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HEADER HYDROLASE/INHIBITOR 08-MAY-18 5ZUN
TITLE CRYSTAL STRUCTURE OF HUMAN MONOACYLGLYCEROL LIPASE IN COMPLEX WITH
TITLE 2 COMPOUND 3L
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;
COMPND 8 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: MGLL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MONOACYLGLYCEROL LIPASE, HYDROLASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SOGABE,Y.ZAMA,W.LANE,G.SNELL
REVDAT 1 17-OCT-18 5ZUN 0
JRNL AUTH J.AIDA,M.FUSHIMI,T.KUSUMOTO,H.SUGIYAMA,N.ARIMURA,S.IKEDA,
JRNL AUTH 2 M.SASAKI,S.SOGABE,K.AOYAMA,T.KOIKE
JRNL TITL DESIGN, SYNTHESIS, AND EVALUATION OF PIPERAZINYL
JRNL TITL 2 PYRROLIDIN-2-ONES AS A NOVEL SERIES OF REVERSIBLE
JRNL TITL 3 MONOACYLGLYCEROL LIPASE INHIBITORS
JRNL REF J. MED. CHEM. 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 30251836
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00824
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0222
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 74657
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3916
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4314
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE SET COUNT : 243
REMARK 3 BIN FREE R VALUE : 0.2860
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 : 78
REMARK 3 SOLVENT ATOMS : 297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.38000
REMARK 3 B22 (A**2) : -0.69000
REMARK 3 B33 (A**2) : -0.68000
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): 0.042
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.042
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.029
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.479
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.971
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2468 ; 0.011 ; 0.015
REMARK 3 BOND LENGTHS OTHERS (A): 2291 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3357 ; 1.603 ; 1.765
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5380 ; 0.550 ; 1.732
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 321 ; 5.832 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 84 ;27.758 ;19.048
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 370 ;13.097 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;18.116 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 308 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2781 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 456 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1194 ; 0.834 ; 1.007
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1195 ; 0.833 ; 1.008
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1501 ; 1.424 ; 1.509
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1502 ; 1.428 ; 1.511
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1274 ; 1.284 ; 1.185
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1274 ; 1.282 ; 1.185
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1840 ; 2.007 ; 1.692
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2766 ; 4.353 ;13.663
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2696 ; 4.001 ;12.948
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 7 A 295
REMARK 3 RESIDUE RANGE : A 401 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9288 20.0718 -1.3645
REMARK 3 T TENSOR
REMARK 3 T11: 0.0084 T22: 0.0042
REMARK 3 T33: 0.0033 T12: 0.0047
REMARK 3 T13: 0.0041 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.2329 L22: 0.6617
REMARK 3 L33: 0.6598 L12: -0.0208
REMARK 3 L13: -0.0394 L23: 0.1407
REMARK 3 S TENSOR
REMARK 3 S11: -0.0186 S12: -0.0239 S13: -0.0025
REMARK 3 S21: 0.0038 S22: 0.0010 S23: 0.0065
REMARK 3 S31: -0.0132 S32: 0.0154 S33: 0.0176
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5ZUN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE DEPOSITION ID IS D_1300007684.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78596
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07400
REMARK 200 FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.85200
REMARK 200 FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3PE6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS, 10% PEG3350, PH 6.0,
REMARK 280 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 30.12500
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 30.12500
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 47.57450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.61200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 47.57450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.61200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 30.12500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 47.57450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.61200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 30.12500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 47.57450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.61200
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: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 502 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 707 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 776 LIES ON A SPECIAL POSITION.
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 GLY A -1
REMARK 465 SER 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 O HOH A 625 O HOH A 675 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 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 57 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -4.3 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 13.71 87.83
REMARK 500 SER A 13 21.67 81.78
REMARK 500 GLU A 53 -151.15 -121.99
REMARK 500 SER A 122 -126.04 62.50
REMARK 500 GLU A 274 -162.04 -102.77
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 797 DISTANCE = 6.29 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9JX A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 411
DBREF 5ZUN A 1 303 UNP Q99685 MGLL_HUMAN 1 303
SEQADV 5ZUN GLY A -1 UNP Q99685 EXPRESSION TAG
SEQADV 5ZUN SER A 0 UNP Q99685 EXPRESSION TAG
SEQADV 5ZUN ALA A 36 UNP Q99685 LYS 36 ENGINEERED MUTATION
SEQADV 5ZUN SER A 169 UNP Q99685 LEU 169 ENGINEERED MUTATION
SEQADV 5ZUN SER A 176 UNP Q99685 LEU 176 ENGINEERED MUTATION
SEQRES 1 A 305 GLY SER MET PRO GLU GLU SER SER PRO ARG ARG THR PRO
SEQRES 2 A 305 GLN SER ILE PRO TYR GLN ASP LEU PRO HIS LEU VAL ASN
SEQRES 3 A 305 ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR TRP ALA PRO
SEQRES 4 A 305 THR GLY THR PRO LYS ALA LEU ILE PHE VAL SER HIS GLY
SEQRES 5 A 305 ALA GLY GLU HIS SER GLY ARG TYR GLU GLU LEU ALA ARG
SEQRES 6 A 305 MET LEU MET GLY LEU ASP LEU LEU VAL PHE ALA HIS ASP
SEQRES 7 A 305 HIS VAL GLY HIS GLY GLN SER GLU GLY GLU ARG MET VAL
SEQRES 8 A 305 VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL LEU GLN
SEQRES 9 A 305 HIS VAL ASP SER MET GLN LYS ASP TYR PRO GLY LEU PRO
SEQRES 10 A 305 VAL PHE LEU LEU GLY HIS SER MET GLY GLY ALA ILE ALA
SEQRES 11 A 305 ILE LEU THR ALA ALA GLU ARG PRO GLY HIS PHE ALA GLY
SEQRES 12 A 305 MET VAL LEU ILE SER PRO LEU VAL LEU ALA ASN PRO GLU
SEQRES 13 A 305 SER ALA THR THR PHE LYS VAL LEU ALA ALA LYS VAL LEU
SEQRES 14 A 305 ASN SER VAL LEU PRO ASN LEU SER SER GLY PRO ILE ASP
SEQRES 15 A 305 SER SER VAL LEU SER ARG ASN LYS THR GLU VAL ASP ILE
SEQRES 16 A 305 TYR ASN SER ASP PRO LEU ILE CYS ARG ALA GLY LEU LYS
SEQRES 17 A 305 VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA VAL SER ARG
SEQRES 18 A 305 VAL GLU ARG ALA LEU PRO LYS LEU THR VAL PRO PHE LEU
SEQRES 19 A 305 LEU LEU GLN GLY SER ALA ASP ARG LEU CYS ASP SER LYS
SEQRES 20 A 305 GLY ALA TYR LEU LEU MET GLU LEU ALA LYS SER GLN ASP
SEQRES 21 A 305 LYS THR LEU LYS ILE TYR GLU GLY ALA TYR HIS VAL LEU
SEQRES 22 A 305 HIS LYS GLU LEU PRO GLU VAL THR ASN SER VAL PHE HIS
SEQRES 23 A 305 GLU ILE ASN MET TRP VAL SER GLN ARG THR ALA THR ALA
SEQRES 24 A 305 GLY THR ALA SER PRO PRO
HET 9JX A 401 32
HET PG4 A 402 13
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 4
HET EDO A 409 4
HET EDO A 410 4
HET CL A 411 1
HETNAM 9JX (4R)-1-(2'-CHLORO[1,1'-BIPHENYL]-3-YL)-4-[4-(1,3-
HETNAM 2 9JX THIAZOLE-2-CARBONYL)PIPERAZIN-1-YL]PYRROLIDIN-2-ONE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 9JX C24 H23 CL N4 O2 S
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 EDO 8(C2 H6 O2)
FORMUL 12 CL CL 1-
FORMUL 13 HOH *297(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 SER A 122 ARG A 135 1 14
HELIX 6 AA6 ASN A 152 ASN A 168 1 17
HELIX 7 AA7 ASP A 180 LEU A 184 5 5
HELIX 8 AA8 ASN A 187 SER A 196 1 10
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 ARG A 293 1 19
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 VAL A 47 O PHE A 73
SHEET 5 AA1 8 VAL A 116 HIS A 121 1 O LEU A 119 N SER A 48
SHEET 6 AA1 8 GLY A 141 ILE A 145 1 O VAL A 143 N LEU A 118
SHEET 7 AA1 8 PHE A 231 GLY A 236 1 O LEU A 232 N LEU A 144
SHEET 8 AA1 8 LYS A 259 TYR A 264 1 O THR A 260 N LEU A 233
SITE 1 AC1 24 GLY A 50 ALA A 51 GLU A 53 ARG A 57
SITE 2 AC1 24 MET A 88 HIS A 121 SER A 122 MET A 123
SITE 3 AC1 24 GLY A 177 PRO A 178 ILE A 179 SER A 181
SITE 4 AC1 24 LEU A 184 SER A 185 GLU A 190 VAL A 191
SITE 5 AC1 24 TYR A 194 LEU A 205 LEU A 241 VAL A 270
SITE 6 AC1 24 LYS A 273 PG4 A 402 HOH A 542 HOH A 585
SITE 1 AC2 6 THR A 158 9JX A 401 EDO A 403 HOH A 501
SITE 2 AC2 6 HOH A 519 HOH A 532
SITE 1 AC3 5 ILE A 179 ASP A 180 PG4 A 402 HOH A 522
SITE 2 AC3 5 HOH A 673
SITE 1 AC4 6 GLU A 190 HIS A 272 LYS A 273 PHE A 283
SITE 2 AC4 6 HOH A 546 HOH A 658
SITE 1 AC5 7 GLN A 12 GLY A 81 ARG A 87 LEU A 199
SITE 2 AC5 7 HOH A 565 HOH A 621 HOH A 677
SITE 1 AC6 5 ILE A 14 HOH A 563 HOH A 589 HOH A 597
SITE 2 AC6 5 HOH A 632
SITE 1 AC7 8 TYR A 34 HIS A 103 SER A 106 MET A 107
SITE 2 AC7 8 SER A 196 ARG A 202 HOH A 508 HOH A 574
SITE 1 AC8 5 HIS A 54 GLY A 56 ARG A 57 ILE A 193
SITE 2 AC8 5 ASP A 197
SITE 1 AC9 5 ARG A 9 THR A 10 PRO A 11 GLU A 84
SITE 2 AC9 5 GLY A 85
SITE 1 AD1 3 ASN A 215 ARG A 219 ARG A 222
SITE 1 AD2 3 HIS A 94 ARG A 219 HOH A 791
CRYST1 95.149 127.224 60.250 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 0.010510 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007860 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016598 0.00000
TER 2325 ALA A 295
MASTER 419 0 11 13 8 0 24 6 2613 1 77 24
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