HEADER SIGNALING PROTEIN 16-OCT-14 4WOL
TITLE CRYSTAL STRUCTURE OF THE DAP12 TRANSMEMBRANE DOMAIN IN LIPIDIC CUBIC
TITLE 2 PHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYRO PROTEIN TYROSINE KINASE-BINDING PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 35-67;
COMPND 5 SYNONYM: DNAX-ACTIVATION PROTEIN 12,KILLER-ACTIVATING RECEPTOR-
COMPND 6 ASSOCIATED PROTEIN,KAR-ASSOCIATED PROTEIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TYROBP, DAP12, KARAP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-HELIX TRANSMEMBRANE SIGNALLING, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.CALL,M.E.CALL,K.KNOBLICH
REVDAT 5 01-JAN-20 4WOL 1 REMARK
REVDAT 4 27-SEP-17 4WOL 1 REMARK
REVDAT 3 23-AUG-17 4WOL 1 SOURCE REMARK
REVDAT 2 10-JUN-15 4WOL 1 JRNL
REVDAT 1 03-JUN-15 4WOL 0
JRNL AUTH K.KNOBLICH,S.PARK,M.LUTFI,L.VAN 'T HAG,C.E.CONN,
JRNL AUTH 2 S.A.SEABROOK,J.NEWMAN,P.E.CZABOTAR,W.IM,M.E.CALL,M.J.CALL
JRNL TITL TRANSMEMBRANE COMPLEXES OF DAP12 CRYSTALLIZED IN LIPID
JRNL TITL 2 MEMBRANES PROVIDE INSIGHTS INTO CONTROL OF OLIGOMERIZATION
JRNL TITL 3 IN IMMUNORECEPTOR ASSEMBLY.
JRNL REF CELL REP V. 11 1184 2015
JRNL REFN ESSN 2211-1247
JRNL PMID 25981043
JRNL DOI 10.1016/J.CELREP.2015.04.045
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 7407
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.980
REMARK 3 FREE R VALUE TEST SET COUNT : 739
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.6754 - 3.0262 0.99 1485 165 0.1536 0.1947
REMARK 3 2 3.0262 - 2.4022 1.00 1425 159 0.1693 0.1948
REMARK 3 3 2.4022 - 2.0986 0.93 1279 139 0.2140 0.2808
REMARK 3 4 2.0986 - 1.9067 0.85 1176 132 0.2358 0.2809
REMARK 3 5 1.9067 - 1.7701 0.95 1303 144 0.2700 0.2922
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 767
REMARK 3 ANGLE : 0.900 1020
REMARK 3 CHIRALITY : 0.036 137
REMARK 3 PLANARITY : 0.005 116
REMARK 3 DIHEDRAL : 15.543 286
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 8 THROUGH 12 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8012 16.9746 74.1459
REMARK 3 T TENSOR
REMARK 3 T11: 0.7887 T22: 0.3292
REMARK 3 T33: 0.3409 T12: 0.0881
REMARK 3 T13: 0.0482 T23: 0.1679
REMARK 3 L TENSOR
REMARK 3 L11: 3.6750 L22: 0.8727
REMARK 3 L33: 5.9069 L12: 1.7911
REMARK 3 L13: -3.7754 L23: -1.8145
REMARK 3 S TENSOR
REMARK 3 S11: -0.0229 S12: -0.5975 S13: -0.4615
REMARK 3 S21: 0.6136 S22: 0.0802 S23: 0.3953
REMARK 3 S31: 0.3558 S32: -0.1844 S33: -0.0206
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 13 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7472 15.2826 47.8214
REMARK 3 T TENSOR
REMARK 3 T11: 0.1041 T22: 0.1180
REMARK 3 T33: 0.1688 T12: -0.0020
REMARK 3 T13: 0.0118 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.4393 L22: 1.7564
REMARK 3 L33: 2.0622 L12: 0.4689
REMARK 3 L13: 0.7566 L23: 0.2437
REMARK 3 S TENSOR
REMARK 3 S11: 0.0103 S12: 0.0514 S13: -0.0146
REMARK 3 S21: -0.0425 S22: 0.1625 S23: 0.0022
REMARK 3 S31: -0.1109 S32: 0.0688 S33: -0.1313
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 8 THROUGH 12 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9653 14.7514 73.4573
REMARK 3 T TENSOR
REMARK 3 T11: 0.8917 T22: 0.5477
REMARK 3 T33: 0.2049 T12: -0.0299
REMARK 3 T13: 0.1164 T23: 0.0646
REMARK 3 L TENSOR
REMARK 3 L11: 4.5094 L22: 1.1861
REMARK 3 L33: 1.3785 L12: -2.2663
REMARK 3 L13: -0.5302 L23: 0.0175
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: -0.0486 S13: 0.5139
REMARK 3 S21: 0.1868 S22: 0.0849 S23: -0.0742
REMARK 3 S31: -1.4806 S32: 0.6782 S33: -0.0981
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 13 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2183 13.8699 50.6473
REMARK 3 T TENSOR
REMARK 3 T11: 0.1094 T22: 0.0924
REMARK 3 T33: 0.1586 T12: -0.0114
REMARK 3 T13: -0.0050 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.6745 L22: 1.4941
REMARK 3 L33: 1.3710 L12: -0.4683
REMARK 3 L13: -0.2720 L23: -0.4562
REMARK 3 S TENSOR
REMARK 3 S11: 0.0023 S12: 0.0838 S13: -0.0506
REMARK 3 S21: -0.0039 S22: 0.0227 S23: 0.0806
REMARK 3 S31: -0.0255 S32: 0.0802 S33: -0.0682
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 11 THROUGH 12 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2678 21.5596 71.0064
REMARK 3 T TENSOR
REMARK 3 T11: 0.6023 T22: 0.7444
REMARK 3 T33: 0.2599 T12: -0.0076
REMARK 3 T13: -0.2603 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 6.2906 L22: 2.0000
REMARK 3 L33: 2.0001 L12: -1.7888
REMARK 3 L13: 4.0289 L23: 4.3900
REMARK 3 S TENSOR
REMARK 3 S11: 0.0392 S12: 0.2268 S13: -0.0872
REMARK 3 S21: 0.0068 S22: 0.1398 S23: -0.3946
REMARK 3 S31: 0.5900 S32: 0.8605 S33: -0.1797
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 13 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5569 22.9906 49.4170
REMARK 3 T TENSOR
REMARK 3 T11: 0.1446 T22: 0.1320
REMARK 3 T33: 0.1506 T12: 0.0140
REMARK 3 T13: -0.0048 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 1.7908 L22: 0.9924
REMARK 3 L33: 3.8438 L12: 0.1416
REMARK 3 L13: -1.7868 L23: 0.6198
REMARK 3 S TENSOR
REMARK 3 S11: 0.1251 S12: -0.0540 S13: 0.1857
REMARK 3 S21: -0.0462 S22: 0.1723 S23: -0.0151
REMARK 3 S31: -0.3615 S32: 0.0516 S33: -0.2439
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4WOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000204176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-14
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7502
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 33.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : 0.13570
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <I/SIGMA(I)> 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: NULL
REMARK 200 STARTING MODEL: 1AFO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.4% W/V PEG 3350, 0.149 M POTASSIUM
REMARK 280 THIOCYANATE, LIPIDIC CUBIC PHASE, 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 10.38750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.53500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 17.85450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.53500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 10.38750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 17.85450
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER B 9
REMARK 465 THR B 10
REMARK 465 CYS C 8
REMARK 465 SER C 9
REMARK 465 THR C 10
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 CYS B 8 N CA C O CB
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 101 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 23 OD1
REMARK 620 2 ASP A 23 OD2 45.0
REMARK 620 3 THR A 27 OG1 80.3 85.4
REMARK 620 4 ASP B 23 OD1 94.0 65.2 141.5
REMARK 620 5 THR B 27 OG1 144.1 99.3 96.6 66.3
REMARK 620 6 ASP C 23 OD2 66.5 94.6 130.6 78.6 131.7
REMARK 620 7 THR C 27 OG1 113.1 158.0 92.6 124.1 102.7 70.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC C 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC C 103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WO1 RELATED DB: PDB
REMARK 900 4WO1 IS TETRAMERIC FORM
REMARK 900 RELATED ID: 2L34 RELATED DB: PDB
REMARK 900 2L34 WAS SOLVED BY NMR
REMARK 900 RELATED ID: 2L35 RELATED DB: PDB
REMARK 900 2L35 WAS SOLVED BY NMR
DBREF 4WOL A 8 40 UNP O43914 TYOBP_HUMAN 35 67
DBREF 4WOL B 8 40 UNP O43914 TYOBP_HUMAN 35 67
DBREF 4WOL C 8 40 UNP O43914 TYOBP_HUMAN 35 67
SEQADV 4WOL VAL A 21 UNP O43914 MET 48 ENGINEERED MUTATION
SEQADV 4WOL VAL B 21 UNP O43914 MET 48 ENGINEERED MUTATION
SEQADV 4WOL VAL C 21 UNP O43914 MET 48 ENGINEERED MUTATION
SEQRES 1 A 33 CYS SER THR VAL SER PRO GLY VAL LEU ALA GLY ILE VAL
SEQRES 2 A 33 VAL GLY ASP LEU VAL LEU THR VAL LEU ILE ALA LEU ALA
SEQRES 3 A 33 VAL TYR PHE LEU GLY ARG LEU
SEQRES 1 B 33 CYS SER THR VAL SER PRO GLY VAL LEU ALA GLY ILE VAL
SEQRES 2 B 33 VAL GLY ASP LEU VAL LEU THR VAL LEU ILE ALA LEU ALA
SEQRES 3 B 33 VAL TYR PHE LEU GLY ARG LEU
SEQRES 1 C 33 CYS SER THR VAL SER PRO GLY VAL LEU ALA GLY ILE VAL
SEQRES 2 C 33 VAL GLY ASP LEU VAL LEU THR VAL LEU ILE ALA LEU ALA
SEQRES 3 C 33 VAL TYR PHE LEU GLY ARG LEU
HET K A 101 1
HET OLC B 101 25
HET OLC C 101 25
HET OLC C 102 25
HET OLC C 103 25
HETNAM K POTASSIUM ION
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 4 K K 1+
FORMUL 5 OLC 4(C21 H40 O4)
FORMUL 9 HOH *36(H2 O)
HELIX 1 AA1 SER A 12 ARG A 39 1 28
HELIX 2 AA2 SER B 12 GLY B 38 1 27
HELIX 3 AA3 SER C 12 ARG C 39 1 28
SSBOND 1 CYS A 8 CYS B 8 1555 1555 2.03
LINK OD1 ASP A 23 K K A 101 1555 1555 2.86
LINK OD2 ASP A 23 K K A 101 1555 1555 2.83
LINK OG1 THR A 27 K K A 101 1555 1555 2.88
LINK OD1 ASP B 23 K K A 101 1555 1555 3.02
LINK OG1 THR B 27 K K A 101 1555 1555 2.75
LINK OD2 ASP C 23 K K A 101 1555 1555 2.69
LINK OG1 THR C 27 K K A 101 1555 1555 2.83
SITE 1 AC1 6 ASP A 23 THR A 27 ASP B 23 THR B 27
SITE 2 AC1 6 ASP C 23 THR C 27
SITE 1 AC2 12 GLY A 22 ASP A 23 VAL A 34 GLY A 38
SITE 2 AC2 12 PRO B 13 LEU B 16 ALA B 17 ASP B 23
SITE 3 AC2 12 LEU B 29 ARG B 39 OLC C 101 HOH C 201
SITE 1 AC3 11 VAL A 11 LEU A 16 GLY A 18 LEU A 37
SITE 2 AC3 11 ILE B 19 ASP B 23 LEU B 26 OLC B 101
SITE 3 AC3 11 ASP C 23 HOH C 201 HOH C 204
SITE 1 AC4 10 VAL A 20 VAL A 25 ALA B 33 VAL C 25
SITE 2 AC4 10 VAL C 28 LEU C 29 PHE C 36 ARG C 39
SITE 3 AC4 10 OLC C 103 HOH C 211
SITE 1 AC5 11 LEU B 37 GLY B 38 HOH B 201 GLY C 14
SITE 2 AC5 11 VAL C 15 GLY C 18 GLY C 22 LEU C 26
SITE 3 AC5 11 OLC C 102 HOH C 202 HOH C 205
CRYST1 20.775 35.709 101.070 90.00 90.00 90.00 P 21 21 21 12
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 0.048135 0.000000 0.000000 0.00000
SCALE2 0.000000 0.028004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009894 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
