HEADER IMMUNE SYSTEM 16-JAN-17 5WYZ
TITLE CRYSTAL STRUCTURE OF HUMAN TLR8 IN COMPLEX WITH CU-CPT9B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLL-LIKE RECEPTOR 8;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, 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
KEYWDS IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR H.TANJI,U.OHTO,T.SHIMIZU
REVDAT 3 29-JUL-20 5WYZ 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 27-DEC-17 5WYZ 1 JRNL
REVDAT 1 13-DEC-17 5WYZ 0
JRNL AUTH S.ZHANG,Z.HU,H.TANJI,S.JIANG,N.DAS,J.LI,K.SAKANIWA,J.JIN,
JRNL AUTH 2 Y.BIAN,U.OHTO,T.SHIMIZU,H.YIN
JRNL TITL SMALL-MOLECULE INHIBITION OF TLR8 THROUGH STABILIZATION OF
JRNL TITL 2 ITS RESTING STATE
JRNL REF NAT. CHEM. BIOL. V. 14 58 2018
JRNL REFN ESSN 1552-4469
JRNL PMID 29155428
JRNL DOI 10.1038/NCHEMBIO.2518
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 132.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 78165
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4197
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5768
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 299
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12042
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 361
REMARK 3 SOLVENT ATOMS : 197
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.328
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.244
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.193
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.978
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12691 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 12097 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17248 ; 1.675 ; 2.003
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27741 ; 1.075 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1488 ; 7.281 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 600 ;38.876 ;24.933
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2184 ;16.546 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 62 ;15.666 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2033 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14040 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2924 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5973 ; 4.848 ; 5.821
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5972 ; 4.844 ; 5.821
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7456 ; 6.878 ; 8.718
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7456 ; 6.878 ; 8.719
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6718 ; 5.119 ; 6.257
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6718 ; 5.118 ; 6.257
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 9793 ; 7.634 ; 9.206
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 13886 ;10.186 ;46.275
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 13858 ;10.188 ;46.273
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 32 818 B 32 818 46845 0.12 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5WYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1300002633.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : NULL
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-5A
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 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78179
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 132.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
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: NULL
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 (%): 51.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, CALCIUM CHLORIDE, TRIS-HCL,
REMARK 280 ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 71.81000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.47500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.81000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.47500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 62440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 76.0 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 SER A 31
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 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 ASP A 458
REMARK 465 PHE A 459
REMARK 465 GLU A 460
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 SER B 31
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 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 PHE B 459
REMARK 465 GLU B 460
REMARK 465 SER B 754
REMARK 465 ALA B 755
REMARK 465 LEU B 756
REMARK 465 GLU B 757
REMARK 465 THR B 758
REMARK 465 LYS B 759
REMARK 465 THR B 760
REMARK 465 THR B 761
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 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 OG SER B 295 OE1 GLU B 319 2.07
REMARK 500 O LYS A 753 O LEU A 756 2.14
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 ASN B 80 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 LEU B 213 N - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 CYS B 509 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG B 689 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 689 NE - CZ - NH2 ANGL. DEV. = -3.5 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 ASN A 42 -119.48 55.75
REMARK 500 ASN A 73 -160.95 -126.73
REMARK 500 LEU A 86 54.35 -151.91
REMARK 500 ASN A 156 -161.51 -118.34
REMARK 500 SER A 214 -36.75 61.14
REMARK 500 CYS A 257 62.72 60.28
REMARK 500 ASN A 321 -158.13 -121.67
REMARK 500 SER A 329 -70.36 -107.28
REMARK 500 VAL A 378 102.76 82.34
REMARK 500 ASN A 491 -151.75 -108.72
REMARK 500 ASP A 506 103.30 -59.56
REMARK 500 ASN A 540 -167.05 -125.32
REMARK 500 TYR A 567 22.78 -66.09
REMARK 500 THR A 600 -107.99 -79.79
REMARK 500 SER A 607 132.99 -173.54
REMARK 500 ASN A 618 -162.96 -118.79
REMARK 500 ASN A 674 -146.82 -114.01
REMARK 500 ARG A 696 150.41 -48.12
REMARK 500 ASN A 698 -153.86 -121.18
REMARK 500 ASN A 722 -159.93 -124.07
REMARK 500 VAL A 735 -48.95 55.84
REMARK 500 SER A 736 -74.67 66.19
REMARK 500 SER A 745 50.53 38.74
REMARK 500 ASN A 746 -157.02 -111.40
REMARK 500 GLU A 757 -109.19 -129.01
REMARK 500 THR A 758 130.54 74.06
REMARK 500 THR A 760 -132.14 52.55
REMARK 500 ASN B 42 -141.50 57.42
REMARK 500 CYS B 49 30.80 -140.46
REMARK 500 ASN B 73 -161.73 -126.60
REMARK 500 ASN B 156 -162.17 -120.49
REMARK 500 CYS B 257 63.05 62.97
REMARK 500 ASN B 321 -156.89 -122.85
REMARK 500 SER B 329 -69.82 -108.23
REMARK 500 VAL B 378 103.81 79.90
REMARK 500 ASN B 428 -165.06 -110.16
REMARK 500 ASN B 491 -151.63 -109.90
REMARK 500 ASP B 506 102.49 -58.38
REMARK 500 ASN B 540 -167.67 -129.09
REMARK 500 TYR B 567 20.91 -65.65
REMARK 500 ASP B 601 -64.59 71.85
REMARK 500 SER B 607 134.95 -173.70
REMARK 500 ASN B 618 -164.78 -121.69
REMARK 500 ASN B 674 -159.47 -123.61
REMARK 500 ASN B 698 -156.09 -125.06
REMARK 500 ASN B 722 -162.13 -125.87
REMARK 500 LEU B 732 67.60 69.56
REMARK 500 ASN B 746 -156.69 -111.70
REMARK 500 CYS B 776 54.30 -92.10
REMARK 500 ARG B 810 125.58 -39.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 758 LYS A 759 42.22
REMARK 500 THR B 79 ASN B 80 145.03
REMARK 500 ASN B 80 GLU B 81 39.25
REMARK 500 ASP B 271 GLY B 272 -38.90
REMARK 500 PHE B 731 LEU B 732 -148.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5WYX RELATED DB: PDB
DBREF 5WYZ A 27 827 UNP Q9NR97 TLR8_HUMAN 27 827
DBREF 5WYZ B 27 827 UNP Q9NR97 TLR8_HUMAN 27 827
SEQADV 5WYZ ARG A 23 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ SER A 24 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ PRO A 25 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ TRP A 26 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ GLU A 828 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ PHE A 829 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ LEU A 830 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ VAL A 831 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ PRO A 832 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ ARG A 833 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ ARG B 23 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ SER B 24 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ PRO B 25 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ TRP B 26 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ GLU B 828 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ PHE B 829 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ LEU B 830 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ VAL B 831 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ PRO B 832 UNP Q9NR97 EXPRESSION TAG
SEQADV 5WYZ 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
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 MAN E 4 11
HET MAN E 5 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 MAN H 4 11
HET 7VF A 901 19
HET NAG A 906 14
HET NAG A 914 14
HET NAG A 915 14
HET 7VF B 901 19
HET NAG B 912 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM 7VF 4-(3-METHYL-4-OXIDANYL-PHENYL)QUINOLIN-7-OL
FORMUL 3 NAG 16(C8 H15 N O6)
FORMUL 3 BMA 4(C6 H12 O6)
FORMUL 3 MAN 5(C6 H12 O6)
FORMUL 9 7VF 2(C16 H13 N O2)
FORMUL 15 HOH *197(H2 O)
HELIX 1 AA1 THR A 162 SER A 167 1 6
HELIX 2 AA2 CYS A 270 ALA A 274 5 5
HELIX 3 AA3 ASN A 303 LYS A 308 5 6
HELIX 4 AA4 LEU A 323 SER A 329 1 7
HELIX 5 AA5 GLY A 330 LEU A 336 5 7
HELIX 6 AA6 SER A 360 LEU A 366 5 7
HELIX 7 AA7 ARG A 383 MET A 391 5 9
HELIX 8 AA8 PHE A 411 PHE A 417 5 7
HELIX 9 AA9 LYS A 476 ALA A 481 1 6
HELIX 10 AB1 LEU A 577 PHE A 583 5 7
HELIX 11 AB2 ARG A 619 TRP A 624 1 6
HELIX 12 AB3 PRO A 655 ASN A 661 1 7
HELIX 13 AB4 ASN A 680 PHE A 687 5 8
HELIX 14 AB5 SER A 706 PHE A 710 5 5
HELIX 15 AB6 THR A 777 ASP A 779 5 3
HELIX 16 AB7 ILE A 780 GLU A 789 1 10
HELIX 17 AB8 ARG A 797 VAL A 801 5 5
HELIX 18 AB9 THR B 162 SER B 167 1 6
HELIX 19 AC1 ASN B 303 LYS B 308 5 6
HELIX 20 AC2 LEU B 323 SER B 329 1 7
HELIX 21 AC3 GLY B 330 LEU B 336 5 7
HELIX 22 AC4 SER B 360 LEU B 366 5 7
HELIX 23 AC5 ARG B 383 MET B 391 5 9
HELIX 24 AC6 PHE B 411 PHE B 417 5 7
HELIX 25 AC7 LYS B 476 ALA B 481 1 6
HELIX 26 AC8 LEU B 577 PHE B 583 5 7
HELIX 27 AC9 ARG B 619 TRP B 624 1 6
HELIX 28 AD1 PRO B 655 ASN B 661 1 7
HELIX 29 AD2 ASN B 680 PHE B 687 5 8
HELIX 30 AD3 SER B 706 PHE B 710 5 5
HELIX 31 AD4 THR B 777 ASP B 779 5 3
HELIX 32 AD5 ILE B 780 GLU B 789 1 10
HELIX 33 AD6 ARG B 797 VAL B 801 5 5
SHEET 1 AA128 ASP A 37 GLN A 41 0
SHEET 2 AA128 SER A 44 GLU A 48 -1 O GLU A 48 N ASP A 37
SHEET 3 AA128 VAL A 65 ASP A 69 1 O THR A 66 N VAL A 45
SHEET 4 AA128 LYS A 91 ASN A 93 1 O ASN A 93 N LEU A 68
SHEET 5 AA128 GLU A 129 LEU A 131 1 O LEU A 131 N ILE A 92
SHEET 6 AA128 GLU A 150 SER A 152 1 O GLU A 150 N LEU A 130
SHEET 7 AA128 ASN A 174 TYR A 176 1 O TYR A 176 N LEU A 151
SHEET 8 AA128 LEU A 205 SER A 207 1 O LEU A 205 N LEU A 175
SHEET 9 AA128 LYS A 226 PHE A 228 1 O PHE A 228 N LEU A 206
SHEET 10 AA128 LEU A 250 ASP A 252 1 O LEU A 250 N LEU A 227
SHEET 11 AA128 TYR A 291 ASN A 293 1 O TYR A 291 N LEU A 251
SHEET 12 AA128 VAL A 315 ASP A 317 1 O VAL A 315 N LEU A 292
SHEET 13 AA128 ILE A 341 ASP A 343 1 O ILE A 341 N LEU A 316
SHEET 14 AA128 ALA A 371 HIS A 373 1 O HIS A 373 N LEU A 342
SHEET 15 AA128 THR A 398 ASN A 400 1 O ASN A 400 N LEU A 372
SHEET 16 AA128 ILE A 422 TYR A 424 1 O TYR A 424 N ILE A 399
SHEET 17 AA128 ALA A 485 ASP A 487 1 O ALA A 485 N ILE A 423
SHEET 18 AA128 CYS A 509 ASN A 511 1 O ASN A 511 N LEU A 486
SHEET 19 AA128 TYR A 534 ASP A 536 1 O ASP A 536 N LEU A 510
SHEET 20 AA128 VAL A 558 ASP A 560 1 O VAL A 558 N LEU A 535
SHEET 21 AA128 VAL A 588 ASN A 590 1 O VAL A 588 N LEU A 559
SHEET 22 AA128 GLU A 612 VAL A 614 1 O VAL A 614 N LEU A 589
SHEET 23 AA128 ARG A 643 ASP A 645 1 O ARG A 643 N LEU A 613
SHEET 24 AA128 GLU A 668 HIS A 670 1 O HIS A 670 N LEU A 644
SHEET 25 AA128 LEU A 692 ASP A 694 1 O ASP A 694 N LEU A 669
SHEET 26 AA128 THR A 716 LEU A 718 1 O LEU A 718 N LEU A 693
SHEET 27 AA128 HIS A 740 ASP A 742 1 O ASP A 742 N LEU A 717
SHEET 28 AA128 MET A 766 GLU A 768 1 O MET A 766 N LEU A 741
SHEET 1 AA2 2 HIS A 77 ILE A 78 0
SHEET 2 AA2 2 ASN A 115 ILE A 116 1 O ASN A 115 N ILE A 78
SHEET 1 AA3 2 ASN A 160 ILE A 161 0
SHEET 2 AA3 2 ASN A 191 ILE A 192 1 O ASN A 191 N ILE A 161
SHEET 1 AA4 2 TYR A 236 ILE A 237 0
SHEET 2 AA4 2 ASN A 277 ILE A 278 1 O ASN A 277 N ILE A 237
SHEET 1 AA5 2 GLU A 381 LEU A 382 0
SHEET 2 AA5 2 GLN A 408 ILE A 409 1 O GLN A 408 N LEU A 382
SHEET 1 AA6 2 PHE A 774 GLU A 775 0
SHEET 2 AA6 2 CYS A 803 SER A 805 1 O ALA A 804 N PHE A 774
SHEET 1 AA728 ASP B 37 GLN B 41 0
SHEET 2 AA728 SER B 44 GLU B 48 -1 O GLU B 48 N ASP B 37
SHEET 3 AA728 GLU B 67 ASP B 69 1 O ASP B 69 N ALA B 47
SHEET 4 AA728 LYS B 91 ASN B 93 1 O ASN B 93 N LEU B 68
SHEET 5 AA728 GLU B 129 LEU B 131 1 O LEU B 131 N ILE B 92
SHEET 6 AA728 GLU B 150 SER B 152 1 O GLU B 150 N LEU B 130
SHEET 7 AA728 ASN B 174 TYR B 176 1 O TYR B 176 N LEU B 151
SHEET 8 AA728 LEU B 205 SER B 207 1 O LEU B 205 N LEU B 175
SHEET 9 AA728 LYS B 226 PHE B 228 1 O PHE B 228 N LEU B 206
SHEET 10 AA728 LEU B 250 ASP B 252 1 O LEU B 250 N LEU B 227
SHEET 11 AA728 TYR B 291 ASN B 293 1 O ASN B 293 N LEU B 251
SHEET 12 AA728 VAL B 315 ASP B 317 1 O VAL B 315 N LEU B 292
SHEET 13 AA728 ILE B 341 ASP B 343 1 O ILE B 341 N LEU B 316
SHEET 14 AA728 ALA B 371 HIS B 373 1 O HIS B 373 N LEU B 342
SHEET 15 AA728 THR B 398 ASN B 400 1 O ASN B 400 N LEU B 372
SHEET 16 AA728 ILE B 422 TYR B 424 1 O TYR B 424 N ILE B 399
SHEET 17 AA728 ALA B 485 ASP B 487 1 O ALA B 485 N ILE B 423
SHEET 18 AA728 CYS B 509 ASN B 511 1 O CYS B 509 N LEU B 486
SHEET 19 AA728 TYR B 534 ASP B 536 1 O ASP B 536 N LEU B 510
SHEET 20 AA728 VAL B 558 ASP B 560 1 O VAL B 558 N LEU B 535
SHEET 21 AA728 VAL B 588 ASN B 590 1 O VAL B 588 N LEU B 559
SHEET 22 AA728 GLU B 612 VAL B 614 1 O GLU B 612 N LEU B 589
SHEET 23 AA728 ARG B 643 ASP B 645 1 O ARG B 643 N LEU B 613
SHEET 24 AA728 GLU B 668 HIS B 670 1 O HIS B 670 N LEU B 644
SHEET 25 AA728 LEU B 692 ASP B 694 1 O ASP B 694 N LEU B 669
SHEET 26 AA728 THR B 716 LEU B 718 1 O LEU B 718 N LEU B 693
SHEET 27 AA728 HIS B 740 ASP B 742 1 O ASP B 742 N LEU B 717
SHEET 28 AA728 MET B 766 GLU B 768 1 O MET B 766 N LEU B 741
SHEET 1 AA8 2 HIS B 77 ILE B 78 0
SHEET 2 AA8 2 ASN B 115 ILE B 116 1 O ASN B 115 N ILE B 78
SHEET 1 AA9 2 ASN B 160 ILE B 161 0
SHEET 2 AA9 2 ASN B 191 ILE B 192 1 O ASN B 191 N ILE B 161
SHEET 1 AB1 2 TYR B 236 ILE B 237 0
SHEET 2 AB1 2 ASN B 277 ILE B 278 1 O ASN B 277 N ILE B 237
SHEET 1 AB2 2 GLU B 381 LEU B 382 0
SHEET 2 AB2 2 GLN B 408 ILE B 409 1 O GLN B 408 N LEU B 382
SHEET 1 AB3 2 PHE B 774 GLU B 775 0
SHEET 2 AB3 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 2.05
SSBOND 2 CYS A 181 CYS A 187 1555 1555 2.04
SSBOND 3 CYS A 257 CYS A 270 1555 1555 2.05
SSBOND 4 CYS A 260 CYS A 267 1555 1555 2.03
SSBOND 5 CYS A 479 CYS A 509 1555 1555 2.05
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 2.05
SSBOND 10 CYS B 260 CYS B 267 1555 1555 2.02
SSBOND 11 CYS B 479 CYS B 509 1555 1555 2.02
SSBOND 12 CYS B 776 CYS B 803 1555 1555 2.01
LINK ND2 ASN A 293 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN A 395 C1 NAG A 906 1555 1555 1.47
LINK ND2 ASN A 511 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 590 C1 NAG E 1 1555 1555 1.47
LINK ND2 ASN A 640 C1 NAG A 914 1555 1555 1.45
LINK ND2 ASN A 680 C1 NAG A 915 1555 1555 1.45
LINK ND2 ASN B 293 C1 NAG F 1 1555 1555 1.41
LINK ND2 ASN B 511 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN B 590 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN B 640 C1 NAG B 912 1555 1555 1.48
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.43
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.47
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.46
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.40
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.44
LINK O6 BMA E 3 C1 MAN E 5 1555 1555 1.46
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.40
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44
LINK O6 BMA F 3 C1 MAN F 4 1555 1555 1.47
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.43
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.42
LINK O6 BMA H 3 C1 MAN H 4 1555 1555 1.47
CISPEP 1 TYR A 34 PRO A 35 0 0.38
CISPEP 2 ASN A 97 PRO A 98 0 -0.06
CISPEP 3 SER A 733 GLU A 734 0 -5.87
CISPEP 4 THR A 760 THR A 761 0 11.85
CISPEP 5 SER A 805 PRO A 806 0 -12.47
CISPEP 6 TYR B 34 PRO B 35 0 4.18
CISPEP 7 ASN B 97 PRO B 98 0 1.30
CISPEP 8 SER B 733 GLU B 734 0 0.24
CISPEP 9 SER B 805 PRO B 806 0 -13.82
CRYST1 143.620 98.950 139.520 90.00 108.39 90.00 C 1 2 1 8
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 0.006963 0.000000 0.002315 0.00000
SCALE2 0.000000 0.010106 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007553 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
