALA A 24 -1 N GLY A 15 O LEU A 40 SHEET 5 AB2 5 LEU A 143 GLU A 144 -1 O LEU A 143 N MET A 22 SHEET 1 AB3 9 SER A 34 VAL A 35 0 SHEET 2 AB3 9 LEU A 48 THR A 56 -1 O LEU A 55 N SER A 34 SHEET 3 AB3 9 GLN A 59 LYS A 69 -1 O LEU A 67 N LEU A 48 SHEET 4 AB3 9 LYS A 75 ALA A 78 -1 O THR A 77 N HIS A 68 SHEET 5 AB3 9 ARG A 83 PRO A 89 -1 O VAL A 85 N TYR A 76 SHEET 6 AB3 9 HIS A 95 GLU A 101 -1 O TYR A 99 N PHE A 86 SHEET 7 AB3 9 MET A 111 GLY A 116 -1 O LEU A 115 N TYR A 96 SHEET 8 AB3 9 VAL A 13 ALA A 24 -1 N LYS A 20 O LEU A 114 SHEET 9 AB3 9 LEU A 143 GLU A 144 -1 O LEU A 143 N MET A 22 SSBOND 1 CYS C 22 CYS C 96 1555 1555 2.09 SSBOND 2 CYS C 149 CYS C 205 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.14 SSBOND 4 CYS B 135 CYS B 195 1555 1555 2.02 SSBOND 5 CYS A 60 CYS A 151 1555 1555 2.21 CISPEP 1 PHE C 155 PRO C 156 0 -10.48 CISPEP 2 GLU C 157 PRO C 158 0 -7.08 CISPEP 3 SER B 7 PRO B 8 0 -6.89 CISPEP 4 PRO B 95 PRO B 96 0 -5.32 CISPEP 5 TYR B 141 PRO B 142 0 1.99 CRYST1 54.528 73.950 77.275 90.00 99.59 90.00 P 1 21 1 2 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 0.018339 0.000000 0.003098 0.00000 SCALE2 0.000000 0.013523 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013124 0.00000