HEADER SIGNALING PROTEIN 30-JUN-25 9PD2 TITLE CRYSTAL STRUCTURE OF PILRA IN COMPLEX WITH FAB PORTION OF ANTAGONIST TITLE 2 ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: PAIRED IMMUNOGLOBULIN-LIKE TYPE 2 RECEPTOR ALPHA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CELL SURFACE RECEPTOR FDF03,INHIBITORY RECEPTOR PILR-ALPHA; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ANTI-PILRA FAB HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: ANTI-PILRA FAB LIGHT CHAIN; COMPND 12 CHAIN: L; 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 GENE: PILRA; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; 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: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS RECEPTOR, COMPLEX, FAB, ANTIBODY, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.E.KUNG REVDAT 1 17-DEC-25 9PD2 0 JRNL AUTH T.N.WEERAKKODY,H.SABELSTROM,S.V.ANDREWS,J.P.CHADAREVIAN, JRNL AUTH 2 M.Y.CHIN,D.TATARAKIS,N.E.PROPSON,D.J.KIM,R.THEOLIS, JRNL AUTH 3 G.C.G.PARICO,H.MISKER,J.E.KUNG,A.BANDYOPADHYAY, JRNL AUTH 4 Y.ROBLES COLMENARES,T.N.JACKSON,A.N.QERQEZ,S.BALASUNDAR, JRNL AUTH 5 S.S.DAVIS,C.HA,R.GHOSH,R.RAVI,A.RANA,K.GERMAIN,A.TAO, JRNL AUTH 6 K.XIONG,D.BRAUN,K.RAJU,K.C.HUANG,L.ZHAN,J.L.GUO, JRNL AUTH 7 H.SAFARI YAZD,L.SARRAFHA,J.K.CAPOCCHI,J.HASSELMANN, JRNL AUTH 8 A.L.CHADAREVIAN,C.TU,K.MANSOUR,G.ESKANDARI-SEDIGHI,N.TESI, JRNL AUTH 9 S.VAN DER LEE,M.HULSMAN,G.OSHEGOV,Y.PIJNENBURG,M.CALVERT, JRNL AUTH10 H.HOLSTEGE,J.H.SUH,G.DI PAOLO,H.DAVTYAN,J.W.LEWCOCK, JRNL AUTH11 M.BLURTON-JONES,K.M.MONROE JRNL TITL LOSS OF PILRA PROMOTES MICROGLIAL IMMUNOMETABOLISM TO REDUCE JRNL TITL 2 AMYLOID PATHOLOGY IN CELL AND MOUSE MODELS OF ALZHEIMER'S JRNL TITL 3 DISEASE. JRNL REF SCI TRANSL MED V. 17 W7428 2025 JRNL REFN ESSN 1946-6242 JRNL PMID 41337541 JRNL DOI 10.1126/SCITRANSLMED.ADW7428 REMARK 2 REMARK 2 RESOLUTION. 2.58 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) : 2.58 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.35 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 91.4 REMARK 3 NUMBER OF REFLECTIONS : 18146 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) : 0.226 REMARK 3 FREE R VALUE : 0.277 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.894 REMARK 3 FREE R VALUE TEST SET COUNT : 888 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) : 2.58 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.65 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1104 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.3530 REMARK 3 BIN FREE R VALUE SET COUNT : 47 REMARK 3 BIN FREE R VALUE : 0.3960 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4313 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 27 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.52 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.14100 REMARK 3 B22 (A**2) : 1.46300 REMARK 3 B33 (A**2) : -0.32300 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.377 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.397 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.793 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4461 ; 0.006 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6075 ; 1.594 ; 1.814 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 559 ; 7.324 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 20 ;10.513 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 716 ;16.329 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 670 ; 0.098 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3444 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1583 ; 0.197 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2979 ; 0.304 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 188 ; 0.127 ; 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): 2236 ; 2.551 ; 3.253 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2795 ; 4.177 ; 5.837 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2225 ; 3.494 ; 3.474 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3280 ; 5.385 ; 6.261 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL 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 : 3 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 : Ap 21 Ap 150 REMARK 3 ORIGIN FOR THE GROUP (A): -17.4427 -9.9276 71.6973 REMARK 3 T TENSOR REMARK 3 T11: 0.0320 T22: 0.1354 REMARK 3 T33: 0.0279 T12: 0.0305 REMARK 3 T13: 0.0155 T23: 0.0426 REMARK 3 L TENSOR REMARK 3 L11: 3.7289 L22: 5.0713 REMARK 3 L33: 4.1840 L12: 1.2556 REMARK 3 L13: -0.0293 L23: -0.2188 REMARK 3 S TENSOR REMARK 3 S11: 0.0921 S12: -0.2875 S13: -0.0558 REMARK 3 S21: 0.1294 S22: -0.0467 S23: 0.2531 REMARK 3 S31: 0.2201 S32: -0.0906 S33: -0.0454 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): -5.9425 -2.8906 32.2314 REMARK 3 T TENSOR REMARK 3 T11: 0.0408 T22: 0.1387 REMARK 3 T33: 0.0875 T12: -0.0424 REMARK 3 T13: -0.0184 T23: 0.0108 REMARK 3 L TENSOR REMARK 3 L11: 1.0639 L22: 1.2518 REMARK 3 L33: 3.1301 L12: 0.5433 REMARK 3 L13: -1.0538 L23: -1.2743 REMARK 3 S TENSOR REMARK 3 S11: -0.1048 S12: 0.2586 S13: 0.0262 REMARK 3 S21: -0.1456 S22: -0.0007 S23: 0.0001 REMARK 3 S31: 0.1474 S32: -0.0197 S33: 0.1055 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): -1.5744 14.8856 37.2372 REMARK 3 T TENSOR REMARK 3 T11: 0.2763 T22: 0.3044 REMARK 3 T33: 0.2774 T12: -0.1335 REMARK 3 T13: -0.0250 T23: 0.0913 REMARK 3 L TENSOR REMARK 3 L11: 0.1105 L22: 0.4836 REMARK 3 L33: 4.4295 L12: 0.1466 REMARK 3 L13: -0.3067 L23: -1.2935 REMARK 3 S TENSOR REMARK 3 S11: -0.0143 S12: 0.1234 S13: 0.0907 REMARK 3 S21: 0.0711 S22: -0.0205 S23: 0.0109 REMARK 3 S31: -0.6962 S32: 0.3408 S33: 0.0348 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 NOT BEEN USED REMARK 4 REMARK 4 9PD2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1000297548. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-JUN-25 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 : SSRL REMARK 200 BEAMLINE : BL12-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18280 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.579 REMARK 200 RESOLUTION RANGE LOW (A) : 46.347 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3 REMARK 200 DATA REDUNDANCY : 2.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 8.16 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 46.30 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.6 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 (%): 45.81 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CAPS PH 10.5, 20% PEG 8000, 0.2 REMARK 280 M NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-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 18.92700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 167.52600 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.37650 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 167.52600 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.92700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.37650 REMARK 290 SMTRY3 4 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: 6050 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24880 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L 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 MET A 0 REMARK 465 HIS A 1 REMARK 465 HIS A 2 REMARK 465 HIS A 3 REMARK 465 HIS A 4 REMARK 465 HIS A 5 REMARK 465 HIS A 6 REMARK 465 HIS A 7 REMARK 465 HIS A 8 REMARK 465 GLY A 9 REMARK 465 LEU A 10 REMARK 465 ASN A 11 REMARK 465 ASP A 12 REMARK 465 ILE A 13 REMARK 465 PHE A 14 REMARK 465 GLU A 15 REMARK 465 ALA A 16 REMARK 465 GLN A 17 REMARK 465 LYS A 18 REMARK 465 ILE A 19 REMARK 465 GLU A 20 REMARK 465 SER H 132 REMARK 465 LYS H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 SER H 136 REMARK 465 LYS H 218 REMARK 465 SER H 219 REMARK 465 CYS H 220 REMARK 465 ASP H 221 REMARK 465 LYS H 222 REMARK 465 THR H 223 REMARK 465 HIS H 224 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO H 153 N - CA - CB ANGL. DEV. = -9.6 DEGREES REMARK 500 LEU L 154 CB - CG - CD2 ANGL. DEV. = 11.4 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 ARG H 67 -24.00 -142.25 REMARK 500 THR H 100 -77.77 -100.28 REMARK 500 PRO L 8 -175.58 -63.60 REMARK 500 ALA L 51 -34.87 73.95 REMARK 500 ALA L 84 -178.29 -177.50 REMARK 500 ASN L 138 86.52 25.05 REMARK 500 GLU L 143 31.59 -82.88 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 A 72 0.12 SIDE CHAIN REMARK 500 ARG A 126 0.12 SIDE CHAIN REMARK 500 ARG L 24 0.18 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9PD2 A 32 150 UNP Q9UKJ1 PILRA_HUMAN 32 150 DBREF 9PD2 H 1 224 PDB 9PD2 9PD2 1 224 DBREF 9PD2 L 1 214 PDB 9PD2 9PD2 1 214 SEQADV 9PD2 MET A 0 UNP Q9UKJ1 INITIATING METHIONINE SEQADV 9PD2 HIS A 1 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 HIS A 2 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 HIS A 3 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 HIS A 4 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 HIS A 5 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 HIS A 6 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 HIS A 7 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 HIS A 8 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 GLY A 9 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 LEU A 10 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 ASN A 11 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 ASP A 12 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 ILE A 13 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 PHE A 14 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 GLU A 15 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 ALA A 16 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 GLN A 17 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 LYS A 18 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 ILE A 19 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 GLU A 20 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 TRP A 21 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 HIS A 22 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 GLU A 23 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 LEU A 24 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 GLU A 25 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 VAL A 26 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 LEU A 27 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 PHE A 28 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 GLN A 29 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 GLY A 30 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 PRO A 31 UNP Q9UKJ1 EXPRESSION TAG SEQADV 9PD2 GLY A 78 UNP Q9UKJ1 ARG 78 VARIANT SEQRES 1 A 151 MET HIS HIS HIS HIS HIS HIS HIS HIS GLY LEU ASN ASP SEQRES 2 A 151 ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU LEU GLU SEQRES 3 A 151 VAL LEU PHE GLN GLY PRO LEU TYR GLY VAL THR GLN PRO SEQRES 4 A 151 LYS HIS LEU SER ALA SER MET GLY GLY SER VAL GLU ILE SEQRES 5 A 151 PRO PHE SER PHE TYR TYR PRO TRP GLU LEU ALA THR ALA SEQRES 6 A 151 PRO ASP VAL ARG ILE SER TRP ARG ARG GLY HIS PHE HIS SEQRES 7 A 151 GLY GLN SER PHE TYR SER THR ARG PRO PRO SER ILE HIS SEQRES 8 A 151 LYS ASP TYR VAL ASN ARG LEU PHE LEU ASN TRP THR GLU SEQRES 9 A 151 GLY GLN LYS SER GLY PHE LEU ARG ILE SER ASN LEU GLN SEQRES 10 A 151 LYS GLN ASP GLN SER VAL TYR PHE CYS ARG VAL GLU LEU SEQRES 11 A 151 ASP THR ARG SER SER GLY ARG GLN GLN TRP GLN SER ILE SEQRES 12 A 151 GLU GLY THR LYS LEU SER ILE THR SEQRES 1 H 225 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 225 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 225 TYR THR PHE THR GLU TYR TYR MET TYR TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY GLN GLY LEU GLU LEU ILE GLY ARG ILE ASP SEQRES 5 H 225 PRO GLU ASP GLY GLY THR ASP TYR ILE GLU LYS PHE LYS SEQRES 6 H 225 ASN ARG VAL THR LEU THR ALA ASP THR SER THR SER THR SEQRES 7 H 225 ALA TYR LEU GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA THR THR ILE ARG GLY THR VAL SEQRES 9 H 225 PHE ALA PHE TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 H 225 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 225 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 225 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 225 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 225 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 225 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 225 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 225 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 H 225 ASP LYS THR HIS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLU ASP ILE PHE ASN GLY LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS SER PRO LYS LEU LEU ILE TYR ASN ALA LYS SEQRES 5 L 214 THR LEU HIS THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY SER ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 L 214 TYR ASP TYR PRO LEU THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS FORMUL 4 HOH *27(H2 O) HELIX 1 AA1 TRP A 21 LEU A 24 5 4 HELIX 2 AA2 GLU A 25 GLY A 30 1 6 HELIX 3 AA3 LYS A 91 VAL A 94 5 4 HELIX 4 AA4 GLN A 116 GLN A 120 5 5 HELIX 5 AA5 THR H 28 TYR H 32 5 5 HELIX 6 AA6 ARG H 84 THR H 88 5 5 HELIX 7 AA7 SER H 160 ALA H 162 5 3 HELIX 8 AA8 SER H 191 LEU H 193 5 3 HELIX 9 AA9 GLN L 79 PHE L 83 5 5 HELIX 10 AB1 SER L 121 LYS L 126 1 6 HELIX 11 AB2 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 GLY A 34 THR A 36 0 SHEET 2 AA1 4 SER A 48 TYR A 56 -1 O SER A 54 N THR A 36 SHEET 3 AA1 4 SER A 107 SER A 113 -1 O LEU A 110 N ILE A 51 SHEET 4 AA1 4 LEU A 97 ASN A 100 -1 N PHE A 98 O ARG A 111 SHEET 1 AA2 6 HIS A 40 SER A 44 0 SHEET 2 AA2 6 THR A 145 THR A 150 1 O LYS A 146 N LEU A 41 SHEET 3 AA2 6 VAL A 122 THR A 131 -1 N TYR A 123 O THR A 145 SHEET 4 AA2 6 ASP A 66 ARG A 73 -1 N ARG A 68 O GLU A 128 SHEET 5 AA2 6 GLN A 79 SER A 83 -1 O PHE A 81 N TRP A 71 SHEET 6 AA2 6 SER A 88 ILE A 89 -1 O SER A 88 N SER A 83 SHEET 1 AA3 4 HIS A 40 SER A 44 0 SHEET 2 AA3 4 THR A 145 THR A 150 1 O LYS A 146 N LEU A 41 SHEET 3 AA3 4 VAL A 122 THR A 131 -1 N TYR A 123 O THR A 145 SHEET 4 AA3 4 SER A 134 GLN A 140 -1 O TRP A 139 N VAL A 127 SHEET 1 AA4 4 GLN H 3 GLN H 6 0 SHEET 2 AA4 4 VAL H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA4 4 THR H 78 LEU H 82A-1 O LEU H 81 N VAL H 20 SHEET 4 AA4 4 VAL H 68 ASP H 73 -1 N THR H 69 O GLU H 82 SHEET 1 AA5 6 GLU H 10 LYS H 12 0 SHEET 2 AA5 6 THR H 107 VAL H 111 1 O LEU H 108 N GLU H 10 SHEET 3 AA5 6 ALA H 89 THR H 96 -1 N TYR H 91 O THR H 107 SHEET 4 AA5 6 MET H 34 GLN H 40 -1 N VAL H 38 O TYR H 92 SHEET 5 AA5 6 LEU H 46 ILE H 52 -1 O ILE H 49 N TRP H 37 SHEET 6 AA5 6 THR H 58 TYR H 60 -1 O ASP H 59 N ARG H 51 SHEET 1 AA6 4 GLU H 10 LYS H 12 0 SHEET 2 AA6 4 THR H 107 VAL H 111 1 O LEU H 108 N GLU H 10 SHEET 3 AA6 4 ALA H 89 THR H 96 -1 N TYR H 91 O THR H 107 SHEET 4 AA6 4 PHE H 100B TRP H 103 -1 O ALA H 101 N THR H 95 SHEET 1 AA7 4 SER H 124 LEU H 128 0 SHEET 2 AA7 4 THR H 139 TYR H 149 -1 O LEU H 145 N PHE H 126 SHEET 3 AA7 4 TYR H 180 PRO H 189 -1 O TYR H 180 N TYR H 149 SHEET 4 AA7 4 VAL H 167 THR H 169 -1 N HIS H 168 O VAL H 185 SHEET 1 AA8 4 SER H 124 LEU H 128 0 SHEET 2 AA8 4 THR H 139 TYR H 149 -1 O LEU H 145 N PHE H 126 SHEET 3 AA8 4 TYR H 180 PRO H 189 -1 O TYR H 180 N TYR H 149 SHEET 4 AA8 4 VAL H 173 LEU H 174 -1 N VAL H 173 O SER H 181 SHEET 1 AA9 3 THR H 155 TRP H 158 0 SHEET 2 AA9 3 TYR H 198 HIS H 204 -1 O ASN H 201 N SER H 157 SHEET 3 AA9 3 THR H 209 VAL H 215 -1 O VAL H 215 N TYR H 198 SHEET 1 AB1 4 MET L 4 THR L 5 0 SHEET 2 AB1 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB1 4 ASP L 70 ILE L 75 -1 O TYR L 71 N CYS L 23 SHEET 4 AB1 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AB2 6 SER L 10 ALA L 13 0 SHEET 2 AB2 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AB2 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB2 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB2 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AB3 4 SER L 114 PHE L 118 0 SHEET 2 AB3 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AB3 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AB3 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB4 4 ALA L 153 LEU L 154 0 SHEET 2 AB4 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB4 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB4 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS H 22 CYS H 93 1555 1555 1.96 SSBOND 2 CYS H 144 CYS H 200 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.07 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.04 CISPEP 1 ARG A 85 PRO A 86 0 -8.99 CISPEP 2 PHE H 150 PRO H 151 0 -5.05 CISPEP 3 GLU H 152 PRO H 153 0 8.10 CISPEP 4 SER L 7 PRO L 8 0 -28.79 CISPEP 5 TYR L 94 PRO L 95 0 4.52 CISPEP 6 TYR L 140 PRO L 141 0 -0.07 CRYST1 37.854 46.753 335.052 90.00 90.00 90.00 P 21 21 21 4 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 0.026417 0.000000 0.000000 0.00000 SCALE2 0.000000 0.021389 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002985 0.00000