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HEADER HYDROLASE 04-SEP-14 4UZ7
TITLE STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM VI - 2.2A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN NOTUM HOMOLOG;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 81-451;
COMPND 5 EC: 3.1.1.1;
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 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 4UZ7 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) : 79.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.66
REMARK 3 NUMBER OF REFLECTIONS : 39061
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) : 0.18397
REMARK 3 R VALUE (WORKING SET) : 0.18271
REMARK 3 FREE R VALUE : 0.22864
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.6
REMARK 3 FREE R VALUE TEST SET COUNT : 1063
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) : 2888
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.263
REMARK 3 BIN FREE R VALUE SET COUNT : 78
REMARK 3 BIN FREE R VALUE : 0.332
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5712
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 207
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.807
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.22
REMARK 3 B22 (A**2) : -1.52
REMARK 3 B33 (A**2) : -0.60
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.64
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.252
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.198
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.150
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.298
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5886 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5411 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8017 ; 1.453 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12414 ; 0.819 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 716 ; 6.295 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 282 ;32.758 ;22.482
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 933 ;14.719 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;18.099 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 844 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6693 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1469 ; 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): 2861 ; 1.751 ; 2.642
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2860 ; 1.746 ; 2.641
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3569 ; 2.866 ; 3.949
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3025 ; 2.460 ; 2.994
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 : 2
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 87 A 451
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5568 -25.8751 -19.8335
REMARK 3 T TENSOR
REMARK 3 T11: 0.0188 T22: 0.0655
REMARK 3 T33: 0.0038 T12: -0.0137
REMARK 3 T13: -0.0058 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.3914 L22: 0.4544
REMARK 3 L33: 0.5174 L12: 0.0666
REMARK 3 L13: 0.0495 L23: 0.0710
REMARK 3 S TENSOR
REMARK 3 S11: -0.0475 S12: -0.0025 S13: 0.0162
REMARK 3 S21: -0.0631 S22: 0.0492 S23: 0.0049
REMARK 3 S31: -0.0098 S32: -0.0513 S33: -0.0018
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 87 B 451
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1477 -28.6527 -60.1201
REMARK 3 T TENSOR
REMARK 3 T11: 0.0077 T22: 0.0642
REMARK 3 T33: 0.0156 T12: 0.0056
REMARK 3 T13: 0.0101 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.3322 L22: 0.9198
REMARK 3 L33: 0.4203 L12: -0.0096
REMARK 3 L13: 0.1897 L23: 0.0800
REMARK 3 S TENSOR
REMARK 3 S11: -0.0166 S12: -0.0305 S13: -0.0109
REMARK 3 S21: 0.0760 S22: 0.0286 S23: 0.1077
REMARK 3 S31: 0.0031 S32: -0.0387 S33: -0.0120
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 4UZ7 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-61694.
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 : 8.5
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 : 40126
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 80.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.7
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.50
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 (%): 47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 %V/V GLYCEROL 24 %W/V
REMARK 280 PEG4000 0.160 M MGCL2 0.080 M TRIS-HCL PH 8.5 20MM SOS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 25.79513
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.96250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 79.80320
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 25.79513
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.96250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 79.80320
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CZ2 TRP B 316 LIES ON A SPECIAL POSITION.
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 ASN A 86
REMARK 465 SER A 192
REMARK 465 SER A 193
REMARK 465 LYS A 194
REMARK 465 SER A 195
REMARK 465 GLU A 196
REMARK 465 LYS A 197
REMARK 465 ASN A 198
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 465 GLU B 78
REMARK 465 THR B 79
REMARK 465 GLY B 80
REMARK 465 SER B 81
REMARK 465 ALA B 82
REMARK 465 GLN B 83
REMARK 465 GLN B 84
REMARK 465 LEU B 85
REMARK 465 ASN B 86
REMARK 465 SER B 193
REMARK 465 LYS B 194
REMARK 465 SER B 195
REMARK 465 GLU B 196
REMARK 465 LYS B 197
REMARK 465 ASN B 198
REMARK 465 LEU B 351
REMARK 465 THR B 352
REMARK 465 GLY B 452
REMARK 465 THR B 453
REMARK 465 LYS B 454
REMARK 465 HIS B 455
REMARK 465 HIS B 456
REMARK 465 HIS B 457
REMARK 465 HIS B 458
REMARK 465 HIS B 459
REMARK 465 HIS B 460
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 THR A 284 OG1 CG2
REMARK 470 THR B 277 OG1 CG2
REMARK 470 ASP B 278 CG OD1 OD2
REMARK 470 VAL B 280 CG1 CG2
REMARK 470 ASP B 281 CG OD1 OD2
REMARK 470 THR B 282 OG1 CG2
REMARK 470 ILE B 283 CG1 CG2 CD1
REMARK 470 THR B 284 OG1 CG2
REMARK 470 GLN B 354 CG CD OE1 NE2
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 N PRO B 106 O HOH B 2007 2.08
REMARK 500 CB PRO B 106 O HOH B 2007 1.42
REMARK 500 CG PRO B 106 O HOH B 2007 0.27
REMARK 500 CD PRO B 106 O HOH B 2007 1.29
REMARK 500 OE1B GLU B 167 O HOH B 2039 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2047 O HOH A 2047 2555 2.16
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 CYS B 413 CA - CB - SG ANGL. DEV. = -7.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TRP A 128 -140.07 60.02
REMARK 500 SER A 232 -122.58 52.16
REMARK 500 ASP A 270 30.07 -83.04
REMARK 500 ASN A 271 175.95 -54.71
REMARK 500 CYS A 279 97.97 -59.58
REMARK 500 GLU A 390 161.24 69.47
REMARK 500 ILE A 391 -37.38 -156.35
REMARK 500 TRP B 128 -132.13 58.08
REMARK 500 TYR B 129 172.56 174.69
REMARK 500 SER B 232 -115.19 51.76
REMARK 500 ASP B 270 51.54 -90.50
REMARK 500 CYS B 279 92.56 -64.11
REMARK 500 VAL B 280 -78.16 -110.56
REMARK 500 GLU B 314 40.49 -105.61
REMARK 500 PRO B 355 161.27 -44.55
REMARK 500 GLU B 390 163.86 69.59
REMARK 500 ILE B 391 -37.60 -162.65
REMARK 500 HIS B 444 3.37 82.18
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 CL A1452
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UYU RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACETYLASE NOTUM - CRYSTAL FORM
REMARK 900 I 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: 4UZ9 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 A WNT SIGNAL REGULATOR FROM DROSOPHILA -
REMARK 900 CRYSTAL FORM I - 2.4A
REMARK 900 RELATED ID: 4UZK RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR 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 A WNT SIGNAL REGULATOR COMPLEX - CRYSTAL
REMARK 900 FORM IX - 1.5A
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 C330S ENGINEERED MUTATION
DBREF 4UZ7 A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
DBREF 4UZ7 B 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 4UZ7 GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS A 460 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 4UZ7 GLU B 78 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 THR B 79 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 GLY B 80 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 GLY B 452 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 THR B 453 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 LYS B 454 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS B 455 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS B 456 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS B 457 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS B 458 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS B 459 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 HIS B 460 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZ7 SER B 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
SEQRES 1 B 383 GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG
SEQRES 2 B 383 LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP
SEQRES 3 B 383 GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY
SEQRES 4 B 383 SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR
SEQRES 5 B 383 CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR
SEQRES 6 B 383 MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR
SEQRES 7 B 383 ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU
SEQRES 8 B 383 ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO
SEQRES 9 B 383 TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS
SEQRES 10 B 383 SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE
SEQRES 11 B 383 ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU
SEQRES 12 B 383 SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER SER ALA
SEQRES 13 B 383 GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA
SEQRES 14 B 383 GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL
SEQRES 15 B 383 ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS
SEQRES 16 B 383 GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS
SEQRES 17 B 383 ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP
SEQRES 18 B 383 ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN
SEQRES 19 B 383 GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL
SEQRES 20 B 383 TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP
SEQRES 21 B 383 LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS
SEQRES 22 B 383 LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR
SEQRES 23 B 383 ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS
SEQRES 24 B 383 ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS
SEQRES 25 B 383 GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL
SEQRES 26 B 383 LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP
SEQRES 27 B 383 ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO
SEQRES 28 B 383 LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO
SEQRES 29 B 383 TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS
SEQRES 30 B 383 HIS HIS HIS HIS HIS HIS
HET CL A1452 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL CL 1-
FORMUL 4 HOH *207(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 GLY A 217 1 15
HELIX 5 5 ARG A 218 ALA A 223 5 6
HELIX 6 6 SER A 232 LEU A 252 1 21
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 LEU A 375 1 19
HELIX 14 14 ARG A 394 ASP A 399 5 6
HELIX 15 15 LEU A 407 SER A 421 1 15
HELIX 16 16 ASN B 132 MET B 143 1 12
HELIX 17 17 ARG B 144 MET B 147 5 4
HELIX 18 18 THR B 159 SER B 163 5 5
HELIX 19 19 MET B 203 GLY B 217 1 15
HELIX 20 20 ARG B 218 ALA B 223 5 6
HELIX 21 21 SER B 232 LEU B 252 1 21
HELIX 22 22 ALA B 286 ASN B 299 1 14
HELIX 23 23 PRO B 303 GLN B 309 1 7
HELIX 24 24 GLU B 314 PHE B 319 5 6
HELIX 25 25 PHE B 320 TYR B 325 1 6
HELIX 26 26 PRO B 326 LEU B 328 5 3
HELIX 27 27 GLU B 341 ASP B 347 1 7
HELIX 28 28 GLN B 357 LEU B 375 1 19
HELIX 29 29 ARG B 394 ASP B 399 5 6
HELIX 30 30 LEU B 407 SER B 421 1 15
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 LEU A 436 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
SHEET 1 BA10 THR B 155 ARG B 156 0
SHEET 2 BA10 LEU B 89 LEU B 93 -1 O LEU B 89 N ARG B 156
SHEET 3 BA10 GLY B 108 LYS B 112 -1 O TYR B 109 N HIS B 92
SHEET 4 BA10 ASN B 176 ILE B 180 -1 O MET B 177 N LYS B 112
SHEET 5 BA10 ARG B 119 LEU B 124 1 O ARG B 119 N ASN B 176
SHEET 6 BA10 VAL B 225 SER B 231 1 O VAL B 225 N TRP B 120
SHEET 7 BA10 GLN B 258 ASP B 264 1 O GLN B 258 N LEU B 226
SHEET 8 BA10 VAL B 332 VAL B 335 1 O PHE B 333 N ALA B 263
SHEET 9 BA10 SER B 381 ALA B 383 1 N PHE B 382 O VAL B 334
SHEET 10 BA10 LEU B 436 VAL B 437 1 O LEU B 436 N ALA B 383
SHEET 1 BB 2 PHE B 339 ASP B 340 0
SHEET 2 BB 2 LEU B 387 SER B 388 1 N SER B 388 O PHE B 339
SHEET 1 BC 2 GLN B 401 VAL B 402 0
SHEET 2 BC 2 THR B 405 SER B 406 -1 O THR B 405 N VAL B 402
SSBOND 1 CYS A 101 CYS A 183 1555 1555 2.07
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.06
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.06
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.10
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.01
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.12
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.06
SSBOND 8 CYS B 101 CYS B 183 1555 1555 2.11
SSBOND 9 CYS B 130 CYS B 136 1555 1555 2.04
SSBOND 10 CYS B 279 CYS B 285 1555 1555 2.04
SSBOND 11 CYS B 306 CYS B 318 1555 1555 2.10
SSBOND 12 CYS B 386 CYS B 449 1555 1555 2.01
SSBOND 13 CYS B 413 CYS B 432 1555 1555 2.11
SSBOND 14 CYS B 440 CYS B 445 1555 1555 2.08
SITE 1 AC1 1 SER A 395
CRYST1 62.863 79.925 160.004 90.00 94.04 90.00 I 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 0.015908 0.000000 0.001124 0.00000
SCALE2 0.000000 0.012512 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006265 0.00000
MTRIX1 1 1.000000 -0.001000 -0.010000 25.00600 1
MTRIX2 1 -0.001000 -1.000000 0.011000 -53.64300 1
MTRIX3 1 -0.010000 -0.011000 -1.000000 -80.51300 1
TER 2868 THR A 451
TER 5714 THR B 451
MASTER 490 0 1 30 28 0 1 9 5921 2 28 60
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