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HEADER SIGNALING PROTEIN 24-JUL-20 6ZVL
TITLE ARUK3000263 COMPLEX WITH NOTUM
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 NOTUM, INHIBITOR, WNT, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHAO,R.RUZA
REVDAT 1 11-NOV-20 6ZVL 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. 1.30 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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 81770
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 3945
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 52.8300 - 3.9500 1.00 3072 129 0.1894 0.2075
REMARK 3 2 3.9500 - 3.1300 1.00 2902 159 0.1824 0.1920
REMARK 3 3 3.1300 - 2.7400 1.00 2890 144 0.1816 0.1770
REMARK 3 4 2.7400 - 2.4900 1.00 2862 137 0.1826 0.1981
REMARK 3 5 2.4900 - 2.3100 1.00 2869 130 0.1735 0.1953
REMARK 3 6 2.3100 - 2.1700 1.00 2813 158 0.1716 0.2090
REMARK 3 7 2.1700 - 2.0600 1.00 2842 142 0.1693 0.1812
REMARK 3 8 2.0600 - 1.9700 1.00 2856 137 0.1696 0.1944
REMARK 3 9 1.9700 - 1.9000 1.00 2809 135 0.1772 0.2081
REMARK 3 10 1.9000 - 1.8300 0.99 2825 128 0.1859 0.2212
REMARK 3 11 1.8300 - 1.7800 0.99 2821 127 0.1911 0.2242
REMARK 3 12 1.7800 - 1.7200 1.00 2754 174 0.1975 0.2381
REMARK 3 13 1.7200 - 1.6800 0.99 2793 152 0.2046 0.2410
REMARK 3 14 1.6800 - 1.6400 0.99 2786 126 0.2161 0.2174
REMARK 3 15 1.6400 - 1.6000 0.99 2785 151 0.2218 0.2525
REMARK 3 16 1.6000 - 1.5700 0.98 2749 130 0.2319 0.2162
REMARK 3 17 1.5700 - 1.5400 0.99 2743 147 0.2300 0.2962
REMARK 3 18 1.5400 - 1.5100 0.98 2796 124 0.2495 0.2817
REMARK 3 19 1.5100 - 1.4800 0.98 2766 128 0.2662 0.3031
REMARK 3 20 1.4800 - 1.4500 0.98 2714 151 0.2797 0.2995
REMARK 3 21 1.4500 - 1.4300 0.98 2728 151 0.2902 0.3364
REMARK 3 22 1.4300 - 1.4100 0.97 2727 142 0.3175 0.3567
REMARK 3 23 1.4100 - 1.3900 0.97 2714 141 0.3383 0.3891
REMARK 3 24 1.3900 - 1.3700 0.97 2698 125 0.3413 0.4065
REMARK 3 25 1.3700 - 1.3500 0.96 2672 164 0.3606 0.3800
REMARK 3 26 1.3500 - 1.3300 0.95 2668 145 0.3553 0.4200
REMARK 3 27 1.3300 - 1.3200 0.96 2675 145 0.3836 0.4299
REMARK 3 28 1.3200 - 1.3000 0.90 2496 123 0.3878 0.3917
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.090
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.86
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 86 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2018 81.7283 79.0635
REMARK 3 T TENSOR
REMARK 3 T11: 0.1296 T22: 0.0851
REMARK 3 T33: 0.1402 T12: 0.0049
REMARK 3 T13: -0.0153 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 1.1274 L22: 1.1616
REMARK 3 L33: 3.0162 L12: -0.1419
REMARK 3 L13: -0.4691 L23: -0.5351
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: -0.0029 S13: 0.1194
REMARK 3 S21: -0.0253 S22: 0.0019 S23: 0.0257
REMARK 3 S31: -0.1954 S32: -0.0531 S33: -0.0092
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5945 70.4609 79.1641
REMARK 3 T TENSOR
REMARK 3 T11: 0.0811 T22: 0.1027
REMARK 3 T33: 0.1082 T12: 0.0090
REMARK 3 T13: 0.0086 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 1.6893 L22: 2.1276
REMARK 3 L33: 0.5568 L12: 0.1388
REMARK 3 L13: -0.0284 L23: 0.3953
REMARK 3 S TENSOR
REMARK 3 S11: 0.0339 S12: 0.1018 S13: 0.0424
REMARK 3 S21: -0.1140 S22: -0.0289 S23: -0.1934
REMARK 3 S31: -0.0861 S32: 0.0351 S33: -0.0690
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 298 THROUGH 320 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8693 69.7736 76.6535
REMARK 3 T TENSOR
REMARK 3 T11: 0.1148 T22: 0.1491
REMARK 3 T33: 0.1577 T12: -0.0179
REMARK 3 T13: 0.0257 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 5.3254 L22: 4.1559
REMARK 3 L33: 3.4330 L12: -2.6853
REMARK 3 L13: 1.6611 L23: -2.6535
REMARK 3 S TENSOR
REMARK 3 S11: -0.0546 S12: 0.1192 S13: 0.3012
REMARK 3 S21: 0.0371 S22: -0.0875 S23: -0.3640
REMARK 3 S31: -0.1924 S32: 0.2288 S33: 0.1316
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 452 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8518 57.5091 83.9456
REMARK 3 T TENSOR
REMARK 3 T11: 0.0917 T22: 0.0997
REMARK 3 T33: 0.1100 T12: 0.0012
REMARK 3 T13: 0.0026 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.2367 L22: 1.4497
REMARK 3 L33: 1.5824 L12: 0.1565
REMARK 3 L13: -0.2893 L23: 0.7789
REMARK 3 S TENSOR
REMARK 3 S11: -0.0428 S12: 0.0346 S13: -0.1053
REMARK 3 S21: 0.0381 S22: -0.0060 S23: 0.0731
REMARK 3 S31: 0.0782 S32: -0.0895 S33: 0.0559
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 6ZVL 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_1292110293.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-18
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) : 0.9159
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83089
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 59.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.32
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 : 1.800
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 (%): 36.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM
REMARK 280 CITRATE, PH 4.2, 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 29.90250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.01800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.89550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.01800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.90250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.89550
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: 1620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 HIS A 276
REMARK 465 THR A 277
REMARK 465 ASP A 278
REMARK 465 CYS A 279
REMARK 465 VAL A 280
REMARK 465 ASP A 281
REMARK 465 THR A 282
REMARK 465 ILE A 283
REMARK 465 THR A 284
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 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 HH12 ARG A 409 O1 SO4 A 502 1.20
REMARK 500 HH22 ARG A 409 O4 SO4 A 502 1.56
REMARK 500 OD1 ASN A 366 NH2 ARG A 369 1.88
REMARK 500 NH1 ARG A 409 O1 SO4 A 502 2.02
REMARK 500 NE2 GLN A 209 OE1 GLN A 248 2.10
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 H ARG A 144 O3 SO4 A 502 2574 1.59
REMARK 500 N ARG A 144 O3 SO4 A 502 2574 2.14
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 LYS A 197 CD - CE - NZ ANGL. DEV. = -17.8 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 GLU A 87 66.65 -108.29
REMARK 500 TRP A 128 -142.55 59.61
REMARK 500 ALA A 191 57.52 -144.94
REMARK 500 SER A 232 -122.52 59.08
REMARK 500 SER A 232 -122.17 58.47
REMARK 500 GLN A 311 -177.34 70.10
REMARK 500 GLU A 390 158.61 63.06
REMARK 500 ILE A 391 -34.97 -147.61
REMARK 500 HIS A 444 12.01 92.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ZUV RELATED DB: PDB
DBREF 6ZVL A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 6ZVL GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 6ZVL GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 6ZVL 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 28
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET DMS A 506 10
HET DMS A 507 10
HET EDO A 508 10
HET QR2 A 509 17
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM QR2 5-[4-CHLORANYL-3-(TRIFLUOROMETHYL)PHENYL]-3~{H}-1,3,4-
HETNAM 2 QR2 OXADIAZOL-2-ONE
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 4(O4 S 2-)
FORMUL 7 DMS 2(C2 H6 O S)
FORMUL 9 EDO C2 H6 O2
FORMUL 10 QR2 C9 H4 CL F3 N2 O2
FORMUL 11 HOH *120(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 GLY A 253 1 22
HELIX 7 AA7 ALA A 286 ASN A 299 1 14
HELIX 8 AA8 PRO A 303 GLN A 311 1 9
HELIX 9 AA9 GLU A 314 PHE A 319 5 6
HELIX 10 AB1 PHE A 320 TYR A 325 1 6
HELIX 11 AB2 PRO A 326 LEU A 328 5 3
HELIX 12 AB3 GLU A 341 ASP A 347 1 7
HELIX 13 AB4 GLN A 357 LYS A 376 1 20
HELIX 14 AB5 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 SER A 381
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 2.04
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.03
SSBOND 3 CYS A 306 CYS A 318 1555 1555 2.04
SSBOND 4 CYS A 386 CYS A 449 1555 1555 2.03
SSBOND 5 CYS A 413 CYS A 432 1555 1555 2.02
SSBOND 6 CYS A 440 CYS A 445 1555 1555 2.02
LINK ND2 ASN A 96 C1 NAG A 501 1555 1555 1.43
CRYST1 59.805 71.791 78.036 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 0.016721 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013929 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012815 0.00000
TER 5546 GLY A 452
MASTER 403 0 9 14 14 0 0 6 2973 1 108 30
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