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HEADER ONCOPROTEIN 17-DEC-19 6TR7
TITLE N-[2-(5-FLUORO-1H-INDOL-3-YL)ETHYL]ACETAMIDE-NOTUM COMPLEX
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
KEYWDS WNT RECEPTOR FRIZZLED8 CARBAMAZEPINE, ONCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHAO,E.Y.JONES
REVDAT 1 08-JAN-20 6TR7 0
JRNL AUTH Y.ZHAO,J.REN,J.HILLIER,M.JONES,W.LU,E.Y.JONES
JRNL TITL STRUCTURAL CHARACTERISATION OF MELATONIN AS AN INHIBITOR OF
JRNL TITL 2 THE WNT DEACYLASE NOTUM.
JRNL REF J. PINEAL RES. 12630 2019
JRNL REFN ISSN 1600-079X
JRNL PMID 31876313
JRNL DOI 10.1111/JPI.12630
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 59603
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3011
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 4.1185 - 3.2691 1.00 2690 136 0.1695 0.1774
REMARK 3 2 3.2691 - 2.8559 1.00 2627 150 0.1793 0.1870
REMARK 3 3 2.8559 - 2.5948 1.00 2638 137 0.1786 0.1928
REMARK 3 4 2.5948 - 2.4088 1.00 2591 145 0.1815 0.2273
REMARK 3 5 2.4088 - 2.2668 1.00 2619 129 0.1761 0.2375
REMARK 3 6 2.2668 - 2.1533 1.00 2571 140 0.1682 0.2163
REMARK 3 7 2.1533 - 2.0595 0.99 2566 163 0.1755 0.1981
REMARK 3 8 2.0595 - 1.9802 0.99 2573 138 0.1748 0.2195
REMARK 3 9 1.9802 - 1.9119 0.99 2583 144 0.1864 0.2227
REMARK 3 10 1.9119 - 1.8521 0.99 2546 152 0.1989 0.2823
REMARK 3 11 1.8521 - 1.7992 0.99 2547 153 0.2127 0.2276
REMARK 3 12 1.7992 - 1.7518 0.99 2583 123 0.2200 0.2324
REMARK 3 13 1.7518 - 1.7091 0.99 2551 126 0.2368 0.2394
REMARK 3 14 1.7091 - 1.6702 0.99 2549 125 0.2447 0.3021
REMARK 3 15 1.6702 - 1.6347 0.98 2554 121 0.2691 0.3395
REMARK 3 16 1.6347 - 1.6020 0.98 2543 122 0.2600 0.2653
REMARK 3 17 1.6020 - 1.5717 0.98 2549 133 0.2842 0.2960
REMARK 3 18 1.5717 - 1.5437 0.98 2532 116 0.2947 0.3011
REMARK 3 19 1.5437 - 1.5175 0.98 2514 134 0.3169 0.3445
REMARK 3 20 4.0000 - 1.5000 1.00 2761 186 0.1880 0.2030
REMARK 3 21 1.5175 - 1.4930 0.97 2476 126 0.3527 0.3434
REMARK 3 22 1.4930 - 1.4700 0.94 2429 112 0.3814 0.4441
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.700
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.87
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): 7.5759 10.4987 -0.5057
REMARK 3 T TENSOR
REMARK 3 T11: 0.1567 T22: 0.1175
REMARK 3 T33: 0.1611 T12: -0.0088
REMARK 3 T13: -0.0167 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.0084 L22: 1.1463
REMARK 3 L33: 1.3954 L12: 0.1299
REMARK 3 L13: -0.0831 L23: 0.3258
REMARK 3 S TENSOR
REMARK 3 S11: -0.0148 S12: 0.0038 S13: 0.1692
REMARK 3 S21: 0.0048 S22: -0.0019 S23: 0.0022
REMARK 3 S31: -0.1985 S32: 0.0230 S33: 0.0061
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 286 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3645 -1.7328 -3.1593
REMARK 3 T TENSOR
REMARK 3 T11: 0.1253 T22: 0.1391
REMARK 3 T33: 0.1435 T12: 0.0050
REMARK 3 T13: 0.0068 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 1.0484 L22: 1.6879
REMARK 3 L33: 0.8056 L12: 0.0861
REMARK 3 L13: -0.0801 L23: -0.3684
REMARK 3 S TENSOR
REMARK 3 S11: -0.0175 S12: -0.0389 S13: 0.0090
REMARK 3 S21: 0.1256 S22: 0.0366 S23: 0.1417
REMARK 3 S31: -0.1242 S32: -0.0537 S33: -0.0248
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 287 THROUGH 320 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5318 -2.0603 4.9737
REMARK 3 T TENSOR
REMARK 3 T11: 0.1471 T22: 0.1846
REMARK 3 T33: 0.2077 T12: 0.0081
REMARK 3 T13: 0.0335 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 2.0080 L22: 2.0528
REMARK 3 L33: 1.4809 L12: 1.0797
REMARK 3 L13: 0.7198 L23: 1.2756
REMARK 3 S TENSOR
REMARK 3 S11: 0.0483 S12: -0.1298 S13: 0.1443
REMARK 3 S21: 0.0762 S22: -0.1113 S23: 0.2899
REMARK 3 S31: -0.0572 S32: -0.2263 S33: 0.0785
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 452 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7210 -12.6454 -5.4972
REMARK 3 T TENSOR
REMARK 3 T11: 0.1183 T22: 0.1499
REMARK 3 T33: 0.1411 T12: -0.0074
REMARK 3 T13: 0.0004 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.5064 L22: 0.7959
REMARK 3 L33: 0.3792 L12: -0.1914
REMARK 3 L13: -0.1254 L23: 0.0485
REMARK 3 S TENSOR
REMARK 3 S11: -0.0276 S12: -0.0080 S13: -0.0847
REMARK 3 S21: -0.0146 S22: 0.0264 S23: -0.0218
REMARK 3 S31: 0.0670 S32: 0.0376 S33: 0.0109
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 6TR7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1292105935.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JAN-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) : 0.92819
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 : 60282
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.470
REMARK 200 RESOLUTION RANGE LOW (A) : 79.020
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 : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
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: XIA2
REMARK 200 STARTING MODEL: 4UZQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM
REMARK 280 CITRATE PH 4.2, 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 30.15350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.51000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.68250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.51000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.15350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.68250
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: 3680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 ASP A 278
REMARK 465 CYS A 279
REMARK 465 VAL A 280
REMARK 465 CYS A 285
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 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 OD1 ASN A 366 NH2 ARG A 369 2.12
REMARK 500 N HIS A 435 O4 SO4 A 504 2.14
REMARK 500 O LEU A 252 O1 EDO A 508 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 O2 SO4 A 504 O1 EDO A 508 3544 2.03
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 -141.66 60.06
REMARK 500 SER A 232 -123.15 63.22
REMARK 500 SER A 232 -123.43 63.65
REMARK 500 GLN A 311 179.91 68.94
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 SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HWH A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HWH A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 519 bound
REMARK 800 to ASN A 96
DBREF 6TR7 A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 6TR7 GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 6TR7 GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR7 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 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 EDO A 507 4
HET EDO A 508 4
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 EDO A 515 4
HET EDO A 516 4
HET EDO A 517 4
HET EDO A 518 4
HET NAG A 519 14
HET HWH A 520 16
HET HWH A 521 16
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM HWH ~{N}-[2-(5-FLUORANYL-1~{H}-INDOL-3-YL)ETHYL]ETHANAMIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 SO4 6(O4 S 2-)
FORMUL 8 EDO 12(C2 H6 O2)
FORMUL 20 NAG C8 H15 N O6
FORMUL 21 HWH 2(C12 H13 F N2 O)
FORMUL 23 HOH *150(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 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 2.05
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.05
SSBOND 3 CYS A 306 CYS A 318 1555 1555 2.12
SSBOND 4 CYS A 386 CYS A 449 1555 1555 2.03
SSBOND 5 CYS A 413 CYS A 432 1555 1555 2.04
SSBOND 6 CYS A 440 CYS A 445 1555 1555 2.04
LINK ND2 ASN A 96 C1 NAG A 519 1555 1555 1.44
SITE 1 AC1 8 PRO A 255 ALA A 256 ARG A 372 LYS A 403
SITE 2 AC1 8 VAL A 437 HOH A 632 HOH A 673 HOH A 699
SITE 1 AC2 8 ARG A 133 LYS A 197 ASN A 198 GLU A 199
SITE 2 AC2 8 ARG A 275 TYR A 297 HOH A 676 HOH A 693
SITE 1 AC3 5 ARG A 119 TYR A 171 TRP A 172 TRP A 173
SITE 2 AC3 5 ASN A 174
SITE 1 AC4 6 LEU A 252 PRO A 433 VAL A 434 HIS A 435
SITE 2 AC4 6 EDO A 508 HOH A 606
SITE 1 AC5 3 ARG A 305 GLU A 358 ARG A 361
SITE 1 AC6 8 THR A 142 MET A 143 ARG A 144 ARG A 145
SITE 2 AC6 8 ARG A 409 HIS A 412 ARG A 416 HOH A 639
SITE 1 AC7 5 GLY A 127 TRP A 128 SER A 232 ALA A 233
SITE 2 AC7 5 HWH A 520
SITE 1 AC8 5 LEU A 252 GLY A 253 TYR A 254 PRO A 428
SITE 2 AC8 5 SO4 A 504
SITE 1 AC9 3 ARG A 90 GLU A 113 HOH A 642
SITE 1 AD1 6 TYR A 325 LEU A 328 SER A 330 PRO A 331
SITE 2 AD1 6 VAL A 332 HOH A 601
SITE 1 AD2 5 ARG A 394 TRP A 397 VAL A 400 LEU A 407
SITE 2 AD2 5 HOH A 621
SITE 1 AD3 4 GLU A 390 ARG A 394 PRO A 450 THR A 451
SITE 1 AD4 3 ARG A 145 ARG A 416 HIS A 419
SITE 1 AD5 4 ARG A 372 HIS A 373 LYS A 376 HOH A 662
SITE 1 AD6 4 TYR A 110 TRP A 152 ARG A 156 HOH A 710
SITE 1 AD7 4 ARG A 156 THR A 157 THR A 159 PHE A 179
SITE 1 AD8 6 GLN A 401 LYS A 403 GLY A 404 ASN A 446
SITE 2 AD8 6 PRO A 447 HWH A 521
SITE 1 AD9 3 ARG A 154 LYS A 430 NAG A 519
SITE 1 AE1 9 TRP A 128 TYR A 129 THR A 236 PHE A 268
SITE 2 AE1 9 PRO A 287 PHE A 319 VAL A 346 EDO A 507
SITE 3 AE1 9 HOH A 612
SITE 1 AE2 7 LEU A 269 ASP A 270 ASN A 271 PRO A 287
SITE 2 AE2 7 THR A 288 SER A 448 EDO A 517
SITE 1 AE3 8 ASN A 96 SER A 98 VAL A 99 PRO A 153
SITE 2 AE3 8 ARG A 154 THR A 155 EDO A 518 HOH A 603
CRYST1 60.307 73.365 79.020 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 0.016582 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013630 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012655 0.00000
TER 2888 THR A 451
MASTER 451 0 21 14 14 0 35 6 3084 1 137 30
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