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HEADER HYDROLASE/INHIBITOR 21-DEC-20 7L4W
TITLE CRYSTAL STRUCTURE OF HUMAN MONOACYLGLYCEROL LIPASE IN COMPLEX WITH
TITLE 2 COMPOUND 2D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOGLYCERIDE LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 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 INHIBITOR, SERINE HYDROLASE, HYDROLASE, HYDROLASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.QIN,W.LANE,R.J.SKENE
REVDAT 1 11-AUG-21 7L4W 0
JRNL AUTH S.IKEDA,H.SUGIYAMA,H.TOKUHARA,M.MURAKAMI,M.NAKAMURA,Y.OGURO,
JRNL AUTH 2 J.AIDA,N.MORISHITA,S.SOGABE,D.R.DOUGAN,S.C.GAY,L.QIN,
JRNL AUTH 3 N.ARIMURA,Y.TAKAHASHI,M.SASAKI,Y.KAMADA,K.AOYAMA,K.KIMOTO,
JRNL AUTH 4 M.KAMATA
JRNL TITL DESIGN AND SYNTHESIS OF NOVEL SPIRO DERIVATIVES AS POTENT
JRNL TITL 2 AND REVERSIBLE MONOACYLGLYCEROL LIPASE (MAGL) INHIBITORS:
JRNL TITL 3 BIOISOSTERIC TRANSFORMATION FROM 3-OXO-3,4-DIHYDRO-2 H
JRNL TITL 4 -BENZO[ B ][1,4]OXAZIN-6-YL MOIETY.
JRNL REF J.MED.CHEM. 2021
JRNL REFN ISSN 0022-2623
JRNL PMID 34328319
JRNL DOI 10.1021/ACS.JMEDCHEM.1C00432
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0257
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 38970
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2031
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2713
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.3410
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4457
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.66000
REMARK 3 B22 (A**2) : -3.09000
REMARK 3 B33 (A**2) : 1.43000
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): 0.199
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.171
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.170
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.805
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4623 ; 0.007 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4273 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6290 ; 1.450 ; 1.650
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9894 ; 1.240 ; 1.566
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 576 ; 6.607 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 218 ;30.272 ;21.651
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 747 ;13.955 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;11.367 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 580 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5159 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 941 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
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 294
REMARK 3 RESIDUE RANGE : A 401 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): -21.108 -10.810 -50.302
REMARK 3 T TENSOR
REMARK 3 T11: 0.1932 T22: 0.0282
REMARK 3 T33: 0.1553 T12: -0.0386
REMARK 3 T13: -0.0027 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.2823 L22: 2.7232
REMARK 3 L33: 0.2227 L12: -0.4899
REMARK 3 L13: -0.1260 L23: -0.3238
REMARK 3 S TENSOR
REMARK 3 S11: -0.0708 S12: 0.0545 S13: 0.0494
REMARK 3 S21: -0.0617 S22: 0.0798 S23: -0.1933
REMARK 3 S31: 0.0463 S32: -0.0731 S33: -0.0090
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 5 B 294
REMARK 3 RESIDUE RANGE : B 401 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): -26.572 12.247 -18.183
REMARK 3 T TENSOR
REMARK 3 T11: 0.2060 T22: 0.0176
REMARK 3 T33: 0.1188 T12: 0.0363
REMARK 3 T13: 0.0817 T23: 0.0441
REMARK 3 L TENSOR
REMARK 3 L11: 0.0344 L22: 2.1142
REMARK 3 L33: 0.7986 L12: -0.0218
REMARK 3 L13: -0.1005 L23: -0.5229
REMARK 3 S TENSOR
REMARK 3 S11: -0.0649 S12: -0.0075 S13: -0.0244
REMARK 3 S21: 0.1131 S22: -0.0012 S23: 0.0379
REMARK 3 S31: 0.0036 S32: 0.0055 S33: 0.0660
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 7L4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1000253718.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JAN-16
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 : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41130
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.98700
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: 5ZUN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NAOAC PH 5.5, 32-38% MPD, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+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 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 46.31150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.60750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 67.98050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.31150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.60750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 67.98050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.31150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.60750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 67.98050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.31150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.60750
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 67.98050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 -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 GLY A -9
REMARK 465 SER A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
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 ALA A 295
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 465 MET B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 GLY B -9
REMARK 465 SER B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
REMARK 465 ALA B 295
REMARK 465 THR B 296
REMARK 465 ALA B 297
REMARK 465 GLY B 298
REMARK 465 THR B 299
REMARK 465 ALA B 300
REMARK 465 SER B 301
REMARK 465 PRO B 302
REMARK 465 PRO B 303
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 109 CE NZ
REMARK 470 GLU A 154 CG CD OE1 OE2
REMARK 470 LYS A 160 CG CD CE NZ
REMARK 470 GLU B 154 CG CD OE1 OE2
REMARK 470 LYS B 160 CG CD CE NZ
REMARK 470 LYS B 188 CD CE NZ
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 PRO A 11 -8.20 -57.12
REMARK 500 SER A 13 26.06 81.50
REMARK 500 GLU A 53 -159.70 -116.00
REMARK 500 VAL A 78 129.71 -39.83
REMARK 500 SER A 122 -123.54 62.04
REMARK 500 SER A 146 62.05 35.84
REMARK 500 ALA A 203 154.50 -46.60
REMARK 500 TYR A 268 -149.02 -89.33
REMARK 500 GLU B 53 -159.54 -98.73
REMARK 500 SER B 122 -122.15 54.93
REMARK 500 VAL B 170 -74.06 -96.97
REMARK 500 SER B 256 130.21 -38.97
REMARK 500 TYR B 268 -155.38 -83.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue XOV A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue XOV B 401
DBREF1 7L4W A 0 303 UNP A0A0C4DFN3_HUMAN
DBREF2 7L4W A A0A0C4DFN3 10 313
DBREF1 7L4W B 0 303 UNP A0A0C4DFN3_HUMAN
DBREF2 7L4W B A0A0C4DFN3 10 313
SEQADV 7L4W MET A -16 UNP A0A0C4DFN INITIATING METHIONINE
SEQADV 7L4W HIS A -15 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W HIS A -14 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W HIS A -13 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W HIS A -12 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W HIS A -11 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W HIS A -10 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W GLY A -9 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W SER A -8 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W GLU A -7 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W ASN A -6 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W LEU A -5 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W TYR A -4 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W PHE A -3 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W GLN A -2 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W GLY A -1 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W ALA A 36 UNP A0A0C4DFN LYS 46 CONFLICT
SEQADV 7L4W SER A 169 UNP A0A0C4DFN LEU 179 CONFLICT
SEQADV 7L4W SER A 176 UNP A0A0C4DFN LEU 186 CONFLICT
SEQADV 7L4W MET B -16 UNP A0A0C4DFN INITIATING METHIONINE
SEQADV 7L4W HIS B -15 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W HIS B -14 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W HIS B -13 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W HIS B -12 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W HIS B -11 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W HIS B -10 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W GLY B -9 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W SER B -8 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W GLU B -7 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W ASN B -6 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W LEU B -5 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W TYR B -4 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W PHE B -3 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W GLN B -2 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W GLY B -1 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4W ALA B 36 UNP A0A0C4DFN LYS 46 CONFLICT
SEQADV 7L4W SER B 169 UNP A0A0C4DFN LEU 179 CONFLICT
SEQADV 7L4W SER B 176 UNP A0A0C4DFN LEU 186 CONFLICT
SEQRES 1 A 320 MET HIS HIS HIS HIS HIS HIS GLY SER GLU ASN LEU TYR
SEQRES 2 A 320 PHE GLN GLY SER MET PRO GLU GLU SER SER PRO ARG ARG
SEQRES 3 A 320 THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS LEU
SEQRES 4 A 320 VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR TRP
SEQRES 5 A 320 ALA PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL SER
SEQRES 6 A 320 HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU LEU
SEQRES 7 A 320 ALA ARG MET LEU MET GLY LEU ASP LEU LEU VAL PHE ALA
SEQRES 8 A 320 HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU ARG
SEQRES 9 A 320 MET VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL
SEQRES 10 A 320 LEU GLN HIS VAL ASP SER MET GLN LYS ASP TYR PRO GLY
SEQRES 11 A 320 LEU PRO VAL PHE LEU LEU GLY HIS SER MET GLY GLY ALA
SEQRES 12 A 320 ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS PHE
SEQRES 13 A 320 ALA GLY MET VAL LEU ILE SER PRO LEU VAL LEU ALA ASN
SEQRES 14 A 320 PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA LYS
SEQRES 15 A 320 VAL LEU ASN SER VAL LEU PRO ASN LEU SER SER GLY PRO
SEQRES 16 A 320 ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU VAL
SEQRES 17 A 320 ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA GLY
SEQRES 18 A 320 LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA VAL
SEQRES 19 A 320 SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL PRO
SEQRES 20 A 320 PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS ASP
SEQRES 21 A 320 SER LYS GLY ALA TYR LEU LEU MET GLU LEU ALA LYS SER
SEQRES 22 A 320 GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR HIS
SEQRES 23 A 320 VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER VAL
SEQRES 24 A 320 PHE HIS GLU ILE ASN MET TRP VAL SER GLN ARG THR ALA
SEQRES 25 A 320 THR ALA GLY THR ALA SER PRO PRO
SEQRES 1 B 320 MET HIS HIS HIS HIS HIS HIS GLY SER GLU ASN LEU TYR
SEQRES 2 B 320 PHE GLN GLY SER MET PRO GLU GLU SER SER PRO ARG ARG
SEQRES 3 B 320 THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS LEU
SEQRES 4 B 320 VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR TRP
SEQRES 5 B 320 ALA PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL SER
SEQRES 6 B 320 HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU LEU
SEQRES 7 B 320 ALA ARG MET LEU MET GLY LEU ASP LEU LEU VAL PHE ALA
SEQRES 8 B 320 HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU ARG
SEQRES 9 B 320 MET VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL
SEQRES 10 B 320 LEU GLN HIS VAL ASP SER MET GLN LYS ASP TYR PRO GLY
SEQRES 11 B 320 LEU PRO VAL PHE LEU LEU GLY HIS SER MET GLY GLY ALA
SEQRES 12 B 320 ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS PHE
SEQRES 13 B 320 ALA GLY MET VAL LEU ILE SER PRO LEU VAL LEU ALA ASN
SEQRES 14 B 320 PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA LYS
SEQRES 15 B 320 VAL LEU ASN SER VAL LEU PRO ASN LEU SER SER GLY PRO
SEQRES 16 B 320 ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU VAL
SEQRES 17 B 320 ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA GLY
SEQRES 18 B 320 LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA VAL
SEQRES 19 B 320 SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL PRO
SEQRES 20 B 320 PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS ASP
SEQRES 21 B 320 SER LYS GLY ALA TYR LEU LEU MET GLU LEU ALA LYS SER
SEQRES 22 B 320 GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR HIS
SEQRES 23 B 320 VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER VAL
SEQRES 24 B 320 PHE HIS GLU ILE ASN MET TRP VAL SER GLN ARG THR ALA
SEQRES 25 B 320 THR ALA GLY THR ALA SER PRO PRO
HET XOV A 401 27
HET XOV B 401 27
HETNAM XOV (2S,4R)-2-{4-[(2-CHLORO-4-FLUOROPHENOXY)
HETNAM 2 XOV METHYL]PIPERIDINE-1-CARBONYL}-7-OXA-5-
HETNAM 3 XOV AZASPIRO[3.4]OCTAN-6-ONE
FORMUL 3 XOV 2(C19 H22 CL F N2 O4)
FORMUL 5 HOH *131(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 GLY A 67 1 10
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 ASN A 152 ALA A 156 5 5
HELIX 7 AA7 THR A 157 SER A 169 1 13
HELIX 8 AA8 ASP A 180 SER A 185 5 6
HELIX 9 AA9 ASN A 187 ASN A 195 1 9
HELIX 10 AB1 LYS A 206 LEU A 224 1 19
HELIX 11 AB2 PRO A 225 LEU A 227 5 3
HELIX 12 AB3 ASP A 243 ALA A 254 1 12
HELIX 13 AB4 VAL A 270 GLU A 274 5 5
HELIX 14 AB5 LEU A 275 ARG A 293 1 19
HELIX 15 AB6 PRO B 15 LEU B 19 5 5
HELIX 16 AB7 HIS B 54 ARG B 57 5 4
HELIX 17 AB8 TYR B 58 GLY B 67 1 10
HELIX 18 AB9 PHE B 93 TYR B 111 1 19
HELIX 19 AC1 MET B 123 ARG B 135 1 13
HELIX 20 AC2 THR B 157 LEU B 171 1 15
HELIX 21 AC3 ASP B 180 LEU B 184 5 5
HELIX 22 AC4 ASN B 187 ASP B 197 1 11
HELIX 23 AC5 LYS B 206 LEU B 224 1 19
HELIX 24 AC6 PRO B 225 LEU B 227 5 3
HELIX 25 AC7 SER B 244 ALA B 254 1 11
HELIX 26 AC8 VAL B 270 GLU B 274 5 5
HELIX 27 AC9 LEU B 275 GLN B 292 1 18
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 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 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
SHEET 1 AA2 8 HIS B 21 VAL B 23 0
SHEET 2 AA2 8 TYR B 29 TRP B 35 -1 O LEU B 30 N LEU B 22
SHEET 3 AA2 8 LEU B 70 HIS B 75 -1 O VAL B 72 N TRP B 35
SHEET 4 AA2 8 ALA B 43 SER B 48 1 N ALA B 43 O LEU B 71
SHEET 5 AA2 8 VAL B 116 SER B 122 1 O PHE B 117 N LEU B 44
SHEET 6 AA2 8 GLY B 141 PRO B 147 1 O ILE B 145 N GLY B 120
SHEET 7 AA2 8 PHE B 231 GLY B 236 1 O LEU B 234 N SER B 146
SHEET 8 AA2 8 LYS B 259 TYR B 264 1 O THR B 260 N LEU B 233
SITE 1 AC1 13 GLY A 50 ALA A 51 GLU A 53 ARG A 57
SITE 2 AC1 13 HIS A 121 SER A 122 MET A 123 TYR A 194
SITE 3 AC1 13 LEU A 205 GLY A 210 HIS A 269 VAL A 270
SITE 4 AC1 13 HOH A 519
SITE 1 AC2 14 GLY B 50 ALA B 51 GLU B 53 ARG B 57
SITE 2 AC2 14 HIS B 121 SER B 122 MET B 123 LEU B 148
SITE 3 AC2 14 LEU B 205 GLY B 210 LEU B 213 HIS B 269
SITE 4 AC2 14 VAL B 270 HOH B 513
CRYST1 92.623 127.215 135.961 90.00 90.00 90.00 I 2 2 2 16
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 0.010796 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007861 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007355 0.00000
TER 2224 THR A 294
TER 4459 THR B 294
MASTER 419 0 2 27 16 0 8 6 4642 2 54 50
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