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HEADER SIGNALING PROTEIN 24-OCT-20 7ARG
TITLE NOTUM IN COMPLEX WITH ARUK3002704
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_TAXID: 9606
KEYWDS NOTUM INHIBITOR, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHAO,E.Y.JONES
REVDAT 1 04-AUG-21 7ARG 0
JRNL AUTH Y.ZHAO,F.SVENSSON,D.STEADMAN,S.FREW,A.MONAGHAN,M.BICTASH,
JRNL AUTH 2 T.MOREIRA,R.CHALK,W.LU,P.V.FISH,E.Y.JONES
JRNL TITL STRUCTURAL INSIGHTS INTO NOTUM COVALENT INHIBITION.
JRNL REF J.MED.CHEM. 2021
JRNL REFN ISSN 0022-2623
JRNL PMID 34292747
JRNL DOI 10.1021/ACS.JMEDCHEM.1C00701
REMARK 2
REMARK 2 RESOLUTION. 1.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
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) : 1.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 95315
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4759
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 52.8200 - 3.8500 1.00 3308 134 0.1772 0.1907
REMARK 3 2 3.8500 - 3.0600 1.00 3113 161 0.1747 0.1883
REMARK 3 3 3.0600 - 2.6700 1.00 3089 157 0.1834 0.2032
REMARK 3 4 2.6700 - 2.4300 1.00 3092 153 0.1880 0.2111
REMARK 3 5 2.4300 - 2.2500 1.00 3070 132 0.1789 0.1935
REMARK 3 6 2.2500 - 2.1200 1.00 3055 141 0.1699 0.1836
REMARK 3 7 2.1200 - 2.0100 1.00 3057 168 0.1731 0.1778
REMARK 3 8 2.0100 - 1.9300 1.00 2990 169 0.1692 0.1926
REMARK 3 9 1.9300 - 1.8500 1.00 3044 155 0.1731 0.1930
REMARK 3 10 1.8500 - 1.7900 1.00 3010 159 0.1699 0.1926
REMARK 3 11 1.7900 - 1.7300 1.00 3039 156 0.1665 0.2001
REMARK 3 12 1.7300 - 1.6800 1.00 3019 167 0.1737 0.2018
REMARK 3 13 1.6800 - 1.6400 1.00 2973 183 0.1736 0.1810
REMARK 3 14 1.6400 - 1.6000 1.00 3027 153 0.1713 0.2324
REMARK 3 15 1.6000 - 1.5600 1.00 2998 142 0.1754 0.1762
REMARK 3 16 1.5600 - 1.5300 1.00 3020 135 0.1710 0.1840
REMARK 3 17 1.5300 - 1.5000 1.00 2995 170 0.1825 0.1938
REMARK 3 18 1.5000 - 1.4700 1.00 2968 177 0.1824 0.2223
REMARK 3 19 1.4700 - 1.4400 1.00 2992 161 0.1915 0.2267
REMARK 3 20 1.4400 - 1.4200 1.00 2979 166 0.1931 0.1981
REMARK 3 21 1.4200 - 1.4000 1.00 2965 170 0.2130 0.2551
REMARK 3 22 1.4000 - 1.3800 1.00 2998 155 0.2187 0.2532
REMARK 3 23 1.3800 - 1.3500 1.00 2959 169 0.2197 0.2420
REMARK 3 24 1.3500 - 1.3400 0.99 3012 145 0.2217 0.2350
REMARK 3 25 1.3400 - 1.3200 1.00 2953 182 0.2223 0.2488
REMARK 3 26 1.3200 - 1.3000 0.99 2963 154 0.2367 0.2645
REMARK 3 27 1.3000 - 1.2800 0.99 2979 170 0.2381 0.2535
REMARK 3 28 1.2800 - 1.2700 1.00 2971 157 0.2497 0.2541
REMARK 3 29 1.2700 - 1.2500 0.99 2931 176 0.2612 0.2743
REMARK 3 30 1.2500 - 1.2400 0.99 2987 142 0.2796 0.3074
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.01
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): -7.4437 -10.2862 -0.5936
REMARK 3 T TENSOR
REMARK 3 T11: 0.2009 T22: 0.1459
REMARK 3 T33: 0.1972 T12: 0.0010
REMARK 3 T13: 0.0114 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 0.9837 L22: 1.1993
REMARK 3 L33: 2.0303 L12: 0.1313
REMARK 3 L13: -0.0533 L23: -0.1156
REMARK 3 S TENSOR
REMARK 3 S11: -0.0244 S12: 0.0157 S13: -0.1195
REMARK 3 S21: 0.0437 S22: 0.0233 S23: 0.0129
REMARK 3 S31: 0.2470 S32: 0.0239 S33: -0.0209
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 286 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2681 1.9562 -1.9730
REMARK 3 T TENSOR
REMARK 3 T11: 0.1432 T22: 0.1430
REMARK 3 T33: 0.1358 T12: -0.0004
REMARK 3 T13: -0.0113 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.4478 L22: 3.3241
REMARK 3 L33: 1.5894 L12: 0.1375
REMARK 3 L13: 0.2598 L23: 1.5859
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: -0.0500 S13: -0.0156
REMARK 3 S21: 0.2713 S22: 0.0043 S23: -0.1155
REMARK 3 S31: 0.2229 S32: 0.0697 S33: -0.0598
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 287 THROUGH 320 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5914 1.9462 4.5829
REMARK 3 T TENSOR
REMARK 3 T11: 0.1464 T22: 0.2700
REMARK 3 T33: 0.1901 T12: -0.0116
REMARK 3 T13: -0.0413 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 4.1459 L22: 5.2242
REMARK 3 L33: 2.6573 L12: 2.5589
REMARK 3 L13: -0.4464 L23: -2.7582
REMARK 3 S TENSOR
REMARK 3 S11: 0.1769 S12: -0.6292 S13: -0.2027
REMARK 3 S21: 0.1552 S22: -0.3754 S23: -0.3560
REMARK 3 S31: 0.0033 S32: 0.2078 S33: 0.1676
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 451 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8587 14.1835 -6.2460
REMARK 3 T TENSOR
REMARK 3 T11: 0.1517 T22: 0.1571
REMARK 3 T33: 0.1722 T12: -0.0054
REMARK 3 T13: -0.0023 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.9022 L22: 1.1097
REMARK 3 L33: 0.9339 L12: -0.1497
REMARK 3 L13: 0.3256 L23: 0.4714
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: -0.0317 S13: 0.0955
REMARK 3 S21: -0.0567 S22: 0.0055 S23: 0.0867
REMARK 3 S31: -0.0791 S32: -0.0513 S33: 0.0375
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 7ARG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1292111972.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-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) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95627
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.240
REMARK 200 RESOLUTION RANGE LOW (A) : 59.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 39.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.26
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.50000
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: PHENIX
REMARK 200 STARTING MODEL: 6TV4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM
REMARK 280 CITRIC, PH4.6, EVAPORATION, TEMPERATURE 296K
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 29.86500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.01000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.89000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.01000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.86500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.89000
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: 2380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 352
REMARK 465 GLY A 353
REMARK 465 GLN A 354
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 1.85
REMARK 500 OE1 GLU A 113 NH1 ARG A 115 2.19
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 CYS A 432 CB - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 CYS A 432 CA - CB - SG ANGL. DEV. = 7.1 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 -136.27 58.63
REMARK 500 MET A 143 44.21 -141.23
REMARK 500 ALA A 191 52.26 -144.28
REMARK 500 SER A 232 -122.53 58.53
REMARK 500 ASP A 278 44.19 -98.33
REMARK 500 CYS A 279 -120.92 40.28
REMARK 500 VAL A 280 -71.09 68.78
REMARK 500 GLN A 311 -179.51 69.32
REMARK 500 SER A 388 -164.61 -166.59
REMARK 500 HIS A 389 119.45 -167.75
REMARK 500 GLU A 390 164.76 65.78
REMARK 500 ILE A 391 -43.18 -153.74
REMARK 500 ASP A 420 88.51 -50.32
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7ARG A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 7ARG GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 7ARG GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG LYS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 7ARG 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 SO4 A 505 5
HET DMS A 506 4
HET EDO A 507 4
HET EDO A 508 4
HET SO4 A 509 5
HET SO4 A 510 5
HET EDO A 511 4
HET EDO A 512 4
HET EDO A 513 10
HET RW8 A 514 15
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM RW8 METHYL 4-(2,3-DIHYDROINDOL-1-YL)-4-OXIDANYLIDENE-
HETNAM 2 RW8 BUTANOATE
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 6(O4 S 2-)
FORMUL 7 DMS C2 H6 O S
FORMUL 8 EDO 5(C2 H6 O2)
FORMUL 15 RW8 C13 H15 N O3
FORMUL 16 HOH *130(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 LEU A 252 1 21
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 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 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 2.08
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.02
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.02
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.12
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.03
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.05
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.02
LINK ND2 ASN A 96 C1 NAG A 501 1555 1555 1.43
LINK OG SER A 232 C03 RW8 A 514 1555 1555 1.37
CRYST1 59.730 71.780 78.020 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 0.016742 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013931 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012817 0.00000
TER 2870 THR A 451
MASTER 376 0 14 14 14 0 0 6 3064 1 105 30
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