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HEADER HYDROLASE 14-JUL-23 8PTQ
TITLE COMPLEX CRYSTAL STRUCTURE OF MUTANT HUMAN MONOGLYCERIDE LIPASE WITH
TITLE 2 COMPOUND 5L
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOGLYCERIDE LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MGL,HU-K5,LYSOPHOSPHOLIPASE HOMOLOG,LYSOPHOSPHOLIPASE-LIKE,
COMPND 5 MONOACYLGLYCEROL LIPASE,MAGL;
COMPND 6 EC: 3.1.1.23;
COMPND 7 ENGINEERED: YES
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 ALPHA/BETA HYDROLASE, HYDROLASE, SERINE ESTERASE;
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BUTINI,U.GRETHER,J.BENZ,L.LEIBROCK,S.MARAMAI,A.PAPA,G.CARULLO,
AUTHOR 2 S.FEDERICO,A.GRILLO,B.DI GUGLIELMO,S.LAMPONI,S.GEMMA,G.CAMPIANI
REVDAT 1 31-JAN-24 8PTQ 0
JRNL AUTH S.BUTINI,U.GRETHER,K.M.JUNG,A.LIGRESTI,M.ALLARA,
JRNL AUTH 2 A.G.J.POSTMUS,S.MARAMAI,S.BROGI,A.PAPA,G.CARULLO,D.SYKES,
JRNL AUTH 3 D.VEPRINTSEV,S.FEDERICO,A.GRILLO,B.DI GUGLIELMO,A.RAMUNNO,
JRNL AUTH 4 A.F.STEVENS,D.HEER,S.LAMPONI,S.GEMMA,J.BENZ,V.DI MARZO,
JRNL AUTH 5 M.VAN DER STELT,D.PIOMELLI,G.CAMPIANI
JRNL TITL DEVELOPMENT OF POTENT AND SELECTIVE MONOACYLGLYCEROL LIPASE
JRNL TITL 2 INHIBITORS. SARS, STRUCTURAL ANALYSIS, AND BIOLOGICAL
JRNL TITL 3 CHARACTERIZATION.
JRNL REF J.MED.CHEM. 2024
JRNL REFN ISSN 0022-2623
JRNL PMID 38241614
JRNL DOI 10.1021/ACS.JMEDCHEM.3C01278
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.8
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 50664
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2694
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.56
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4383
REMARK 3 BIN FREE R VALUE : 0.3940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 58
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2172
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.17610
REMARK 3 B22 (A**2) : 4.77670
REMARK 3 B33 (A**2) : 1.39950
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.250
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.078
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.080
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.075
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.078
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2328 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3175 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 819 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 402 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2328 ; 10.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 296 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2363 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.49
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.44
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1697 -20.0468 -0.5162
REMARK 3 T TENSOR
REMARK 3 T11: 0.0735 T22: -0.075
REMARK 3 T33: -0.0308 T12: -0.0059
REMARK 3 T13: -0.0052 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0 L22: 1.4653
REMARK 3 L33: 0.5621 L12: -0.3085
REMARK 3 L13: -0.0915 L23: -0.1024
REMARK 3 S TENSOR
REMARK 3 S11: -0.003 S12: -0.0303 S13: 0.0348
REMARK 3 S21: -0.0303 S22: -0.0394 S23: 0.007
REMARK 3 S31: 0.0348 S32: 0.007 S33: 0.0425
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8PTQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUL-23.
REMARK 100 THE DEPOSITION ID IS D_1292131958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-19
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50732
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 46.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.550
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.4900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.98000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5, 6 TO 13% PEG MME 5K,
REMARK 280 12% ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.13550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.13550
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 45.47900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.22400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.47900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.22400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 30.13550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.47900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.22400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 30.13550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.47900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.22400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 608 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER 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 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY 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 LEU A 167
REMARK 465 ASN A 168
REMARK 465 SER A 169
REMARK 465 VAL A 170
REMARK 465 LEU A 171
REMARK 465 PRO A 172
REMARK 465 ASN A 173
REMARK 465 LEU A 174
REMARK 465 SER A 175
REMARK 465 SER A 176
REMARK 465 THR A 296
REMARK 465 ALA A 297
REMARK 465 GLY A 298
REMARK 465 THR A 299
REMARK 465 ALA A 300
REMARK 465 SER A 301
REMARK 465 PRO A 302
REMARK 465 PRO A 303
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 13 13.07 82.43
REMARK 500 SER A 13 15.58 80.82
REMARK 500 GLU A 53 -157.37 -107.53
REMARK 500 SER A 122 -122.42 53.69
REMARK 500 TYR A 268 -148.74 -88.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 742 DISTANCE = 6.61 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8PTC RELATED DB: PDB
DBREF 8PTQ A 1 303 UNP Q99685 MGLL_HUMAN 1 303
SEQADV 8PTQ MET A -19 UNP Q99685 INITIATING METHIONINE
SEQADV 8PTQ GLY A -18 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ SER A -17 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ SER A -16 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ HIS A -15 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ HIS A -14 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ HIS A -13 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ HIS A -12 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ HIS A -11 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ HIS A -10 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ SER A -9 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ SER A -8 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ GLY A -7 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ GLU A -6 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ ASN A -5 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ LEU A -4 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ TYR A -3 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ PHE A -2 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ GLN A -1 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ GLY A 0 UNP Q99685 EXPRESSION TAG
SEQADV 8PTQ ALA A 36 UNP Q99685 LYS 36 ENGINEERED MUTATION
SEQADV 8PTQ SER A 169 UNP Q99685 LEU 169 ENGINEERED MUTATION
SEQADV 8PTQ SER A 176 UNP Q99685 LEU 176 ENGINEERED MUTATION
SEQRES 1 A 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 323 GLU ASN LEU TYR PHE GLN GLY MET PRO GLU GLU SER SER
SEQRES 3 A 323 PRO ARG ARG THR PRO GLN SER ILE PRO TYR GLN ASP LEU
SEQRES 4 A 323 PRO HIS LEU VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS
SEQRES 5 A 323 ARG TYR TRP ALA PRO THR GLY THR PRO LYS ALA LEU ILE
SEQRES 6 A 323 PHE VAL SER HIS GLY ALA GLY GLU HIS SER GLY ARG TYR
SEQRES 7 A 323 GLU GLU LEU ALA ARG MET LEU MET GLY LEU ASP LEU LEU
SEQRES 8 A 323 VAL PHE ALA HIS ASP HIS VAL GLY HIS GLY GLN SER GLU
SEQRES 9 A 323 GLY GLU ARG MET VAL VAL SER ASP PHE HIS VAL PHE VAL
SEQRES 10 A 323 ARG ASP VAL LEU GLN HIS VAL ASP SER MET GLN LYS ASP
SEQRES 11 A 323 TYR PRO GLY LEU PRO VAL PHE LEU LEU GLY HIS SER MET
SEQRES 12 A 323 GLY GLY ALA ILE ALA ILE LEU THR ALA ALA GLU ARG PRO
SEQRES 13 A 323 GLY HIS PHE ALA GLY MET VAL LEU ILE SER PRO LEU VAL
SEQRES 14 A 323 LEU ALA ASN PRO GLU SER ALA THR THR PHE LYS VAL LEU
SEQRES 15 A 323 ALA ALA LYS VAL LEU ASN SER VAL LEU PRO ASN LEU SER
SEQRES 16 A 323 SER GLY PRO ILE ASP SER SER VAL LEU SER ARG ASN LYS
SEQRES 17 A 323 THR GLU VAL ASP ILE TYR ASN SER ASP PRO LEU ILE CYS
SEQRES 18 A 323 ARG ALA GLY LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU
SEQRES 19 A 323 ASN ALA VAL SER ARG VAL GLU ARG ALA LEU PRO LYS LEU
SEQRES 20 A 323 THR VAL PRO PHE LEU LEU LEU GLN GLY SER ALA ASP ARG
SEQRES 21 A 323 LEU CYS ASP SER LYS GLY ALA TYR LEU LEU MET GLU LEU
SEQRES 22 A 323 ALA LYS SER GLN ASP LYS THR LEU LYS ILE TYR GLU GLY
SEQRES 23 A 323 ALA TYR HIS VAL LEU HIS LYS GLU LEU PRO GLU VAL THR
SEQRES 24 A 323 ASN SER VAL PHE HIS GLU ILE ASN MET TRP VAL SER GLN
SEQRES 25 A 323 ARG THR ALA THR ALA GLY THR ALA SER PRO PRO
HET EJI A 401 30
HET EDO A 402 4
HET EDO A 403 4
HETNAM EJI METHYL 4-[(2~{S},3~{R})-3-(4-FLUOROPHENYL)-1-(1-
HETNAM 2 EJI METHANOYLPIPERIDIN-4-YL)-4-OXIDANYLIDENE-AZETIDIN-2-
HETNAM 3 EJI YL]BENZOATE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EJI C23 H23 F N2 O4
FORMUL 3 EDO 2(C2 H6 O2)
FORMUL 5 HOH *242(H2 O)
HELIX 1 AA1 PRO A 15 LEU A 19 5 5
HELIX 2 AA2 HIS A 54 ARG A 57 5 4
HELIX 3 AA3 TYR A 58 LEU A 68 1 11
HELIX 4 AA4 PHE A 93 TYR A 111 1 19
HELIX 5 AA5 MET A 123 ARG A 135 1 13
HELIX 6 AA6 ASN A 152 ALA A 164 1 13
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 ALA A 295 1 21
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 ILE A 145 N GLY A 120
SHEET 7 AA1 8 PHE A 231 GLY A 236 1 O LEU A 234 N SER A 146
SHEET 8 AA1 8 LYS A 259 TYR A 264 1 O THR A 260 N LEU A 233
LINK OG SER A 122 C16 EJI A 401 1555 1555 1.41
CRYST1 90.958 126.448 60.271 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010994 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007908 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016592 0.00000
TER 2225 ALA A 295
MASTER 339 0 3 13 8 0 0 6 2452 1 39 25
END |