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HEADER SIGNALING PROTEIN 23-JUL-20 6ZUV
TITLE NOTUM FRAGMENT 286
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PALMITOLEOYL-PROTEIN CARBOXYLESTERASE NOTUM;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HNOTUM;
COMPND 5 EC: 3.1.1.98;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NOTUM, OK/SW-CL.30;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS WNT NOTUM INHIBITOR COMPLEX, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHAO,E.Y.JONES
REVDAT 1 11-NOV-20 6ZUV 0
JRNL AUTH W.MAHY,N.J.WILLIS,Y.ZHAO,H.L.WOODWARD,F.SVENSSON,J.SIPTHORP,
JRNL AUTH 2 L.VECCHIA,R.R.RUZA,J.HILLIER,S.KJAER,S.FREW,A.MONAGHAN,
JRNL AUTH 3 M.BICTASH,P.C.SALINAS,P.WHITING,J.P.VINCENT,E.Y.JONES,
JRNL AUTH 4 P.V.FISH
JRNL TITL 5-PHENYL-1,3,4-OXADIAZOL-2(3 H )-ONES ARE POTENT INHIBITORS
JRNL TITL 2 OF NOTUM CARBOXYLESTERASE ACTIVITY IDENTIFIED BY THE
JRNL TITL 3 OPTIMIZATION OF A CRYSTALLOGRAPHIC FRAGMENT SCREENING HIT.
JRNL REF J.MED.CHEM. 2020
JRNL REFN ISSN 0022-2623
JRNL PMID 33124429
JRNL DOI 10.1021/ACS.JMEDCHEM.0C01391
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 51471
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2522
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 53.3300 - 4.0400 1.00 2941 161 0.1888 0.2362
REMARK 3 2 4.0400 - 3.2000 1.00 2828 138 0.1806 0.2388
REMARK 3 3 3.2000 - 2.8000 1.00 2782 148 0.1963 0.2468
REMARK 3 4 2.8000 - 2.5400 1.00 2779 130 0.1972 0.2566
REMARK 3 5 2.5400 - 2.3600 1.00 2767 131 0.1967 0.2206
REMARK 3 6 2.3600 - 2.2200 1.00 2715 168 0.1942 0.2383
REMARK 3 7 2.2200 - 2.1100 1.00 2747 136 0.1873 0.2458
REMARK 3 8 2.1100 - 2.0200 1.00 2712 133 0.2011 0.2617
REMARK 3 9 2.0200 - 1.9400 0.99 2739 136 0.2119 0.2433
REMARK 3 10 1.9400 - 1.8700 0.99 2691 152 0.2232 0.3090
REMARK 3 11 1.8700 - 1.8200 0.99 2701 135 0.2503 0.2773
REMARK 3 12 1.8200 - 1.7600 1.00 2708 147 0.2655 0.3067
REMARK 3 13 1.7600 - 1.7200 0.99 2665 153 0.2975 0.3415
REMARK 3 14 1.7200 - 1.6800 0.99 2689 141 0.3028 0.3198
REMARK 3 15 1.6800 - 1.6400 0.98 2655 126 0.3217 0.3705
REMARK 3 16 1.6400 - 1.6000 0.97 2626 136 0.3410 0.3850
REMARK 3 17 1.6000 - 1.5700 0.97 2649 120 0.3622 0.3958
REMARK 3 18 1.5700 - 1.5400 0.94 2555 131 0.3685 0.4009
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 224 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4384 10.4868 -0.4075
REMARK 3 T TENSOR
REMARK 3 T11: 0.1764 T22: 0.1242
REMARK 3 T33: 0.1769 T12: -0.0018
REMARK 3 T13: -0.0194 T23: 0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 1.0405 L22: 1.2916
REMARK 3 L33: 2.3049 L12: 0.1100
REMARK 3 L13: -0.5302 L23: 0.4161
REMARK 3 S TENSOR
REMARK 3 S11: -0.0090 S12: 0.0360 S13: 0.1367
REMARK 3 S21: 0.0440 S22: 0.0003 S23: 0.0022
REMARK 3 S31: -0.2151 S32: 0.0156 S33: -0.0003
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 286 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6587 -2.0457 -1.6275
REMARK 3 T TENSOR
REMARK 3 T11: 0.1296 T22: 0.1359
REMARK 3 T33: 0.1292 T12: 0.0013
REMARK 3 T13: 0.0128 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 1.6012 L22: 2.1258
REMARK 3 L33: 0.2526 L12: -0.2417
REMARK 3 L13: -0.0827 L23: -0.1335
REMARK 3 S TENSOR
REMARK 3 S11: -0.0489 S12: -0.0228 S13: 0.0201
REMARK 3 S21: 0.1755 S22: 0.0185 S23: 0.1125
REMARK 3 S31: -0.1303 S32: -0.0903 S33: -0.0104
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 287 THROUGH 320 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7338 -2.0743 4.7566
REMARK 3 T TENSOR
REMARK 3 T11: 0.1345 T22: 0.1668
REMARK 3 T33: 0.1867 T12: -0.0070
REMARK 3 T13: 0.0379 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 4.6626 L22: 5.5618
REMARK 3 L33: 2.9266 L12: 2.2534
REMARK 3 L13: 1.3872 L23: 2.5336
REMARK 3 S TENSOR
REMARK 3 S11: 0.1374 S12: -0.2303 S13: 0.2665
REMARK 3 S21: 0.0869 S22: -0.2490 S23: 0.3229
REMARK 3 S31: -0.1248 S32: -0.1953 S33: 0.0530
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 451 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3790 -14.3361 -5.6032
REMARK 3 T TENSOR
REMARK 3 T11: 0.1484 T22: 0.1606
REMARK 3 T33: 0.1937 T12: -0.0027
REMARK 3 T13: 0.0129 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.9139 L22: 1.5686
REMARK 3 L33: 1.7706 L12: -0.1037
REMARK 3 L13: -0.4826 L23: -0.8949
REMARK 3 S TENSOR
REMARK 3 S11: -0.0644 S12: -0.0134 S13: -0.1190
REMARK 3 S21: -0.0766 S22: -0.0285 S23: -0.1329
REMARK 3 S31: 0.1250 S32: 0.1248 S33: 0.1013
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ZUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1292110251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
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) : 0.9282
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52038
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540
REMARK 200 RESOLUTION RANGE LOW (A) : 79.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 6TR5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM
REMARK 280 CITRATE, PH4.2, EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 30.33650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.50050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.14200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.50050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.33650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.14200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 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 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 GLU A 87
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 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: 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 NH1 ARG A 296 O HOH A 601 2.16
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 OE1 GLU A 167 OG1 THR A 282 2554 2.08
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 ARG A 305 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 ARG A 329 CD - NE - CZ ANGL. DEV. = 14.8 DEGREES
REMARK 500 ARG A 329 NE - CZ - NH2 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 -140.79 53.18
REMARK 500 MET A 143 43.80 -141.64
REMARK 500 MET A 147 -1.66 -143.42
REMARK 500 SER A 148 147.46 -171.30
REMARK 500 ALA A 191 57.31 -145.26
REMARK 500 ALA A 191 56.58 -145.26
REMARK 500 SER A 232 -126.80 61.43
REMARK 500 CYS A 279 91.20 -64.76
REMARK 500 GLN A 311 -178.90 72.10
REMARK 500 VAL A 356 -179.72 -57.29
REMARK 500 GLU A 390 163.38 64.39
REMARK 500 ILE A 391 -33.74 -163.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 329 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6ZUV A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 6ZUV GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 6ZUV GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZUV HIS A 460 UNP Q6P988 EXPRESSION TAG
SEQRES 1 A 383 GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG
SEQRES 2 A 383 LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP
SEQRES 3 A 383 GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY
SEQRES 4 A 383 SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR
SEQRES 5 A 383 CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR
SEQRES 6 A 383 MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR
SEQRES 7 A 383 ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU
SEQRES 8 A 383 ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO
SEQRES 9 A 383 TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS
SEQRES 10 A 383 SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE
SEQRES 11 A 383 ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU
SEQRES 12 A 383 SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER SER ALA
SEQRES 13 A 383 GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA
SEQRES 14 A 383 GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL
SEQRES 15 A 383 ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS
SEQRES 16 A 383 GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS
SEQRES 17 A 383 ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP
SEQRES 18 A 383 ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN
SEQRES 19 A 383 GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL
SEQRES 20 A 383 TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP
SEQRES 21 A 383 LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS
SEQRES 22 A 383 LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR
SEQRES 23 A 383 ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS
SEQRES 24 A 383 ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS
SEQRES 25 A 383 GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL
SEQRES 26 A 383 LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP
SEQRES 27 A 383 ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO
SEQRES 28 A 383 LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO
SEQRES 29 A 383 TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS
SEQRES 30 A 383 HIS HIS HIS HIS HIS HIS
HET NAG A 501 14
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET SO4 A 506 5
HET SO4 A 507 5
HET EDO A 508 4
HET EDO A 509 4
HET EDO A 510 10
HET B1J A 511 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM B1J [1-(4-CHLOROPHENYL)-1,2,3-TRIAZOL-4-YL]METHANOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 9 EDO 3(C2 H6 O2)
FORMUL 12 B1J C9 H8 CL N3 O
FORMUL 13 HOH *133(H2 O)
HELIX 1 AA1 ASN A 132 MET A 143 1 12
HELIX 2 AA2 ARG A 144 MET A 147 5 4
HELIX 3 AA3 THR A 159 SER A 163 5 5
HELIX 4 AA4 MET A 203 GLY A 217 1 15
HELIX 5 AA5 ARG A 218 ALA A 223 5 6
HELIX 6 AA6 SER A 232 LEU A 252 1 21
HELIX 7 AA7 ASP A 281 CYS A 285 5 5
HELIX 8 AA8 ALA A 286 ASN A 299 1 14
HELIX 9 AA9 PRO A 303 GLN A 311 1 9
HELIX 10 AB1 GLU A 314 PHE A 319 5 6
HELIX 11 AB2 PHE A 320 TYR A 325 1 6
HELIX 12 AB3 PRO A 326 LEU A 328 5 3
HELIX 13 AB4 GLU A 341 ASP A 347 1 7
HELIX 14 AB5 GLN A 357 LEU A 375 1 19
HELIX 15 AB6 LEU A 407 LEU A 418 1 12
SHEET 1 AA110 THR A 155 ARG A 156 0
SHEET 2 AA110 LEU A 89 LEU A 93 -1 N LEU A 89 O ARG A 156
SHEET 3 AA110 GLY A 108 LYS A 112 -1 O TYR A 109 N HIS A 92
SHEET 4 AA110 ASN A 176 ILE A 180 -1 O PHE A 179 N TYR A 110
SHEET 5 AA110 ARG A 119 LEU A 124 1 N PHE A 123 O ILE A 180
SHEET 6 AA110 VAL A 225 SER A 231 1 O LEU A 227 N TRP A 120
SHEET 7 AA110 GLN A 258 ASP A 264 1 O ARG A 260 N LEU A 228
SHEET 8 AA110 VAL A 332 VAL A 335 1 O VAL A 335 N ALA A 263
SHEET 9 AA110 SER A 381 ALA A 383 1 O PHE A 382 N VAL A 334
SHEET 10 AA110 HIS A 435 VAL A 437 1 O LEU A 436 N ALA A 383
SHEET 1 AA2 2 PHE A 339 ASP A 340 0
SHEET 2 AA2 2 LEU A 387 SER A 388 1 O SER A 388 N PHE A 339
SHEET 1 AA3 2 GLN A 401 VAL A 402 0
SHEET 2 AA3 2 THR A 405 SER A 406 -1 O THR A 405 N VAL A 402
SSBOND 1 CYS A 101 CYS A 183 1555 1555 2.03
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.03
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.04
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.06
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.02
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.04
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.03
LINK ND2 ASN A 96 C1 NAG A 501 1555 1555 1.44
CRYST1 60.673 72.284 79.001 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016482 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013834 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012658 0.00000
TER 2872 THR A 451
MASTER 399 0 11 15 14 0 0 6 3044 1 91 30
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