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HEADER HYDROLASE 01-MAY-20 6YXI
TITLE STRUCTURE OF NOTUM IN COMPLEX WITH A 1-(3-CHLOROPHENYL)-2,5-DIMETHYL-
TITLE 2 1H-PYRROLE-3-CARBOXYLIC ACID INHIBITOR
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;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NOTUM, OK/SW-CL.30;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS INHIBITOR, COMPLEX, WNT PATHWAY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.VECCHIA,E.Y.JONES,R.R.RUZA,J.HILLIER,Y.ZHAO
REVDAT 1 19-AUG-20 6YXI 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 DOI 10.1021/ACS.JMEDCHEM.0C00660
REMARK 2
REMARK 2 RESOLUTION. 1.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_3699
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 75866
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3828
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 52.9500 - 4.0200 1.00 2879 157 0.1788 0.1677
REMARK 3 2 4.0200 - 3.1900 1.00 2766 144 0.1589 0.1955
REMARK 3 3 3.1900 - 2.7900 1.00 2721 139 0.1715 0.2053
REMARK 3 4 2.7900 - 2.5300 1.00 2687 152 0.1688 0.1876
REMARK 3 5 2.5300 - 2.3500 1.00 2700 153 0.1520 0.1703
REMARK 3 6 2.3500 - 2.2100 1.00 2686 134 0.1472 0.1860
REMARK 3 7 2.2100 - 2.1000 1.00 2670 153 0.1352 0.1579
REMARK 3 8 2.1000 - 2.0100 1.00 2642 175 0.1411 0.1636
REMARK 3 9 2.0100 - 1.9300 1.00 2676 127 0.1364 0.1575
REMARK 3 10 1.9300 - 1.8700 1.00 2679 134 0.1353 0.1615
REMARK 3 11 1.8700 - 1.8100 1.00 2638 142 0.1300 0.1924
REMARK 3 12 1.8100 - 1.7600 1.00 2671 146 0.1290 0.1742
REMARK 3 13 1.7600 - 1.7100 1.00 2676 136 0.1236 0.1746
REMARK 3 14 1.7100 - 1.6700 1.00 2654 129 0.1327 0.1758
REMARK 3 15 1.6700 - 1.6300 1.00 2662 139 0.1272 0.1783
REMARK 3 16 1.6300 - 1.6000 1.00 2623 137 0.1282 0.2089
REMARK 3 17 1.6000 - 1.5600 1.00 2642 124 0.1377 0.1943
REMARK 3 18 1.5600 - 1.5300 1.00 2641 144 0.1384 0.2012
REMARK 3 19 1.5300 - 1.5100 1.00 2657 134 0.1465 0.1918
REMARK 3 20 1.5100 - 1.4800 1.00 2653 140 0.1542 0.2124
REMARK 3 21 1.4800 - 1.4600 1.00 2654 138 0.1704 0.2235
REMARK 3 22 1.4600 - 1.4300 1.00 2644 144 0.1803 0.2446
REMARK 3 23 1.4300 - 1.4100 1.00 2604 149 0.2054 0.2491
REMARK 3 24 1.4100 - 1.3900 1.00 2643 149 0.2172 0.3172
REMARK 3 25 1.3900 - 1.3700 1.00 2642 138 0.2315 0.3138
REMARK 3 26 1.3700 - 1.3600 0.99 2625 132 0.2581 0.3062
REMARK 3 27 1.3600 - 1.3400 0.99 2603 139 0.2766 0.3307
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) : 0.152
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.384
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.85
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.51
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 : 0.006 3075
REMARK 3 ANGLE : 0.786 4187
REMARK 3 CHIRALITY : 0.080 436
REMARK 3 PLANARITY : 0.006 551
REMARK 3 DIHEDRAL : 18.810 1132
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6YXI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-MAY-20.
REMARK 100 THE DEPOSITION ID IS D_1292108442.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979499
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75943
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.340
REMARK 200 RESOLUTION RANGE LOW (A) : 59.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.36
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: PHASER
REMARK 200 STARTING MODEL: 4UZ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M AMMONIUM SULPHATE, 0.1 M CITRIC
REMARK 280 ACID, PH 4, 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 29.76000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.96500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.08000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.96500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.76000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.08000
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 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 ALA A 286
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 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: 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 -135.80 56.40
REMARK 500 TYR A 129 169.54 179.56
REMARK 500 ALA A 191 57.61 -143.45
REMARK 500 SER A 232 -121.71 62.74
REMARK 500 SER A 232 -123.57 64.24
REMARK 500 GLN A 311 -177.41 68.29
REMARK 500 SER A 388 -168.20 -167.71
REMARK 500 GLU A 390 160.75 68.24
REMARK 500 ILE A 391 -43.14 -154.55
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6YXI A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 6YXI GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 6YXI GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 6YXI 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 PZ8 A1501 17
HET NAG A1502 14
HET DMS A1503 4
HET SO4 A1504 5
HET SO4 A1505 5
HET SO4 A1506 5
HET SO4 A1507 5
HET SO4 A1508 5
HET SO4 A1509 5
HET SO4 A1510 5
HET EDO A1511 4
HET EDO A1512 4
HETNAM PZ8 1-(3-CHLOROPHENYL)-2,5-DIMETHYL-PYRROLE-3-CARBOXYLIC
HETNAM 2 PZ8 ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
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 PZ8 C13 H12 CL N O2
FORMUL 3 NAG C8 H15 N O6
FORMUL 4 DMS C2 H6 O S
FORMUL 5 SO4 7(O4 S 2-)
FORMUL 12 EDO 2(C2 H6 O2)
FORMUL 14 HOH *198(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 THR A 288 ASN A 299 1 12
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 SER A 381
SHEET 1 AA2 2 PHE A 339 ASP A 340 0
SHEET 2 AA2 2 LEU A 387 SER A 388 1 O SER A 388 N PHE A 339
SHEET 1 AA3 2 GLN A 401 VAL A 402 0
SHEET 2 AA3 2 THR A 405 SER A 406 -1 O THR A 405 N VAL A 402
SSBOND 1 CYS A 101 CYS A 183 1555 1555 2.04
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.03
SSBOND 3 CYS A 306 CYS A 318 1555 1555 2.06
SSBOND 4 CYS A 386 CYS A 449 1555 1555 2.03
SSBOND 5 CYS A 413 CYS A 432 1555 1555 2.03
SSBOND 6 CYS A 440 CYS A 445 1555 1555 2.02
LINK ND2 ASN A 96 C1 NAG A1502 1555 1555 1.43
CRYST1 59.520 72.160 77.930 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 0.016801 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013858 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012832 0.00000
TER 2921 GLY A 452
MASTER 278 0 12 14 14 0 0 6 3092 1 91 30
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