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HEADER HYDROLASE 22-APR-20 6YSK
TITLE 1-PHENYLPYRROLES AND 1-ENYLPYRROLIDINES AS INHIBITORS OF 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_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS NOTUM INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHAO,E.Y.JONES,P.FISH
REVDAT 1 16-SEP-20 6YSK 0
JRNL AUTH W.MAHY,M.PATEL,D.STEADMAN,H.L.WOODWARD,B.N.ATKINSON,
JRNL AUTH 2 F.SVENSSON,N.J.WILLIS,A.FLINT,D.PAPATHEODOROU,Y.ZHAO,
JRNL AUTH 3 L.VECCHIA,R.R.RUZA,J.HILLIER,S.FREW,A.MONAGHAN,A.COSTA,
JRNL AUTH 4 M.BICTASH,M.W.WALTER,E.Y.JONES,P.V.FISH
JRNL TITL SCREENING OF A CUSTOM-DESIGNED ACID FRAGMENT LIBRARY
JRNL TITL 2 IDENTIFIES 1-PHENYLPYRROLES AND 1-PHENYLPYRROLIDINES AS
JRNL TITL 3 INHIBITORS OF NOTUM CARBOXYLESTERASE ACTIVITY.
JRNL REF J.MED.CHEM. 2020
JRNL REFN ISSN 0022-2623
JRNL PMID 32787107
JRNL DOI 10.1021/ACS.JMEDCHEM.0C00660
REMARK 2
REMARK 2 RESOLUTION. 1.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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) : 1.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 103744
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 5035
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 39.7000 - 3.7600 1.00 3524 193 0.1770 0.1835
REMARK 3 2 3.7600 - 2.9800 1.00 3405 159 0.1880 0.2173
REMARK 3 3 2.9800 - 2.6100 1.00 3361 158 0.2014 0.1954
REMARK 3 4 2.6100 - 2.3700 1.00 3364 163 0.1938 0.2124
REMARK 3 5 2.3700 - 2.2000 1.00 3301 197 0.1854 0.1981
REMARK 3 6 2.2000 - 2.0700 1.00 3288 169 0.1841 0.1880
REMARK 3 7 2.0700 - 1.9700 1.00 3325 166 0.1855 0.2089
REMARK 3 8 1.9700 - 1.8800 1.00 3312 150 0.1854 0.1962
REMARK 3 9 1.8800 - 1.8100 1.00 3303 156 0.1850 0.2048
REMARK 3 10 1.8100 - 1.7500 1.00 3297 152 0.1806 0.2096
REMARK 3 11 1.7500 - 1.6900 1.00 3283 177 0.1804 0.2063
REMARK 3 12 1.6900 - 1.6400 1.00 3267 174 0.1835 0.2073
REMARK 3 13 1.6400 - 1.6000 1.00 3273 169 0.1820 0.2283
REMARK 3 14 1.6000 - 1.5600 1.00 3259 180 0.1816 0.2112
REMARK 3 15 1.5600 - 1.5200 1.00 3268 170 0.1925 0.2119
REMARK 3 16 1.5200 - 1.4900 1.00 3294 150 0.1991 0.2260
REMARK 3 17 1.4900 - 1.4600 1.00 3262 155 0.2102 0.2531
REMARK 3 18 1.4600 - 1.4300 1.00 3284 171 0.2183 0.2585
REMARK 3 19 1.4300 - 1.4100 1.00 3271 165 0.2276 0.2534
REMARK 3 20 1.4100 - 1.3900 1.00 3273 157 0.2379 0.2345
REMARK 3 21 1.3900 - 1.3600 1.00 3245 158 0.2408 0.2519
REMARK 3 22 1.3600 - 1.3400 1.00 3252 193 0.2502 0.2684
REMARK 3 23 1.3400 - 1.3200 1.00 3266 168 0.2556 0.2577
REMARK 3 24 1.3200 - 1.3000 1.00 3239 174 0.2679 0.2980
REMARK 3 25 1.3000 - 1.2900 1.00 3211 193 0.2879 0.3020
REMARK 3 26 1.2900 - 1.2700 1.00 3255 178 0.2981 0.3138
REMARK 3 27 1.2700 - 1.2500 1.00 3273 167 0.3140 0.3078
REMARK 3 28 1.2500 - 1.2400 1.00 3258 154 0.3208 0.3470
REMARK 3 29 1.2400 - 1.2200 1.00 3223 166 0.3358 0.3281
REMARK 3 30 1.2200 - 1.2100 1.00 3273 153 0.3552 0.3577
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) : 22.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.61
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 : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9856 -10.8857 2.4789
REMARK 3 T TENSOR
REMARK 3 T11: 0.1680 T22: 0.1239
REMARK 3 T33: 0.1636 T12: 0.0038
REMARK 3 T13: 0.0116 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.8940 L22: 1.5618
REMARK 3 L33: 2.5326 L12: -0.0387
REMARK 3 L13: -0.3839 L23: 0.3397
REMARK 3 S TENSOR
REMARK 3 S11: -0.0759 S12: -0.0057 S13: -0.0799
REMARK 3 S21: 0.1131 S22: 0.0387 S23: 0.0555
REMARK 3 S31: 0.3161 S32: 0.0309 S33: 0.0222
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 224 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5257 -9.2982 -4.2819
REMARK 3 T TENSOR
REMARK 3 T11: 0.1558 T22: 0.1147
REMARK 3 T33: 0.1527 T12: -0.0041
REMARK 3 T13: 0.0168 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 1.4699 L22: 1.6273
REMARK 3 L33: 2.7128 L12: -0.0969
REMARK 3 L13: 0.4005 L23: 0.0336
REMARK 3 S TENSOR
REMARK 3 S11: -0.0147 S12: 0.0538 S13: -0.2100
REMARK 3 S21: 0.0281 S22: 0.0781 S23: -0.0350
REMARK 3 S31: 0.3063 S32: 0.1346 S33: -0.1054
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 286 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4445 1.9897 -2.0141
REMARK 3 T TENSOR
REMARK 3 T11: 0.1095 T22: 0.1326
REMARK 3 T33: 0.1351 T12: -0.0092
REMARK 3 T13: -0.0108 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 1.3102 L22: 2.9802
REMARK 3 L33: 2.2640 L12: 0.3999
REMARK 3 L13: 0.5854 L23: 1.5845
REMARK 3 S TENSOR
REMARK 3 S11: 0.0310 S12: -0.0491 S13: 0.0224
REMARK 3 S21: 0.1616 S22: -0.0198 S23: -0.1488
REMARK 3 S31: 0.1315 S32: 0.0819 S33: -0.0545
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 287 THROUGH 320 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6784 2.4737 4.2213
REMARK 3 T TENSOR
REMARK 3 T11: 0.1547 T22: 0.2636
REMARK 3 T33: 0.2268 T12: 0.0082
REMARK 3 T13: -0.0447 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 3.3045 L22: 2.6696
REMARK 3 L33: 2.1622 L12: 1.2953
REMARK 3 L13: -1.7523 L23: -1.7727
REMARK 3 S TENSOR
REMARK 3 S11: 0.0509 S12: -0.3598 S13: -0.1206
REMARK 3 S21: 0.0512 S22: -0.1223 S23: -0.2481
REMARK 3 S31: 0.0268 S32: 0.3771 S33: 0.0928
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 418 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2822 13.6592 -4.0056
REMARK 3 T TENSOR
REMARK 3 T11: 0.1428 T22: 0.1630
REMARK 3 T33: 0.1726 T12: -0.0032
REMARK 3 T13: -0.0017 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.9652 L22: 1.1999
REMARK 3 L33: 1.4643 L12: 0.3269
REMARK 3 L13: 0.6718 L23: 0.6834
REMARK 3 S TENSOR
REMARK 3 S11: -0.0283 S12: -0.0970 S13: 0.1264
REMARK 3 S21: 0.0103 S22: -0.0109 S23: 0.0563
REMARK 3 S31: -0.0905 S32: -0.0687 S33: 0.0647
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 419 THROUGH 453 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7765 16.6454 -11.3059
REMARK 3 T TENSOR
REMARK 3 T11: 0.1478 T22: 0.1425
REMARK 3 T33: 0.2075 T12: -0.0065
REMARK 3 T13: -0.0309 T23: 0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 2.0060 L22: 2.8767
REMARK 3 L33: 4.6927 L12: 0.0632
REMARK 3 L13: 0.1899 L23: 0.8186
REMARK 3 S TENSOR
REMARK 3 S11: 0.0170 S12: 0.0267 S13: 0.0830
REMARK 3 S21: -0.1436 S22: 0.0154 S23: 0.1030
REMARK 3 S31: -0.0494 S32: 0.0654 S33: -0.0323
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 6YSK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-APR-20.
REMARK 100 THE DEPOSITION ID IS D_1292108193.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 500K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103841
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.210
REMARK 200 RESOLUTION RANGE LOW (A) : 59.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.700
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 (%): 36.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 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 29.97000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.20500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.20500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.97000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.95000
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: 2610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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 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 O HOH A 604 O HOH A 624 1.91
REMARK 500 NH2 ARG A 296 O HOH A 601 1.99
REMARK 500 OD2 ASP A 151 O HOH A 602 2.00
REMARK 500 O HOH A 637 O HOH A 684 2.19
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 O GLY A 431 O HOH A 602 2454 2.10
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 115 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 GLU A 196 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 CYS A 440 CA - CB - SG ANGL. DEV. = 6.9 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 -142.97 59.53
REMARK 500 TYR A 129 174.10 178.64
REMARK 500 ALA A 191 46.05 -141.77
REMARK 500 SER A 232 -123.65 64.85
REMARK 500 TYR A 254 63.81 -119.78
REMARK 500 GLN A 311 176.78 67.77
REMARK 500 GLU A 390 115.83 64.86
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6YSK A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 6YSK GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 6YSK GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 6YSK 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 DMS A 505 4
HET EDO A 506 4
HET EDO A 507 4
HET PJK A 508 19
HET EDO A 509 4
HET EDO A 510 4
HET EDO A 511 4
HET EDO A 512 4
HET EDO A 513 4
HET EDO A 514 4
HET SO4 A 515 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PJK (3~{S})-1-[4-CHLORANYL-3-(TRIFLUOROMETHYL)
HETNAM 2 PJK PHENYL]PYRROLIDINE-3-CARBOXYLIC ACID
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 6 DMS C2 H6 O S
FORMUL 7 EDO 8(C2 H6 O2)
FORMUL 9 PJK C12 H11 CL F3 N O2
FORMUL 17 HOH *123(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 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 2.07
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.05
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.06
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.16
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.03
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.04
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.03
LINK ND2 ASN A 96 C1 NAG A 501 1555 1555 1.42
CRYST1 59.940 71.900 78.410 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 0.016683 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013908 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012753 0.00000
TER 2911 THR A 453
MASTER 418 0 15 14 14 0 0 6 3088 1 105 30
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