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HEADER HYDROLASE 08-OCT-19 6T2K
TITLE FURANO[2,3-D]PRYMIDINE AMIDES AS NOTUM INHIBITORS
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_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-
KEYWDS SUBSTRATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHAO,E.Y.JONES
REVDAT 1 01-JAN-20 6T2K 0
JRNL AUTH B.N.ATKINSON,D.STEADMAN,W.MAHY,Y.ZHAO,J.SIPTHORP,E.D.BAYLE,
JRNL AUTH 2 F.SVENSSON,G.PAPAGEORGIOU,F.JEGANATHAN,S.FREW,A.MONAGHAN,
JRNL AUTH 3 M.BICTASH,E.Y.JONES,P.V.FISH
JRNL TITL SCAFFOLD-HOPPING IDENTIFIES FURANO[2,3-D]PYRIMIDINE AMIDES
JRNL TITL 2 AS POTENT NOTUM INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. 26751 2019
JRNL REFN ESSN 1464-3405
JRNL PMID 31862412
JRNL DOI 10.1016/J.BMCL.2019.126751
REMARK 2
REMARK 2 RESOLUTION. 1.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_3488
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 69815
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 3458
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 4.7380 - 4.0344 1.00 2882 140 0.1922 0.2021
REMARK 3 2 4.0344 - 3.2024 1.00 2736 134 0.1738 0.1997
REMARK 3 3 3.2024 - 2.7977 1.00 2724 122 0.1871 0.2098
REMARK 3 4 2.7977 - 2.5419 1.00 2688 143 0.1850 0.1831
REMARK 3 5 2.5419 - 2.3597 1.00 2690 124 0.1775 0.2136
REMARK 3 6 2.3597 - 2.2206 1.00 2672 128 0.1696 0.2081
REMARK 3 7 2.2206 - 2.1094 1.00 2677 136 0.1660 0.2106
REMARK 3 8 2.1094 - 2.0176 1.00 2647 163 0.1700 0.1891
REMARK 3 9 2.0176 - 1.9399 1.00 2628 145 0.1722 0.2009
REMARK 3 10 1.9399 - 1.8730 1.00 2644 119 0.1734 0.2148
REMARK 3 11 1.8730 - 1.8144 1.00 2663 127 0.1770 0.2505
REMARK 3 12 1.8144 - 1.7625 1.00 2622 141 0.1837 0.2290
REMARK 3 13 1.7625 - 1.7161 1.00 2635 146 0.1815 0.2575
REMARK 3 14 1.7161 - 1.6743 1.00 2633 142 0.1955 0.2414
REMARK 3 15 1.6743 - 1.6362 1.00 2638 136 0.2020 0.2212
REMARK 3 16 1.6362 - 1.6014 1.00 2628 144 0.2018 0.2792
REMARK 3 17 1.6014 - 1.5693 1.00 2623 148 0.2121 0.2640
REMARK 3 18 1.5693 - 1.5397 1.00 2598 164 0.2169 0.2358
REMARK 3 19 1.5397 - 1.5122 1.00 2612 138 0.2238 0.2446
REMARK 3 20 1.5122 - 1.4866 1.00 2601 150 0.2398 0.2451
REMARK 3 21 1.4866 - 1.4626 1.00 2661 118 0.2583 0.3227
REMARK 3 22 1.4626 - 1.4401 1.00 2596 135 0.2690 0.3008
REMARK 3 23 1.4401 - 1.4189 1.00 2603 137 0.2884 0.3087
REMARK 3 24 1.4189 - 1.3989 1.00 2645 135 0.3040 0.3302
REMARK 3 25 1.3989 - 1.3800 1.00 2611 143 0.3019 0.3211
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.59
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 : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9910 11.0193 2.5731
REMARK 3 T TENSOR
REMARK 3 T11: 0.1846 T22: 0.1597
REMARK 3 T33: 0.2011 T12: -0.0082
REMARK 3 T13: -0.0178 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 1.3667 L22: 1.8275
REMARK 3 L33: 3.0493 L12: -0.0620
REMARK 3 L13: -0.0682 L23: 0.4793
REMARK 3 S TENSOR
REMARK 3 S11: -0.0290 S12: -0.0273 S13: 0.1578
REMARK 3 S21: 0.0815 S22: 0.0218 S23: -0.0911
REMARK 3 S31: -0.2498 S32: 0.0824 S33: 0.0016
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0818 7.3969 -1.8526
REMARK 3 T TENSOR
REMARK 3 T11: 0.1428 T22: 0.0827
REMARK 3 T33: 0.1402 T12: -0.0087
REMARK 3 T13: -0.0299 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 1.8072 L22: 1.9499
REMARK 3 L33: 3.7464 L12: -0.0592
REMARK 3 L13: -0.8500 L23: 0.5419
REMARK 3 S TENSOR
REMARK 3 S11: 0.1131 S12: 0.0029 S13: 0.1881
REMARK 3 S21: 0.0388 S22: -0.0233 S23: -0.0595
REMARK 3 S31: -0.3409 S32: -0.0406 S33: -0.0701
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 204 THROUGH 224 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8719 14.6824 -9.8867
REMARK 3 T TENSOR
REMARK 3 T11: 0.2495 T22: 0.1989
REMARK 3 T33: 0.2452 T12: 0.0079
REMARK 3 T13: -0.0321 T23: 0.0697
REMARK 3 L TENSOR
REMARK 3 L11: 1.8854 L22: 2.7647
REMARK 3 L33: 8.9876 L12: 0.5799
REMARK 3 L13: -1.2169 L23: -1.4090
REMARK 3 S TENSOR
REMARK 3 S11: -0.0249 S12: 0.3121 S13: 0.4053
REMARK 3 S21: -0.0948 S22: 0.0247 S23: -0.1044
REMARK 3 S31: -0.8419 S32: -0.0815 S33: -0.0155
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 286 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4535 -1.0889 -5.2761
REMARK 3 T TENSOR
REMARK 3 T11: 0.1187 T22: 0.1296
REMARK 3 T33: 0.1304 T12: -0.0033
REMARK 3 T13: 0.0081 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.9281 L22: 4.8009
REMARK 3 L33: 3.0954 L12: -0.7276
REMARK 3 L13: 0.7513 L23: -2.6870
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: 0.0174 S13: 0.0500
REMARK 3 S21: 0.0672 S22: 0.0306 S23: 0.2234
REMARK 3 S31: -0.1468 S32: -0.0820 S33: -0.1001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 287 THROUGH 320 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4369 -2.1562 4.6528
REMARK 3 T TENSOR
REMARK 3 T11: 0.1787 T22: 0.2365
REMARK 3 T33: 0.2373 T12: -0.0058
REMARK 3 T13: 0.0426 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 4.0570 L22: 5.2447
REMARK 3 L33: 4.7352 L12: 3.1220
REMARK 3 L13: 0.6474 L23: 4.0198
REMARK 3 S TENSOR
REMARK 3 S11: 0.1445 S12: -0.4741 S13: 0.1343
REMARK 3 S21: 0.3320 S22: -0.3645 S23: 0.4305
REMARK 3 S31: -0.0028 S32: -0.3033 S33: 0.2070
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 357 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8774 -11.6978 -0.3064
REMARK 3 T TENSOR
REMARK 3 T11: 0.1395 T22: 0.1332
REMARK 3 T33: 0.1433 T12: -0.0149
REMARK 3 T13: 0.0068 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 2.0338 L22: 2.4651
REMARK 3 L33: 2.7589 L12: -0.4833
REMARK 3 L13: -0.0672 L23: -1.5622
REMARK 3 S TENSOR
REMARK 3 S11: -0.0581 S12: -0.1733 S13: -0.1666
REMARK 3 S21: 0.1786 S22: 0.0205 S23: -0.0249
REMARK 3 S31: -0.0478 S32: 0.0427 S33: 0.0383
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 358 THROUGH 375 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6029 -23.1658 1.9817
REMARK 3 T TENSOR
REMARK 3 T11: 0.1822 T22: 0.1930
REMARK 3 T33: 0.2505 T12: 0.0048
REMARK 3 T13: 0.0354 T23: 0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 4.8055 L22: 4.7583
REMARK 3 L33: 8.8562 L12: -4.2801
REMARK 3 L13: 5.1625 L23: -5.9933
REMARK 3 S TENSOR
REMARK 3 S11: 0.0226 S12: -0.2850 S13: -0.3989
REMARK 3 S21: -0.2075 S22: 0.0343 S23: 0.0360
REMARK 3 S31: 0.4790 S32: -0.0620 S33: -0.0686
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 376 THROUGH 406 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8675 -11.2370 -8.0086
REMARK 3 T TENSOR
REMARK 3 T11: 0.1710 T22: 0.1874
REMARK 3 T33: 0.2044 T12: 0.0002
REMARK 3 T13: 0.0133 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 2.3227 L22: 2.0107
REMARK 3 L33: 1.8168 L12: -0.4698
REMARK 3 L13: -0.7335 L23: -1.5341
REMARK 3 S TENSOR
REMARK 3 S11: -0.0295 S12: 0.0003 S13: 0.0082
REMARK 3 S21: 0.0137 S22: -0.0721 S23: -0.1995
REMARK 3 S31: 0.0564 S32: 0.1793 S33: 0.1502
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 407 THROUGH 451 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6929 -13.8218 -14.3547
REMARK 3 T TENSOR
REMARK 3 T11: 0.1741 T22: 0.1759
REMARK 3 T33: 0.1890 T12: -0.0108
REMARK 3 T13: 0.0234 T23: -0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 1.5459 L22: 3.1051
REMARK 3 L33: 2.2263 L12: -0.3992
REMARK 3 L13: 0.0225 L23: -1.5183
REMARK 3 S TENSOR
REMARK 3 S11: 0.0664 S12: 0.1589 S13: -0.1170
REMARK 3 S21: -0.2777 S22: -0.0483 S23: -0.0412
REMARK 3 S31: 0.1967 S32: 0.0921 S33: 0.0494
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 6T2K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104745.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-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 : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9726
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 : 69891
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.380
REMARK 200 RESOLUTION RANGE LOW (A) : 47.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
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: 6R8P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULFATE 0.1 M SODIUM
REMARK 280 CITRATE PH4.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 300K
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 29.81000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.04500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.06500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.04500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.81000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.06500
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: 1860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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 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 CYS A 285
REMARK 465 LEU A 351
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 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 NZ LYS A 272 O HOH A 601 1.88
REMARK 500 OD1 ASP A 264 O HOH A 602 1.90
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 NZ LYS A 376 O HOH A 733 3544 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 196 CB GLU A 196 CG -0.124
REMARK 500 LYS A 430 CB LYS A 430 CG -0.226
REMARK 500 LYS A 430 CG LYS A 430 CD -0.277
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 416 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LYS A 430 CG - CD - CE ANGL. DEV. = -22.7 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 -145.76 59.75
REMARK 500 MET A 143 46.85 -140.33
REMARK 500 SER A 232 -123.00 62.93
REMARK 500 SER A 232 -123.79 64.07
REMARK 500 GLN A 311 -176.25 65.12
REMARK 500 HIS A 389 -83.48 -118.72
REMARK 500 ILE A 391 -44.79 -133.05
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 ILE A 391 ILE A 392 -143.59
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 SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue M9K A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 502 bound
REMARK 800 to ASN A 96
DBREF 6T2K A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 6T2K GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 6T2K GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 6T2K 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 SO4 A 501 5
HET NAG A 502 14
HET M9K A 503 18
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 4
HET EDO A 511 4
HETNAM SO4 SULFATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM M9K 2-(6-CHLORANYL-7-CYCLOPROPYL-THIENO[3,2-D]PYRIMIDIN-4-
HETNAM 2 M9K YL)SULFANYLETHANOIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 SO4 5(O4 S 2-)
FORMUL 3 NAG C8 H15 N O6
FORMUL 4 M9K C11 H9 CL N2 O2 S2
FORMUL 9 EDO 4(C2 H6 O2)
FORMUL 13 HOH *146(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 PRO A 287 ASN A 299 1 13
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 LEU A 375 1 19
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 ALA A 229 N LEU A 124
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 2.09
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.02
SSBOND 3 CYS A 306 CYS A 318 1555 1555 2.13
SSBOND 4 CYS A 386 CYS A 449 1555 1555 2.04
SSBOND 5 CYS A 413 CYS A 432 1555 1555 1.98
SSBOND 6 CYS A 440 CYS A 445 1555 1555 2.02
LINK ND2 ASN A 96 C1 NAG A 502 1555 1555 1.42
SITE 1 AC1 9 THR A 142 MET A 143 ARG A 144 ARG A 145
SITE 2 AC1 9 ARG A 409 HIS A 412 ARG A 416 HOH A 608
SITE 3 AC1 9 HOH A 626
SITE 1 AC2 9 GLY A 127 TRP A 128 SER A 232 ALA A 233
SITE 2 AC2 9 PHE A 268 PRO A 287 PHE A 319 PHE A 320
SITE 3 AC2 9 HIS A 389
SITE 1 AC3 6 PRO A 255 ARG A 372 LYS A 403 VAL A 437
SITE 2 AC3 6 HOH A 616 HOH A 705
SITE 1 AC4 7 ARG A 133 LYS A 197 ASN A 198 GLU A 199
SITE 2 AC4 7 ARG A 275 TYR A 297 HOH A 700
SITE 1 AC5 4 ARG A 305 GLN A 357 GLU A 358 ARG A 361
SITE 1 AC6 5 TYR A 274 ARG A 275 LEU A 360 HOH A 637
SITE 2 AC6 5 HOH A 677
SITE 1 AC7 7 LEU A 252 PRO A 433 VAL A 434 HIS A 435
SITE 2 AC7 7 HOH A 635 HOH A 656 HOH A 708
SITE 1 AC8 2 ARG A 90 GLU A 113
SITE 1 AC9 7 TYR A 325 LEU A 328 SER A 330 PRO A 331
SITE 2 AC9 7 VAL A 332 HOH A 603 HOH A 639
SITE 1 AD1 2 SER A 117 ARG A 118
SITE 1 AD2 7 ASN A 96 SER A 98 VAL A 99 PRO A 153
SITE 2 AD2 7 ARG A 154 THR A 155 HOH A 609
CRYST1 59.620 72.130 78.090 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 0.016773 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013864 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012806 0.00000
TER 2792 THR A 451
MASTER 551 0 11 14 14 0 21 6 2977 1 86 30
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