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HEADER HYDROLASE 02-APR-19 6R8R
TITLE STRUCTURE OF THE WNT DEACYLASE NOTUM IN COMPLEX WITH ISOQUINOLINE 45
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PALMITOLEOYL-PROTEIN CARBOXYLESTERASE NOTUM;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HNOTUM;
COMPND 5 EC: 3.1.1.98;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NOTUM, OK/SW-CL.30;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-
KEYWDS WNT SIGNALLING, NOTUM INHIBITOR, CRYSTALLOGRAPHIC FRAGMENT SCREEN,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.VECCHIA,Y.ZHAO,R.R.RUZA,E.Y.JONES
REVDAT 1 08-MAY-19 6R8R 0
JRNL AUTH B.N.ATKINSON,D.STEADMAN,Y.ZHAO,J.SIPTHORP,L.VECCHIA,
JRNL AUTH 2 R.R.RUZA,F.JEGNATHAN,G.LINES,S.FREW,A.MONAGHAN,S.KJAER,
JRNL AUTH 3 M.BICTASH,Y.JONES,P.V.FISH
JRNL TITL DISCOVERY OF 2-PHENOXYACETAMIDES AS INHIBITORS OF THE
JRNL TITL 2 WNT-DEPALMITOLEATING ENZYME NOTUM FROM AN X-RAY FRAGMENT
JRNL TITL 3 SCREEN
JRNL REF MEDCHEMCOMM 2019
JRNL REFN ESSN 2040-2511
JRNL DOI 10.1039/C9MD00096H
REMARK 2
REMARK 2 RESOLUTION. 1.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15RC3_3435
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 89931
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4507
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 24.2041 - 3.9407 1.00 3098 128 0.1714 0.1626
REMARK 3 2 3.9407 - 3.1300 1.00 2928 158 0.1526 0.1562
REMARK 3 3 3.1300 - 2.7350 1.00 2921 159 0.1522 0.1724
REMARK 3 4 2.7350 - 2.4852 1.00 2914 124 0.1499 0.1863
REMARK 3 5 2.4852 - 2.3072 1.00 2877 131 0.1365 0.1951
REMARK 3 6 2.3072 - 2.1713 1.00 2880 141 0.1275 0.1619
REMARK 3 7 2.1713 - 2.0626 1.00 2869 148 0.1168 0.1586
REMARK 3 8 2.0626 - 1.9728 1.00 2856 149 0.1143 0.1597
REMARK 3 9 1.9728 - 1.8969 1.00 2843 151 0.1209 0.1809
REMARK 3 10 1.8969 - 1.8315 1.00 2840 152 0.1148 0.1500
REMARK 3 11 1.8315 - 1.7742 1.00 2845 146 0.1138 0.1875
REMARK 3 12 1.7742 - 1.7235 1.00 2836 157 0.1131 0.1763
REMARK 3 13 1.7235 - 1.6782 1.00 2819 161 0.1117 0.1542
REMARK 3 14 1.6782 - 1.6372 1.00 2839 140 0.1067 0.1504
REMARK 3 15 1.6372 - 1.6000 1.00 2852 158 0.1124 0.1380
REMARK 3 16 1.6000 - 1.5660 1.00 2830 127 0.1179 0.1734
REMARK 3 17 1.5660 - 1.5347 1.00 2853 138 0.1282 0.2020
REMARK 3 18 1.5347 - 1.5057 1.00 2804 157 0.1396 0.1923
REMARK 3 19 1.5057 - 1.4788 1.00 2813 173 0.1378 0.2023
REMARK 3 20 1.4788 - 1.4538 1.00 2804 164 0.1529 0.1944
REMARK 3 21 1.4538 - 1.4303 1.00 2805 155 0.1652 0.2172
REMARK 3 22 1.4303 - 1.4083 1.00 2814 143 0.1802 0.2315
REMARK 3 23 1.4083 - 1.3876 1.00 2846 147 0.2081 0.2620
REMARK 3 24 1.3876 - 1.3681 1.00 2813 152 0.2150 0.2523
REMARK 3 25 1.3681 - 1.3496 1.00 2795 160 0.2305 0.2823
REMARK 3 26 1.3496 - 1.3320 1.00 2807 163 0.2297 0.2810
REMARK 3 27 1.3320 - 1.3154 1.00 2807 151 0.2314 0.2824
REMARK 3 28 1.3154 - 1.2995 1.00 2780 167 0.2429 0.2952
REMARK 3 29 1.2995 - 1.2844 1.00 2783 147 0.2512 0.2801
REMARK 3 30 1.2844 - 1.2700 1.00 2853 160 0.2779 0.3334
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.41
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.25
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6R8R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1292101554.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91587
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90021
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.270
REMARK 200 RESOLUTION RANGE LOW (A) : 24.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.29
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 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: PHASER
REMARK 200 STARTING MODEL: 4UZ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M AMMONIUM SULPHATE, 0.1 M CITRIC
REMARK 280 ACID, PH 4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 300K
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 30.17000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.06500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.86000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.06500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.17000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.86000
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 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 GLU A 78
REMARK 465 THR A 79
REMARK 465 GLY A 80
REMARK 465 SER A 81
REMARK 465 ALA A 82
REMARK 465 GLN A 83
REMARK 465 GLN A 84
REMARK 465 LEU A 85
REMARK 465 SER A 421
REMARK 465 HIS A 422
REMARK 465 LYS A 423
REMARK 465 ALA A 424
REMARK 465 SER A 425
REMARK 465 LYS A 426
REMARK 465 LYS A 454
REMARK 465 HIS A 455
REMARK 465 HIS A 456
REMARK 465 HIS A 457
REMARK 465 HIS A 458
REMARK 465 HIS A 459
REMARK 465 HIS A 460
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 TRP A 128 -145.19 59.27
REMARK 500 ALA A 191 57.91 -143.49
REMARK 500 SER A 232 -127.45 65.30
REMARK 500 SER A 232 -126.24 63.40
REMARK 500 GLN A 311 -175.80 63.77
REMARK 500 GLU A 390 153.45 74.65
REMARK 500 ILE A 391 -38.94 -149.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue JV8 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound
REMARK 800 to ASN A 96
DBREF 6R8R A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 6R8R GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 6R8R GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 6R8R HIS A 460 UNP Q6P988 EXPRESSION TAG
SEQRES 1 A 383 GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG
SEQRES 2 A 383 LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP
SEQRES 3 A 383 GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY
SEQRES 4 A 383 SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR
SEQRES 5 A 383 CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR
SEQRES 6 A 383 MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR
SEQRES 7 A 383 ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU
SEQRES 8 A 383 ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO
SEQRES 9 A 383 TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS
SEQRES 10 A 383 SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE
SEQRES 11 A 383 ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU
SEQRES 12 A 383 SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER SER ALA
SEQRES 13 A 383 GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA
SEQRES 14 A 383 GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL
SEQRES 15 A 383 ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS
SEQRES 16 A 383 GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS
SEQRES 17 A 383 ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP
SEQRES 18 A 383 ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN
SEQRES 19 A 383 GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL
SEQRES 20 A 383 TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP
SEQRES 21 A 383 LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS
SEQRES 22 A 383 LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR
SEQRES 23 A 383 ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS
SEQRES 24 A 383 ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS
SEQRES 25 A 383 GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL
SEQRES 26 A 383 LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP
SEQRES 27 A 383 ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO
SEQRES 28 A 383 LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO
SEQRES 29 A 383 TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS
SEQRES 30 A 383 HIS HIS HIS HIS HIS HIS
HET NAG A 501 14
HET JV8 A 502 22
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET SO4 A 506 5
HET SO4 A 507 5
HET SO4 A 508 5
HET SO4 A 509 5
HET SO4 A 510 5
HET DMS A 511 4
HET DMS A 512 4
HET DMS A 513 4
HET DMS A 514 4
HET DMS A 515 4
HET EDO A 516 4
HET EDO A 517 4
HET EDO A 518 4
HET EDO A 519 4
HET EDO A 520 4
HET EDO A 521 4
HET EDO A 522 4
HET EDO A 523 4
HET EDO A 524 4
HET EDO A 525 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM JV8 ~{N}-ISOQUINOLIN-6-YL-2-(2-METHYLPHENOXY)ETHANAMIDE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 JV8 C18 H16 N2 O2
FORMUL 4 SO4 8(O4 S 2-)
FORMUL 12 DMS 5(C2 H6 O S)
FORMUL 17 EDO 10(C2 H6 O2)
FORMUL 27 HOH *183(H2 O)
HELIX 1 AA1 ASN A 132 MET A 143 1 12
HELIX 2 AA2 ARG A 144 MET A 147 5 4
HELIX 3 AA3 THR A 159 SER A 163 5 5
HELIX 4 AA4 MET A 203 GLY A 217 1 15
HELIX 5 AA5 ARG A 218 ALA A 223 5 6
HELIX 6 AA6 SER A 232 LEU A 252 1 21
HELIX 7 AA7 ALA A 286 ASN A 299 1 14
HELIX 8 AA8 PRO A 303 GLN A 311 1 9
HELIX 9 AA9 GLU A 314 PHE A 319 5 6
HELIX 10 AB1 PHE A 320 TYR A 325 1 6
HELIX 11 AB2 PRO A 326 LEU A 328 5 3
HELIX 12 AB3 GLU A 341 ASP A 347 1 7
HELIX 13 AB4 GLN A 357 LYS A 376 1 20
HELIX 14 AB5 LEU A 407 LEU A 418 1 12
SHEET 1 AA110 THR A 155 THR A 157 0
SHEET 2 AA110 ASP A 88 LEU A 93 -1 N LEU A 89 O ARG A 156
SHEET 3 AA110 GLY A 108 LYS A 112 -1 O TYR A 109 N HIS A 92
SHEET 4 AA110 ASN A 176 ILE A 180 -1 O PHE A 179 N TYR A 110
SHEET 5 AA110 ARG A 119 LEU A 124 1 N PHE A 123 O ILE A 180
SHEET 6 AA110 VAL A 225 SER A 231 1 O LEU A 227 N TRP A 120
SHEET 7 AA110 GLN A 258 ASP A 264 1 O ARG A 260 N LEU A 228
SHEET 8 AA110 VAL A 332 VAL A 335 1 O VAL A 335 N ALA A 263
SHEET 9 AA110 SER A 381 ALA A 383 1 O PHE A 382 N VAL A 334
SHEET 10 AA110 HIS A 435 VAL A 437 1 O LEU A 436 N ALA A 383
SHEET 1 AA2 2 PHE A 339 ASP A 340 0
SHEET 2 AA2 2 LEU A 387 SER A 388 1 O SER A 388 N PHE A 339
SHEET 1 AA3 2 GLN A 401 VAL A 402 0
SHEET 2 AA3 2 THR A 405 SER A 406 -1 O THR A 405 N VAL A 402
SSBOND 1 CYS A 101 CYS A 183 1555 1555 2.07
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.04
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.04
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.23
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.02
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.01
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.04
LINK ND2 ASN A 96 C1 NAG A 501 1555 1555 1.43
SITE 1 AC1 7 TRP A 128 TYR A 129 PHE A 268 ILE A 291
SITE 2 AC1 7 THR A 345 SO4 A 507 HOH A 619
SITE 1 AC2 5 ARG A 305 ARG A 308 GLN A 357 GLU A 358
SITE 2 AC2 5 ARG A 361
SITE 1 AC3 4 HIS A 373 LYS A 376 HOH A 604 HOH A 701
SITE 1 AC4 8 THR A 142 MET A 143 ARG A 144 ARG A 145
SITE 2 AC4 8 ARG A 409 HIS A 412 ARG A 416 HOH A 668
SITE 1 AC5 4 TYR A 274 ARG A 275 LEU A 360 HOH A 730
SITE 1 AC6 7 GLY A 127 TRP A 128 SER A 232 ALA A 233
SITE 2 AC6 7 HIS A 389 JV8 A 502 HOH A 603
SITE 1 AC7 9 ARG A 133 LYS A 197 ASN A 198 GLU A 199
SITE 2 AC7 9 ARG A 275 TYR A 297 HOH A 717 HOH A 719
SITE 3 AC7 9 HOH A 728
SITE 1 AC8 5 ARG A 244 GLU A 247 VAL A 302 ARG A 307
SITE 2 AC8 5 HOH A 671
SITE 1 AC9 3 ARG A 90 HIS A 92 ARG A 218
SITE 1 AD1 4 TYR A 171 TRP A 172 TRP A 173 ASN A 174
SITE 1 AD2 7 TYR A 325 LEU A 328 ARG A 329 SER A 330
SITE 2 AD2 7 PRO A 331 VAL A 332 HOH A 602
SITE 1 AD3 6 TYR A 110 GLU A 125 TRP A 152 ARG A 156
SITE 2 AD3 6 PHE A 179 PRO A 181
SITE 1 AD4 3 ARG A 394 SER A 395 HIS A 396
SITE 1 AD5 6 PRO A 255 ARG A 372 LYS A 403 VAL A 437
SITE 2 AD5 6 HOH A 631 HOH A 718
SITE 1 AD6 6 TRP A 128 TYR A 129 ARG A 139 MET A 143
SITE 2 AD6 6 EDO A 524 HOH A 609
SITE 1 AD7 5 ARG A 156 THR A 157 GLY A 158 THR A 159
SITE 2 AD7 5 PHE A 179
SITE 1 AD8 7 TYR A 254 LYS A 376 ASP A 377 VAL A 378
SITE 2 AD8 7 PRO A 379 HIS A 435 HOH A 688
SITE 1 AD9 8 LEU A 269 ASP A 270 ASN A 271 GLN A 273
SITE 2 AD9 8 PRO A 287 THR A 288 VAL A 346 ASP A 347
SITE 1 AE1 5 ASP A 103 LYS A 194 GLU A 199 TYR A 200
SITE 2 AE1 5 EDO A 525
SITE 1 AE2 6 TYR A 322 TYR A 325 PRO A 326 THR A 374
SITE 2 AE2 6 HOH A 678 HOH A 699
SITE 1 AE3 4 GLN A 401 LYS A 403 GLY A 404 ASN A 446
SITE 1 AE4 6 SER A 192 ASN A 198 ARG A 296 TYR A 297
SITE 2 AE4 6 ASN A 299 HOH A 601
SITE 1 AE5 7 SER A 138 ARG A 139 THR A 142 MET A 143
SITE 2 AE5 7 PRO A 170 TRP A 173 EDO A 516
SITE 1 AE6 5 ASP A 103 LYS A 194 THR A 277 ASP A 278
SITE 2 AE6 5 EDO A 520
SITE 1 AE7 8 ASN A 96 SER A 98 VAL A 99 PRO A 153
SITE 2 AE7 8 ARG A 154 THR A 155 ARG A 213 HOH A 690
CRYST1 60.340 71.720 78.130 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 0.016573 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013943 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012799 0.00000
TER 2969 THR A 453
MASTER 370 0 25 14 14 0 45 6 3212 1 153 30
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