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HEADER HYDROLASE 17-DEC-19 6TR5
TITLE MELATONIN-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 NOTUM INHIBITOR MELATONIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHAO,E.Y.JONES
REVDAT 1 15-JAN-20 6TR5 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 PMID 31876313
JRNL DOI 10.1111/JPI.12630
REMARK 2
REMARK 2 RESOLUTION. 1.51 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 54785
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 2808
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 53.6800 - 4.0962 1.00 2880 109 0.1848 0.1987
REMARK 3 2 4.0962 - 3.2514 1.00 2702 159 0.1715 0.1893
REMARK 3 3 3.2514 - 2.8404 1.00 2662 156 0.1841 0.2221
REMARK 3 4 2.8404 - 2.5807 1.00 2650 163 0.1905 0.2378
REMARK 3 5 2.5807 - 2.3957 1.00 2638 144 0.1885 0.1885
REMARK 3 6 2.3957 - 2.2545 1.00 2608 154 0.1820 0.2380
REMARK 3 7 2.2545 - 2.1416 1.00 2633 148 0.1776 0.2047
REMARK 3 8 2.1416 - 2.0484 1.00 2602 156 0.1842 0.2227
REMARK 3 9 2.0484 - 1.9695 1.00 2623 132 0.1814 0.2221
REMARK 3 10 1.9695 - 1.9015 1.00 2614 135 0.1851 0.2278
REMARK 3 11 1.9015 - 1.8421 0.99 2620 125 0.1983 0.2252
REMARK 3 12 1.8421 - 1.7894 0.99 2588 140 0.2133 0.2341
REMARK 3 13 1.7894 - 1.7423 0.99 2605 119 0.2186 0.2712
REMARK 3 14 1.7423 - 1.6998 0.99 2594 141 0.2464 0.3028
REMARK 3 15 1.6998 - 1.6612 0.99 2538 152 0.2620 0.2706
REMARK 3 16 1.6612 - 1.6258 0.98 2567 135 0.2930 0.3403
REMARK 3 17 1.6258 - 1.5933 0.97 2570 124 0.3109 0.3259
REMARK 3 18 1.5933 - 1.5632 0.95 2481 138 0.3323 0.3876
REMARK 3 19 1.5632 - 1.5353 0.95 2470 132 0.3517 0.3822
REMARK 3 20 1.5353 - 1.5093 0.91 2332 146 0.3765 0.4083
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.50
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 : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 451 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3626 -14.6874 -5.7761
REMARK 3 T TENSOR
REMARK 3 T11: 0.1176 T22: 0.1554
REMARK 3 T33: 0.1490 T12: -0.0191
REMARK 3 T13: 0.0043 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.6497 L22: 1.0360
REMARK 3 L33: 0.7068 L12: -0.1078
REMARK 3 L13: -0.3124 L23: -0.3485
REMARK 3 S TENSOR
REMARK 3 S11: -0.0459 S12: 0.0328 S13: -0.0992
REMARK 3 S21: -0.0628 S22: -0.0006 S23: -0.0785
REMARK 3 S31: 0.0589 S32: 0.0469 S33: -0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 452 THROUGH 452 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2095 -10.8571 2.2161
REMARK 3 T TENSOR
REMARK 3 T11: 0.8397 T22: 0.8580
REMARK 3 T33: 0.7030 T12: -0.1707
REMARK 3 T13: 0.0928 T23: -0.2801
REMARK 3 L TENSOR
REMARK 3 L11: 2.0000 L22: 2.0000
REMARK 3 L33: 2.0000 L12: 2.0000
REMARK 3 L13: 2.0000 L23: 2.0000
REMARK 3 S TENSOR
REMARK 3 S11: 2.3786 S12: 0.2401 S13: 0.6823
REMARK 3 S21: 4.5398 S22: -3.1109 S23: 5.4692
REMARK 3 S31: -0.1511 S32: -4.2971 S33: 0.7260
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8131 10.8891 1.2456
REMARK 3 T TENSOR
REMARK 3 T11: 0.1989 T22: 0.1450
REMARK 3 T33: 0.1904 T12: -0.0075
REMARK 3 T13: -0.0092 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.0559 L22: 1.3798
REMARK 3 L33: 0.3752 L12: 0.1301
REMARK 3 L13: 0.2496 L23: 0.5464
REMARK 3 S TENSOR
REMARK 3 S11: 0.0324 S12: 0.0263 S13: 0.2043
REMARK 3 S21: 0.0271 S22: -0.0415 S23: 0.0102
REMARK 3 S31: -0.2930 S32: -0.0096 S33: 0.0005
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 143 THROUGH 252 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6293 8.8049 -3.7583
REMARK 3 T TENSOR
REMARK 3 T11: 0.1784 T22: 0.1319
REMARK 3 T33: 0.1760 T12: -0.0031
REMARK 3 T13: -0.0120 T23: 0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 1.0188 L22: 0.9185
REMARK 3 L33: 0.9616 L12: 0.1661
REMARK 3 L13: -0.0125 L23: 0.1700
REMARK 3 S TENSOR
REMARK 3 S11: -0.0260 S12: 0.0521 S13: 0.2189
REMARK 3 S21: 0.0265 S22: 0.0366 S23: 0.0172
REMARK 3 S31: -0.1794 S32: -0.0198 S33: -0.0002
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 253 THROUGH 320 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6767 -4.0904 2.0125
REMARK 3 T TENSOR
REMARK 3 T11: 0.1538 T22: 0.1904
REMARK 3 T33: 0.1813 T12: 0.0071
REMARK 3 T13: -0.0014 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 1.1560 L22: 0.8029
REMARK 3 L33: 0.2687 L12: 0.2530
REMARK 3 L13: -0.0980 L23: 0.3049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: -0.0456 S13: 0.0999
REMARK 3 S21: 0.0603 S22: -0.0609 S23: 0.1635
REMARK 3 S31: -0.0542 S32: -0.0273 S33: -0.0054
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 6TR5 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_1292105933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-OCT-16
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 : 55371
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.509
REMARK 200 RESOLUTION RANGE LOW (A) : 73.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
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 (%): 38.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
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 30.12950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.50050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.58250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.50050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.12950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.58250
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: 2950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 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 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 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 427
REMARK 465 GLY A 452
REMARK 465 THR A 453
REMARK 465 LYS A 454
REMARK 465 HIS A 455
REMARK 465 HIS A 456
REMARK 465 HIS A 457
REMARK 465 HIS A 458
REMARK 465 HIS A 459
REMARK 465 HIS A 460
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 296 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 312 CG CD OE1 OE2
REMARK 470 ARG A 329 CG CD NE CZ NH1 NH2
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 608 O HOH A 679 2.01
REMARK 500 O HOH A 693 O HOH A 702 2.16
REMARK 500 O HOH A 611 O HOH A 696 2.18
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 -143.71 58.58
REMARK 500 SER A 232 -117.60 58.92
REMARK 500 GLN A 311 -176.81 70.89
REMARK 500 PHE A 339 65.96 -119.61
REMARK 500 GLU A 390 155.09 71.04
REMARK 500 ILE A 391 -36.22 -153.94
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 ML1 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ML1 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 503
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 SO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 504 bound
REMARK 800 to ASN A 96
DBREF 6TR5 A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 6TR5 GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 6TR5 GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 6TR5 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 ML1 A 501 17
HET ML1 A 502 17
HET DMS A 503 4
HET NAG A 504 14
HET SO4 A 505 5
HET SO4 A 506 5
HET SO4 A 507 5
HET SO4 A 508 5
HET SO4 A 509 5
HET SO4 A 510 5
HET SO4 A 511 5
HET SO4 A 512 5
HETNAM ML1 N-[2-(5-METHOXY-1H-INDOL-3-YL)ETHYL]ACETAMIDE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SO4 SULFATE ION
HETSYN ML1 MELATONIN
FORMUL 2 ML1 2(C13 H16 N2 O2)
FORMUL 4 DMS C2 H6 O S
FORMUL 5 NAG C8 H15 N O6
FORMUL 6 SO4 8(O4 S 2-)
FORMUL 14 HOH *116(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 2.03
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.04
SSBOND 3 CYS A 306 CYS A 318 1555 1555 2.07
SSBOND 4 CYS A 386 CYS A 449 1555 1555 2.02
SSBOND 5 CYS A 413 CYS A 432 1555 1555 2.03
SSBOND 6 CYS A 440 CYS A 445 1555 1555 2.04
LINK ND2 ASN A 96 C1 NAG A 504 1555 1555 1.43
SITE 1 AC1 9 LEU A 269 ASP A 270 ASN A 271 LYS A 272
SITE 2 AC1 9 PRO A 287 THR A 288 GLN A 401 PRO A 447
SITE 3 AC1 9 SER A 448
SITE 1 AC2 7 SER A 232 ALA A 233 THR A 236 PHE A 268
SITE 2 AC2 7 PRO A 287 PHE A 319 VAL A 346
SITE 1 AC3 5 TYR A 110 TRP A 152 PRO A 153 ARG A 156
SITE 2 AC3 5 PRO A 181
SITE 1 AC4 4 PRO A 255 ARG A 372 LYS A 403 VAL A 437
SITE 1 AC5 4 ARG A 305 ARG A 308 GLU A 358 ARG A 361
SITE 1 AC6 3 ARG A 244 GLU A 247 GLU A 304
SITE 1 AC7 3 ARG A 394 SER A 395 HIS A 396
SITE 1 AC8 3 ARG A 145 ARG A 416 HIS A 419
SITE 1 AC9 7 THR A 142 MET A 143 ARG A 144 ARG A 145
SITE 2 AC9 7 ARG A 409 HIS A 412 ARG A 416
SITE 1 AD1 7 ARG A 133 LYS A 197 ASN A 198 GLU A 199
SITE 2 AD1 7 ARG A 275 TYR A 297 HOH A 662
SITE 1 AD2 5 ARG A 90 LYS A 112 GLU A 113 ARG A 115
SITE 2 AD2 5 HOH A 610
SITE 1 AD3 5 ASN A 96 VAL A 99 PRO A 153 ARG A 154
SITE 2 AD3 5 THR A 155
CRYST1 60.259 73.165 79.001 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016595 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013668 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012658 0.00000
TER 2771 THR A 451
MASTER 425 0 12 14 14 0 20 6 2965 1 105 30
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