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HEADER HYDROLASE/INHIBITOR 21-DEC-20 7L4U
TITLE CRYSTAL STRUCTURE OF HUMAN MONOACYLGLYCEROL LIPASE IN COMPLEX WITH
TITLE 2 COMPOUND 1H
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,D.DOUGAN
REVDAT 1 11-AUG-21 7L4U 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. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 33182
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1651
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1297
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 48.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.3530
REMARK 3 BIN FREE R VALUE SET COUNT : 59
REMARK 3 BIN FREE R VALUE : 0.4020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4434
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.78000
REMARK 3 B22 (A**2) : 0.72000
REMARK 3 B33 (A**2) : 0.07000
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): 0.260
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.217
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.207
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.680
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4604 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4289 ; 0.002 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6251 ; 1.547 ; 1.648
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9940 ; 1.243 ; 1.569
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 572 ; 6.920 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 219 ;31.257 ;21.689
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 760 ;16.092 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;12.619 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 577 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5120 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 936 ; 0.002 ; 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 6 A 295
REMARK 3 RESIDUE RANGE : A 401 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): 19.399 115.123 290.128
REMARK 3 T TENSOR
REMARK 3 T11: 0.2720 T22: 0.0106
REMARK 3 T33: 0.1677 T12: -0.0179
REMARK 3 T13: -0.0872 T23: 0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 0.0303 L22: 2.7454
REMARK 3 L33: 0.7013 L12: 0.2135
REMARK 3 L13: 0.0177 L23: -0.4985
REMARK 3 S TENSOR
REMARK 3 S11: -0.0647 S12: -0.0012 S13: 0.0224
REMARK 3 S21: -0.1594 S22: -0.0694 S23: 0.0235
REMARK 3 S31: -0.0086 S32: 0.0316 S33: 0.1341
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 7 B 294
REMARK 3 RESIDUE RANGE : A 402 A 402
REMARK 3 RESIDUE RANGE : B 401 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): 25.212 138.375 322.203
REMARK 3 T TENSOR
REMARK 3 T11: 0.1984 T22: 0.0542
REMARK 3 T33: 0.2409 T12: 0.0399
REMARK 3 T13: 0.0258 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 0.2734 L22: 2.8387
REMARK 3 L33: 0.0949 L12: 0.7805
REMARK 3 L13: 0.0289 L23: -0.1514
REMARK 3 S TENSOR
REMARK 3 S11: -0.0356 S12: -0.0656 S13: -0.0099
REMARK 3 S21: 0.0004 S22: -0.0356 S23: -0.2000
REMARK 3 S31: -0.0217 S32: -0.0645 S33: 0.0712
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 7L4U 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_1000253717.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-DEC-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 : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
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 : 34850
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
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 (%) : 90.6
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.56300
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 (%): 56.74
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 46.26400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.72650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 67.95550
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.26400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.72650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 67.95550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.26400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.72650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 67.95550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.26400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.72650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 67.95550
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 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 559 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 563 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 580 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 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 ALA A 151
REMARK 465 ASN A 152
REMARK 465 PRO A 153
REMARK 465 GLU A 154
REMARK 465 SER A 155
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 SER B 5
REMARK 465 SER B 6
REMARK 465 ILE B 179
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 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 53 -159.34 -102.18
REMARK 500 SER A 122 -121.20 50.97
REMARK 500 SER A 146 68.73 39.42
REMARK 500 VAL A 170 -102.64 -70.93
REMARK 500 PRO A 225 -9.70 -57.97
REMARK 500 SER A 244 -39.44 -35.96
REMARK 500 TYR A 268 -154.93 -84.05
REMARK 500 LYS A 273 40.98 -143.91
REMARK 500 GLU A 274 -167.16 -102.99
REMARK 500 THR B 10 158.07 -47.90
REMARK 500 THR B 40 110.66 -37.31
REMARK 500 GLU B 53 -157.82 -113.81
REMARK 500 SER B 122 -121.97 62.11
REMARK 500 SER B 146 64.30 32.52
REMARK 500 SER B 155 32.40 -80.05
REMARK 500 TYR B 268 -147.99 -89.66
REMARK 500 LYS B 273 43.26 -140.83
REMARK 500 GLU B 274 -161.86 -104.23
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 XP7 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue XP7 B 401
DBREF1 7L4U A 0 303 UNP A0A0C4DFN3_HUMAN
DBREF2 7L4U A A0A0C4DFN3 10 313
DBREF1 7L4U B 0 303 UNP A0A0C4DFN3_HUMAN
DBREF2 7L4U B A0A0C4DFN3 10 313
SEQADV 7L4U MET A -16 UNP A0A0C4DFN INITIATING METHIONINE
SEQADV 7L4U HIS A -15 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U HIS A -14 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U HIS A -13 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U HIS A -12 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U HIS A -11 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U HIS A -10 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U GLY A -9 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U SER A -8 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U GLU A -7 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U ASN A -6 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U LEU A -5 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U TYR A -4 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U PHE A -3 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U GLN A -2 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U GLY A -1 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U ALA A 36 UNP A0A0C4DFN LYS 46 CONFLICT
SEQADV 7L4U SER A 169 UNP A0A0C4DFN LEU 179 CONFLICT
SEQADV 7L4U SER A 176 UNP A0A0C4DFN LEU 186 CONFLICT
SEQADV 7L4U MET B -16 UNP A0A0C4DFN INITIATING METHIONINE
SEQADV 7L4U HIS B -15 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U HIS B -14 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U HIS B -13 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U HIS B -12 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U HIS B -11 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U HIS B -10 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U GLY B -9 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U SER B -8 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U GLU B -7 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U ASN B -6 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U LEU B -5 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U TYR B -4 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U PHE B -3 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U GLN B -2 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U GLY B -1 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4U ALA B 36 UNP A0A0C4DFN LYS 46 CONFLICT
SEQADV 7L4U SER B 169 UNP A0A0C4DFN LEU 179 CONFLICT
SEQADV 7L4U 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 XP7 A 401 26
HET CL A 402 1
HET XP7 B 401 26
HETNAM XP7 (5S)-5-(3-{4-[(2-CHLORO-4-FLUOROPHENOXY)
HETNAM 2 XP7 METHYL]PIPERIDIN-1-YL}-3-OXOPROPYL)PYRROLIDIN-2-ONE
HETNAM CL CHLORIDE ION
FORMUL 3 XP7 2(C19 H24 CL F N2 O3)
FORMUL 4 CL CL 1-
FORMUL 6 HOH *159(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 THR A 158 ASN A 168 1 11
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 SER A 244 ALA A 254 1 11
HELIX 12 AB3 VAL A 270 GLU A 274 5 5
HELIX 13 AB4 LEU A 275 GLN A 292 1 18
HELIX 14 AB5 PRO B 15 LEU B 19 5 5
HELIX 15 AB6 HIS B 54 ARG B 57 5 4
HELIX 16 AB7 TYR B 58 GLY B 67 1 10
HELIX 17 AB8 PHE B 93 TYR B 111 1 19
HELIX 18 AB9 SER B 122 GLU B 134 1 13
HELIX 19 AC1 THR B 157 SER B 169 1 13
HELIX 20 AC2 ASN B 187 ASN B 195 1 9
HELIX 21 AC3 LYS B 206 LEU B 224 1 19
HELIX 22 AC4 PRO B 225 LEU B 227 5 3
HELIX 23 AC5 SER B 244 ALA B 254 1 11
HELIX 24 AC6 VAL B 270 GLU B 274 5 5
HELIX 25 AC7 LEU B 275 ARG B 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 ALA A 43 O LEU A 71
SHEET 5 AA1 8 VAL A 116 SER A 122 1 O PHE A 117 N LEU A 44
SHEET 6 AA1 8 GLY A 141 PRO A 147 1 O ILE A 145 N GLY A 120
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 ALA B 74 N ARG B 33
SHEET 4 AA2 8 ALA B 43 SER B 48 1 N VAL B 47 O PHE B 73
SHEET 5 AA2 8 VAL B 116 HIS B 121 1 O LEU B 119 N SER B 48
SHEET 6 AA2 8 GLY B 141 ILE B 145 1 O VAL B 143 N LEU B 118
SHEET 7 AA2 8 PHE B 231 GLY B 236 1 O LEU B 232 N LEU B 144
SHEET 8 AA2 8 LYS B 259 TYR B 264 1 O THR B 260 N LEU B 233
SITE 1 AC1 12 GLY A 50 ALA A 51 GLU A 53 ARG A 57
SITE 2 AC1 12 HIS A 121 SER A 122 MET A 123 TYR A 194
SITE 3 AC1 12 LEU A 205 GLY A 210 VAL A 270 HOH A 513
SITE 1 AC2 3 HIS A 94 LEU A 130 ARG A 219
SITE 1 AC3 13 GLY B 50 ALA B 51 GLU B 53 ARG B 57
SITE 2 AC3 13 HIS B 121 SER B 122 MET B 123 TYR B 194
SITE 3 AC3 13 LEU B 205 GLY B 210 HIS B 269 VAL B 270
SITE 4 AC3 13 HOH B 515
CRYST1 92.528 127.453 135.911 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 0.010808 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007846 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007358 0.00000
TER 2210 ALA A 295
TER 4445 THR B 294
MASTER 433 0 3 25 16 0 8 6 4646 2 52 50
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