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HEADER HYDROLASE 04-SEP-14 4UZ9
TITLE STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM VII -
TITLE 2 SOS COMPLEX - 2.2A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN NOTUM HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 81-451;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: GLYCOSYLATED AT N96
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS HYDROLASE, WNT, ESTERASE, EXTRACELLULAR, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZEBISCH,E.Y.JONES
REVDAT 1 25-FEB-15 4UZ9 0
JRNL AUTH S.KAKUGAWA,P.F.LANGTON,M.ZEBISCH,S.A.HOWELL,T.-H.CHANG,
JRNL AUTH 2 Y.LIU,T.FEIZI,G.BINEVA,N.O'REILLY,A.P.SNIJDERS,E.Y.JONES,
JRNL AUTH 3 J.-P.VINCENT
JRNL TITL NOTUM DEACYLATES WNT PROTEINS TO SUPPRESS SIGNALLING
JRNL TITL 2 ACTIVITY
JRNL REF NATURE 2015
JRNL REFN ESSN 1476-4687
JRNL DOI 10.1038/NATURE14259
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.97
REMARK 3 NUMBER OF REFLECTIONS : 24266
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) : 0.19196
REMARK 3 R VALUE (WORKING SET) : 0.19007
REMARK 3 FREE R VALUE : 0.23653
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1030
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) : 2.200
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.257
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1743
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.263
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.305
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2875
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 115
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.040
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.19
REMARK 3 B22 (A**2) : 1.19
REMARK 3 B33 (A**2) : -2.38
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.214
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.187
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.138
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.304
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3033 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2753 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4149 ; 1.674 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6315 ; 0.864 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 360 ; 6.581 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;32.934 ;22.585
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 477 ;15.456 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;22.521 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 446 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3388 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 747 ; 0.001 ; 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): 1428 ; 2.223 ; 2.572
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1427 ; 2.224 ; 2.572
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1783 ; 3.599 ; 3.841
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1605 ; 3.441 ; 3.275
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 86 A 451
REMARK 3 ORIGIN FOR THE GROUP (A): -34.1646 1.1693 -5.0749
REMARK 3 T TENSOR
REMARK 3 T11: 0.0132 T22: 0.0286
REMARK 3 T33: 0.1584 T12: -0.0120
REMARK 3 T13: 0.0157 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.5446 L22: 0.7960
REMARK 3 L33: 0.9861 L12: 0.2896
REMARK 3 L13: 0.0419 L23: -0.0344
REMARK 3 S TENSOR
REMARK 3 S11: 0.0440 S12: -0.0372 S13: -0.0658
REMARK 3 S21: -0.0021 S22: -0.0728 S23: -0.0636
REMARK 3 S31: 0.0186 S32: 0.0132 S33: 0.0288
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4UZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-SEP-14.
REMARK 100 THE PDBE ID CODE IS EBI-61696.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25372
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 97.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.1
REMARK 200 R MERGE (I) : 0.16
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.40
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM AMMONIUM SULFATE 100 MM
REMARK 280 MES 6.5 35 % W/V PEP 629 20MM SOS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 97.57400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.81500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.81500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.78700
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.81500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.81500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 146.36100
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.81500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.81500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 48.78700
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.81500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.81500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 146.36100
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 97.57400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 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 THR A 427
REMARK 465 PRO A 428
REMARK 465 LEU A 429
REMARK 465 LYS A 430
REMARK 465 GLY A 431
REMARK 465 GLY A 452
REMARK 465 THR A 453
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 -140.64 54.92
REMARK 500 MET A 143 53.55 -142.57
REMARK 500 SER A 232 -123.51 64.28
REMARK 500 SER A 388 -169.80 -160.41
REMARK 500 GLU A 390 160.49 70.55
REMARK 500 ILE A 391 -38.20 -158.01
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 SCR A1453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1454
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1452 BOUND TO ASN A 96
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UYU RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I
REMARK 900 IODIDE COMPLEX - 2.3A
REMARK 900 RELATED ID: 4UYW RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I
REMARK 900 HEPARIN FRAGMENT COMPLEX - 1.7A
REMARK 900 RELATED ID: 4UYZ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM II
REMARK 900 - 2.8A
REMARK 900 RELATED ID: 4UZ1 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM
REMARK 900 III - 1.4A
REMARK 900 RELATED ID: 4UZ5 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM IV
REMARK 900 - 2.1A
REMARK 900 RELATED ID: 4UZ6 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM V
REMARK 900 - SOS COMPLEX - 1.9A
REMARK 900 RELATED ID: 4UZ7 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACETYLASE NOTUM - CRYSTAL FORM
REMARK 900 VII - SOS COMPLEX - 2.2A
REMARK 900 RELATED ID: 4UZA RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM
REMARK 900 VIII - PHOSPHATE COMPLEX - 2.4A
REMARK 900 RELATED ID: 4UZJ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM
REMARK 900 III - 1.4A
REMARK 900 RELATED ID: 4UZK RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM FROM DROSOPHILA -
REMARK 900 CRYSTAL FORM II - 1.9A
REMARK 900 RELATED ID: 4UZL RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I
REMARK 900 MYRISTOLEATE COMPLEX - 2.1A
REMARK 900 RELATED ID: 4UZQ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM IN COMPLEX WITH
REMARK 900 O-PALMITOLEOYL SERINE - CRYSTAL FORM IX - 1.5A
REMARK 900 RELATED ID: 4WBH RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 C330S ENGINEERED MUTATION
DBREF 4UZ9 A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 4UZ9 GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 HIS A 460 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ9 SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
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 A1452 14
HET SCR A1453 55
HET CL A1454 1
HETNAM CL CHLORIDE ION
HETNAM SCR SUCROSE OCTASULFATE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 CL CL 1-
FORMUL 3 SCR C12 H22 O35 S8
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 HOH *115(H2 O)
HELIX 1 1 ASN A 132 MET A 143 1 12
HELIX 2 2 ARG A 144 MET A 147 5 4
HELIX 3 3 THR A 159 SER A 163 5 5
HELIX 4 4 MET A 203 ARG A 218 1 16
HELIX 5 5 GLY A 219 ALA A 223 5 5
HELIX 6 6 SER A 232 GLY A 253 1 22
HELIX 7 7 ALA A 286 ASN A 299 1 14
HELIX 8 8 PRO A 303 ARG A 308 1 6
HELIX 9 9 GLU A 314 PHE A 319 5 6
HELIX 10 10 PHE A 320 TYR A 325 1 6
HELIX 11 11 PRO A 326 LEU A 328 5 3
HELIX 12 12 GLU A 341 ASP A 347 1 7
HELIX 13 13 GLN A 357 LYS A 376 1 20
HELIX 14 14 ARG A 394 ASP A 399 5 6
HELIX 15 15 LEU A 407 ASP A 420 1 14
SHEET 1 AA10 THR A 155 ARG A 156 0
SHEET 2 AA10 LEU A 89 LEU A 93 -1 O LEU A 89 N ARG A 156
SHEET 3 AA10 GLY A 108 LYS A 112 -1 O TYR A 109 N HIS A 92
SHEET 4 AA10 ASN A 176 ILE A 180 -1 O MET A 177 N LYS A 112
SHEET 5 AA10 ARG A 119 LEU A 124 1 O ARG A 119 N ASN A 176
SHEET 6 AA10 VAL A 225 SER A 231 1 O VAL A 225 N TRP A 120
SHEET 7 AA10 GLN A 258 ASP A 264 1 O GLN A 258 N LEU A 226
SHEET 8 AA10 VAL A 332 VAL A 335 1 O PHE A 333 N ALA A 263
SHEET 9 AA10 SER A 381 ALA A 383 1 N PHE A 382 O VAL A 334
SHEET 10 AA10 HIS A 435 VAL A 437 1 O LEU A 436 N ALA A 383
SHEET 1 AB 2 PHE A 339 ASP A 340 0
SHEET 2 AB 2 LEU A 387 SER A 388 0
SHEET 1 AC 2 GLN A 401 VAL A 402 0
SHEET 2 AC 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 2.13
SSBOND 2 CYS A 130 CYS A 136 1555 1555 1.99
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.06
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.11
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.06
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.04
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.04
LINK ND2 ASN A 96 C1 NAG A1452 1555 1555 1.45
SITE 1 AC1 15 SER A 117 ARG A 118 ARG A 119 ASN A 174
SITE 2 AC1 15 LYS A 224 LYS A 272 HIS A 276 GLU A 289
SITE 3 AC1 15 ARG A 292 HIS A 412 ARG A 416 HIS A 419
SITE 4 AC1 15 HOH A2088 HOH A2114 HOH A2115
SITE 1 AC2 1 ARG A 90
SITE 1 AC3 4 ASN A 96 VAL A 99 SER A 193 PRO A 447
CRYST1 69.630 69.630 195.148 90.00 90.00 90.00 P 41 21 2 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 0.014362 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014362 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005124 0.00000
TER 2876 THR A 451
MASTER 378 0 3 15 14 0 6 6 3060 1 84 30
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