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HEADER HYDROLASE 12-AUG-22 8AQF
TITLE CRYSTAL STRUCTURE OF HUMAN MONOGLYCERIDE LIPASE WITH COMPOUND LEI-515
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOGLYCERIDE LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MGL,HU-K5,LYSOPHOSPHOLIPASE HOMOLOG,LYSOPHOSPHOLIPASE-LIKE,
COMPND 5 MONOACYLGLYCEROL LIPASE,MAGL;
COMPND 6 EC: 3.1.1.23;
COMPND 7 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: MGLL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MONOACYLGLYCEROL LIPASE, MAGL, INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.JIANG,M.HUIZENGA,J.WIRT,J.PALOCZI,A.AMEDI,R.VAN DER BERG,J.BENZ,
AUTHOR 2 L.COLLIN,H.DENG,W.DRIEVER,B.FLOREA,U.GRETHER,A.JANSSEN,L.HEITMAN,
AUTHOR 3 T.W.LAM,F.MOHR,A.PAVLOVIC,I.RUF,H.RUTJES,F.STEVENS,D.VAN DER VLIET,
AUTHOR 4 T.VAN DER WEL,M.WITTWER,C.BOECKEL,P.PACHER,A.HOHMANN,M.VAN DER STELT
REVDAT 1 23-AUG-23 8AQF 0
JRNL AUTH M.JIANG,M.VAN DER STELT
JRNL TITL DISCOVERY OF A PERIPHERAL RESTRICTED, REVERSIBLE
JRNL TITL 2 MONOACYLGLYCEROL LIPASE INHIBITOR THAT REDUCES LIVER INJURY
JRNL TITL 3 AND CHEMOTHERAPY-INDUCED NEUROPATHY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 51370
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.812
REMARK 3 FREE R VALUE TEST SET COUNT : 2472
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3528
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.3580
REMARK 3 BIN FREE R VALUE SET COUNT : 194
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2238
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.71100
REMARK 3 B22 (A**2) : -2.04800
REMARK 3 B33 (A**2) : -0.66300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.064
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.065
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.062
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.972
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.975
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2403 ; 0.017 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2315 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3286 ; 2.019 ; 1.634
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5351 ; 1.530 ; 1.585
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 316 ; 6.378 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 110 ;30.594 ;21.727
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 407 ;14.443 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;17.641 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 306 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2707 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 531 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 521 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 40 ; 0.169 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1178 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 235 ; 0.198 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1186 ; 1.875 ; 2.162
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1185 ; 1.872 ; 2.160
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1489 ; 2.637 ; 3.234
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1490 ; 2.638 ; 3.236
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1217 ; 2.786 ; 2.457
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1218 ; 2.785 ; 2.458
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1784 ; 4.304 ; 3.573
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1785 ; 4.303 ; 3.573
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 7 A 295
REMARK 3 ORIGIN FOR THE GROUP (A): 120.3284 19.9573 -0.7198
REMARK 3 T TENSOR
REMARK 3 T11: 0.0036 T22: 0.0601
REMARK 3 T33: 0.0783 T12: 0.0028
REMARK 3 T13: 0.0057 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 0.1798 L22: 1.3934
REMARK 3 L33: 1.0209 L12: -0.1824
REMARK 3 L13: 0.0036 L23: -0.0210
REMARK 3 S TENSOR
REMARK 3 S11: -0.0142 S12: -0.0072 S13: 0.0111
REMARK 3 S21: 0.0005 S22: -0.0340 S23: -0.0560
REMARK 3 S31: 0.0466 S32: 0.0594 S33: 0.0482
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8AQF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-22.
REMARK 100 THE DEPOSITION ID IS D_1292124933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-21
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00009
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51415
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 45.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.620
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06310
REMARK 200 FOR THE DATA SET : 11.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
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) : 0.78850
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: 3PE6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5, 6 TO 13% PEG MME5K,
REMARK 280 12% ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.17900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.17900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 45.81250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.78400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.81250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.78400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 30.17900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.81250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.78400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 30.17900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.81250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.78400
REMARK 290 SMTRY3 8 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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 THR A 296
REMARK 465 ALA A 297
REMARK 465 GLY A 298
REMARK 465 THR A 299
REMARK 465 ALA A 300
REMARK 465 SER A 301
REMARK 465 PRO A 302
REMARK 465 PRO A 303
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 OG SER A 122 C18 NUX A 401 1.61
REMARK 500 O HOH A 708 O HOH A 802 1.86
REMARK 500 O HOH A 720 O HOH A 752 2.09
REMARK 500 O HOH A 738 O HOH A 817 2.19
REMARK 500 O HOH A 630 O HOH A 751 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE A 31 C PHE A 31 O 0.127
REMARK 500 GLU A 59 CD GLU A 59 OE2 -0.077
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 PRO A 7 N - CA - CB ANGL. DEV. = 7.5 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 SER A 13 4.27 88.90
REMARK 500 GLU A 53 -156.37 -103.15
REMARK 500 ASP A 69 32.09 70.87
REMARK 500 SER A 122 -128.99 58.56
REMARK 500 PRO A 178 152.86 -46.93
REMARK 500 ALA A 203 164.00 -46.51
REMARK 500 TYR A 268 -156.90 -88.23
REMARK 500 LYS A 273 44.79 -143.73
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 819 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH A 820 DISTANCE = 6.77 ANGSTROMS
DBREF 8AQF A 1 303 UNP Q99685 MGLL_HUMAN 1 303
SEQADV 8AQF MET A -19 UNP Q99685 INITIATING METHIONINE
SEQADV 8AQF GLY A -18 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF SER A -17 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF SER A -16 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF HIS A -15 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF HIS A -14 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF HIS A -13 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF HIS A -12 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF HIS A -11 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF HIS A -10 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF SER A -9 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF SER A -8 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF GLY A -7 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF GLU A -6 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF ASN A -5 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF LEU A -4 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF TYR A -3 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF PHE A -2 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF GLN A -1 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF GLY A 0 UNP Q99685 EXPRESSION TAG
SEQADV 8AQF ALA A 36 UNP Q99685 LYS 36 ENGINEERED MUTATION
SEQADV 8AQF SER A 169 UNP Q99685 LEU 169 ENGINEERED MUTATION
SEQADV 8AQF SER A 176 UNP Q99685 LEU 176 ENGINEERED MUTATION
SEQRES 1 A 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 323 GLU ASN LEU TYR PHE GLN GLY MET PRO GLU GLU SER SER
SEQRES 3 A 323 PRO ARG ARG THR PRO GLN SER ILE PRO TYR GLN ASP LEU
SEQRES 4 A 323 PRO HIS LEU VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS
SEQRES 5 A 323 ARG TYR TRP ALA PRO THR GLY THR PRO LYS ALA LEU ILE
SEQRES 6 A 323 PHE VAL SER HIS GLY ALA GLY GLU HIS SER GLY ARG TYR
SEQRES 7 A 323 GLU GLU LEU ALA ARG MET LEU MET GLY LEU ASP LEU LEU
SEQRES 8 A 323 VAL PHE ALA HIS ASP HIS VAL GLY HIS GLY GLN SER GLU
SEQRES 9 A 323 GLY GLU ARG MET VAL VAL SER ASP PHE HIS VAL PHE VAL
SEQRES 10 A 323 ARG ASP VAL LEU GLN HIS VAL ASP SER MET GLN LYS ASP
SEQRES 11 A 323 TYR PRO GLY LEU PRO VAL PHE LEU LEU GLY HIS SER MET
SEQRES 12 A 323 GLY GLY ALA ILE ALA ILE LEU THR ALA ALA GLU ARG PRO
SEQRES 13 A 323 GLY HIS PHE ALA GLY MET VAL LEU ILE SER PRO LEU VAL
SEQRES 14 A 323 LEU ALA ASN PRO GLU SER ALA THR THR PHE LYS VAL LEU
SEQRES 15 A 323 ALA ALA LYS VAL LEU ASN SER VAL LEU PRO ASN LEU SER
SEQRES 16 A 323 SER GLY PRO ILE ASP SER SER VAL LEU SER ARG ASN LYS
SEQRES 17 A 323 THR GLU VAL ASP ILE TYR ASN SER ASP PRO LEU ILE CYS
SEQRES 18 A 323 ARG ALA GLY LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU
SEQRES 19 A 323 ASN ALA VAL SER ARG VAL GLU ARG ALA LEU PRO LYS LEU
SEQRES 20 A 323 THR VAL PRO PHE LEU LEU LEU GLN GLY SER ALA ASP ARG
SEQRES 21 A 323 LEU CYS ASP SER LYS GLY ALA TYR LEU LEU MET GLU LEU
SEQRES 22 A 323 ALA LYS SER GLN ASP LYS THR LEU LYS ILE TYR GLU GLY
SEQRES 23 A 323 ALA TYR HIS VAL LEU HIS LYS GLU LEU PRO GLU VAL THR
SEQRES 24 A 323 ASN SER VAL PHE HIS GLU ILE ASN MET TRP VAL SER GLN
SEQRES 25 A 323 ARG THR ALA THR ALA GLY THR ALA SER PRO PRO
HET NUX A 401 34
HETNAM NUX 1-[(~{R})-[2-CHLORANYL-4-[(2~{S},3~{S})-4-(3-
HETNAM 2 NUX CHLOROPHENYL)-2,3-DIMETHYL-PIPERAZIN-1-YL]CARBONYL-
HETNAM 3 NUX PHENYL]SULFINYL]-3,3-BIS(FLUORANYL)PENTAN-2-ONE
HETSYN NUX 1-[2-CHLORANYL-4-[(2~{S},3~{S})-4-(3-CHLOROPHENYL)-2,3-
HETSYN 2 NUX DIMETHYL-PIPERAZIN-1-YL]CARBONYL-PHENYL]SULFINYL-3,3-
HETSYN 3 NUX BIS(FLUORANYL)PENTAN-2-ONE
FORMUL 2 NUX C24 H26 CL2 F2 N2 O3 S
FORMUL 3 HOH *320(H2 O)
HELIX 1 AA1 PRO A 15 LEU A 19 5 5
HELIX 2 AA2 HIS A 54 ARG A 57 5 4
HELIX 3 AA3 TYR A 58 LEU A 68 1 11
HELIX 4 AA4 PHE A 93 TYR A 111 1 19
HELIX 5 AA5 MET A 123 ARG A 135 1 13
HELIX 6 AA6 THR A 157 SER A 169 1 13
HELIX 7 AA7 ASP A 180 LEU A 184 5 5
HELIX 8 AA8 ASN A 187 ASP A 197 1 11
HELIX 9 AA9 LYS A 206 LEU A 224 1 19
HELIX 10 AB1 PRO A 225 LEU A 227 5 3
HELIX 11 AB2 ASP A 243 ALA A 254 1 12
HELIX 12 AB3 VAL A 270 GLU A 274 5 5
HELIX 13 AB4 LEU A 275 ALA A 295 1 21
SHEET 1 AA1 8 HIS A 21 VAL A 23 0
SHEET 2 AA1 8 TYR A 29 TRP A 35 -1 O LEU A 30 N LEU A 22
SHEET 3 AA1 8 LEU A 70 HIS A 75 -1 O VAL A 72 N TRP A 35
SHEET 4 AA1 8 ALA A 43 SER A 48 1 N ALA A 43 O LEU A 71
SHEET 5 AA1 8 VAL A 116 SER A 122 1 O LEU A 119 N SER A 48
SHEET 6 AA1 8 GLY A 141 PRO A 147 1 O VAL A 143 N GLY A 120
SHEET 7 AA1 8 PHE A 231 GLY A 236 1 O LEU A 234 N SER A 146
SHEET 8 AA1 8 LYS A 259 TYR A 264 1 O THR A 260 N LEU A 233
CRYST1 91.625 127.568 60.358 90.00 90.00 90.00 C 2 2 21 8
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 0.010914 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007839 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016568 0.00000
TER 2300 ALA A 295
MASTER 406 0 1 13 8 0 0 6 2592 1 34 25
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