4UZA-pdb | HEADER HYDROLASE 04-SEP-14 4UZA
TITLE STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM VIII -
TITLE 2 PHOSPHATE COMPLEX - 2.4A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN NOTUM HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 80-452;
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 4UZA 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. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 134.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.89
REMARK 3 NUMBER OF REFLECTIONS : 20561
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) : 0.21013
REMARK 3 R VALUE (WORKING SET) : 0.20710
REMARK 3 FREE R VALUE : 0.27106
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.8
REMARK 3 FREE R VALUE TEST SET COUNT : 1032
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) : 2.400
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.463
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1487
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.322
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.412
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2840
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 23
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.956
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00
REMARK 3 B22 (A**2) : 0.00
REMARK 3 B33 (A**2) : 0.00
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): 0.286
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.248
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.208
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.279
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2948 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2705 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4013 ; 1.537 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6204 ; 0.828 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 354 ; 6.647 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 142 ;35.132 ;22.887
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 471 ;16.139 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;17.253 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 425 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3335 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 728 ; 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): 1419 ; 2.833 ; 4.350
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1418 ; 2.830 ; 4.349
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1769 ; 4.389 ; 6.514
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1529 ; 3.923 ; 4.986
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 1 A 451
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9694 -58.1932 -32.7489
REMARK 3 T TENSOR
REMARK 3 T11: 0.0264 T22: 0.1472
REMARK 3 T33: 0.1823 T12: -0.0291
REMARK 3 T13: 0.0561 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 1.0881 L22: 1.4717
REMARK 3 L33: 1.0602 L12: -0.6169
REMARK 3 L13: 0.5161 L23: 0.2722
REMARK 3 S TENSOR
REMARK 3 S11: 0.1057 S12: -0.2591 S13: 0.0926
REMARK 3 S21: -0.0930 S22: -0.0012 S23: -0.1937
REMARK 3 S31: 0.0444 S32: -0.1553 S33: -0.1045
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 4UZA 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-61697.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
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) : 0.9793
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21598
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 70.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 21.2
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.00
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 (%): 59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.630 M K2HPO4 1.170 M NAH2PO4 6.300
REMARK 280 PH FINAL PH
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 4 3 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 Y,X,-Z
REMARK 290 14555 -Y,-X,-Z
REMARK 290 15555 Y,-X,Z
REMARK 290 16555 -Y,X,Z
REMARK 290 17555 X,Z,-Y
REMARK 290 18555 -X,Z,Y
REMARK 290 19555 -X,-Z,-Y
REMARK 290 20555 X,-Z,Y
REMARK 290 21555 Z,Y,-X
REMARK 290 22555 Z,-Y,X
REMARK 290 23555 -Z,Y,X
REMARK 290 24555 -Z,-Y,-X
REMARK 290 25555 X,Y+1/2,Z+1/2
REMARK 290 26555 -X,-Y+1/2,Z+1/2
REMARK 290 27555 -X,Y+1/2,-Z+1/2
REMARK 290 28555 X,-Y+1/2,-Z+1/2
REMARK 290 29555 Z,X+1/2,Y+1/2
REMARK 290 30555 Z,-X+1/2,-Y+1/2
REMARK 290 31555 -Z,-X+1/2,Y+1/2
REMARK 290 32555 -Z,X+1/2,-Y+1/2
REMARK 290 33555 Y,Z+1/2,X+1/2
REMARK 290 34555 -Y,Z+1/2,-X+1/2
REMARK 290 35555 Y,-Z+1/2,-X+1/2
REMARK 290 36555 -Y,-Z+1/2,X+1/2
REMARK 290 37555 Y,X+1/2,-Z+1/2
REMARK 290 38555 -Y,-X+1/2,-Z+1/2
REMARK 290 39555 Y,-X+1/2,Z+1/2
REMARK 290 40555 -Y,X+1/2,Z+1/2
REMARK 290 41555 X,Z+1/2,-Y+1/2
REMARK 290 42555 -X,Z+1/2,Y+1/2
REMARK 290 43555 -X,-Z+1/2,-Y+1/2
REMARK 290 44555 X,-Z+1/2,Y+1/2
REMARK 290 45555 Z,Y+1/2,-X+1/2
REMARK 290 46555 Z,-Y+1/2,X+1/2
REMARK 290 47555 -Z,Y+1/2,X+1/2
REMARK 290 48555 -Z,-Y+1/2,-X+1/2
REMARK 290 49555 X+1/2,Y,Z+1/2
REMARK 290 50555 -X+1/2,-Y,Z+1/2
REMARK 290 51555 -X+1/2,Y,-Z+1/2
REMARK 290 52555 X+1/2,-Y,-Z+1/2
REMARK 290 53555 Z+1/2,X,Y+1/2
REMARK 290 54555 Z+1/2,-X,-Y+1/2
REMARK 290 55555 -Z+1/2,-X,Y+1/2
REMARK 290 56555 -Z+1/2,X,-Y+1/2
REMARK 290 57555 Y+1/2,Z,X+1/2
REMARK 290 58555 -Y+1/2,Z,-X+1/2
REMARK 290 59555 Y+1/2,-Z,-X+1/2
REMARK 290 60555 -Y+1/2,-Z,X+1/2
REMARK 290 61555 Y+1/2,X,-Z+1/2
REMARK 290 62555 -Y+1/2,-X,-Z+1/2
REMARK 290 63555 Y+1/2,-X,Z+1/2
REMARK 290 64555 -Y+1/2,X,Z+1/2
REMARK 290 65555 X+1/2,Z,-Y+1/2
REMARK 290 66555 -X+1/2,Z,Y+1/2
REMARK 290 67555 -X+1/2,-Z,-Y+1/2
REMARK 290 68555 X+1/2,-Z,Y+1/2
REMARK 290 69555 Z+1/2,Y,-X+1/2
REMARK 290 70555 Z+1/2,-Y,X+1/2
REMARK 290 71555 -Z+1/2,Y,X+1/2
REMARK 290 72555 -Z+1/2,-Y,-X+1/2
REMARK 290 73555 X+1/2,Y+1/2,Z
REMARK 290 74555 -X+1/2,-Y+1/2,Z
REMARK 290 75555 -X+1/2,Y+1/2,-Z
REMARK 290 76555 X+1/2,-Y+1/2,-Z
REMARK 290 77555 Z+1/2,X+1/2,Y
REMARK 290 78555 Z+1/2,-X+1/2,-Y
REMARK 290 79555 -Z+1/2,-X+1/2,Y
REMARK 290 80555 -Z+1/2,X+1/2,-Y
REMARK 290 81555 Y+1/2,Z+1/2,X
REMARK 290 82555 -Y+1/2,Z+1/2,-X
REMARK 290 83555 Y+1/2,-Z+1/2,-X
REMARK 290 84555 -Y+1/2,-Z+1/2,X
REMARK 290 85555 Y+1/2,X+1/2,-Z
REMARK 290 86555 -Y+1/2,-X+1/2,-Z
REMARK 290 87555 Y+1/2,-X+1/2,Z
REMARK 290 88555 -Y+1/2,X+1/2,Z
REMARK 290 89555 X+1/2,Z+1/2,-Y
REMARK 290 90555 -X+1/2,Z+1/2,Y
REMARK 290 91555 -X+1/2,-Z+1/2,-Y
REMARK 290 92555 X+1/2,-Z+1/2,Y
REMARK 290 93555 Z+1/2,Y+1/2,-X
REMARK 290 94555 Z+1/2,-Y+1/2,X
REMARK 290 95555 -Z+1/2,Y+1/2,X
REMARK 290 96555 -Z+1/2,-Y+1/2,-X
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 49 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 49 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 49 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY1 50 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 50 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 50 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY1 51 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 51 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 51 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY1 52 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 52 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 52 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY1 53 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY2 53 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 53 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY1 54 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY2 54 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 54 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY1 55 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY2 55 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 55 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY1 56 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY2 56 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 56 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY1 57 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY2 57 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 57 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 58 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY2 58 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 58 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 59 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY2 59 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 59 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 60 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY2 60 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 60 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 61 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY2 61 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 61 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY1 62 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY2 62 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 62 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY1 63 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY2 63 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 63 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY1 64 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY2 64 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 64 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY1 65 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 65 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 65 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY1 66 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 66 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 66 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY1 67 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 67 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 67 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY1 68 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 68 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 68 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY1 69 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY2 69 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 69 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 70 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY2 70 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 70 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 71 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY2 71 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 71 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 72 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY2 72 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 72 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY1 73 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 73 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY3 73 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 74 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 74 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY3 74 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 75 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 75 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY3 75 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 76 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 76 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY3 76 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 77 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY2 77 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 77 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 78 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY2 78 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 78 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 79 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY2 79 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 79 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 80 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY2 80 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 80 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 81 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY2 81 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY3 81 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 82 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY2 82 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY3 82 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 83 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY2 83 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY3 83 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 84 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY2 84 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY3 84 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 85 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY2 85 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 85 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 86 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY2 86 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 86 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 87 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY2 87 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 87 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 88 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY2 88 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY3 88 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 89 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 89 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY3 89 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 90 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 90 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY3 90 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 91 -1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 91 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY3 91 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 92 1.000000 0.000000 0.000000 116.17350
REMARK 290 SMTRY2 92 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY3 92 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 93 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY2 93 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY3 93 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 94 0.000000 0.000000 1.000000 116.17350
REMARK 290 SMTRY2 94 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY3 94 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 95 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY2 95 0.000000 1.000000 0.000000 116.17350
REMARK 290 SMTRY3 95 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 96 0.000000 0.000000 -1.000000 116.17350
REMARK 290 SMTRY2 96 0.000000 -1.000000 0.000000 116.17350
REMARK 290 SMTRY3 96 -1.000000 0.000000 0.000000 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.6 KCAL/MOL
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 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 1.000000 0.000000 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 HOH A2013 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2014 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 LEU A 351
REMARK 465 THR A 352
REMARK 465 GLY A 353
REMARK 465 GLN A 354
REMARK 465 ASP A 420
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 THR A 427
REMARK 465 PRO A 428
REMARK 465 LEU A 429
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: 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 A 285 CA - CB - SG ANGL. DEV. = -7.1 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 -141.60 56.10
REMARK 500 MET A 143 46.97 -149.48
REMARK 500 SER A 148 148.42 -175.44
REMARK 500 ARG A 218 22.99 -141.55
REMARK 500 SER A 232 -131.34 62.65
REMARK 500 VAL A 280 -60.94 -125.92
REMARK 500 GLN A 336 114.58 -166.01
REMARK 500 ASN A 348 41.85 70.38
REMARK 500 GLU A 390 157.60 64.66
REMARK 500 ILE A 391 -36.90 -159.03
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 PO4 A1453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
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 A WNT SIGNAL REGULATOR - IODIDE COMPLEX
REMARK 900 AT 2.3A
REMARK 900 RELATED ID: 4UYW RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR - CRYSTAL FORM I
REMARK 900 - LIGAND 1 - 1.7A
REMARK 900 RELATED ID: 4UYZ RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR - CRYSTAL FORM II
REMARK 900 - 2.8A
REMARK 900 RELATED ID: 4UZ1 RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR - CRYSTAL FORM III
REMARK 900 - 1.4A
REMARK 900 RELATED ID: 4UZ5 RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR - CRYSTAL FORM IV
REMARK 900 - 2.1A
REMARK 900 RELATED ID: 4UZ6 RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR - CRYSTAL FORM V
REMARK 900 - 1.9A
REMARK 900 RELATED ID: 4UZ7 RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR - CRYSTAL FORM VI
REMARK 900 - 2.2A
REMARK 900 RELATED ID: 4UZ9 RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR - CRYSTAL FORM VII
REMARK 900 - 2.2A
DBREF 4UZA A 80 452 UNP Q6P988 NOTUM_HUMAN 80 452
SEQADV 4UZA GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZA THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZA THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZA LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZA HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZA HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZA HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZA HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZA HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZA HIS A 460 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZA SER A 144 UNP Q6P988 ARG 144 ENGINEERED MUTATION
SEQADV 4UZA SER A 145 UNP Q6P988 ARG 145 ENGINEERED MUTATION
SEQADV 4UZA 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 SER SER 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 PO4 A1453 5
HETNAM PO4 PHOSPHATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 PO4 O4 P 3-
FORMUL 3 NAG C8 H15 N O6
FORMUL 4 HOH *23(H2 O)
HELIX 1 1 GLN A 84 ASP A 88 5 5
HELIX 2 2 ASN A 132 SER A 144 1 13
HELIX 3 3 SER A 145 MET A 147 5 3
HELIX 4 4 THR A 159 SER A 163 5 5
HELIX 5 5 MET A 203 GLY A 217 1 15
HELIX 6 6 ARG A 218 ALA A 223 5 6
HELIX 7 7 SER A 232 LEU A 252 1 21
HELIX 8 8 ALA A 286 ASN A 299 1 14
HELIX 9 9 PRO A 303 ARG A 308 1 6
HELIX 10 10 GLU A 314 PHE A 319 5 6
HELIX 11 11 PHE A 320 TYR A 325 1 6
HELIX 12 12 PRO A 326 LEU A 328 5 3
HELIX 13 13 GLU A 341 ASP A 347 1 7
HELIX 14 14 GLN A 357 LYS A 376 1 20
HELIX 15 15 LEU A 407 SER A 417 1 11
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 2.04
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.01
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.08
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.03
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.04
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.07
LINK ND2 ASN A 96 C1 NAG A1452 1555 1555 1.47
SITE 1 AC1 6 LYS A 403 ARG A 409 HIS A 412 ARG A 416
SITE 2 AC1 6 CYS A 432 SER A 439
SITE 1 AC2 2 ASN A 96 ARG A 213
CRYST1 232.347 232.347 232.347 90.00 90.00 90.00 F 4 3 2 96
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 0.004304 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004304 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004304 0.00000
TER 2846 THR A 451
MASTER 756 0 2 15 14 0 3 6 2887 1 34 30
END
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