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HEADER HYDROLASE 18-OCT-23 8QVF
TITLE COMPARISON OF ROOM-TEMPERATURE AND CRYOGENIC STRUCTURES OF SOLUBLE
TITLE 2 EPOXIDE HYDROLASE WITH LIGANDS BOUND.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A;
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: EPHX2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7106
KEYWDS INHIBITOR, SERIAL CRYSTALLOGRAPHY, DRUG DISCOVERY, FIXED TARGET, ROOM
KEYWDS 2 TEMPERATURE, MICROCRYSTALS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DUNGE,O.UWANGUE,C.PHAN,M.BJELCIC,J.GUNNARSSON,G.WEHLANDER,H.KACK,
AUTHOR 2 G.BRANDEN
REVDAT 1 14-AUG-24 8QVF 0
JRNL AUTH A.DUNGE,C.PHAN,O.UWANGUE,M.BJELCIC,J.GUNNARSSON,G.WEHLANDER,
JRNL AUTH 2 H.KACK,G.BRANDEN
JRNL TITL EXPLORING SERIAL CRYSTALLOGRAPHY FOR DRUG DISCOVERY.
JRNL REF IUCRJ 2024
JRNL REFN ESSN 2052-2525
JRNL PMID 39072424
JRNL DOI 10.1107/S2052252524006134
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 26621
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1338
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.42
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
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) : 0.3072
REMARK 3 BIN FREE R VALUE : 0.2893
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 32
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 : 4309
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.75650
REMARK 3 B22 (A**2) : -5.75650
REMARK 3 B33 (A**2) : 11.51310
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) : 0.290
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.338
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.220
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.316
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.218
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 : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4471 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6069 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1555 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 744 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4471 ; 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 : 565 ; 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 : 3169 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 0.94
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.08
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.91
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8QVF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-23.
REMARK 100 THE DEPOSITION ID IS D_1292133959.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-21
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX IV
REMARK 200 BEAMLINE : BIOMAX
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL
REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63304
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 44.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 15.44
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.4900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: RODS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 3350, 0.1M LI2SO4 AND 0.1M
REMARK 280 TRIS-HCL (PH 8.2), BATCH MODE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 162.86000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.43000
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 122.14500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.71500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 203.57500
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 162.86000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 81.43000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 40.71500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 122.14500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 203.57500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
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 BIOMT1 2 0.500000 0.866025 0.000000 -47.70500
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 82.62748
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -40.71500
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 GLY A 0
REMARK 465 MET A 1
REMARK 465 ASN A 548
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 GLU A 76 CG CD OE1 OE2
REMARK 470 LYS A 94 CG CD CE NZ
REMARK 470 PHE A 497 CG CD1 CD2 CE1 CE2 CZ
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 VAL A 13 -53.89 -129.29
REMARK 500 GLU A 269 -146.77 -114.49
REMARK 500 ASP A 335 -124.76 59.83
REMARK 500 ASN A 359 -43.94 71.70
REMARK 500 VAL A 498 -61.06 -100.87
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8QVF A 1 548 UNP P34913 HYES_HUMAN 1 548
SEQADV 8QVF GLY A 0 UNP P34913 EXPRESSION TAG
SEQRES 1 A 549 GLY MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY
SEQRES 2 A 549 VAL LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG
SEQRES 3 A 549 THR GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN
SEQRES 4 A 549 ASP ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR
SEQRES 5 A 549 ARG LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE
SEQRES 6 A 549 PRO LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR
SEQRES 7 A 549 ALA LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU
SEQRES 8 A 549 ILE PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG
SEQRES 9 A 549 PRO MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY
SEQRES 10 A 549 PHE THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP
SEQRES 11 A 549 ARG ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU
SEQRES 12 A 549 LEU LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN
SEQRES 13 A 549 VAL GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE
SEQRES 14 A 549 LEU LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL
SEQRES 15 A 549 PHE LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG
SEQRES 16 A 549 ASP LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP
SEQRES 17 A 549 THR ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN
SEQRES 18 A 549 LEU LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN
SEQRES 19 A 549 PRO SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO
SEQRES 20 A 549 ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO
SEQRES 21 A 549 ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR
SEQRES 22 A 549 SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY
SEQRES 23 A 549 TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU
SEQRES 24 A 549 SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU
SEQRES 25 A 549 VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU
SEQRES 26 A 549 GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY
SEQRES 27 A 549 GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU
SEQRES 28 A 549 ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE
SEQRES 29 A 549 PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS
SEQRES 30 A 549 ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU
SEQRES 31 A 549 PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER
SEQRES 32 A 549 ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER
SEQRES 33 A 549 VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU
SEQRES 34 A 549 PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET
SEQRES 35 A 549 VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE
SEQRES 36 A 549 LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG
SEQRES 37 A 549 ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU
SEQRES 38 A 549 GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA
SEQRES 39 A 549 GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS
SEQRES 40 A 549 MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE
SEQRES 41 A 549 GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR
SEQRES 42 A 549 GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP
SEQRES 43 A 549 ALA ARG ASN
HET XQ9 A 601 24
HETNAM XQ9 1-(1-ADAMANTYL)-3-(1-METHYLSULFONYLPIPERIDIN-4-YL)UREA
FORMUL 2 XQ9 C17 H29 N3 O3 S
FORMUL 3 HOH *98(H2 O)
HELIX 1 AA1 ALA A 18 LEU A 30 1 13
HELIX 2 AA2 GLY A 35 LYS A 43 1 9
HELIX 3 AA3 GLY A 44 GLU A 47 5 4
HELIX 4 AA4 GLY A 48 LYS A 55 1 8
HELIX 5 AA5 THR A 59 ALA A 78 1 20
HELIX 6 AA6 SER A 87 ARG A 99 1 13
HELIX 7 AA7 ASN A 102 LYS A 115 1 14
HELIX 8 AA8 ARG A 133 MET A 145 1 13
HELIX 9 AA9 SER A 153 GLY A 157 1 5
HELIX 10 AB1 GLU A 162 LYS A 174 1 13
HELIX 11 AB2 SER A 176 SER A 178 5 3
HELIX 12 AB3 ILE A 186 GLY A 197 1 12
HELIX 13 AB4 ASP A 205 GLY A 218 1 14
HELIX 14 AB5 ASN A 233 MET A 237 5 5
HELIX 15 AB6 SER A 270 ARG A 275 5 6
HELIX 16 AB7 GLN A 277 GLY A 285 1 9
HELIX 17 AB8 GLU A 304 TYR A 308 5 5
HELIX 18 AB9 CYS A 309 GLY A 325 1 17
HELIX 19 AC1 ASP A 335 TYR A 348 1 14
HELIX 20 AC2 SER A 370 ASN A 378 1 9
HELIX 21 AC3 PRO A 379 PHE A 381 5 3
HELIX 22 AC4 ASP A 382 PHE A 387 1 6
HELIX 23 AC5 GLY A 391 ASN A 400 1 10
HELIX 24 AC6 ASN A 400 PHE A 409 1 10
HELIX 25 AC7 LYS A 421 GLY A 426 1 6
HELIX 26 AC8 THR A 443 GLY A 458 1 16
HELIX 27 AC9 PHE A 459 TRP A 465 1 7
HELIX 28 AD1 ASN A 468 CYS A 477 1 10
HELIX 29 AD2 LYS A 478 LEU A 480 5 3
HELIX 30 AD3 VAL A 500 GLN A 505 5 6
HELIX 31 AD4 HIS A 506 TRP A 510 5 5
HELIX 32 AD5 TRP A 525 LYS A 530 1 6
HELIX 33 AD6 LYS A 530 ALA A 546 1 17
SHEET 1 AA1 5 PHE A 149 GLU A 152 0
SHEET 2 AA1 5 THR A 118 THR A 123 1 N ILE A 121 O ILE A 151
SHEET 3 AA1 5 ALA A 5 PHE A 8 1 N PHE A 8 O ALA A 120
SHEET 4 AA1 5 VAL A 180 ASP A 184 1 O VAL A 181 N VAL A 7
SHEET 5 AA1 5 VAL A 199 LEU A 202 1 O VAL A 199 N PHE A 182
SHEET 1 AA2 2 ALA A 15 LEU A 16 0
SHEET 2 AA2 2 LYS A 100 ILE A 101 -1 O LYS A 100 N LEU A 16
SHEET 1 AA3 8 SER A 238 LYS A 245 0
SHEET 2 AA3 8 VAL A 248 LEU A 255 -1 O PHE A 252 N GLY A 240
SHEET 3 AA3 8 ARG A 287 MET A 291 -1 O VAL A 288 N LEU A 255
SHEET 4 AA3 8 ALA A 260 CYS A 264 1 N VAL A 261 O ARG A 287
SHEET 5 AA3 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 AA3 8 VAL A 352 LEU A 358 1 O ALA A 354 N PHE A 331
SHEET 7 AA3 8 ALA A 488 ALA A 493 1 O VAL A 491 N SER A 357
SHEET 8 AA3 8 LYS A 515 ILE A 519 1 O LYS A 515 N ALA A 488
CISPEP 1 LEU A 16 PRO A 17 0 -0.71
CISPEP 2 LYS A 160 PRO A 161 0 9.66
CISPEP 3 PHE A 267 PRO A 268 0 -11.71
CRYST1 95.410 95.410 244.290 90.00 90.00 120.00 P 65 2 2 12
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 0.010481 0.006051 0.000000 0.00000
SCALE2 0.000000 0.012103 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004093 0.00000
TER 4338 ARG A 547
MASTER 292 0 1 33 15 0 0 6 4431 1 24 43
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