HEADER DNA BINDING PROTEIN 11-JAN-14 3WPF
TITLE CRYSTAL STRUCTURE OF MOUSE TLR9 (UNLIGANDED FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLL-LIKE RECEPTOR 9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 26-818;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: TLR9;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 8 EXPRESSION_SYSTEM_CELL: SCHNEIDER 2(S2);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS LEUCINE RICH REPEAT, RECEPTOR, INNATE IMMUNITY, DNA BINDING,
KEYWDS 2 GLYCOSYLATION, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR U.OHTO,T.SHIMIZU
REVDAT 4 08-NOV-23 3WPF 1 HETSYN
REVDAT 3 29-JUL-20 3WPF 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK SITE
REVDAT 2 06-MAY-15 3WPF 1 JRNL
REVDAT 1 11-FEB-15 3WPF 0
JRNL AUTH U.OHTO,T.SHIBATA,H.TANJI,H.ISHIDA,E.KRAYUKHINA,S.UCHIYAMA,
JRNL AUTH 2 K.MIYAKE,T.SHIMIZU
JRNL TITL STRUCTURAL BASIS OF CPG AND INHIBITORY DNA RECOGNITION BY
JRNL TITL 2 TOLL-LIKE RECEPTOR 9
JRNL REF NATURE V. 520 702 2015
JRNL REFN ISSN 0028-0836
JRNL PMID 25686612
JRNL DOI 10.1038/NATURE14138
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 79109
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 3971
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 44.6253 - 5.9441 0.86 2520 145 0.2359 0.2376
REMARK 3 2 5.9441 - 4.7197 0.94 2663 149 0.1991 0.2212
REMARK 3 3 4.7197 - 4.1236 0.96 2672 139 0.1723 0.1719
REMARK 3 4 4.1236 - 3.7468 0.97 2677 142 0.1694 0.2460
REMARK 3 5 3.7468 - 3.4784 0.98 2722 126 0.1845 0.2278
REMARK 3 6 3.4784 - 3.2733 0.98 2685 145 0.2039 0.2700
REMARK 3 7 3.2733 - 3.1095 0.98 2686 140 0.2234 0.3438
REMARK 3 8 3.1095 - 2.9741 0.99 2718 134 0.2183 0.2495
REMARK 3 9 2.9741 - 2.8597 0.99 2702 134 0.2180 0.2534
REMARK 3 10 2.8597 - 2.7610 0.99 2690 154 0.2170 0.2459
REMARK 3 11 2.7610 - 2.6747 0.99 2691 156 0.2199 0.2681
REMARK 3 12 2.6747 - 2.5982 0.99 2723 136 0.2177 0.2792
REMARK 3 13 2.5982 - 2.5298 0.99 2687 150 0.2292 0.2472
REMARK 3 14 2.5298 - 2.4681 0.99 2715 128 0.2331 0.2676
REMARK 3 15 2.4681 - 2.4120 0.99 2693 151 0.2330 0.3117
REMARK 3 16 2.4120 - 2.3607 1.00 2676 153 0.2465 0.3157
REMARK 3 17 2.3607 - 2.3135 1.00 2749 120 0.2491 0.2815
REMARK 3 18 2.3135 - 2.2698 1.00 2693 138 0.2476 0.2836
REMARK 3 19 2.2698 - 2.2293 1.00 2720 142 0.2493 0.3059
REMARK 3 20 2.2293 - 2.1915 1.00 2708 134 0.2654 0.2730
REMARK 3 21 2.1915 - 2.1561 1.00 2701 141 0.2774 0.3234
REMARK 3 22 2.1561 - 2.1230 1.00 2703 134 0.2868 0.3275
REMARK 3 23 2.1230 - 2.0917 1.00 2673 147 0.2932 0.3370
REMARK 3 24 2.0917 - 2.0623 1.00 2714 144 0.3104 0.3538
REMARK 3 25 2.0623 - 2.0344 1.00 2678 128 0.3133 0.3672
REMARK 3 26 2.0344 - 2.0080 1.00 2684 152 0.3344 0.3697
REMARK 3 27 2.0080 - 1.9829 0.98 2618 163 0.3628 0.3981
REMARK 3 28 1.9829 - 1.9590 0.96 2577 146 0.3742 0.4101
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.35
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.74
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 : 0.006 6088
REMARK 3 ANGLE : 1.170 8253
REMARK 3 CHIRALITY : 0.085 956
REMARK 3 PLANARITY : 0.004 1037
REMARK 3 DIHEDRAL : 16.201 2208
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6459 4.9480 22.5513
REMARK 3 T TENSOR
REMARK 3 T11: 0.1429 T22: 0.0834
REMARK 3 T33: 0.1738 T12: 0.0693
REMARK 3 T13: 0.0459 T23: -0.0439
REMARK 3 L TENSOR
REMARK 3 L11: 0.7802 L22: 0.3695
REMARK 3 L33: 1.7978 L12: 0.0890
REMARK 3 L13: 0.5054 L23: -0.2561
REMARK 3 S TENSOR
REMARK 3 S11: -0.0410 S12: -0.0875 S13: -0.0249
REMARK 3 S21: -0.0001 S22: 0.0301 S23: -0.0411
REMARK 3 S31: -0.0712 S32: -0.0058 S33: 0.0101
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 3WPF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000096626.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79163
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.959
REMARK 200 RESOLUTION RANGE LOW (A) : 48.110
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: MOLREP
REMARK 200 STARTING MODEL: 3W3J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6-8% PEG 8000, 0.4M AMMONIUM SULFATE,
REMARK 280 0.1M TRIS PH 8.0, 10% DMSO , 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 35.63000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.20500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.64000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.20500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.63000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.64000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ARG A 22
REMARK 465 SER A 23
REMARK 465 PRO A 24
REMARK 465 TRP A 25
REMARK 465 LEU A 26
REMARK 465 GLY A 27
REMARK 465 SER A 57
REMARK 465 ALA A 58
REMARK 465 ALA A 59
REMARK 465 PRO A 105
REMARK 465 LEU A 106
REMARK 465 HIS A 107
REMARK 465 PHE A 108
REMARK 465 LEU A 433
REMARK 465 SER A 434
REMARK 465 GLU A 435
REMARK 465 ALA A 436
REMARK 465 THR A 437
REMARK 465 PRO A 438
REMARK 465 GLU A 439
REMARK 465 GLU A 440
REMARK 465 ALA A 441
REMARK 465 ASP A 442
REMARK 465 ASP A 443
REMARK 465 ALA A 444
REMARK 465 GLU A 445
REMARK 465 GLN A 446
REMARK 465 GLU A 447
REMARK 465 GLU A 448
REMARK 465 LEU A 449
REMARK 465 LEU A 450
REMARK 465 SER A 451
REMARK 465 ALA A 452
REMARK 465 ASP A 453
REMARK 465 PRO A 454
REMARK 465 HIS A 455
REMARK 465 PRO A 456
REMARK 465 ALA A 457
REMARK 465 PRO A 458
REMARK 465 LEU A 459
REMARK 465 SER A 460
REMARK 465 THR A 461
REMARK 465 PRO A 462
REMARK 465 ALA A 463
REMARK 465 SER A 464
REMARK 465 LYS A 465
REMARK 465 SER A 561
REMARK 465 MET A 562
REMARK 465 LYS A 563
REMARK 465 LEU A 811
REMARK 465 ASP A 812
REMARK 465 GLU A 813
REMARK 465 VAL A 814
REMARK 465 LEU A 815
REMARK 465 SER A 816
REMARK 465 TRP A 817
REMARK 465 ASP A 818
REMARK 465 GLU A 819
REMARK 465 PHE A 820
REMARK 465 LEU A 821
REMARK 465 VAL A 822
REMARK 465 PRO A 823
REMARK 465 ARG A 824
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ALA A 164 O HOH A 1185 2.11
REMARK 500 O GLU A 322 OG1 THR A 325 2.19
REMARK 500 ND2 ASN A 210 O5 NAG A 903 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1191 O HOH A 1214 2455 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 GLY A 165 N - CA - C ANGL. DEV. = -15.2 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 PRO A 39 -34.83 -34.12
REMARK 500 HIS A 40 33.46 -59.25
REMARK 500 PHE A 49 13.77 57.69
REMARK 500 ASN A 73 -156.47 -88.79
REMARK 500 PRO A 100 -161.43 -64.36
REMARK 500 LEU A 103 -69.24 -156.55
REMARK 500 THR A 153 -160.52 -113.38
REMARK 500 CYS A 178 68.13 -163.70
REMARK 500 ASN A 230 -142.61 -104.57
REMARK 500 LEU A 243 55.04 -98.72
REMARK 500 ASN A 318 -158.21 -114.99
REMARK 500 HIS A 326 -12.86 -154.35
REMARK 500 PHE A 375 110.02 75.26
REMARK 500 ALA A 416 20.05 -141.96
REMARK 500 ASN A 425 -159.66 -138.33
REMARK 500 ASP A 469 60.38 -65.23
REMARK 500 CYS A 471 -13.87 87.72
REMARK 500 ASN A 473 -39.96 55.74
REMARK 500 ASN A 483 -154.80 -113.05
REMARK 500 ASN A 507 -159.04 -110.90
REMARK 500 ASN A 514 15.27 -150.65
REMARK 500 ASN A 532 -158.67 -125.88
REMARK 500 LEU A 545 78.20 -114.72
REMARK 500 ARG A 591 36.26 -94.12
REMARK 500 ASN A 609 -158.61 -104.97
REMARK 500 LEU A 644 89.12 -151.98
REMARK 500 ASN A 664 -164.94 -112.10
REMARK 500 ASN A 688 -146.46 -95.84
REMARK 500 GLN A 689 50.43 -143.99
REMARK 500 ASN A 712 -151.20 -101.72
REMARK 500 ASN A 736 -158.45 -115.85
REMARK 500 ALA A 769 105.73 -54.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WPB RELATED DB: PDB
REMARK 900 RELATED ID: 3WPC RELATED DB: PDB
REMARK 900 RELATED ID: 3WPD RELATED DB: PDB
REMARK 900 RELATED ID: 3WPE RELATED DB: PDB
REMARK 900 RELATED ID: 3WPG RELATED DB: PDB
REMARK 900 RELATED ID: 3WPH RELATED DB: PDB
REMARK 900 RELATED ID: 3WPI RELATED DB: PDB
DBREF 3WPF A 26 818 UNP Q9EQU3 TLR9_MOUSE 26 818
SEQADV 3WPF ARG A 22 UNP Q9EQU3 EXPRESSION TAG
SEQADV 3WPF SER A 23 UNP Q9EQU3 EXPRESSION TAG
SEQADV 3WPF PRO A 24 UNP Q9EQU3 EXPRESSION TAG
SEQADV 3WPF TRP A 25 UNP Q9EQU3 EXPRESSION TAG
SEQADV 3WPF GLN A 200 UNP Q9EQU3 ASN 200 ENGINEERED MUTATION
SEQADV 3WPF GLN A 242 UNP Q9EQU3 ASN 242 ENGINEERED MUTATION
SEQADV 3WPF GLN A 309 UNP Q9EQU3 ASN 309 ENGINEERED MUTATION
SEQADV 3WPF GLN A 495 UNP Q9EQU3 ASN 495 ENGINEERED MUTATION
SEQADV 3WPF GLN A 568 UNP Q9EQU3 ASN 568 ENGINEERED MUTATION
SEQADV 3WPF GLN A 695 UNP Q9EQU3 ASN 695 ENGINEERED MUTATION
SEQADV 3WPF GLN A 752 UNP Q9EQU3 ASN 752 ENGINEERED MUTATION
SEQADV 3WPF GLU A 819 UNP Q9EQU3 EXPRESSION TAG
SEQADV 3WPF PHE A 820 UNP Q9EQU3 EXPRESSION TAG
SEQADV 3WPF LEU A 821 UNP Q9EQU3 EXPRESSION TAG
SEQADV 3WPF VAL A 822 UNP Q9EQU3 EXPRESSION TAG
SEQADV 3WPF PRO A 823 UNP Q9EQU3 EXPRESSION TAG
SEQADV 3WPF ARG A 824 UNP Q9EQU3 EXPRESSION TAG
SEQRES 1 A 803 ARG SER PRO TRP LEU GLY THR LEU PRO ALA PHE LEU PRO
SEQRES 2 A 803 CYS GLU LEU LYS PRO HIS GLY LEU VAL ASP CYS ASN TRP
SEQRES 3 A 803 LEU PHE LEU LYS SER VAL PRO ARG PHE SER ALA ALA ALA
SEQRES 4 A 803 SER CYS SER ASN ILE THR ARG LEU SER LEU ILE SER ASN
SEQRES 5 A 803 ARG ILE HIS HIS LEU HIS ASN SER ASP PHE VAL HIS LEU
SEQRES 6 A 803 SER ASN LEU ARG GLN LEU ASN LEU LYS TRP ASN CYS PRO
SEQRES 7 A 803 PRO THR GLY LEU SER PRO LEU HIS PHE SER CYS HIS MET
SEQRES 8 A 803 THR ILE GLU PRO ARG THR PHE LEU ALA MET ARG THR LEU
SEQRES 9 A 803 GLU GLU LEU ASN LEU SER TYR ASN GLY ILE THR THR VAL
SEQRES 10 A 803 PRO ARG LEU PRO SER SER LEU VAL ASN LEU SER LEU SER
SEQRES 11 A 803 HIS THR ASN ILE LEU VAL LEU ASP ALA ASN SER LEU ALA
SEQRES 12 A 803 GLY LEU TYR SER LEU ARG VAL LEU PHE MET ASP GLY ASN
SEQRES 13 A 803 CYS TYR TYR LYS ASN PRO CYS THR GLY ALA VAL LYS VAL
SEQRES 14 A 803 THR PRO GLY ALA LEU LEU GLY LEU SER GLN LEU THR HIS
SEQRES 15 A 803 LEU SER LEU LYS TYR ASN ASN LEU THR LYS VAL PRO ARG
SEQRES 16 A 803 GLN LEU PRO PRO SER LEU GLU TYR LEU LEU VAL SER TYR
SEQRES 17 A 803 ASN LEU ILE VAL LYS LEU GLY PRO GLU ASP LEU ALA GLN
SEQRES 18 A 803 LEU THR SER LEU ARG VAL LEU ASP VAL GLY GLY ASN CYS
SEQRES 19 A 803 ARG ARG CYS ASP HIS ALA PRO ASN PRO CYS ILE GLU CYS
SEQRES 20 A 803 GLY GLN LYS SER LEU HIS LEU HIS PRO GLU THR PHE HIS
SEQRES 21 A 803 HIS LEU SER HIS LEU GLU GLY LEU VAL LEU LYS ASP SER
SEQRES 22 A 803 SER LEU HIS THR LEU ASN SER SER TRP PHE GLN GLY LEU
SEQRES 23 A 803 VAL GLN LEU SER VAL LEU ASP LEU SER GLU ASN PHE LEU
SEQRES 24 A 803 TYR GLU SER ILE THR HIS THR ASN ALA PHE GLN ASN LEU
SEQRES 25 A 803 THR ARG LEU ARG LYS LEU ASN LEU SER PHE ASN TYR ARG
SEQRES 26 A 803 LYS LYS VAL SER PHE ALA ARG LEU HIS LEU ALA SER SER
SEQRES 27 A 803 PHE LYS ASN LEU VAL SER LEU GLN GLU LEU ASN MET ASN
SEQRES 28 A 803 GLY ILE PHE PHE ARG LEU LEU ASN LYS TYR THR LEU ARG
SEQRES 29 A 803 TRP LEU ALA ASP LEU PRO LYS LEU HIS THR LEU HIS LEU
SEQRES 30 A 803 GLN MET ASN PHE ILE ASN GLN ALA GLN LEU SER ILE PHE
SEQRES 31 A 803 GLY THR PHE ARG ALA LEU ARG PHE VAL ASP LEU SER ASP
SEQRES 32 A 803 ASN ARG ILE SER GLY PRO SER THR LEU SER GLU ALA THR
SEQRES 33 A 803 PRO GLU GLU ALA ASP ASP ALA GLU GLN GLU GLU LEU LEU
SEQRES 34 A 803 SER ALA ASP PRO HIS PRO ALA PRO LEU SER THR PRO ALA
SEQRES 35 A 803 SER LYS ASN PHE MET ASP ARG CYS LYS ASN PHE LYS PHE
SEQRES 36 A 803 THR MET ASP LEU SER ARG ASN ASN LEU VAL THR ILE LYS
SEQRES 37 A 803 PRO GLU MET PHE VAL GLN LEU SER ARG LEU GLN CYS LEU
SEQRES 38 A 803 SER LEU SER HIS ASN SER ILE ALA GLN ALA VAL ASN GLY
SEQRES 39 A 803 SER GLN PHE LEU PRO LEU THR ASN LEU GLN VAL LEU ASP
SEQRES 40 A 803 LEU SER HIS ASN LYS LEU ASP LEU TYR HIS TRP LYS SER
SEQRES 41 A 803 PHE SER GLU LEU PRO GLN LEU GLN ALA LEU ASP LEU SER
SEQRES 42 A 803 TYR ASN SER GLN PRO PHE SER MET LYS GLY ILE GLY HIS
SEQRES 43 A 803 GLN PHE SER PHE VAL THR HIS LEU SER MET LEU GLN SER
SEQRES 44 A 803 LEU SER LEU ALA HIS ASN ASP ILE HIS THR ARG VAL SER
SEQRES 45 A 803 SER HIS LEU ASN SER ASN SER VAL ARG PHE LEU ASP PHE
SEQRES 46 A 803 SER GLY ASN GLY MET GLY ARG MET TRP ASP GLU GLY GLY
SEQRES 47 A 803 LEU TYR LEU HIS PHE PHE GLN GLY LEU SER GLY LEU LEU
SEQRES 48 A 803 LYS LEU ASP LEU SER GLN ASN ASN LEU HIS ILE LEU ARG
SEQRES 49 A 803 PRO GLN ASN LEU ASP ASN LEU PRO LYS SER LEU LYS LEU
SEQRES 50 A 803 LEU SER LEU ARG ASP ASN TYR LEU SER PHE PHE ASN TRP
SEQRES 51 A 803 THR SER LEU SER PHE LEU PRO ASN LEU GLU VAL LEU ASP
SEQRES 52 A 803 LEU ALA GLY ASN GLN LEU LYS ALA LEU THR GLN GLY THR
SEQRES 53 A 803 LEU PRO ASN GLY THR LEU LEU GLN LYS LEU ASP VAL SER
SEQRES 54 A 803 SER ASN SER ILE VAL SER VAL VAL PRO ALA PHE PHE ALA
SEQRES 55 A 803 LEU ALA VAL GLU LEU LYS GLU VAL ASN LEU SER HIS ASN
SEQRES 56 A 803 ILE LEU LYS THR VAL ASP ARG SER TRP PHE GLY PRO ILE
SEQRES 57 A 803 VAL MET GLN LEU THR VAL LEU ASP VAL ARG SER ASN PRO
SEQRES 58 A 803 LEU HIS CYS ALA CYS GLY ALA ALA PHE VAL ASP LEU LEU
SEQRES 59 A 803 LEU GLU VAL GLN THR LYS VAL PRO GLY LEU ALA ASN GLY
SEQRES 60 A 803 VAL LYS CYS GLY SER PRO GLY GLN LEU GLN GLY ARG SER
SEQRES 61 A 803 ILE PHE ALA GLN ASP LEU ARG LEU CYS LEU ASP GLU VAL
SEQRES 62 A 803 LEU SER TRP ASP GLU PHE LEU VAL PRO ARG
MODRES 3WPF ASN A 210 ASN GLYCOSYLATION SITE
MODRES 3WPF ASN A 332 ASN GLYCOSYLATION SITE
MODRES 3WPF ASN A 732 ASN GLYCOSYLATION SITE
HET NAG A 901 14
HET NAG A 902 14
HET NAG A 903 14
HET SO4 A 904 5
HET SO4 A 905 5
HET SO4 A 906 5
HET SO4 A 907 5
HET SO4 A 908 5
HET SO4 A 909 5
HET SO4 A 910 5
HET SO4 A 911 5
HET SO4 A 912 5
HET SO4 A 913 5
HET SO4 A 914 5
HET SO4 A 915 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 5 SO4 12(O4 S 2-)
FORMUL 17 HOH *236(H2 O)
HELIX 1 1 PHE A 83 SER A 87 5 5
HELIX 2 2 ASP A 159 ALA A 164 5 6
HELIX 3 3 GLY A 236 LEU A 240 5 5
HELIX 4 4 ASN A 300 GLN A 305 1 6
HELIX 5 5 LEU A 320 THR A 325 1 6
HELIX 6 6 ALA A 357 LEU A 363 5 7
HELIX 7 7 LEU A 384 ALA A 388 5 5
HELIX 8 8 LEU A 408 THR A 413 5 6
HELIX 9 9 LYS A 489 VAL A 494 5 6
HELIX 10 10 PHE A 569 LEU A 575 5 7
HELIX 11 11 GLY A 610 ASP A 616 1 7
HELIX 12 12 ARG A 645 ASN A 651 1 7
HELIX 13 13 ASN A 670 LEU A 677 5 8
HELIX 14 14 ASP A 742 GLN A 752 5 11
HELIX 15 15 ALA A 770 VAL A 778 1 9
HELIX 16 16 GLN A 779 VAL A 782 5 4
HELIX 17 17 ASP A 806 CYS A 810 5 5
SHEET 1 A28 GLU A 36 LYS A 38 0
SHEET 2 A28 LEU A 42 ASP A 44 -1 O ASP A 44 N GLU A 36
SHEET 3 A28 ARG A 67 SER A 69 1 O SER A 69 N VAL A 43
SHEET 4 A28 GLN A 91 ASN A 93 1 O GLN A 91 N LEU A 68
SHEET 5 A28 GLU A 127 ASN A 129 1 O ASN A 129 N LEU A 92
SHEET 6 A28 ASN A 147 SER A 149 1 O ASN A 147 N LEU A 128
SHEET 7 A28 VAL A 171 PHE A 173 1 O PHE A 173 N LEU A 148
SHEET 8 A28 HIS A 203 SER A 205 1 O HIS A 203 N LEU A 172
SHEET 9 A28 TYR A 224 LEU A 226 1 O LEU A 226 N LEU A 204
SHEET 10 A28 VAL A 248 ASP A 250 1 O ASP A 250 N LEU A 225
SHEET 11 A28 GLY A 288 VAL A 290 1 O VAL A 290 N LEU A 249
SHEET 12 A28 VAL A 312 ASP A 314 1 O VAL A 312 N LEU A 289
SHEET 13 A28 LYS A 338 ASN A 340 1 O ASN A 340 N LEU A 313
SHEET 14 A28 GLU A 368 ASN A 370 1 O ASN A 370 N LEU A 339
SHEET 15 A28 THR A 395 HIS A 397 1 O HIS A 397 N LEU A 369
SHEET 16 A28 PHE A 419 ASP A 421 1 O ASP A 421 N LEU A 396
SHEET 17 A28 THR A 477 ASP A 479 1 O ASP A 479 N VAL A 420
SHEET 18 A28 CYS A 501 SER A 503 1 O CYS A 501 N MET A 478
SHEET 19 A28 VAL A 526 ASP A 528 1 O VAL A 526 N LEU A 502
SHEET 20 A28 ALA A 550 ASP A 552 1 O ASP A 552 N LEU A 527
SHEET 21 A28 SER A 580 SER A 582 1 O SER A 582 N LEU A 551
SHEET 22 A28 PHE A 603 ASP A 605 1 O PHE A 603 N LEU A 581
SHEET 23 A28 LYS A 633 ASP A 635 1 O LYS A 633 N LEU A 604
SHEET 24 A28 LEU A 658 SER A 660 1 O SER A 660 N LEU A 634
SHEET 25 A28 VAL A 682 ASP A 684 1 O VAL A 682 N LEU A 659
SHEET 26 A28 LYS A 706 ASP A 708 1 O LYS A 706 N LEU A 683
SHEET 27 A28 GLU A 730 ASN A 732 1 O GLU A 730 N LEU A 707
SHEET 28 A28 VAL A 755 ASP A 757 1 O VAL A 755 N VAL A 731
SHEET 1 B 2 HIS A 77 LEU A 78 0
SHEET 2 B 2 THR A 113 ILE A 114 1 O THR A 113 N LEU A 78
SHEET 1 C 2 VAL A 157 LEU A 158 0
SHEET 2 C 2 LYS A 189 VAL A 190 1 O LYS A 189 N LEU A 158
SHEET 1 D 2 LYS A 234 LEU A 235 0
SHEET 2 D 2 HIS A 274 LEU A 275 1 O HIS A 274 N LEU A 235
SHEET 1 E 2 LEU A 378 LEU A 379 0
SHEET 2 E 2 GLN A 405 ALA A 406 1 O GLN A 405 N LEU A 379
SHEET 1 F 2 ASN A 597 SER A 598 0
SHEET 2 F 2 GLY A 627 LEU A 628 1 O GLY A 627 N SER A 598
SHEET 1 G 2 LEU A 763 HIS A 764 0
SHEET 2 G 2 CYS A 791 SER A 793 1 O GLY A 792 N LEU A 763
SSBOND 1 CYS A 35 CYS A 45 1555 1555 2.03
SSBOND 2 CYS A 98 CYS A 110 1555 1555 2.03
SSBOND 3 CYS A 178 CYS A 184 1555 1555 2.04
SSBOND 4 CYS A 255 CYS A 268 1555 1555 2.04
SSBOND 5 CYS A 258 CYS A 265 1555 1555 2.02
SSBOND 6 CYS A 471 CYS A 501 1555 1555 2.04
SSBOND 7 CYS A 765 CYS A 791 1555 1555 2.03
SSBOND 8 CYS A 767 CYS A 810 1555 1555 2.04
LINK ND2 ASN A 210 C1 NAG A 903 1555 1555 1.44
LINK ND2 ASN A 332 C1 NAG A 902 1555 1555 1.47
LINK ND2 ASN A 732 C1 NAG A 901 1555 1555 1.52
CISPEP 1 LEU A 33 PRO A 34 0 3.79
CISPEP 2 THR A 101 GLY A 102 0 -6.29
CISPEP 3 ALA A 164 GLY A 165 0 -22.03
CISPEP 4 ARG A 470 CYS A 471 0 -6.81
CISPEP 5 GLN A 695 GLY A 696 0 -0.19
CISPEP 6 ASN A 700 GLY A 701 0 -15.09
CISPEP 7 SER A 793 PRO A 794 0 3.52
CRYST1 71.260 119.280 130.410 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 0.014033 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008384 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007668 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
