| content |
HEADER HYDROLASE 10-JUN-25 9RHW
TITLE M. TUBERCULOSIS MEETS EUROPEAN LEAD FACTORY: IDENTIFICATION AND
TITLE 2 STRUCTURAL CHARACTERIZATION OF NOVEL RV0183 INHIBITORS USING X-RAY
TITLE 3 CRYSTALLOGRAPHY: ELF1
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
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,T.SAGMEISTER
REVDAT 1 13-AUG-25 9RHW 0
JRNL AUTH L.RIEGLER-BERKET,L.GOEDL,M.OBERER,T.SAGMEISTER
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: ELF1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC5
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 83267
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.155
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 4142
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2130
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 277
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.090
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9RHW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUN-25.
REMARK 100 THE DEPOSITION ID IS D_1292148153.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-23
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) : 1.03272
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 : 83281
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.250
REMARK 200 RESOLUTION RANGE LOW (A) : 45.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.9200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.30
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 (%): 45.56
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 41.26750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.29550
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.26750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.29550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 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 LYS A 74 CG CD CE NZ
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 HH12 ARG A 191 O HOH A 403 1.42
REMARK 500 HH21 ARG A 79 O HOH A 408 1.50
REMARK 500 O HOH A 403 O HOH A 609 1.86
REMARK 500 O HOH A 530 O HOH A 663 1.86
REMARK 500 OE1 GLU A 165 O HOH A 401 1.87
REMARK 500 O HOH A 616 O HOH A 617 1.87
REMARK 500 O HOH A 593 O HOH A 594 1.89
REMARK 500 O HOH A 550 O HOH A 580 1.92
REMARK 500 O HOH A 569 O HOH A 591 1.97
REMARK 500 O HOH A 461 O HOH A 530 2.00
REMARK 500 O HOH A 437 O HOH A 530 2.03
REMARK 500 O HOH A 596 O HOH A 602 2.10
REMARK 500 O HOH A 596 O HOH A 599 2.10
REMARK 500 O ARG A 79 O HOH A 402 2.10
REMARK 500 O HOH A 413 O HOH A 550 2.18
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 OE1 GLU A 176 O HOH A 502 1655 2.13
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 ASP A 125 CB - CG - OD1 ANGL. DEV. = 6.8 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 GLU A 41 -152.09 -103.45
REMARK 500 VAL A 76 27.99 47.02
REMARK 500 SER A 110 -119.87 62.67
REMARK 500 ALA A 134 58.63 39.07
REMARK 500 ALA A 138 53.40 -145.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 8 0.15 SIDE CHAIN
REMARK 500 ARG A 66 0.12 SIDE CHAIN
REMARK 500 ARG A 198 0.20 SIDE CHAIN
REMARK 500 ARG A 209 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 675 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 676 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A 677 DISTANCE = 6.89 ANGSTROMS
DBREF 9RHW A 1 279 UNP O07427 MGLL_MYCTU 1 279
SEQADV 9RHW MET A -27 UNP O07427 INITIATING METHIONINE
SEQADV 9RHW SER A -26 UNP O07427 EXPRESSION TAG
SEQADV 9RHW TYR A -25 UNP O07427 EXPRESSION TAG
SEQADV 9RHW TYR A -24 UNP O07427 EXPRESSION TAG
SEQADV 9RHW HIS A -23 UNP O07427 EXPRESSION TAG
SEQADV 9RHW HIS A -22 UNP O07427 EXPRESSION TAG
SEQADV 9RHW HIS A -21 UNP O07427 EXPRESSION TAG
SEQADV 9RHW HIS A -20 UNP O07427 EXPRESSION TAG
SEQADV 9RHW HIS A -19 UNP O07427 EXPRESSION TAG
SEQADV 9RHW HIS A -18 UNP O07427 EXPRESSION TAG
SEQADV 9RHW ASP A -17 UNP O07427 EXPRESSION TAG
SEQADV 9RHW TYR A -16 UNP O07427 EXPRESSION TAG
SEQADV 9RHW ASP A -15 UNP O07427 EXPRESSION TAG
SEQADV 9RHW ILE A -14 UNP O07427 EXPRESSION TAG
SEQADV 9RHW PRO A -13 UNP O07427 EXPRESSION TAG
SEQADV 9RHW THR A -12 UNP O07427 EXPRESSION TAG
SEQADV 9RHW THR A -11 UNP O07427 EXPRESSION TAG
SEQADV 9RHW GLU A -10 UNP O07427 EXPRESSION TAG
SEQADV 9RHW ASN A -9 UNP O07427 EXPRESSION TAG
SEQADV 9RHW LEU A -8 UNP O07427 EXPRESSION TAG
SEQADV 9RHW TYR A -7 UNP O07427 EXPRESSION TAG
SEQADV 9RHW PHE A -6 UNP O07427 EXPRESSION TAG
SEQADV 9RHW GLN A -5 UNP O07427 EXPRESSION TAG
SEQADV 9RHW GLY A -4 UNP O07427 EXPRESSION TAG
SEQADV 9RHW ALA A -3 UNP O07427 EXPRESSION TAG
SEQADV 9RHW MET A -2 UNP O07427 EXPRESSION TAG
SEQADV 9RHW GLY A -1 UNP O07427 EXPRESSION TAG
SEQADV 9RHW SER A 0 UNP O07427 EXPRESSION TAG
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 LYS 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 7WW A 301 96
HET PO4 A 302 5
HET MPD A 303 20
HET DMS A 304 10
HET EOH A 305 8
HET EOH A 306 8
HET EDO A 307 8
HET EOH A 308 8
HET MPD A 309 20
HETNAM 7WW [5-(2-CHLOROPHENYL)-1-(4-METHOXYPHENYL)PYRAZOL-3-YL]-
HETNAM 2 7WW [(3R)-3-OXIDANYLPYRROLIDIN-1-YL]METHANONE
HETNAM PO4 PHOSPHATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EOH ETHANOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 7WW C21 H20 CL N3 O3
FORMUL 3 PO4 O4 P 3-
FORMUL 4 MPD 2(C6 H14 O2)
FORMUL 5 DMS C2 H6 O S
FORMUL 6 EOH 3(C2 H6 O)
FORMUL 8 EDO C2 H6 O2
FORMUL 11 HOH *277(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 THR A 206 1 13
HELIX 11 AB2 THR A 206 ALA A 211 1 6
HELIX 12 AB3 PRO A 212 LEU A 214 5 3
HELIX 13 AB4 ILE A 231 VAL A 241 1 11
HELIX 14 AB5 GLU A 257 GLU A 261 5 5
HELIX 15 AB6 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 THR A 60 N TRP A 23
SHEET 4 AA1 8 ALA A 31 ALA A 36 1 N VAL A 33 O TYR A 61
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 40.485 82.535 90.591 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 0.024701 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012116 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011039 0.00000
TER 4855 LEU A 279
MASTER 375 0 9 15 10 0 0 6 2473 1 183 24
END |