HEADER IMMUNE SYSTEM/MEMBRANE PROTEIN 24-OCT-02 1O77
TITLE CRYSTAL STRUCTURE OF THE C713S MUTANT OF THE TIR DOMAIN OF HUMAN TLR2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLL-LIKE RECEPTOR 2;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 FRAGMENT: TIR DOMAIN, RESIDUES 639-784;
COMPND 5 SYNONYM: TOLL/INTERLEUKIN 1 RECEPTOR-LIKE PROTEIN 4, TLR2, TIL4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET
KEYWDS IMMUNE SYSTEM/MEMBRANE PROTEIN, KNOWN BIOLOGICAL ACTIVITY RECEPTOR,
KEYWDS 2 IMMUNE RESPONSE, INFLAMMATORY RESPONSE, TRANSMEMBRANE, LEUCINE-RICH
KEYWDS 3 REPEAT, GLYCOPROTEIN, 3D-STRUCTURE., IMMUNE SYSTEM-MEMBRANE PROTEIN
KEYWDS 4 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.TAO,Y.XU,Z.YE,A.A.BEG,L.TONG
REVDAT 4 13-DEC-23 1O77 1 REMARK
REVDAT 3 09-JUN-09 1O77 1 REMARK
REVDAT 2 24-FEB-09 1O77 1 VERSN
REVDAT 1 21-NOV-02 1O77 0
JRNL AUTH X.TAO,Y.XU,Y.ZHENG,A.A.BEG,L.TONG
JRNL TITL AN EXTENSIVELY ASSOCIATED DIMER IN THE STRUCTURE OF THE
JRNL TITL 2 C713S MUTANT OF THE TIR DOMAIN OF HUMAN TLR2
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 299 216 2002
JRNL REFN ISSN 0006-291X
JRNL PMID 12437972
JRNL DOI 10.1016/S0006-291X(02)02581-0
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.9
REMARK 3 NUMBER OF REFLECTIONS : 19713
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 SET) : 0.249
REMARK 3 FREE R VALUE : 0.315
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1453
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 58.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2045
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 166
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5824
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.12000
REMARK 3 B22 (A**2) : 13.77000
REMARK 3 B33 (A**2) : -9.64000
REMARK 3 B12 (A**2) : -7.86000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.39
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.53
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.52
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 61.33
REMARK 3
REMARK 3 NCS MODEL : CONSTRAINED
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1O77 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1290011593.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 32-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9876
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23135
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.39900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: COMO
REMARK 200 STARTING MODEL: PDB ENTRY 1FYW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M (NH4)2HPO4, 0.1M MES PH 6.5, PH
REMARK 280 7.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 241.86667
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 120.93333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 181.40000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 60.46667
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 302.33333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 241.86667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 120.93333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 60.46667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 181.40000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 302.33333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: CHAINS A,B,C AND D FORM A TETRAMER-
REMARK 300 LIKE ASSOCIATIONIN THE ASYMMETRIC UNIT
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: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED MUTATION CYS 713 SER IN CHAINS A, B, C D AND E
REMARK 400
REMARK 400 MEDIATES THE INNATE IMMUNE RESPONSE TO BACTERIAL LIPOPROTEINS
REMARK 400 AND OTHER MICROBIAL CELL WALL COMPONENTS LEADING TO THE
REMARK 400 ACTIVATION OF NF-KAPPA-B, SECRETION OF CYTOKINES AND AN
REMARK 400 INFLAMMATORY RESPONSE. HIGH LEVEL OF EXPRESSION IN PERIPHERAL
REMARK 400 BLOOD LEUKOCYTES (MONOCYTES), BONE MARROW AND SPLEEN.
REMARK 400 SIMILAR TO THE TOLL FAMILY OF RECEPTORS.
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 ASP A 726
REMARK 465 GLU A 727
REMARK 465 ASN A 728
REMARK 465 ASN A 729
REMARK 465 ASP A 730
REMARK 465 ASP B 718
REMARK 465 PHE B 719
REMARK 465 SER B 720
REMARK 465 HIS B 721
REMARK 465 PHE B 722
REMARK 465 ARG B 723
REMARK 465 ASP B 726
REMARK 465 GLU B 727
REMARK 465 ASN B 728
REMARK 465 ASN B 729
REMARK 465 ASP B 730
REMARK 465 SER C 720
REMARK 465 HIS C 721
REMARK 465 PHE C 722
REMARK 465 ARG C 723
REMARK 465 LEU C 724
REMARK 465 PHE C 725
REMARK 465 ASP C 726
REMARK 465 GLU C 727
REMARK 465 ASN C 728
REMARK 465 ASN C 729
REMARK 465 ASP C 730
REMARK 465 ASP D 726
REMARK 465 GLU D 727
REMARK 465 ASN D 728
REMARK 465 ASN D 729
REMARK 465 ASP D 730
REMARK 465 SER E 720
REMARK 465 HIS E 721
REMARK 465 PHE E 722
REMARK 465 ARG E 723
REMARK 465 ASP E 726
REMARK 465 GLU E 727
REMARK 465 ASN E 728
REMARK 465 ASN E 729
REMARK 465 ASP E 730
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 CYS C 750 CA - CB - SG ANGL. DEV. = -15.8 DEGREES
REMARK 500 PRO D 765 C - N - CA ANGL. DEV. = 9.6 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 ASP A 651 42.07 -84.87
REMARK 500 LEU A 658 -54.14 -124.39
REMARK 500 PHE A 666 152.39 -39.79
REMARK 500 HIS A 675 -105.83 -47.30
REMARK 500 LYS A 676 57.10 -69.81
REMARK 500 ARG A 677 -20.78 -169.01
REMARK 500 ASP A 678 37.78 -152.40
REMARK 500 PRO A 681 -152.83 -59.79
REMARK 500 ILE A 686 -34.29 -39.89
REMARK 500 LYS A 695 35.38 -82.30
REMARK 500 SER A 704 131.46 171.62
REMARK 500 GLU A 711 -35.18 -133.65
REMARK 500 LEU A 717 -75.32 -130.74
REMARK 500 ARG A 723 43.79 36.15
REMARK 500 MET A 756 -3.85 -55.63
REMARK 500 THR A 760 68.78 -112.35
REMARK 500 GLU A 768 -32.01 -34.01
REMARK 500 ALA B 643 143.63 -175.11
REMARK 500 ASN B 657 -68.86 -98.19
REMARK 500 LEU B 663 -56.16 -134.72
REMARK 500 LYS B 683 140.80 92.56
REMARK 500 TRP B 684 -161.93 -172.68
REMARK 500 ILE B 685 -89.73 -155.24
REMARK 500 ASP B 687 155.98 -39.03
REMARK 500 ASN B 688 -95.21 27.36
REMARK 500 ILE B 689 -82.12 2.69
REMARK 500 GLU B 694 -6.86 -54.14
REMARK 500 SER B 704 173.81 179.04
REMARK 500 SER B 713 -44.38 -25.30
REMARK 500 ALA B 744 -6.77 -42.83
REMARK 500 PRO B 746 164.40 -49.32
REMARK 500 PHE B 749 68.21 -103.23
REMARK 500 CYS B 750 -75.41 -70.05
REMARK 500 LYS B 751 -38.31 -30.07
REMARK 500 LYS B 754 -74.54 -48.75
REMARK 500 MET B 756 -92.78 -60.70
REMARK 500 ASN B 757 -42.54 -26.45
REMARK 500 LYS B 759 32.72 71.17
REMARK 500 THR B 760 32.07 -84.80
REMARK 500 GLU B 772 -38.99 -38.60
REMARK 500 VAL B 776 -46.19 -27.76
REMARK 500 CYS C 640 -24.65 -159.31
REMARK 500 GLU C 656 0.29 -58.81
REMARK 500 ASN C 657 -83.34 -125.55
REMARK 500 LEU C 663 -56.81 -132.04
REMARK 500 PHE C 666 -151.14 -84.95
REMARK 500 ASN C 667 109.76 -173.11
REMARK 500 PRO C 681 65.59 -67.99
REMARK 500 LYS C 683 129.93 78.17
REMARK 500 TRP C 684 -159.69 -167.08
REMARK 500
REMARK 500 THIS ENTRY HAS 108 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FYW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TIR DOMAIN OF HUMAN TLR2
DBREF 1O77 A 639 784 UNP O60603 TLR2_HUMAN 639 784
DBREF 1O77 B 639 784 UNP O60603 TLR2_HUMAN 639 784
DBREF 1O77 C 639 784 UNP O60603 TLR2_HUMAN 639 784
DBREF 1O77 D 639 784 UNP O60603 TLR2_HUMAN 639 784
DBREF 1O77 E 639 784 UNP O60603 TLR2_HUMAN 639 784
SEQADV 1O77 SER A 713 UNP O60603 CYS 713 ENGINEERED MUTATION
SEQADV 1O77 SER B 713 UNP O60603 CYS 713 ENGINEERED MUTATION
SEQADV 1O77 SER C 713 UNP O60603 CYS 713 ENGINEERED MUTATION
SEQADV 1O77 SER D 713 UNP O60603 CYS 713 ENGINEERED MUTATION
SEQADV 1O77 SER E 713 UNP O60603 CYS 713 ENGINEERED MUTATION
SEQRES 1 A 146 ILE CYS TYR ASP ALA PHE VAL SER TYR SER GLU ARG ASP
SEQRES 2 A 146 ALA TYR TRP VAL GLU ASN LEU MET VAL GLN GLU LEU GLU
SEQRES 3 A 146 ASN PHE ASN PRO PRO PHE LYS LEU CYS LEU HIS LYS ARG
SEQRES 4 A 146 ASP PHE ILE PRO GLY LYS TRP ILE ILE ASP ASN ILE ILE
SEQRES 5 A 146 ASP SER ILE GLU LYS SER HIS LYS THR VAL PHE VAL LEU
SEQRES 6 A 146 SER GLU ASN PHE VAL LYS SER GLU TRP SER LYS TYR GLU
SEQRES 7 A 146 LEU ASP PHE SER HIS PHE ARG LEU PHE ASP GLU ASN ASN
SEQRES 8 A 146 ASP ALA ALA ILE LEU ILE LEU LEU GLU PRO ILE GLU LYS
SEQRES 9 A 146 LYS ALA ILE PRO GLN ARG PHE CYS LYS LEU ARG LYS ILE
SEQRES 10 A 146 MET ASN THR LYS THR TYR LEU GLU TRP PRO MET ASP GLU
SEQRES 11 A 146 ALA GLN ARG GLU GLY PHE TRP VAL ASN LEU ARG ALA ALA
SEQRES 12 A 146 ILE LYS SER
SEQRES 1 B 146 ILE CYS TYR ASP ALA PHE VAL SER TYR SER GLU ARG ASP
SEQRES 2 B 146 ALA TYR TRP VAL GLU ASN LEU MET VAL GLN GLU LEU GLU
SEQRES 3 B 146 ASN PHE ASN PRO PRO PHE LYS LEU CYS LEU HIS LYS ARG
SEQRES 4 B 146 ASP PHE ILE PRO GLY LYS TRP ILE ILE ASP ASN ILE ILE
SEQRES 5 B 146 ASP SER ILE GLU LYS SER HIS LYS THR VAL PHE VAL LEU
SEQRES 6 B 146 SER GLU ASN PHE VAL LYS SER GLU TRP SER LYS TYR GLU
SEQRES 7 B 146 LEU ASP PHE SER HIS PHE ARG LEU PHE ASP GLU ASN ASN
SEQRES 8 B 146 ASP ALA ALA ILE LEU ILE LEU LEU GLU PRO ILE GLU LYS
SEQRES 9 B 146 LYS ALA ILE PRO GLN ARG PHE CYS LYS LEU ARG LYS ILE
SEQRES 10 B 146 MET ASN THR LYS THR TYR LEU GLU TRP PRO MET ASP GLU
SEQRES 11 B 146 ALA GLN ARG GLU GLY PHE TRP VAL ASN LEU ARG ALA ALA
SEQRES 12 B 146 ILE LYS SER
SEQRES 1 C 146 ILE CYS TYR ASP ALA PHE VAL SER TYR SER GLU ARG ASP
SEQRES 2 C 146 ALA TYR TRP VAL GLU ASN LEU MET VAL GLN GLU LEU GLU
SEQRES 3 C 146 ASN PHE ASN PRO PRO PHE LYS LEU CYS LEU HIS LYS ARG
SEQRES 4 C 146 ASP PHE ILE PRO GLY LYS TRP ILE ILE ASP ASN ILE ILE
SEQRES 5 C 146 ASP SER ILE GLU LYS SER HIS LYS THR VAL PHE VAL LEU
SEQRES 6 C 146 SER GLU ASN PHE VAL LYS SER GLU TRP SER LYS TYR GLU
SEQRES 7 C 146 LEU ASP PHE SER HIS PHE ARG LEU PHE ASP GLU ASN ASN
SEQRES 8 C 146 ASP ALA ALA ILE LEU ILE LEU LEU GLU PRO ILE GLU LYS
SEQRES 9 C 146 LYS ALA ILE PRO GLN ARG PHE CYS LYS LEU ARG LYS ILE
SEQRES 10 C 146 MET ASN THR LYS THR TYR LEU GLU TRP PRO MET ASP GLU
SEQRES 11 C 146 ALA GLN ARG GLU GLY PHE TRP VAL ASN LEU ARG ALA ALA
SEQRES 12 C 146 ILE LYS SER
SEQRES 1 D 146 ILE CYS TYR ASP ALA PHE VAL SER TYR SER GLU ARG ASP
SEQRES 2 D 146 ALA TYR TRP VAL GLU ASN LEU MET VAL GLN GLU LEU GLU
SEQRES 3 D 146 ASN PHE ASN PRO PRO PHE LYS LEU CYS LEU HIS LYS ARG
SEQRES 4 D 146 ASP PHE ILE PRO GLY LYS TRP ILE ILE ASP ASN ILE ILE
SEQRES 5 D 146 ASP SER ILE GLU LYS SER HIS LYS THR VAL PHE VAL LEU
SEQRES 6 D 146 SER GLU ASN PHE VAL LYS SER GLU TRP SER LYS TYR GLU
SEQRES 7 D 146 LEU ASP PHE SER HIS PHE ARG LEU PHE ASP GLU ASN ASN
SEQRES 8 D 146 ASP ALA ALA ILE LEU ILE LEU LEU GLU PRO ILE GLU LYS
SEQRES 9 D 146 LYS ALA ILE PRO GLN ARG PHE CYS LYS LEU ARG LYS ILE
SEQRES 10 D 146 MET ASN THR LYS THR TYR LEU GLU TRP PRO MET ASP GLU
SEQRES 11 D 146 ALA GLN ARG GLU GLY PHE TRP VAL ASN LEU ARG ALA ALA
SEQRES 12 D 146 ILE LYS SER
SEQRES 1 E 146 ILE CYS TYR ASP ALA PHE VAL SER TYR SER GLU ARG ASP
SEQRES 2 E 146 ALA TYR TRP VAL GLU ASN LEU MET VAL GLN GLU LEU GLU
SEQRES 3 E 146 ASN PHE ASN PRO PRO PHE LYS LEU CYS LEU HIS LYS ARG
SEQRES 4 E 146 ASP PHE ILE PRO GLY LYS TRP ILE ILE ASP ASN ILE ILE
SEQRES 5 E 146 ASP SER ILE GLU LYS SER HIS LYS THR VAL PHE VAL LEU
SEQRES 6 E 146 SER GLU ASN PHE VAL LYS SER GLU TRP SER LYS TYR GLU
SEQRES 7 E 146 LEU ASP PHE SER HIS PHE ARG LEU PHE ASP GLU ASN ASN
SEQRES 8 E 146 ASP ALA ALA ILE LEU ILE LEU LEU GLU PRO ILE GLU LYS
SEQRES 9 E 146 LYS ALA ILE PRO GLN ARG PHE CYS LYS LEU ARG LYS ILE
SEQRES 10 E 146 MET ASN THR LYS THR TYR LEU GLU TRP PRO MET ASP GLU
SEQRES 11 E 146 ALA GLN ARG GLU GLY PHE TRP VAL ASN LEU ARG ALA ALA
SEQRES 12 E 146 ILE LYS SER
HELIX 1 1 ASP A 651 LEU A 658 1 8
HELIX 2 2 LEU A 658 ASN A 665 1 8
HELIX 3 3 LYS A 676 ASP A 678 5 3
HELIX 4 4 TRP A 684 LYS A 695 1 12
HELIX 5 5 SER A 704 GLU A 711 1 8
HELIX 6 6 GLU A 711 LEU A 717 1 7
HELIX 7 7 PHE A 719 ARG A 723 5 5
HELIX 8 8 GLU A 741 ILE A 745 5 5
HELIX 9 9 PHE A 749 LYS A 759 1 11
HELIX 10 10 ASP A 767 LYS A 783 1 17
HELIX 11 11 ASP B 651 ASN B 657 1 7
HELIX 12 12 ASN B 657 ASN B 665 1 9
HELIX 13 13 HIS B 675 PHE B 679 1 5
HELIX 14 14 ASN B 688 GLU B 694 1 7
HELIX 15 15 SER B 704 GLU B 711 1 8
HELIX 16 16 GLU B 711 LEU B 717 1 7
HELIX 17 17 PHE B 749 THR B 758 1 10
HELIX 18 18 ASP B 767 ALA B 769 5 3
HELIX 19 19 GLN B 770 LYS B 783 1 14
HELIX 20 20 SER C 648 ARG C 650 5 3
HELIX 21 21 ASP C 651 GLU C 656 1 6
HELIX 22 22 ASN C 657 LEU C 663 1 7
HELIX 23 23 HIS C 675 PHE C 679 1 5
HELIX 24 24 ILE C 689 GLU C 694 1 6
HELIX 25 25 SER C 704 GLU C 711 1 8
HELIX 26 26 GLU C 711 LEU C 717 1 7
HELIX 27 27 PHE C 749 THR C 758 1 10
HELIX 28 28 ASP C 767 SER C 784 1 18
HELIX 29 29 ALA D 652 ASN D 665 1 14
HELIX 30 30 HIS D 675 PHE D 679 1 5
HELIX 31 31 TRP D 684 GLU D 694 1 11
HELIX 32 32 SER D 704 TRP D 712 1 9
HELIX 33 33 TRP D 712 LEU D 717 1 6
HELIX 34 34 PHE D 749 THR D 758 1 10
HELIX 35 35 GLY D 773 LYS D 783 1 11
HELIX 36 36 SER E 648 ARG E 650 5 3
HELIX 37 37 ASP E 651 ASN E 657 1 7
HELIX 38 38 ASN E 657 ASN E 665 1 9
HELIX 39 39 HIS E 675 PHE E 679 1 5
HELIX 40 40 TRP E 684 LYS E 695 1 12
HELIX 41 41 GLU E 705 GLU E 711 1 7
HELIX 42 42 TRP E 712 LEU E 717 5 6
HELIX 43 43 PHE E 749 LYS E 759 1 11
HELIX 44 44 GLN E 770 LYS E 783 1 14
SHEET 1 AA 5 LEU A 672 LEU A 674 0
SHEET 2 AA 5 TYR A 641 SER A 646 1 O ALA A 643 N CYS A 673
SHEET 3 AA 5 SER A 696 LEU A 703 1 N HIS A 697 O TYR A 641
SHEET 4 AA 5 ALA A 732 LEU A 736 1 O ILE A 733 N PHE A 701
SHEET 5 AA 5 LEU A 762 GLU A 763 1 O LEU A 762 N LEU A 736
SHEET 1 BA 5 LEU B 672 LEU B 674 0
SHEET 2 BA 5 ALA B 643 SER B 646 1 O ALA B 643 N CYS B 673
SHEET 3 BA 5 THR B 699 LEU B 703 1 O VAL B 700 N SER B 646
SHEET 4 BA 5 ALA B 732 LEU B 736 1 O ILE B 733 N PHE B 701
SHEET 5 BA 5 TYR B 761 GLU B 763 1 O LEU B 762 N LEU B 736
SHEET 1 CA 5 LEU C 672 LEU C 674 0
SHEET 2 CA 5 ALA C 643 SER C 646 1 O ALA C 643 N CYS C 673
SHEET 3 CA 5 THR C 699 PHE C 701 1 O VAL C 700 N SER C 646
SHEET 4 CA 5 ALA C 732 LEU C 736 1 O ILE C 733 N PHE C 701
SHEET 5 CA 5 TYR C 761 GLU C 763 1 O LEU C 762 N LEU C 736
SHEET 1 DA 4 LEU D 672 LEU D 674 0
SHEET 2 DA 4 TYR D 641 SER D 646 1 O ALA D 643 N CYS D 673
SHEET 3 DA 4 SER D 696 PHE D 701 1 N HIS D 697 O TYR D 641
SHEET 4 DA 4 ALA D 732 ILE D 733 1 O ILE D 733 N PHE D 701
SHEET 1 DB 2 ILE D 735 LEU D 736 0
SHEET 2 DB 2 LEU D 762 GLU D 763 1 O LEU D 762 N LEU D 736
SHEET 1 EA 5 LEU E 672 LEU E 674 0
SHEET 2 EA 5 TYR E 641 SER E 646 1 O ALA E 643 N CYS E 673
SHEET 3 EA 5 SER E 696 LEU E 703 1 N HIS E 697 O TYR E 641
SHEET 4 EA 5 ALA E 732 LEU E 736 1 O ILE E 733 N PHE E 701
SHEET 5 EA 5 LEU E 762 GLU E 763 1 O LEU E 762 N LEU E 736
SSBOND 1 CYS A 640 CYS C 750 1555 1555 2.04
SSBOND 2 CYS A 750 CYS B 640 1555 1555 2.04
SSBOND 3 CYS B 750 CYS D 640 1555 1555 2.04
SSBOND 4 CYS C 640 CYS D 750 1555 1555 2.03
CISPEP 1 ASN A 667 PRO A 668 0 -0.24
CISPEP 2 ASN B 667 PRO B 668 0 -0.24
CISPEP 3 ASN C 667 PRO C 668 0 0.04
CISPEP 4 ASN D 667 PRO D 668 0 -0.12
CISPEP 5 ASN E 667 PRO E 668 0 -0.26
CRYST1 112.300 112.300 362.800 90.00 90.00 120.00 P 65 2 2 60
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 0.008905 0.005141 0.000000 0.00000
SCALE2 0.000000 0.010282 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002756 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
