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HEADER HYDROLASE/HYDROLASE INHIBITOR 15-MAR-13 4JNC
TITLE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH A CARBOXAMIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: CYTOSOLIC EPOXIDE HYDROLASE 2, CEH, EPOXIDE HYDRATASE,
COMPND 6 SOLUBLE EPOXIDE HYDROLASE, SEH, LIPID-PHOSPHATE PHOSPHATASE;
COMPND 7 EC: 3.3.2.10, 3.1.3.76;
COMPND 8 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: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS EPOXIDE HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.SHEWCHUK
REVDAT 1 05-JUN-13 4JNC 0
JRNL AUTH R.K.THALJI,J.J.MCATEE,S.BELYANSKAYA,M.BRANDT,G.D.BROWN,
JRNL AUTH 2 M.H.COSTELL,Y.DING,J.W.DODSON,S.H.EISENNAGEL,R.E.FRIES,
JRNL AUTH 3 J.W.GROSS,M.R.HARPEL,D.A.HOLT,D.I.ISRAEL,L.J.JOLIVETTE,
JRNL AUTH 4 D.KROSKY,H.LI,Q.LU,T.MANDICHAK,T.ROETHKE,C.G.SCHNACKENBERG,
JRNL AUTH 5 B.SCHWARTZ,L.M.SHEWCHUK,W.XIE,D.J.BEHM,S.A.DOUGLAS,A.L.SHAW,
JRNL AUTH 6 J.P.MARINO
JRNL TITL DISCOVERY OF 1-(1,3,5-TRIAZIN-2-YL)PIPERIDINE-4-CARBOXAMIDES
JRNL TITL 2 AS INHIBITORS OF SOLUBLE EPOXIDE HYDROLASE.
JRNL REF BIOORG.MED.CHEM.LETT. V. 23 3584 2013
JRNL REFN ISSN 0960-894X
JRNL PMID 23664879
JRNL DOI 10.1016/J.BMCL.2013.04.019
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 23361
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) : 0.187
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1254
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) : 1.96
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1493
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.3040
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2478
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 238
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.18000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : 0.29000
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): 0.179
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.092
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.002
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2635 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3595 ; 0.970 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 329 ; 5.181 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 117 ;32.797 ;24.017
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 432 ;11.851 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;13.461 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 375 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2033 ; 0.004 ; 0.021
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): 1586 ; 0.282 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2561 ; 0.540 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1049 ; 0.774 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1025 ; 1.311 ; 4.500
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 : 1
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 237 A 548
REMARK 3 RESIDUE RANGE : A 701 A 938
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3060 19.0320 -15.3560
REMARK 3 T TENSOR
REMARK 3 T11: 0.0222 T22: 0.0360
REMARK 3 T33: 0.0537 T12: 0.0088
REMARK 3 T13: -0.0056 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.8682 L22: 0.6488
REMARK 3 L33: 1.0977 L12: 0.0061
REMARK 3 L13: -0.0822 L23: 0.0561
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: -0.0210 S13: 0.0620
REMARK 3 S21: 0.0229 S22: 0.0046 S23: 0.0304
REMARK 3 S31: -0.1157 S32: -0.0280 S33: 0.0053
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4JNC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-13.
REMARK 100 THE RCSB ID CODE IS RCSB078262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23361
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 60.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 33.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.19000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1VJ5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1 M BISTRIS, 0.2M
REMARK 280 NH4OAC, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 40.14250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.97550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.14250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.97550
REMARK 290 SMTRY3 4 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 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 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 PRO A 549
REMARK 465 ALA A 550
REMARK 465 ASP A 551
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 ARG A 247 NE CZ NH1 NH2
REMARK 470 ARG A 353 CZ NH1 NH2
REMARK 470 LYS A 376 CG CD CE NZ
REMARK 470 ASN A 378 CG OD1 ND2
REMARK 470 SER A 418 OG
REMARK 470 LYS A 421 CG CD CE NZ
REMARK 470 GLU A 424 CG CD OE1 OE2
REMARK 470 LYS A 456 CG CD CE NZ
REMARK 470 SER A 457 OG
REMARK 470 GLN A 502 CD OE1 NE2
REMARK 470 ARG A 547 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 548 CG OD1 ND2
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 269 -143.87 -119.64
REMARK 500 ASP A 335 -126.53 62.29
REMARK 500 ASN A 359 -43.56 78.23
REMARK 500 VAL A 498 -60.88 -104.15
REMARK 500 SER A 544 -89.57 -122.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET A 291 ASP A 292 146.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1LF A 601
DBREF 4JNC A 238 549 UNP P34913 HYES_HUMAN 238 549
SEQADV 4JNC GLY A 237 UNP P34913 EXPRESSION TAG
SEQADV 4JNC ALA A 550 UNP P34913 EXPRESSION TAG
SEQADV 4JNC ASP A 551 UNP P34913 EXPRESSION TAG
SEQRES 1 A 315 GLY SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG
SEQRES 2 A 315 LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS
SEQRES 3 A 315 LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG
SEQRES 4 A 315 TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL
SEQRES 5 A 315 LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA
SEQRES 6 A 315 PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS
SEQRES 7 A 315 LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER
SEQRES 8 A 315 GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU
SEQRES 9 A 315 VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG
SEQRES 10 A 315 ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN
SEQRES 11 A 315 PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO
SEQRES 12 A 315 VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL
SEQRES 13 A 315 ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE
SEQRES 14 A 315 LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER
SEQRES 15 A 315 MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN
SEQRES 16 A 315 SER PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU
SEQRES 17 A 315 GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER
SEQRES 18 A 315 GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU
SEQRES 19 A 315 ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS
SEQRES 20 A 315 ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP
SEQRES 21 A 315 PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP
SEQRES 22 A 315 TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS
SEQRES 23 A 315 GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN
SEQRES 24 A 315 GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN
SEQRES 25 A 315 PRO ALA ASP
HET 1LF A 601 29
HETNAM 1LF 1-[4-METHYL-6-(METHYLAMINO)-1,3,5-TRIAZIN-2-YL]-N-[2-
HETNAM 2 1LF (TRIFLUOROMETHYL)BENZYL]PIPERIDINE-4-CARBOXAMIDE
FORMUL 2 1LF C19 H23 F3 N6 O
FORMUL 3 HOH *238(H2 O)
HELIX 1 1 SER A 270 ARG A 275 5 6
HELIX 2 2 TYR A 276 ALA A 284 1 9
HELIX 3 3 GLU A 304 TYR A 308 5 5
HELIX 4 4 CYS A 309 GLY A 325 1 17
HELIX 5 5 ASP A 335 TYR A 348 1 14
HELIX 6 6 SER A 370 LYS A 376 1 7
HELIX 7 7 ASN A 378 PHE A 381 5 4
HELIX 8 8 ASP A 382 PHE A 387 1 6
HELIX 9 9 GLY A 391 ASN A 400 1 10
HELIX 10 10 ASN A 400 PHE A 409 1 10
HELIX 11 11 ALA A 411 SER A 415 5 5
HELIX 12 12 SER A 418 HIS A 420 5 3
HELIX 13 13 LYS A 421 GLY A 426 1 6
HELIX 14 14 THR A 443 LYS A 456 1 14
HELIX 15 15 PHE A 459 TRP A 465 1 7
HELIX 16 16 ASN A 468 LYS A 478 1 11
HELIX 17 17 VAL A 500 GLN A 505 5 6
HELIX 18 18 HIS A 506 TRP A 510 5 5
HELIX 19 19 TRP A 525 LYS A 530 1 6
HELIX 20 20 LYS A 530 ASP A 543 1 14
SHEET 1 A 8 SER A 238 LYS A 245 0
SHEET 2 A 8 VAL A 248 LEU A 255 -1 O PHE A 252 N GLY A 240
SHEET 3 A 8 ARG A 287 MET A 291 -1 O VAL A 288 N LEU A 255
SHEET 4 A 8 ALA A 260 CYS A 264 1 N VAL A 261 O LEU A 289
SHEET 5 A 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 A 8 VAL A 352 LEU A 358 1 O LEU A 358 N GLY A 333
SHEET 7 A 8 ALA A 488 ALA A 493 1 O VAL A 491 N SER A 357
SHEET 8 A 8 LYS A 515 ILE A 519 1 O LYS A 515 N ALA A 488
CISPEP 1 PHE A 267 PRO A 268 0 -9.14
SITE 1 AC1 13 PHE A 267 ASP A 335 TRP A 336 MET A 339
SITE 2 AC1 13 PHE A 381 TYR A 383 LEU A 408 MET A 419
SITE 3 AC1 13 TYR A 466 LEU A 499 HIS A 524 TRP A 525
SITE 4 AC1 13 HOH A 760
CRYST1 80.285 91.951 45.870 90.00 90.00 90.00 P 21 21 2 4
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 0.012456 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010875 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021801 0.00000
TER 2521 ASN A 548
MASTER 316 0 1 20 8 0 4 6 2745 1 29 25
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