longtext: 7l4t-pdb

content
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
END