HEADER IMMUNE SYSTEM 04-AUG-25 9PWN TITLE CRYSTAL STRUCTURE OF FABS 7411 IN COMPLEX WITH TREM2 PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: 7411 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 7411 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: TREM-2 STALK PEPTIDE; COMPND 11 CHAIN: A; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606 KEYWDS FAB, ANTIBODY, COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.W.ARNDT,Q.CHAO,H.A.COOKE,A.D.S.ALMEIDA REVDAT 1 10-SEP-25 9PWN 0 JRNL AUTH A.DA SILVA ALMEIDA,M.L.GEDDIE,A.BHATE,C.QUAN,J.W.ARNDT, JRNL AUTH 2 Y.JIAO,J.C.SANTORO,L.NOIMAN,R.VIJAYAKUMAR,J.SANCHEZ-SALAZAR, JRNL AUTH 3 A.DATTA,G.ANTOGNETTI,C.A.HARTANA,X.F.WANG,B.A.SMITH, JRNL AUTH 4 D.BARTLETT,D.DUNCAN,C.C.LIU,K.OTERO GUTIERREZ,T.O.CAMERON, JRNL AUTH 5 S.KOIRALA,H.A.COOKE JRNL TITL BUILDING A POTENT TREM2 AGONISTIC, BIPARATOPIC, COMMON LIGHT JRNL TITL 2 CHAIN ANTIBODY. JRNL REF MABS V. 17 46554 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 40803893 JRNL DOI 10.1080/19420862.2025.2546554 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0430 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.96 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2 REMARK 3 NUMBER OF REFLECTIONS : 33550 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.180 REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.218 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1766 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) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2515 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.11 REMARK 3 BIN R VALUE (WORKING SET) : 0.2740 REMARK 3 BIN FREE R VALUE SET COUNT : 132 REMARK 3 BIN FREE R VALUE : 0.2640 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3352 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 81 REMARK 3 SOLVENT ATOMS : 178 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.69 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.80000 REMARK 3 B22 (A**2) : -0.11000 REMARK 3 B33 (A**2) : -0.69000 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): 0.144 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.133 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.736 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3518 ; 0.005 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 3191 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4779 ; 1.299 ; 1.791 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7398 ; 0.454 ; 1.729 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 447 ; 7.558 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 13 ; 5.963 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 544 ;12.346 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 542 ; 0.069 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4042 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 764 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL 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): 1791 ; 2.157 ; 2.136 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1791 ; 2.153 ; 2.135 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2237 ; 3.053 ; 3.822 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2238 ; 3.052 ; 3.822 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1727 ; 3.372 ; 2.506 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1728 ; 3.371 ; 2.508 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2543 ; 4.933 ; 4.415 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3697 ; 6.794 ;24.490 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3667 ; 6.762 ;24.000 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 : H 1 H 221 REMARK 3 ORIGIN FOR THE GROUP (A): -8.5179 -39.6306 4.6768 REMARK 3 T TENSOR REMARK 3 T11: 0.0353 T22: 0.0208 REMARK 3 T33: 0.0787 T12: -0.0228 REMARK 3 T13: 0.0100 T23: -0.0230 REMARK 3 L TENSOR REMARK 3 L11: 2.0143 L22: 1.6656 REMARK 3 L33: 0.2888 L12: 1.1676 REMARK 3 L13: -0.4141 L23: -0.1853 REMARK 3 S TENSOR REMARK 3 S11: 0.0976 S12: -0.1386 S13: 0.1973 REMARK 3 S21: 0.0798 S22: -0.0417 S23: -0.0824 REMARK 3 S31: -0.0956 S32: 0.0747 S33: -0.0559 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 : L 1 L 212 REMARK 3 ORIGIN FOR THE GROUP (A): -16.0926 -26.8592 15.7602 REMARK 3 T TENSOR REMARK 3 T11: 0.0846 T22: 0.0350 REMARK 3 T33: 0.1121 T12: -0.0164 REMARK 3 T13: 0.0368 T23: -0.0268 REMARK 3 L TENSOR REMARK 3 L11: 0.7992 L22: 2.1678 REMARK 3 L33: 0.0092 L12: 1.3034 REMARK 3 L13: 0.0800 L23: 0.1281 REMARK 3 S TENSOR REMARK 3 S11: 0.0679 S12: -0.0638 S13: 0.0396 REMARK 3 S21: 0.0684 S22: -0.0827 S23: 0.0001 REMARK 3 S31: 0.0017 S32: -0.0067 S33: 0.0148 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 131 A 147 REMARK 3 ORIGIN FOR THE GROUP (A): -29.6557 -59.6755 14.6694 REMARK 3 T TENSOR REMARK 3 T11: 0.1050 T22: 0.0870 REMARK 3 T33: 0.0295 T12: 0.0285 REMARK 3 T13: -0.0170 T23: 0.0041 REMARK 3 L TENSOR REMARK 3 L11: 11.0170 L22: 4.8827 REMARK 3 L33: 7.0958 L12: 0.9843 REMARK 3 L13: 1.4595 L23: -0.6727 REMARK 3 S TENSOR REMARK 3 S11: -0.0204 S12: -0.7630 S13: -0.2733 REMARK 3 S21: 0.4298 S22: 0.0267 S23: -0.3084 REMARK 3 S31: 0.5079 S32: 0.2565 S33: -0.0063 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK 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 THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 9PWN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1000298621. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-DEC-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000070 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 : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 174028 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 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 (%) : 99.8 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.5200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7 REMARK 200 DATA REDUNDANCY IN SHELL : 2.70 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 11% W/V PEG 8000, 240 MM AMMONIUM REMARK 280 SULFATE, 100 MM MES, PH 6, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K 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 25.82500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.76500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.88000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.76500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.82500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.88000 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: 7980 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19390 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, 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 H 137 REMARK 465 LYS H 138 REMARK 465 SER H 139 REMARK 465 THR H 140 REMARK 465 SER H 141 REMARK 465 GLU A 148 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 GLU H 1 CG CD OE1 OE2 REMARK 470 LYS L 169 CG CD CE NZ REMARK 470 ARG A 136 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 ALA H 92 162.49 179.74 REMARK 500 VAL H 105 -49.90 -135.26 REMARK 500 SER L 30 -124.93 52.06 REMARK 500 ALA L 51 -36.73 78.79 REMARK 500 SER L 52 -19.85 -141.20 REMARK 500 SER L 77 75.05 37.12 REMARK 500 ALA L 84 179.06 179.05 REMARK 500 ASN L 152 -8.77 77.19 REMARK 500 REMARK 500 REMARK: NULL DBREF 9PWN H 1 221 PDB 9PWN 9PWN 1 221 DBREF 9PWN L 1 212 PDB 9PWN 9PWN 1 212 DBREF 9PWN A 131 148 UNP Q9NZC2 TREM2_HUMAN 131 148 SEQRES 1 H 221 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 221 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 221 PHE THR PHE SER GLU ARG ALA MET THR TRP VAL ARG GLN SEQRES 4 H 221 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5 H 221 GLY SER GLY VAL LYS THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 221 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 221 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 221 ALA VAL TYR TYR CYS ALA LYS THR PRO SER PRO LYS TYR SEQRES 9 H 221 VAL GLY SER VAL PHE ASP LEU TRP GLY ARG GLY THR LEU SEQRES 10 H 221 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 221 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 221 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 221 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 221 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 221 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 221 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 221 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 1 L 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 212 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 212 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 212 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 212 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 212 TYR SER THR PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 L 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 212 PHE ASN ARG GLY SEQRES 1 A 18 ASP PRO LEU ASP HIS ARG ASP ALA GLY ASP LEU TRP PHE SEQRES 2 A 18 PRO GLY GLU SER GLU HET PEG H 301 7 HET GOL H 302 6 HET GOL H 303 6 HET GOL H 304 6 HET SO4 H 305 5 HET SO4 H 306 5 HET SO4 H 307 5 HET SO4 H 308 5 HET SO4 H 309 5 HET EDO H 310 4 HET SO4 L 301 5 HET SO4 L 302 5 HET SO4 L 303 5 HET EDO L 304 4 HET EDO L 305 4 HET EDO L 306 4 HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETNAM EDO 1,2-ETHANEDIOL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 4 PEG C4 H10 O3 FORMUL 5 GOL 3(C3 H8 O3) FORMUL 8 SO4 8(O4 S 2-) FORMUL 13 EDO 4(C2 H6 O2) FORMUL 20 HOH *178(H2 O) HELIX 1 AA1 THR H 28 ARG H 32 5 5 HELIX 2 AA2 ASN H 74 LYS H 76 5 3 HELIX 3 AA3 ARG H 87 THR H 91 5 5 HELIX 4 AA4 SER H 165 ALA H 167 5 3 HELIX 5 AA5 SER H 196 LEU H 198 5 3 HELIX 6 AA6 LYS H 210 ASN H 213 5 4 HELIX 7 AA7 GLN L 79 PHE L 83 5 5 HELIX 8 AA8 SER L 121 SER L 127 1 7 HELIX 9 AA9 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA1 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA1 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AA2 6 ALA H 92 THR H 99 -1 N TYR H 94 O THR H 116 SHEET 4 AA2 6 ALA H 33 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O TYR H 59 N SER H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AA3 4 ALA H 92 THR H 99 -1 N TYR H 94 O THR H 116 SHEET 4 AA3 4 LEU H 111 TRP H 112 -1 O LEU H 111 N LYS H 98 SHEET 1 AA4 4 SER H 129 LEU H 133 0 SHEET 2 AA4 4 THR H 144 TYR H 154 -1 O GLY H 148 N LEU H 133 SHEET 3 AA4 4 TYR H 185 PRO H 194 -1 O VAL H 191 N LEU H 147 SHEET 4 AA4 4 VAL H 172 THR H 174 -1 N HIS H 173 O VAL H 190 SHEET 1 AA5 4 SER H 129 LEU H 133 0 SHEET 2 AA5 4 THR H 144 TYR H 154 -1 O GLY H 148 N LEU H 133 SHEET 3 AA5 4 TYR H 185 PRO H 194 -1 O VAL H 191 N LEU H 147 SHEET 4 AA5 4 VAL H 178 LEU H 179 -1 N VAL H 178 O SER H 186 SHEET 1 AA6 3 THR H 160 TRP H 163 0 SHEET 2 AA6 3 TYR H 203 HIS H 209 -1 O ASN H 208 N THR H 160 SHEET 3 AA6 3 THR H 214 GLU H 221 -1 O VAL H 220 N TYR H 203 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA8 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N ASN L 34 O GLN L 89 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 ALA L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA9 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 HIS L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.10 SSBOND 2 CYS H 149 CYS H 205 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.10 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.02 CISPEP 1 PHE H 155 PRO H 156 0 -9.99 CISPEP 2 GLU H 157 PRO H 158 0 -2.23 CISPEP 3 SER L 7 PRO L 8 0 -6.86 CISPEP 4 THR L 94 PRO L 95 0 -6.14 CISPEP 5 TYR L 140 PRO L 141 0 5.03 CRYST1 51.650 71.760 105.530 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 0.019361 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013935 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009476 0.00000