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HEADER HYDROLASE/INHIBITOR 21-DEC-20 7L4T
TITLE CRYSTAL STRUCTURE OF HUMAN MONOACYLGLYCEROL LIPASE IN COMPLEX WITH
TITLE 2 COMPOUND 1
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 7L4T 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) : 42.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 38667
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2012
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2790
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.3130
REMARK 3 BIN FREE R VALUE SET COUNT : 139
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4451
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 308
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.14000
REMARK 3 B22 (A**2) : -3.51000
REMARK 3 B33 (A**2) : 0.37000
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): 0.197
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.486
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4627 ; 0.006 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6289 ; 1.227 ; 1.638
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 576 ; 6.124 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 218 ;30.530 ;21.651
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 752 ;15.795 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ; 8.641 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 583 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3522 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 2501 A 2502
REMARK 3 ORIGIN FOR THE GROUP (A): -18.977 11.693 -49.794
REMARK 3 T TENSOR
REMARK 3 T11: 0.1465 T22: 0.0325
REMARK 3 T33: 0.1173 T12: -0.0148
REMARK 3 T13: 0.0342 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.1001 L22: 2.2942
REMARK 3 L33: 0.9124 L12: -0.1247
REMARK 3 L13: -0.2089 L23: 0.1574
REMARK 3 S TENSOR
REMARK 3 S11: -0.0000 S12: 0.0510 S13: 0.0640
REMARK 3 S21: -0.0475 S22: -0.0236 S23: -0.3425
REMARK 3 S31: 0.0968 S32: -0.1601 S33: 0.0237
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 7 B 294
REMARK 3 RESIDUE RANGE : B 401 B 405
REMARK 3 ORIGIN FOR THE GROUP (A): -25.261 -11.260 -18.101
REMARK 3 T TENSOR
REMARK 3 T11: 0.1161 T22: 0.1077
REMARK 3 T33: 0.2430 T12: 0.0172
REMARK 3 T13: -0.0227 T23: -0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 0.1122 L22: 1.9227
REMARK 3 L33: 0.1114 L12: 0.2782
REMARK 3 L13: -0.0518 L23: 0.0657
REMARK 3 S TENSOR
REMARK 3 S11: 0.0246 S12: -0.0507 S13: 0.0042
REMARK 3 S21: -0.0365 S22: -0.0714 S23: 0.5283
REMARK 3 S31: -0.0167 S32: 0.0983 S33: 0.0468
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: U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 7L4T 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_1000253715.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-15
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) : 0.987
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 : 40679
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) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.1000
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 (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.96800
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 (%): 56.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
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 45.90900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.68900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 68.04200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.90900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.68900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.04200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.90900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.68900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.04200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.90900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.68900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 68.04200
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 SER B 5
REMARK 465 SER B 6
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 165 CG CD CE NZ
REMARK 470 LYS A 226 CG CD CE NZ
REMARK 470 GLU B 60 CD OE1 OE2
REMARK 470 GLU B 277 CG CD OE1 OE2
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 -157.96 -96.84
REMARK 500 ASP A 69 27.29 80.16
REMARK 500 SER A 122 -123.40 62.50
REMARK 500 VAL A 149 -36.30 -130.90
REMARK 500 PRO A 225 -5.65 -56.41
REMARK 500 TYR A 268 -144.36 -88.62
REMARK 500 LYS A 273 42.44 -140.80
REMARK 500 GLU A 274 -163.23 -100.14
REMARK 500 PRO B 11 -17.39 -48.20
REMARK 500 GLU B 53 -158.74 -105.95
REMARK 500 SER B 122 -124.95 61.48
REMARK 500 SER B 146 65.96 33.34
REMARK 500 VAL B 149 -30.29 -138.11
REMARK 500 PRO B 225 3.44 -65.06
REMARK 500 TYR B 268 -148.92 -85.34
REMARK 500 LYS B 273 41.47 -140.18
REMARK 500 GLU B 274 -161.29 -101.82
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 B 666 DISTANCE = 6.17 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue XPD A 2501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 2502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 405
DBREF1 7L4T A 0 303 UNP A0A0C4DFN3_HUMAN
DBREF2 7L4T A A0A0C4DFN3 10 313
DBREF1 7L4T B 0 303 UNP A0A0C4DFN3_HUMAN
DBREF2 7L4T B A0A0C4DFN3 10 313
SEQADV 7L4T MET A -16 UNP A0A0C4DFN INITIATING METHIONINE
SEQADV 7L4T HIS A -15 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T HIS A -14 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T HIS A -13 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T HIS A -12 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T HIS A -11 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T HIS A -10 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T GLY A -9 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T SER A -8 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T GLU A -7 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T ASN A -6 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T LEU A -5 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T TYR A -4 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T PHE A -3 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T GLN A -2 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T GLY A -1 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T ALA A 36 UNP A0A0C4DFN LYS 46 CONFLICT
SEQADV 7L4T SER A 169 UNP A0A0C4DFN LEU 179 CONFLICT
SEQADV 7L4T SER A 176 UNP A0A0C4DFN LEU 186 CONFLICT
SEQADV 7L4T MET B -16 UNP A0A0C4DFN INITIATING METHIONINE
SEQADV 7L4T HIS B -15 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T HIS B -14 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T HIS B -13 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T HIS B -12 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T HIS B -11 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T HIS B -10 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T GLY B -9 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T SER B -8 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T GLU B -7 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T ASN B -6 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T LEU B -5 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T TYR B -4 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T PHE B -3 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T GLN B -2 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T GLY B -1 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L4T ALA B 36 UNP A0A0C4DFN LYS 46 CONFLICT
SEQADV 7L4T SER B 169 UNP A0A0C4DFN LEU 179 CONFLICT
SEQADV 7L4T 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 XPD A2501 29
HET ACT A2502 4
HET MPD B 401 8
HET MPD B 402 8
HET MPD B 403 8
HET MPD B 404 8
HET ACT B 405 4
HETNAM XPD 6-{4-[(2-CHLORO-4-FLUOROPHENOXY)METHYL]PIPERIDINE-1-
HETNAM 2 XPD CARBONYL}-2H-1,4-BENZOXAZIN-3(4H)-ONE
HETNAM ACT ACETATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 3 XPD C21 H20 CL F N2 O4
FORMUL 4 ACT 2(C2 H3 O2 1-)
FORMUL 5 MPD 4(C6 H14 O2)
FORMUL 10 HOH *308(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 SER A 122 ARG A 135 1 14
HELIX 6 AA6 THR A 157 LEU A 171 1 15
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 THR A 294 1 20
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 ARG B 135 1 14
HELIX 19 AC1 THR B 157 SER B 169 1 13
HELIX 20 AC2 ASP B 180 LEU B 184 5 5
HELIX 21 AC3 ASN B 187 ASN B 195 1 9
HELIX 22 AC4 LYS B 206 LEU B 224 1 19
HELIX 23 AC5 PRO B 225 LEU B 227 5 3
HELIX 24 AC6 ASP B 243 ALA B 254 1 12
HELIX 25 AC7 VAL B 270 GLU B 274 5 5
HELIX 26 AC8 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 ALA A 74 N ARG A 33
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 HIS A 121 1 O LEU A 119 N SER A 48
SHEET 6 AA1 8 GLY A 141 ILE A 145 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 VAL B 72 N TRP B 35
SHEET 4 AA2 8 ALA B 43 SER B 48 1 N ILE B 45 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 ALA A 51 GLU A 53 ARG A 57 HIS A 121
SITE 2 AC1 12 SER A 122 MET A 123 LEU A 184 TYR A 194
SITE 3 AC1 12 LEU A 205 LEU A 214 HIS A 269 VAL A 270
SITE 1 AC2 1 TYR A 111
SITE 1 AC3 4 LEU B 241 MPD B 402 MPD B 403 HOH B 528
SITE 1 AC4 7 ALA B 151 ASN B 152 SER B 155 LEU B 205
SITE 2 AC4 7 GLY B 210 MPD B 401 HOH B 608
SITE 1 AC5 9 GLY B 50 ALA B 51 GLU B 53 HIS B 121
SITE 2 AC5 9 TYR B 194 VAL B 270 MPD B 401 HOH B 541
SITE 3 AC5 9 HOH B 565
SITE 1 AC6 3 GLN A 102 HOH B 503 HOH B 530
SITE 1 AC7 1 TYR B 111
CRYST1 91.818 127.378 136.084 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 0.010891 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007851 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007348 0.00000
TER 2226 THR A 294
TER 4456 THR B 294
MASTER 455 0 7 26 16 0 12 6 4828 2 69 50
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