HEADER IMMUNE SYSTEM 22-DEC-12 3W3J
TITLE CRYSTAL STRUCTURE OF HUMAN TLR8 IN COMPLEX WITH CL097
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLL-LIKE RECEPTOR 8;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 27-827;
COMPND 5 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: TLR8, UNQ249/PRO286;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7215;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: S2
KEYWDS LEUCINE RICH REPEAT, RNA, GLYCOSYLATION, RNA RECOGNITION, SSRNA,
KEYWDS 2 RECEPTOR, RNA RECEPTOR, INNATE IMMUNITY, RNA BINDING, SECRETED,
KEYWDS 3 CL097, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR H.TANJI,U.OHTO,T.SHIMIZU
REVDAT 2 29-JUL-20 3W3J 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 LINK SITE ATOM
REVDAT 1 03-APR-13 3W3J 0
JRNL AUTH H.TANJI,U.OHTO,T.SHIBATA,K.MIYAKE,T.SHIMIZU
JRNL TITL STRUCTURAL REORGANIZATION OF THE TOLL-LIKE RECEPTOR 8 DIMER
JRNL TITL 2 INDUCED BY AGONISTIC LIGANDS
JRNL REF SCIENCE V. 339 1426 2013
JRNL REFN ISSN 0036-8075
JRNL PMID 23520111
JRNL DOI 10.1126/SCIENCE.1229159
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 114600
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5748
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 40.4394 - 6.2072 0.96 3626 200 0.2197 0.2442
REMARK 3 2 6.2072 - 4.9297 1.00 3745 187 0.1921 0.2130
REMARK 3 3 4.9297 - 4.3073 1.00 3738 179 0.1627 0.2032
REMARK 3 4 4.3073 - 3.9139 1.00 3713 198 0.1548 0.1903
REMARK 3 5 3.9139 - 3.6335 1.00 3714 209 0.1532 0.1929
REMARK 3 6 3.6335 - 3.4194 1.00 3716 190 0.1637 0.2065
REMARK 3 7 3.4194 - 3.2482 1.00 3712 190 0.1694 0.2178
REMARK 3 8 3.2482 - 3.1069 1.00 3687 205 0.1800 0.2471
REMARK 3 9 3.1069 - 2.9873 0.99 3666 208 0.1833 0.2394
REMARK 3 10 2.9873 - 2.8843 0.99 3672 196 0.1936 0.2343
REMARK 3 11 2.8843 - 2.7941 0.98 3616 210 0.1898 0.2417
REMARK 3 12 2.7941 - 2.7143 0.98 3612 210 0.1871 0.2552
REMARK 3 13 2.7143 - 2.6428 0.98 3593 193 0.1918 0.2726
REMARK 3 14 2.6428 - 2.5784 0.97 3570 202 0.1941 0.2359
REMARK 3 15 2.5784 - 2.5197 0.97 3582 198 0.1942 0.2524
REMARK 3 16 2.5197 - 2.4661 0.97 3581 207 0.1884 0.2484
REMARK 3 17 2.4661 - 2.4168 0.96 3563 208 0.1956 0.2680
REMARK 3 18 2.4168 - 2.3712 0.96 3580 167 0.2115 0.2577
REMARK 3 19 2.3712 - 2.3289 0.97 3555 176 0.2146 0.2774
REMARK 3 20 2.3289 - 2.2894 0.97 3592 175 0.2075 0.2451
REMARK 3 21 2.2894 - 2.2525 0.97 3613 176 0.2180 0.2892
REMARK 3 22 2.2525 - 2.2178 0.97 3586 187 0.2221 0.2687
REMARK 3 23 2.2178 - 2.1852 0.97 3610 167 0.2248 0.2835
REMARK 3 24 2.1852 - 2.1544 0.97 3561 205 0.2295 0.2627
REMARK 3 25 2.1544 - 2.1253 0.97 3573 183 0.2378 0.2930
REMARK 3 26 2.1253 - 2.0977 0.98 3616 176 0.2560 0.3306
REMARK 3 27 2.0977 - 2.0715 0.97 3636 190 0.2573 0.3108
REMARK 3 28 2.0715 - 2.0465 0.98 3561 199 0.2667 0.3187
REMARK 3 29 2.0465 - 2.0227 0.98 3658 179 0.2782 0.3440
REMARK 3 30 2.0227 - 2.0000 0.98 3605 178 0.2708 0.3183
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.860
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.26
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 12711
REMARK 3 ANGLE : 1.045 17263
REMARK 3 CHIRALITY : 0.067 2020
REMARK 3 PLANARITY : 0.004 2164
REMARK 3 DIHEDRAL : 19.298 4772
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): 22.8308 4.7130 21.5116
REMARK 3 T TENSOR
REMARK 3 T11: 0.1832 T22: 0.2242
REMARK 3 T33: 0.1964 T12: 0.0246
REMARK 3 T13: -0.0220 T23: 0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.9625 L22: 0.4612
REMARK 3 L33: 0.5561 L12: 0.2740
REMARK 3 L13: -0.3533 L23: -0.1850
REMARK 3 S TENSOR
REMARK 3 S11: 0.0069 S12: -0.2096 S13: 0.1235
REMARK 3 S21: 0.1039 S22: 0.0137 S23: 0.0958
REMARK 3 S31: -0.1138 S32: 0.0934 S33: -0.0213
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 3W3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000095840.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 5.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
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 : 114639
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 42.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14%(W/V) PEG3350, 0.2M POTASSIUM
REMARK 280 FORMATE, 0.1M SODIUM CITRATE, PH 5.1, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 74.37500
REMARK 290 SMTRY3 2 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER (CHAIN A,B) IN THE
REMARK 300 ASSYMMETRIC 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 23
REMARK 465 SER A 24
REMARK 465 PRO A 25
REMARK 465 TRP A 26
REMARK 465 GLU A 27
REMARK 465 GLU A 28
REMARK 465 ASN A 29
REMARK 465 PHE A 30
REMARK 465 ASN A 42
REMARK 465 ASP A 43
REMARK 465 SER A 44
REMARK 465 GLN A 101
REMARK 465 HIS A 102
REMARK 465 GLN A 103
REMARK 465 ASN A 104
REMARK 465 GLY A 105
REMARK 465 ASN A 106
REMARK 465 PRO A 107
REMARK 465 GLY A 108
REMARK 465 ILE A 109
REMARK 465 GLN A 110
REMARK 465 SER A 111
REMARK 465 ASN A 112
REMARK 465 LEU A 433
REMARK 465 VAL A 434
REMARK 465 LYS A 435
REMARK 465 ASP A 436
REMARK 465 THR A 437
REMARK 465 ARG A 438
REMARK 465 GLN A 439
REMARK 465 SER A 440
REMARK 465 TYR A 441
REMARK 465 ALA A 442
REMARK 465 ASN A 443
REMARK 465 SER A 444
REMARK 465 SER A 445
REMARK 465 SER A 446
REMARK 465 PHE A 447
REMARK 465 GLN A 448
REMARK 465 ARG A 449
REMARK 465 HIS A 450
REMARK 465 ILE A 451
REMARK 465 ARG A 452
REMARK 465 LYS A 453
REMARK 465 ARG A 454
REMARK 465 ARG A 455
REMARK 465 SER A 456
REMARK 465 THR A 457
REMARK 465 GLU A 818
REMARK 465 LEU A 819
REMARK 465 THR A 820
REMARK 465 THR A 821
REMARK 465 CYS A 822
REMARK 465 VAL A 823
REMARK 465 SER A 824
REMARK 465 ASP A 825
REMARK 465 VAL A 826
REMARK 465 THR A 827
REMARK 465 GLU A 828
REMARK 465 PHE A 829
REMARK 465 LEU A 830
REMARK 465 VAL A 831
REMARK 465 PRO A 832
REMARK 465 ARG A 833
REMARK 465 ARG B 23
REMARK 465 SER B 24
REMARK 465 PRO B 25
REMARK 465 TRP B 26
REMARK 465 GLU B 27
REMARK 465 GLU B 28
REMARK 465 ASN B 29
REMARK 465 PHE B 30
REMARK 465 ASN B 42
REMARK 465 ASP B 43
REMARK 465 SER B 44
REMARK 465 GLN B 101
REMARK 465 HIS B 102
REMARK 465 GLN B 103
REMARK 465 ASN B 104
REMARK 465 GLY B 105
REMARK 465 ASN B 106
REMARK 465 PRO B 107
REMARK 465 GLY B 108
REMARK 465 ILE B 109
REMARK 465 GLN B 110
REMARK 465 SER B 111
REMARK 465 ASN B 112
REMARK 465 LEU B 433
REMARK 465 VAL B 434
REMARK 465 LYS B 435
REMARK 465 ASP B 436
REMARK 465 THR B 437
REMARK 465 ARG B 438
REMARK 465 GLN B 439
REMARK 465 SER B 440
REMARK 465 TYR B 441
REMARK 465 ALA B 442
REMARK 465 ASN B 443
REMARK 465 SER B 444
REMARK 465 SER B 445
REMARK 465 SER B 446
REMARK 465 PHE B 447
REMARK 465 GLN B 448
REMARK 465 ARG B 449
REMARK 465 HIS B 450
REMARK 465 ILE B 451
REMARK 465 ARG B 452
REMARK 465 LYS B 453
REMARK 465 ARG B 454
REMARK 465 ARG B 455
REMARK 465 SER B 456
REMARK 465 THR B 457
REMARK 465 ASP B 458
REMARK 465 GLU B 818
REMARK 465 LEU B 819
REMARK 465 THR B 820
REMARK 465 THR B 821
REMARK 465 CYS B 822
REMARK 465 VAL B 823
REMARK 465 SER B 824
REMARK 465 ASP B 825
REMARK 465 VAL B 826
REMARK 465 THR B 827
REMARK 465 GLU B 828
REMARK 465 PHE B 829
REMARK 465 LEU B 830
REMARK 465 VAL B 831
REMARK 465 PRO B 832
REMARK 465 ARG B 833
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 SER A 31 OG
REMARK 470 LYS A 40 CG CD CE NZ
REMARK 470 GLN A 41 CG CD OE1 NE2
REMARK 470 VAL A 100 CG1 CG2
REMARK 470 GLU A 757 CG CD OE1 OE2
REMARK 470 THR A 758 OG1 CG2
REMARK 470 LYS A 759 CG CD CE NZ
REMARK 470 THR A 760 OG1 CG2
REMARK 470 THR A 761 OG1 CG2
REMARK 470 THR A 762 OG1 CG2
REMARK 470 LEU A 817 CG CD1 CD2
REMARK 470 SER B 31 OG
REMARK 470 LYS B 40 CG CD CE NZ
REMARK 470 GLN B 41 CG CD OE1 NE2
REMARK 470 GLU B 757 CG CD OE1 OE2
REMARK 470 THR B 758 OG1 CG2
REMARK 470 LYS B 759 CG CD CE NZ
REMARK 470 THR B 760 OG1 CG2
REMARK 470 THR B 761 OG1 CG2
REMARK 470 THR B 762 OG1 CG2
REMARK 470 LEU B 817 CG CD1 CD2
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 OD2 ASP B 386 O HOH B 1204 2.06
REMARK 500 O HOH B 1094 O HOH B 1204 2.10
REMARK 500 O3 SO4 A 1016 O HOH A 1538 2.11
REMARK 500 OD1 ASN A 503 O HOH A 1320 2.13
REMARK 500 O LYS B 677 O HOH B 1371 2.14
REMARK 500 OE2 GLU A 326 O HOH A 1461 2.15
REMARK 500 O HOH A 1248 O HOH A 1431 2.16
REMARK 500 O HOH A 1478 O HOH A 1538 2.17
REMARK 500 OE1 GLN A 288 O HOH A 1474 2.18
REMARK 500 O PHE B 702 O HOH B 1055 2.18
REMARK 500 O HOH A 1501 O HOH A 1508 2.18
REMARK 500 O LEU A 701 O HOH A 1308 2.19
REMARK 500 OD2 ASP B 487 O HOH B 1266 2.19
REMARK 500 OD2 ASP B 462 O6 MAN F 4 2.19
REMARK 500 O HOH A 1296 O HOH A 1341 2.19
REMARK 500 O HOH A 1371 O HOH A 1450 2.19
REMARK 500 O HOH B 1323 O HOH B 1360 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 O3 NAG B 914 O HOH A 1474 1655 2.06
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 A 53 21.39 48.00
REMARK 500 ASN A 73 -152.80 -104.42
REMARK 500 PHE A 83 73.18 -119.36
REMARK 500 LEU A 132 55.30 -115.69
REMARK 500 PHE A 183 -128.66 54.69
REMARK 500 SER A 214 -16.53 61.19
REMARK 500 LEU A 286 53.68 -90.25
REMARK 500 ASN A 321 -162.43 -116.38
REMARK 500 TYR A 353 67.73 -150.04
REMARK 500 VAL A 378 110.33 76.29
REMARK 500 ASN A 419 63.06 -155.50
REMARK 500 GLU A 427 55.83 70.27
REMARK 500 ASN A 428 -150.69 -125.62
REMARK 500 ARG A 472 151.27 -48.97
REMARK 500 ASN A 491 -156.68 -115.60
REMARK 500 ASP A 506 86.22 -69.78
REMARK 500 ASN A 540 -156.62 -108.66
REMARK 500 ASP A 601 -58.46 68.23
REMARK 500 ASN A 618 -165.26 -116.40
REMARK 500 ASN A 674 -150.24 -110.88
REMARK 500 ASN A 698 -155.95 -124.78
REMARK 500 SER A 706 36.96 -142.32
REMARK 500 ASN A 722 -159.62 -123.77
REMARK 500 GLU A 734 -79.00 -57.72
REMARK 500 VAL A 735 -66.66 -5.33
REMARK 500 SER A 736 -31.78 46.71
REMARK 500 ASN A 746 -151.93 -112.03
REMARK 500 GLU A 757 -56.47 49.90
REMARK 500 THR A 777 -152.55 -129.35
REMARK 500 HIS A 790 77.14 -100.02
REMARK 500 TYR B 34 138.74 -173.43
REMARK 500 THR B 60 31.45 -82.12
REMARK 500 ASN B 73 -168.37 -109.67
REMARK 500 LEU B 86 63.57 -115.85
REMARK 500 ASN B 99 54.59 -64.17
REMARK 500 ASN B 156 -168.46 -123.82
REMARK 500 PHE B 183 -134.92 47.27
REMARK 500 SER B 214 -32.21 73.16
REMARK 500 PRO B 264 30.54 -85.43
REMARK 500 MET B 310 61.90 -117.93
REMARK 500 ASN B 321 -156.56 -112.12
REMARK 500 SER B 329 -71.23 -118.14
REMARK 500 VAL B 378 103.15 69.13
REMARK 500 ASN B 419 27.53 -157.25
REMARK 500 ASN B 428 -152.19 -126.65
REMARK 500 ASN B 491 -156.10 -121.19
REMARK 500 PRO B 505 -174.62 -69.47
REMARK 500 ASN B 540 -155.38 -114.87
REMARK 500 ASN B 564 53.66 -118.30
REMARK 500 ASP B 601 -59.61 64.15
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3W3G RELATED DB: PDB
REMARK 900 RELATED ID: 3W3K RELATED DB: PDB
REMARK 900 RELATED ID: 3W3L RELATED DB: PDB
REMARK 900 RELATED ID: 3W3M RELATED DB: PDB
REMARK 900 RELATED ID: 3W3N RELATED DB: PDB
DBREF 3W3J A 27 827 UNP Q9NR97 TLR8_HUMAN 27 827
DBREF 3W3J B 27 827 UNP Q9NR97 TLR8_HUMAN 27 827
SEQADV 3W3J ARG A 23 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J SER A 24 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J PRO A 25 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J TRP A 26 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J GLU A 828 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J PHE A 829 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J LEU A 830 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J VAL A 831 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J PRO A 832 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J ARG A 833 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J ARG B 23 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J SER B 24 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J PRO B 25 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J TRP B 26 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J GLU B 828 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J PHE B 829 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J LEU B 830 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J VAL B 831 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J PRO B 832 UNP Q9NR97 EXPRESSION TAG
SEQADV 3W3J ARG B 833 UNP Q9NR97 EXPRESSION TAG
SEQRES 1 A 811 ARG SER PRO TRP GLU GLU ASN PHE SER ARG SER TYR PRO
SEQRES 2 A 811 CYS ASP GLU LYS LYS GLN ASN ASP SER VAL ILE ALA GLU
SEQRES 3 A 811 CYS SER ASN ARG ARG LEU GLN GLU VAL PRO GLN THR VAL
SEQRES 4 A 811 GLY LYS TYR VAL THR GLU LEU ASP LEU SER ASP ASN PHE
SEQRES 5 A 811 ILE THR HIS ILE THR ASN GLU SER PHE GLN GLY LEU GLN
SEQRES 6 A 811 ASN LEU THR LYS ILE ASN LEU ASN HIS ASN PRO ASN VAL
SEQRES 7 A 811 GLN HIS GLN ASN GLY ASN PRO GLY ILE GLN SER ASN GLY
SEQRES 8 A 811 LEU ASN ILE THR ASP GLY ALA PHE LEU ASN LEU LYS ASN
SEQRES 9 A 811 LEU ARG GLU LEU LEU LEU GLU ASP ASN GLN LEU PRO GLN
SEQRES 10 A 811 ILE PRO SER GLY LEU PRO GLU SER LEU THR GLU LEU SER
SEQRES 11 A 811 LEU ILE GLN ASN ASN ILE TYR ASN ILE THR LYS GLU GLY
SEQRES 12 A 811 ILE SER ARG LEU ILE ASN LEU LYS ASN LEU TYR LEU ALA
SEQRES 13 A 811 TRP ASN CYS TYR PHE ASN LYS VAL CYS GLU LYS THR ASN
SEQRES 14 A 811 ILE GLU ASP GLY VAL PHE GLU THR LEU THR ASN LEU GLU
SEQRES 15 A 811 LEU LEU SER LEU SER PHE ASN SER LEU SER HIS VAL PRO
SEQRES 16 A 811 PRO LYS LEU PRO SER SER LEU ARG LYS LEU PHE LEU SER
SEQRES 17 A 811 ASN THR GLN ILE LYS TYR ILE SER GLU GLU ASP PHE LYS
SEQRES 18 A 811 GLY LEU ILE ASN LEU THR LEU LEU ASP LEU SER GLY ASN
SEQRES 19 A 811 CYS PRO ARG CYS PHE ASN ALA PRO PHE PRO CYS VAL PRO
SEQRES 20 A 811 CYS ASP GLY GLY ALA SER ILE ASN ILE ASP ARG PHE ALA
SEQRES 21 A 811 PHE GLN ASN LEU THR GLN LEU ARG TYR LEU ASN LEU SER
SEQRES 22 A 811 SER THR SER LEU ARG LYS ILE ASN ALA ALA TRP PHE LYS
SEQRES 23 A 811 ASN MET PRO HIS LEU LYS VAL LEU ASP LEU GLU PHE ASN
SEQRES 24 A 811 TYR LEU VAL GLY GLU ILE ALA SER GLY ALA PHE LEU THR
SEQRES 25 A 811 MET LEU PRO ARG LEU GLU ILE LEU ASP LEU SER PHE ASN
SEQRES 26 A 811 TYR ILE LYS GLY SER TYR PRO GLN HIS ILE ASN ILE SER
SEQRES 27 A 811 ARG ASN PHE SER LYS LEU LEU SER LEU ARG ALA LEU HIS
SEQRES 28 A 811 LEU ARG GLY TYR VAL PHE GLN GLU LEU ARG GLU ASP ASP
SEQRES 29 A 811 PHE GLN PRO LEU MET GLN LEU PRO ASN LEU SER THR ILE
SEQRES 30 A 811 ASN LEU GLY ILE ASN PHE ILE LYS GLN ILE ASP PHE LYS
SEQRES 31 A 811 LEU PHE GLN ASN PHE SER ASN LEU GLU ILE ILE TYR LEU
SEQRES 32 A 811 SER GLU ASN ARG ILE SER PRO LEU VAL LYS ASP THR ARG
SEQRES 33 A 811 GLN SER TYR ALA ASN SER SER SER PHE GLN ARG HIS ILE
SEQRES 34 A 811 ARG LYS ARG ARG SER THR ASP PHE GLU PHE ASP PRO HIS
SEQRES 35 A 811 SER ASN PHE TYR HIS PHE THR ARG PRO LEU ILE LYS PRO
SEQRES 36 A 811 GLN CYS ALA ALA TYR GLY LYS ALA LEU ASP LEU SER LEU
SEQRES 37 A 811 ASN SER ILE PHE PHE ILE GLY PRO ASN GLN PHE GLU ASN
SEQRES 38 A 811 LEU PRO ASP ILE ALA CYS LEU ASN LEU SER ALA ASN SER
SEQRES 39 A 811 ASN ALA GLN VAL LEU SER GLY THR GLU PHE SER ALA ILE
SEQRES 40 A 811 PRO HIS VAL LYS TYR LEU ASP LEU THR ASN ASN ARG LEU
SEQRES 41 A 811 ASP PHE ASP ASN ALA SER ALA LEU THR GLU LEU SER ASP
SEQRES 42 A 811 LEU GLU VAL LEU ASP LEU SER TYR ASN SER HIS TYR PHE
SEQRES 43 A 811 ARG ILE ALA GLY VAL THR HIS HIS LEU GLU PHE ILE GLN
SEQRES 44 A 811 ASN PHE THR ASN LEU LYS VAL LEU ASN LEU SER HIS ASN
SEQRES 45 A 811 ASN ILE TYR THR LEU THR ASP LYS TYR ASN LEU GLU SER
SEQRES 46 A 811 LYS SER LEU VAL GLU LEU VAL PHE SER GLY ASN ARG LEU
SEQRES 47 A 811 ASP ILE LEU TRP ASN ASP ASP ASP ASN ARG TYR ILE SER
SEQRES 48 A 811 ILE PHE LYS GLY LEU LYS ASN LEU THR ARG LEU ASP LEU
SEQRES 49 A 811 SER LEU ASN ARG LEU LYS HIS ILE PRO ASN GLU ALA PHE
SEQRES 50 A 811 LEU ASN LEU PRO ALA SER LEU THR GLU LEU HIS ILE ASN
SEQRES 51 A 811 ASP ASN MET LEU LYS PHE PHE ASN TRP THR LEU LEU GLN
SEQRES 52 A 811 GLN PHE PRO ARG LEU GLU LEU LEU ASP LEU ARG GLY ASN
SEQRES 53 A 811 LYS LEU LEU PHE LEU THR ASP SER LEU SER ASP PHE THR
SEQRES 54 A 811 SER SER LEU ARG THR LEU LEU LEU SER HIS ASN ARG ILE
SEQRES 55 A 811 SER HIS LEU PRO SER GLY PHE LEU SER GLU VAL SER SER
SEQRES 56 A 811 LEU LYS HIS LEU ASP LEU SER SER ASN LEU LEU LYS THR
SEQRES 57 A 811 ILE ASN LYS SER ALA LEU GLU THR LYS THR THR THR LYS
SEQRES 58 A 811 LEU SER MET LEU GLU LEU HIS GLY ASN PRO PHE GLU CYS
SEQRES 59 A 811 THR CYS ASP ILE GLY ASP PHE ARG ARG TRP MET ASP GLU
SEQRES 60 A 811 HIS LEU ASN VAL LYS ILE PRO ARG LEU VAL ASP VAL ILE
SEQRES 61 A 811 CYS ALA SER PRO GLY ASP GLN ARG GLY LYS SER ILE VAL
SEQRES 62 A 811 SER LEU GLU LEU THR THR CYS VAL SER ASP VAL THR GLU
SEQRES 63 A 811 PHE LEU VAL PRO ARG
SEQRES 1 B 811 ARG SER PRO TRP GLU GLU ASN PHE SER ARG SER TYR PRO
SEQRES 2 B 811 CYS ASP GLU LYS LYS GLN ASN ASP SER VAL ILE ALA GLU
SEQRES 3 B 811 CYS SER ASN ARG ARG LEU GLN GLU VAL PRO GLN THR VAL
SEQRES 4 B 811 GLY LYS TYR VAL THR GLU LEU ASP LEU SER ASP ASN PHE
SEQRES 5 B 811 ILE THR HIS ILE THR ASN GLU SER PHE GLN GLY LEU GLN
SEQRES 6 B 811 ASN LEU THR LYS ILE ASN LEU ASN HIS ASN PRO ASN VAL
SEQRES 7 B 811 GLN HIS GLN ASN GLY ASN PRO GLY ILE GLN SER ASN GLY
SEQRES 8 B 811 LEU ASN ILE THR ASP GLY ALA PHE LEU ASN LEU LYS ASN
SEQRES 9 B 811 LEU ARG GLU LEU LEU LEU GLU ASP ASN GLN LEU PRO GLN
SEQRES 10 B 811 ILE PRO SER GLY LEU PRO GLU SER LEU THR GLU LEU SER
SEQRES 11 B 811 LEU ILE GLN ASN ASN ILE TYR ASN ILE THR LYS GLU GLY
SEQRES 12 B 811 ILE SER ARG LEU ILE ASN LEU LYS ASN LEU TYR LEU ALA
SEQRES 13 B 811 TRP ASN CYS TYR PHE ASN LYS VAL CYS GLU LYS THR ASN
SEQRES 14 B 811 ILE GLU ASP GLY VAL PHE GLU THR LEU THR ASN LEU GLU
SEQRES 15 B 811 LEU LEU SER LEU SER PHE ASN SER LEU SER HIS VAL PRO
SEQRES 16 B 811 PRO LYS LEU PRO SER SER LEU ARG LYS LEU PHE LEU SER
SEQRES 17 B 811 ASN THR GLN ILE LYS TYR ILE SER GLU GLU ASP PHE LYS
SEQRES 18 B 811 GLY LEU ILE ASN LEU THR LEU LEU ASP LEU SER GLY ASN
SEQRES 19 B 811 CYS PRO ARG CYS PHE ASN ALA PRO PHE PRO CYS VAL PRO
SEQRES 20 B 811 CYS ASP GLY GLY ALA SER ILE ASN ILE ASP ARG PHE ALA
SEQRES 21 B 811 PHE GLN ASN LEU THR GLN LEU ARG TYR LEU ASN LEU SER
SEQRES 22 B 811 SER THR SER LEU ARG LYS ILE ASN ALA ALA TRP PHE LYS
SEQRES 23 B 811 ASN MET PRO HIS LEU LYS VAL LEU ASP LEU GLU PHE ASN
SEQRES 24 B 811 TYR LEU VAL GLY GLU ILE ALA SER GLY ALA PHE LEU THR
SEQRES 25 B 811 MET LEU PRO ARG LEU GLU ILE LEU ASP LEU SER PHE ASN
SEQRES 26 B 811 TYR ILE LYS GLY SER TYR PRO GLN HIS ILE ASN ILE SER
SEQRES 27 B 811 ARG ASN PHE SER LYS LEU LEU SER LEU ARG ALA LEU HIS
SEQRES 28 B 811 LEU ARG GLY TYR VAL PHE GLN GLU LEU ARG GLU ASP ASP
SEQRES 29 B 811 PHE GLN PRO LEU MET GLN LEU PRO ASN LEU SER THR ILE
SEQRES 30 B 811 ASN LEU GLY ILE ASN PHE ILE LYS GLN ILE ASP PHE LYS
SEQRES 31 B 811 LEU PHE GLN ASN PHE SER ASN LEU GLU ILE ILE TYR LEU
SEQRES 32 B 811 SER GLU ASN ARG ILE SER PRO LEU VAL LYS ASP THR ARG
SEQRES 33 B 811 GLN SER TYR ALA ASN SER SER SER PHE GLN ARG HIS ILE
SEQRES 34 B 811 ARG LYS ARG ARG SER THR ASP PHE GLU PHE ASP PRO HIS
SEQRES 35 B 811 SER ASN PHE TYR HIS PHE THR ARG PRO LEU ILE LYS PRO
SEQRES 36 B 811 GLN CYS ALA ALA TYR GLY LYS ALA LEU ASP LEU SER LEU
SEQRES 37 B 811 ASN SER ILE PHE PHE ILE GLY PRO ASN GLN PHE GLU ASN
SEQRES 38 B 811 LEU PRO ASP ILE ALA CYS LEU ASN LEU SER ALA ASN SER
SEQRES 39 B 811 ASN ALA GLN VAL LEU SER GLY THR GLU PHE SER ALA ILE
SEQRES 40 B 811 PRO HIS VAL LYS TYR LEU ASP LEU THR ASN ASN ARG LEU
SEQRES 41 B 811 ASP PHE ASP ASN ALA SER ALA LEU THR GLU LEU SER ASP
SEQRES 42 B 811 LEU GLU VAL LEU ASP LEU SER TYR ASN SER HIS TYR PHE
SEQRES 43 B 811 ARG ILE ALA GLY VAL THR HIS HIS LEU GLU PHE ILE GLN
SEQRES 44 B 811 ASN PHE THR ASN LEU LYS VAL LEU ASN LEU SER HIS ASN
SEQRES 45 B 811 ASN ILE TYR THR LEU THR ASP LYS TYR ASN LEU GLU SER
SEQRES 46 B 811 LYS SER LEU VAL GLU LEU VAL PHE SER GLY ASN ARG LEU
SEQRES 47 B 811 ASP ILE LEU TRP ASN ASP ASP ASP ASN ARG TYR ILE SER
SEQRES 48 B 811 ILE PHE LYS GLY LEU LYS ASN LEU THR ARG LEU ASP LEU
SEQRES 49 B 811 SER LEU ASN ARG LEU LYS HIS ILE PRO ASN GLU ALA PHE
SEQRES 50 B 811 LEU ASN LEU PRO ALA SER LEU THR GLU LEU HIS ILE ASN
SEQRES 51 B 811 ASP ASN MET LEU LYS PHE PHE ASN TRP THR LEU LEU GLN
SEQRES 52 B 811 GLN PHE PRO ARG LEU GLU LEU LEU ASP LEU ARG GLY ASN
SEQRES 53 B 811 LYS LEU LEU PHE LEU THR ASP SER LEU SER ASP PHE THR
SEQRES 54 B 811 SER SER LEU ARG THR LEU LEU LEU SER HIS ASN ARG ILE
SEQRES 55 B 811 SER HIS LEU PRO SER GLY PHE LEU SER GLU VAL SER SER
SEQRES 56 B 811 LEU LYS HIS LEU ASP LEU SER SER ASN LEU LEU LYS THR
SEQRES 57 B 811 ILE ASN LYS SER ALA LEU GLU THR LYS THR THR THR LYS
SEQRES 58 B 811 LEU SER MET LEU GLU LEU HIS GLY ASN PRO PHE GLU CYS
SEQRES 59 B 811 THR CYS ASP ILE GLY ASP PHE ARG ARG TRP MET ASP GLU
SEQRES 60 B 811 HIS LEU ASN VAL LYS ILE PRO ARG LEU VAL ASP VAL ILE
SEQRES 61 B 811 CYS ALA SER PRO GLY ASP GLN ARG GLY LYS SER ILE VAL
SEQRES 62 B 811 SER LEU GLU LEU THR THR CYS VAL SER ASP VAL THR GLU
SEQRES 63 B 811 PHE LEU VAL PRO ARG
MODRES 3W3J ASN A 395 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN A 511 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN B 511 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN B 395 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN B 680 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN B 546 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN B 640 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN A 640 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN A 680 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN A 546 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN A 293 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN B 293 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN B 590 ASN GLYCOSYLATION SITE
MODRES 3W3J ASN A 590 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET MAN F 4 11
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET NAG A1007 14
HET NAG A1011 14
HET NAG A1012 14
HET NAG A1013 14
HET C09 A1014 18
HET SO4 A1015 5
HET SO4 A1016 5
HET SO4 A1017 5
HET SO4 A1018 5
HET SO4 A1019 5
HET SO4 A1020 5
HET SO4 A1021 5
HET SO4 A1022 5
HET C09 B 901 18
HET NAG B 908 14
HET NAG B 912 14
HET NAG B 913 14
HET NAG B 914 14
HET SO4 B 915 5
HET SO4 B 916 5
HET SO4 B 917 5
HET SO4 B 918 5
HET SO4 B 919 5
HET SO4 B 920 5
HET SO4 B 921 5
HET SO4 B 922 5
HET GOL B 923 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM C09 2-(ETHOXYMETHYL)-1H-IMIDAZO[4,5-C]QUINOLIN-4-AMINE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN C09 CL097
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 20(C8 H15 N O6)
FORMUL 3 BMA 4(C6 H12 O6)
FORMUL 3 MAN 2(C6 H12 O6)
FORMUL 13 C09 2(C13 H14 N4 O)
FORMUL 14 SO4 16(O4 S 2-)
FORMUL 35 GOL C3 H8 O3
FORMUL 36 HOH *861(H2 O)
HELIX 1 1 THR A 162 SER A 167 1 6
HELIX 2 2 CYS A 270 ALA A 274 5 5
HELIX 3 3 ASN A 303 LYS A 308 5 6
HELIX 4 4 LEU A 323 SER A 329 1 7
HELIX 5 5 ALA A 331 LEU A 336 5 6
HELIX 6 6 SER A 360 LEU A 366 5 7
HELIX 7 7 ARG A 383 MET A 391 5 9
HELIX 8 8 PHE A 411 PHE A 417 5 7
HELIX 9 9 LYS A 476 ALA A 481 1 6
HELIX 10 10 ASN A 564 ARG A 569 1 6
HELIX 11 11 LEU A 577 PHE A 583 5 7
HELIX 12 12 ARG A 619 TRP A 624 1 6
HELIX 13 13 PRO A 655 ASN A 661 1 7
HELIX 14 14 ASN A 680 PHE A 687 5 8
HELIX 15 15 SER A 706 PHE A 710 5 5
HELIX 16 16 PHE A 731 SER A 736 1 6
HELIX 17 17 ASN A 752 GLU A 757 1 6
HELIX 18 18 THR A 777 ASP A 779 5 3
HELIX 19 19 ILE A 780 HIS A 790 1 11
HELIX 20 20 ARG A 797 VAL A 801 5 5
HELIX 21 21 PRO A 806 ARG A 810 5 5
HELIX 22 22 CYS B 270 ALA B 274 5 5
HELIX 23 23 ASN B 303 LYS B 308 5 6
HELIX 24 24 LEU B 323 SER B 329 1 7
HELIX 25 25 GLY B 330 LEU B 336 5 7
HELIX 26 26 SER B 360 LEU B 366 5 7
HELIX 27 27 GLU B 384 MET B 391 5 8
HELIX 28 28 PHE B 411 PHE B 417 5 7
HELIX 29 29 LYS B 476 ALA B 481 1 6
HELIX 30 30 ASN B 564 ARG B 569 1 6
HELIX 31 31 LEU B 577 PHE B 583 5 7
HELIX 32 32 ARG B 619 TRP B 624 1 6
HELIX 33 33 PRO B 655 ASN B 661 1 7
HELIX 34 34 ASN B 680 PHE B 687 5 8
HELIX 35 35 SER B 706 PHE B 710 5 5
HELIX 36 36 GLY B 730 VAL B 735 1 6
HELIX 37 37 LYS B 753 GLU B 757 5 5
HELIX 38 38 THR B 777 ASP B 779 5 3
HELIX 39 39 ILE B 780 GLU B 789 1 10
HELIX 40 40 ARG B 797 VAL B 801 5 5
HELIX 41 41 SER B 813 LEU B 817 5 5
SHEET 1 A28 ASP A 37 LYS A 39 0
SHEET 2 A28 ILE A 46 GLU A 48 -1 O ILE A 46 N LYS A 39
SHEET 3 A28 GLU A 67 ASP A 69 1 O GLU A 67 N ALA A 47
SHEET 4 A28 LYS A 91 ASN A 93 1 O LYS A 91 N LEU A 68
SHEET 5 A28 GLU A 129 LEU A 131 1 O GLU A 129 N ILE A 92
SHEET 6 A28 GLU A 150 SER A 152 1 O GLU A 150 N LEU A 130
SHEET 7 A28 ASN A 174 TYR A 176 1 O TYR A 176 N LEU A 151
SHEET 8 A28 LEU A 205 SER A 207 1 O SER A 207 N LEU A 175
SHEET 9 A28 LYS A 226 PHE A 228 1 O PHE A 228 N LEU A 206
SHEET 10 A28 LEU A 250 ASP A 252 1 O ASP A 252 N LEU A 227
SHEET 11 A28 TYR A 291 ASN A 293 1 O ASN A 293 N LEU A 251
SHEET 12 A28 VAL A 315 ASP A 317 1 O ASP A 317 N LEU A 292
SHEET 13 A28 ILE A 341 ASP A 343 1 O ILE A 341 N LEU A 316
SHEET 14 A28 ALA A 371 HIS A 373 1 O HIS A 373 N LEU A 342
SHEET 15 A28 THR A 398 ASN A 400 1 O THR A 398 N LEU A 372
SHEET 16 A28 ILE A 422 TYR A 424 1 O TYR A 424 N ILE A 399
SHEET 17 A28 LYS A 484 ASP A 487 1 O ALA A 485 N ILE A 423
SHEET 18 A28 ILE A 507 ASN A 511 1 O CYS A 509 N LEU A 486
SHEET 19 A28 TYR A 534 ASP A 536 1 O ASP A 536 N LEU A 510
SHEET 20 A28 VAL A 558 ASP A 560 1 O VAL A 558 N LEU A 535
SHEET 21 A28 VAL A 588 ASN A 590 1 O VAL A 588 N LEU A 559
SHEET 22 A28 GLU A 612 VAL A 614 1 O GLU A 612 N LEU A 589
SHEET 23 A28 ARG A 643 ASP A 645 1 O ARG A 643 N LEU A 613
SHEET 24 A28 GLU A 668 HIS A 670 1 O HIS A 670 N LEU A 644
SHEET 25 A28 LEU A 692 ASP A 694 1 O ASP A 694 N LEU A 669
SHEET 26 A28 THR A 716 LEU A 718 1 O THR A 716 N LEU A 693
SHEET 27 A28 HIS A 740 ASP A 742 1 O ASP A 742 N LEU A 717
SHEET 28 A28 MET A 766 GLU A 768 1 O MET A 766 N LEU A 741
SHEET 1 B 2 HIS A 77 ILE A 78 0
SHEET 2 B 2 ASN A 115 ILE A 116 1 O ASN A 115 N ILE A 78
SHEET 1 C 2 ASN A 160 ILE A 161 0
SHEET 2 C 2 ASN A 191 ILE A 192 1 O ASN A 191 N ILE A 161
SHEET 1 D 2 TYR A 236 ILE A 237 0
SHEET 2 D 2 ASN A 277 ILE A 278 1 O ASN A 277 N ILE A 237
SHEET 1 E 2 GLU A 381 LEU A 382 0
SHEET 2 E 2 GLN A 408 ILE A 409 1 O GLN A 408 N LEU A 382
SHEET 1 F 2 GLU A 606 SER A 607 0
SHEET 2 F 2 GLY A 637 LEU A 638 1 O GLY A 637 N SER A 607
SHEET 1 G 2 PHE A 774 GLU A 775 0
SHEET 2 G 2 CYS A 803 SER A 805 1 O ALA A 804 N PHE A 774
SHEET 1 H28 ASP B 37 LYS B 39 0
SHEET 2 H28 ILE B 46 GLU B 48 -1 O GLU B 48 N ASP B 37
SHEET 3 H28 GLU B 67 ASP B 69 1 O GLU B 67 N ALA B 47
SHEET 4 H28 LYS B 91 ASN B 93 1 O LYS B 91 N LEU B 68
SHEET 5 H28 GLU B 129 LEU B 131 1 O GLU B 129 N ILE B 92
SHEET 6 H28 GLU B 150 SER B 152 1 O GLU B 150 N LEU B 130
SHEET 7 H28 ASN B 174 TYR B 176 1 O TYR B 176 N LEU B 151
SHEET 8 H28 LEU B 205 SER B 207 1 O LEU B 205 N LEU B 175
SHEET 9 H28 LYS B 226 PHE B 228 1 O PHE B 228 N LEU B 206
SHEET 10 H28 LEU B 250 ASP B 252 1 O ASP B 252 N LEU B 227
SHEET 11 H28 TYR B 291 ASN B 293 1 O ASN B 293 N LEU B 251
SHEET 12 H28 VAL B 315 ASP B 317 1 O ASP B 317 N LEU B 292
SHEET 13 H28 ILE B 341 ASP B 343 1 O ILE B 341 N LEU B 316
SHEET 14 H28 ALA B 371 HIS B 373 1 O HIS B 373 N LEU B 342
SHEET 15 H28 THR B 398 ASN B 400 1 O ASN B 400 N LEU B 372
SHEET 16 H28 ILE B 422 TYR B 424 1 O TYR B 424 N ILE B 399
SHEET 17 H28 LYS B 484 ASP B 487 1 O ALA B 485 N ILE B 423
SHEET 18 H28 ILE B 507 ASN B 511 1 O ALA B 508 N LYS B 484
SHEET 19 H28 TYR B 534 ASP B 536 1 O TYR B 534 N LEU B 510
SHEET 20 H28 VAL B 558 ASP B 560 1 O ASP B 560 N LEU B 535
SHEET 21 H28 VAL B 588 ASN B 590 1 O VAL B 588 N LEU B 559
SHEET 22 H28 GLU B 612 VAL B 614 1 O VAL B 614 N LEU B 589
SHEET 23 H28 ARG B 643 ASP B 645 1 O ARG B 643 N LEU B 613
SHEET 24 H28 GLU B 668 HIS B 670 1 O HIS B 670 N LEU B 644
SHEET 25 H28 LEU B 692 ASP B 694 1 O ASP B 694 N LEU B 669
SHEET 26 H28 THR B 716 LEU B 718 1 O LEU B 718 N LEU B 693
SHEET 27 H28 HIS B 740 ASP B 742 1 O ASP B 742 N LEU B 717
SHEET 28 H28 MET B 766 GLU B 768 1 O MET B 766 N LEU B 741
SHEET 1 I 2 HIS B 77 ILE B 78 0
SHEET 2 I 2 ASN B 115 ILE B 116 1 O ASN B 115 N ILE B 78
SHEET 1 J 2 ASN B 160 ILE B 161 0
SHEET 2 J 2 ASN B 191 ILE B 192 1 O ASN B 191 N ILE B 161
SHEET 1 K 2 TYR B 236 ILE B 237 0
SHEET 2 K 2 ASN B 277 ILE B 278 1 O ASN B 277 N ILE B 237
SHEET 1 L 2 GLU B 381 LEU B 382 0
SHEET 2 L 2 GLN B 408 ILE B 409 1 O GLN B 408 N LEU B 382
SHEET 1 M 2 GLU B 606 SER B 607 0
SHEET 2 M 2 GLY B 637 LEU B 638 1 O GLY B 637 N SER B 607
SHEET 1 N 2 PHE B 774 GLU B 775 0
SHEET 2 N 2 CYS B 803 SER B 805 1 O ALA B 804 N PHE B 774
SSBOND 1 CYS A 36 CYS A 49 1555 1555 2.03
SSBOND 2 CYS A 181 CYS A 187 1555 1555 2.04
SSBOND 3 CYS A 257 CYS A 270 1555 1555 2.03
SSBOND 4 CYS A 260 CYS A 267 1555 1555 2.04
SSBOND 5 CYS A 479 CYS A 509 1555 1555 2.02
SSBOND 6 CYS A 776 CYS A 803 1555 1555 2.02
SSBOND 7 CYS B 36 CYS B 49 1555 1555 2.04
SSBOND 8 CYS B 181 CYS B 187 1555 1555 2.04
SSBOND 9 CYS B 257 CYS B 270 1555 1555 2.04
SSBOND 10 CYS B 260 CYS B 267 1555 1555 2.05
SSBOND 11 CYS B 479 CYS B 509 1555 1555 2.04
SSBOND 12 CYS B 776 CYS B 803 1555 1555 2.03
LINK ND2 ASN A 293 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN A 395 C1 NAG A1012 1555 1555 1.43
LINK ND2 ASN A 511 C1 NAG D 1 1555 1555 1.43
LINK ND2 ASN A 546 C1 NAG A1007 1555 1555 1.45
LINK ND2 ASN A 590 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN A 640 C1 NAG A1013 1555 1555 1.44
LINK ND2 ASN A 680 C1 NAG A1011 1555 1555 1.45
LINK ND2 ASN B 293 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN B 395 C1 NAG B 913 1555 1555 1.44
LINK ND2 ASN B 511 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN B 546 C1 NAG B 908 1555 1555 1.44
LINK ND2 ASN B 590 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN B 640 C1 NAG B 914 1555 1555 1.44
LINK ND2 ASN B 680 C1 NAG B 912 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44
LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.44
CISPEP 1 TYR A 34 PRO A 35 0 3.95
CISPEP 2 ASN A 97 PRO A 98 0 -3.28
CISPEP 3 SER A 805 PRO A 806 0 -0.43
CISPEP 4 TYR B 34 PRO B 35 0 3.30
CISPEP 5 ASN B 97 PRO B 98 0 -5.01
CISPEP 6 SER B 805 PRO B 806 0 -7.74
CRYST1 71.380 148.750 85.770 90.00 103.39 90.00 P 1 21 1 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 0.014010 0.000000 0.003335 0.00000
SCALE2 0.000000 0.006723 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011985 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
