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HEADER HYDROLASE 04-JUN-25 9RF2
TITLE M. TUBERCULOSIS MEETS EUROPEAN LEAD FACTORY: IDENTIFICATION AND
TITLE 2 STRUCTURAL CHARACTERIZATION OF NOVEL RV0183 INHIBITORS USING X-RAY
TITLE 3 CRYSTALLOGRAPHY: ELF5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MGL;
COMPND 5 EC: 3.1.1.23;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 GENE: RV0183;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS RV0183, INHIBITOR, MONOACYLGLYCEROL LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.RIEGLER-BERKET,L.GOEDL,M.OBERER,N.POLIDORI
REVDAT 1 13-AUG-25 9RF2 0
JRNL AUTH L.RIEGLER-BERKET,L.GOEDL,M.OBERER,N.POLIDORI
JRNL TITL M. TUBERCULOSIS MEETS EUROPEAN LEAD FACTORY: IDENTIFICATION
JRNL TITL 2 AND STRUCTURAL CHARACTERIZATION OF NOVEL RV0183 INHIBITORS
JRNL TITL 3 USING X-RAY CRYSTALLOGRAPHY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???)
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 40788
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 1989
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 41.3900 - 3.8600 0.99 2978 154 0.1914 0.1706
REMARK 3 2 3.8600 - 3.0600 1.00 2825 153 0.1720 0.1888
REMARK 3 3 3.0600 - 2.6700 1.00 2802 136 0.1902 0.2167
REMARK 3 4 2.6700 - 2.4300 1.00 2772 171 0.1767 0.2056
REMARK 3 5 2.4300 - 2.2600 1.00 2776 140 0.1783 0.2185
REMARK 3 6 2.2600 - 2.1200 1.00 2769 123 0.1772 0.2135
REMARK 3 7 2.1200 - 2.0200 1.00 2761 138 0.1781 0.2270
REMARK 3 8 2.0200 - 1.9300 1.00 2743 150 0.1850 0.1959
REMARK 3 9 1.9300 - 1.8500 1.00 2781 141 0.2036 0.2394
REMARK 3 10 1.8500 - 1.7900 1.00 2772 141 0.2157 0.2642
REMARK 3 11 1.7900 - 1.7300 1.00 2720 142 0.2377 0.2422
REMARK 3 12 1.7300 - 1.6800 1.00 2716 141 0.2443 0.2854
REMARK 3 13 1.6800 - 1.6400 0.99 2758 129 0.2712 0.3003
REMARK 3 14 1.6400 - 1.6000 0.96 2627 130 0.3200 0.3457
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.191
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.794
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.94
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.84
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 : 0.005 2335
REMARK 3 ANGLE : 0.858 3204
REMARK 3 CHIRALITY : 0.057 359
REMARK 3 PLANARITY : 0.009 425
REMARK 3 DIHEDRAL : 12.909 907
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 9RF2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JUN-25.
REMARK 100 THE DEPOSITION ID IS D_1292148152.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033230
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40806
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 41.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1000, PEG 3350, MPD, HEPES, MOPS,
REMARK 280 CHAPS, CHAPSO, SODIUM GLYCOCHOLATE HYDRATE, TAUROCHOLIC ACID
REMARK 280 SODIUM SALT HYDRATE, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.39200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.35200
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.39200
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.35200
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: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 MET A -27
REMARK 465 SER A -26
REMARK 465 TYR A -25
REMARK 465 TYR A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 ASP A -17
REMARK 465 TYR A -16
REMARK 465 ASP A -15
REMARK 465 ILE A -14
REMARK 465 PRO A -13
REMARK 465 THR A -12
REMARK 465 THR A -11
REMARK 465 GLU A -10
REMARK 465 ASN A -9
REMARK 465 LEU A -8
REMARK 465 TYR A -7
REMARK 465 PHE A -6
REMARK 465 GLN A -5
REMARK 465 GLY A -4
REMARK 465 ALA A -3
REMARK 465 MET A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
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 PRO A 124 O HOH A 401 2.17
REMARK 500 NH1 ARG A 52 OD1 ASP A 269 2.19
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 ASP A 26 40.27 -89.15
REMARK 500 ASP A 26 41.88 -89.15
REMARK 500 GLU A 41 -150.69 -103.51
REMARK 500 SER A 110 -122.10 62.50
REMARK 500 ALA A 134 59.70 37.07
REMARK 500 ALA A 138 47.84 -140.84
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9RF2 A 1 279 UNP O07427 MGLL_MYCTU 1 279
SEQADV 9RF2 MET A -27 UNP O07427 INITIATING METHIONINE
SEQADV 9RF2 SER A -26 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 TYR A -25 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 TYR A -24 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 HIS A -23 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 HIS A -22 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 HIS A -21 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 HIS A -20 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 HIS A -19 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 HIS A -18 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 ASP A -17 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 TYR A -16 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 ASP A -15 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 ILE A -14 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 PRO A -13 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 THR A -12 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 THR A -11 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 GLU A -10 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 ASN A -9 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 LEU A -8 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 TYR A -7 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 PHE A -6 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 GLN A -5 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 GLY A -4 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 ALA A -3 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 MET A -2 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 GLY A -1 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 SER A 0 UNP O07427 EXPRESSION TAG
SEQADV 9RF2 ALA A 74 UNP O07427 LYS 74 ENGINEERED MUTATION
SEQRES 1 A 307 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 307 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 307 GLY SER MET THR THR THR ARG THR GLU ARG ASN PHE ALA
SEQRES 4 A 307 GLY ILE GLY ASP VAL ARG ILE VAL TYR ASP VAL TRP THR
SEQRES 5 A 307 PRO ASP THR ALA PRO GLN ALA VAL VAL VAL LEU ALA HIS
SEQRES 6 A 307 GLY LEU GLY GLU HIS ALA ARG ARG TYR ASP HIS VAL ALA
SEQRES 7 A 307 GLN ARG LEU GLY ALA ALA GLY LEU VAL THR TYR ALA LEU
SEQRES 8 A 307 ASP HIS ARG GLY HIS GLY ARG SER GLY GLY ALA ARG VAL
SEQRES 9 A 307 LEU VAL ARG ASP ILE SER GLU TYR THR ALA ASP PHE ASP
SEQRES 10 A 307 THR LEU VAL GLY ILE ALA THR ARG GLU TYR PRO GLY CYS
SEQRES 11 A 307 LYS ARG ILE VAL LEU GLY HIS SER MET GLY GLY GLY ILE
SEQRES 12 A 307 VAL PHE ALA TYR GLY VAL GLU ARG PRO ASP ASN TYR ASP
SEQRES 13 A 307 LEU MET VAL LEU SER ALA PRO ALA VAL ALA ALA GLN ASP
SEQRES 14 A 307 LEU VAL SER PRO VAL VAL ALA VAL ALA ALA LYS LEU LEU
SEQRES 15 A 307 GLY VAL VAL VAL PRO GLY LEU PRO VAL GLN GLU LEU ASP
SEQRES 16 A 307 PHE THR ALA ILE SER ARG ASP PRO GLU VAL VAL GLN ALA
SEQRES 17 A 307 TYR ASN THR ASP PRO LEU VAL HIS HIS GLY ARG VAL PRO
SEQRES 18 A 307 ALA GLY ILE GLY ARG ALA LEU LEU GLN VAL GLY GLU THR
SEQRES 19 A 307 MET PRO ARG ARG ALA PRO ALA LEU THR ALA PRO LEU LEU
SEQRES 20 A 307 VAL LEU HIS GLY THR ASP ASP ARG LEU ILE PRO ILE GLU
SEQRES 21 A 307 GLY SER ARG ARG LEU VAL GLU CYS VAL GLY SER ALA ASP
SEQRES 22 A 307 VAL GLN LEU LYS GLU TYR PRO GLY LEU TYR HIS GLU VAL
SEQRES 23 A 307 PHE ASN GLU PRO GLU ARG ASN GLN VAL LEU ASP ASP VAL
SEQRES 24 A 307 VAL ALA TRP LEU THR GLU ARG LEU
HET 8KE A 301 28
HET I3F A 302 56
HET CL A 303 1
HETNAM 8KE [1-[6-[(4-METHOXYPHENYL)AMINO]PYRIMIDIN-4-YL]PYRAZOL-4-
HETNAM 2 8KE YL]-[(3S)-3-OXIDANYLPYRROLIDIN-1-YL]METHANONE
HETNAM I3F [1-[6-[(4-METHOXYPHENYL)AMINO]PYRIMIDIN-4-YL]PYRAZOL-4-
HETNAM 2 I3F YL]-[(3R)-3-OXIDANYLPYRROLIDIN-1-YL]METHANONE
HETNAM CL CHLORIDE ION
FORMUL 2 8KE C19 H20 N6 O3
FORMUL 3 I3F C19 H20 N6 O3
FORMUL 4 CL CL 1-
FORMUL 5 HOH *62(H2 O)
HELIX 1 AA1 ILE A 13 ASP A 15 5 3
HELIX 2 AA2 HIS A 42 ARG A 45 5 4
HELIX 3 AA3 TYR A 46 ALA A 56 1 11
HELIX 4 AA4 ASP A 80 TYR A 99 1 20
HELIX 5 AA5 SER A 110 ARG A 123 1 14
HELIX 6 AA6 ALA A 138 LEU A 142 5 5
HELIX 7 AA7 SER A 144 GLY A 155 1 12
HELIX 8 AA8 ASP A 167 ILE A 171 5 5
HELIX 9 AA9 ASP A 174 THR A 183 1 10
HELIX 10 AB1 ALA A 194 ALA A 211 1 18
HELIX 11 AB2 PRO A 212 LEU A 214 5 3
HELIX 12 AB3 ILE A 231 VAL A 241 1 11
HELIX 13 AB4 GLU A 257 GLU A 261 5 5
HELIX 14 AB5 GLU A 263 LEU A 279 1 17
SHEET 1 AA1 8 THR A 3 ALA A 11 0
SHEET 2 AA1 8 ARG A 17 PRO A 25 -1 O ILE A 18 N PHE A 10
SHEET 3 AA1 8 LEU A 58 LEU A 63 -1 O ALA A 62 N ASP A 21
SHEET 4 AA1 8 ALA A 31 ALA A 36 1 N VAL A 33 O VAL A 59
SHEET 5 AA1 8 LYS A 103 HIS A 109 1 O ILE A 105 N VAL A 32
SHEET 6 AA1 8 LEU A 129 SER A 133 1 O SER A 133 N GLY A 108
SHEET 7 AA1 8 LEU A 218 GLY A 223 1 O LEU A 219 N LEU A 132
SHEET 8 AA1 8 VAL A 246 TYR A 251 1 O LYS A 249 N VAL A 220
SHEET 1 AA2 2 PRO A 162 GLN A 164 0
SHEET 2 AA2 2 VAL A 192 PRO A 193 -1 O VAL A 192 N GLN A 164
CRYST1 40.411 82.784 90.704 90.00 90.00 90.00 P 2 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 0.024746 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012080 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011025 0.00000
TER 2190 LEU A 279
MASTER 277 0 3 14 10 0 0 6 2241 1 84 24
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