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HEADER HYDROLASE 03-SEP-14 4UYW
TITLE STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I HEPARIN
TITLE 2 FRAGMENT COMPLEX - 1.7A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN NOTUM HOMOLOG;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 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_VECTOR_TYPE: PLASMID;
SOURCE 10 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 4UYW 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. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 89.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.99
REMARK 3 NUMBER OF REFLECTIONS : 87882
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) : 0.18226
REMARK 3 R VALUE (WORKING SET) : 0.18169
REMARK 3 FREE R VALUE : 0.22092
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.5
REMARK 3 FREE R VALUE TEST SET COUNT : 1328
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) : 1.700
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.744
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6496
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.272
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.283
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5637
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 475
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.082
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.41
REMARK 3 B22 (A**2) : 1.12
REMARK 3 B33 (A**2) : -0.71
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): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.691
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5877 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5416 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8019 ; 1.374 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12407 ; 0.819 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 709 ; 6.077 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 288 ;32.390 ;22.257
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 942 ;12.205 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 65 ;17.460 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 856 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6636 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1480 ; 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): 2786 ; 1.309 ; 1.762
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2785 ; 1.309 ; 1.761
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3475 ; 2.185 ; 2.623
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3089 ; 1.927 ; 2.123
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 85 A 451
REMARK 3 ORIGIN FOR THE GROUP (A): 50.5003 -28.0357 -29.0765
REMARK 3 T TENSOR
REMARK 3 T11: 0.0652 T22: 0.0417
REMARK 3 T33: 0.0749 T12: 0.0243
REMARK 3 T13: -0.0173 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.9482 L22: 0.0806
REMARK 3 L33: 0.2976 L12: -0.0514
REMARK 3 L13: 0.0992 L23: 0.0735
REMARK 3 S TENSOR
REMARK 3 S11: -0.0579 S12: -0.0353 S13: 0.0677
REMARK 3 S21: -0.0171 S22: 0.0199 S23: -0.0343
REMARK 3 S31: -0.0414 S32: -0.0383 S33: 0.0379
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 86 B 451
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5225 -14.9562 -0.7144
REMARK 3 T TENSOR
REMARK 3 T11: 0.0881 T22: 0.0965
REMARK 3 T33: 0.0498 T12: 0.0885
REMARK 3 T13: -0.0154 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 0.5329 L22: 0.4612
REMARK 3 L33: 0.3916 L12: -0.4330
REMARK 3 L13: 0.0219 L23: -0.0960
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: 0.0419 S13: -0.0671
REMARK 3 S21: 0.0727 S22: 0.0211 S23: -0.0060
REMARK 3 S31: -0.0918 S32: -0.1047 S33: -0.0049
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 4UYW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-SEP-14.
REMARK 100 THE PDBE ID CODE IS EBI-61673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
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 : 89279
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.70
REMARK 200 RESOLUTION RANGE LOW (A) : 47.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.7
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.90
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 (%): 47.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 37.03200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 89.28000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.03200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 89.28000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 HOH B2146 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 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 THR A 352
REMARK 465 GLY A 353
REMARK 465 GLN A 354
REMARK 465 PRO A 355
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 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 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 LYS B 197
REMARK 465 ASN B 198
REMARK 465 THR B 352
REMARK 465 GLY B 353
REMARK 465 GLN B 354
REMARK 465 PRO B 355
REMARK 465 VAL B 356
REMARK 465 HIS B 419
REMARK 465 ASP B 420
REMARK 465 SER B 421
REMARK 465 HIS B 422
REMARK 465 LYS B 423
REMARK 465 ALA B 424
REMARK 465 SER B 425
REMARK 465 LYS B 426
REMARK 465 THR B 427
REMARK 465 PRO B 428
REMARK 465 LEU B 429
REMARK 465 LYS B 430
REMARK 465 GLY B 431
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 GLU B 196 CG CD OE1 OE2
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 NH2 ARG B 292 NH2 ARG B 292 2555 1.87
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 A 432 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 PRO A 433 C - N - CA ANGL. DEV. = 12.6 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 -139.10 55.62
REMARK 500 TYR A 129 172.76 179.96
REMARK 500 ASN A 169 75.24 -154.24
REMARK 500 SER A 232 -119.16 52.11
REMARK 500 VAL A 280 -73.68 -125.25
REMARK 500 PHE A 339 69.13 -119.84
REMARK 500 GLU A 390 156.76 72.23
REMARK 500 ILE A 391 -36.04 -160.19
REMARK 500 TRP B 128 -140.05 61.59
REMARK 500 TYR B 129 172.61 176.03
REMARK 500 MET B 143 54.01 -147.07
REMARK 500 SER B 232 -121.34 54.84
REMARK 500 VAL B 280 -60.05 -121.74
REMARK 500 PHE B 339 74.36 -117.99
REMARK 500 GLU B 390 153.55 71.67
REMARK 500 ILE B 391 -34.86 -156.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS A 432 PRO A 433 -146.07
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 H1S 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 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B1452 BOUND TO ASN B 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: 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: 4UZ9 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE 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
DBREF 4UYW A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
DBREF 4UYW B 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 4UYW GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS A 460 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 4UYW GLU B 78 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW THR B 79 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW GLY B 80 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW GLY B 452 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW THR B 453 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW LYS B 454 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS B 455 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS B 456 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS B 457 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS B 458 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS B 459 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW HIS B 460 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYW 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 NAG A1452 14
HET NAG B1452 14
HET H1S A1453 35
HETNAM H1S HEPARIN DISACCHARIDE I-S
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 3 H1S C12 H15 N O19 S3 4-
FORMUL 4 NAG 2(C8 H15 N O6)
FORMUL 5 HOH *475(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 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 HIS A 419 1 13
HELIX 16 16 ASN B 132 MET B 143 1 12
HELIX 17 17 ARG B 144 SER B 148 5 5
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 GLY B 253 1 22
HELIX 22 22 ALA B 286 TRP B 298 1 13
HELIX 23 23 PRO B 303 ARG B 308 1 6
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 LEU B 418 1 12
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 HIS B 435 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 2.13
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.05
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.07
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.14
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.04
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.05
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.02
SSBOND 8 CYS B 101 CYS B 183 1555 1555 2.11
SSBOND 9 CYS B 130 CYS B 136 1555 1555 2.05
SSBOND 10 CYS B 279 CYS B 285 1555 1555 2.06
SSBOND 11 CYS B 306 CYS B 318 1555 1555 2.13
SSBOND 12 CYS B 386 CYS B 449 1555 1555 2.03
SSBOND 13 CYS B 413 CYS B 432 1555 1555 2.04
SSBOND 14 CYS B 440 CYS B 445 1555 1555 2.04
LINK ND2 ASN A 96 C1 NAG A1452 1555 1555 1.44
LINK ND2 ASN B 96 C1 NAG B1452 1555 1555 1.44
SITE 1 AC1 16 ARG A 90 LYS A 112 GLU A 113 ARG A 115
SITE 2 AC1 16 GLU A 247 LYS A 251 GLU A 304 ARG A 305
SITE 3 AC1 16 ARG A 308 ARG A 329 HOH A2012 HOH A2034
SITE 4 AC1 16 HOH A2035 HOH A2037 HOH A2038 HOH A2201
SITE 1 AC2 4 ASN A 96 SER A 98 VAL A 99 HOH A2268
SITE 1 AC3 5 ASN B 96 VAL B 99 SER B 193 HOH B2014
SITE 2 AC3 5 HOH B2207
CRYST1 74.064 178.560 61.193 90.00 90.00 90.00 P 21 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 0.013502 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005600 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016342 0.00000
MTRIX1 1 -0.695000 0.719000 0.005000 72.84200 1
MTRIX2 1 0.717000 0.693000 -0.077000 -29.65100 1
MTRIX3 1 -0.059000 -0.050000 -0.997000 -29.31200 1
TER 2837 THR A 451
TER 5639 THR B 451
MASTER 509 0 3 30 28 0 7 9 6177 2 93 60
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