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HEADER HYDROLASE/HYDROLASE INHIBITOR 08-SEP-10 3ANT
TITLE HUMAN SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH A SYNTHETIC INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HYDROLASE DOMAIN, UNP RESIDUES 230-555;
COMPND 5 SYNONYM: SOLUBLE EPOXIDE HYDROLASE, SEH, EPOXIDE HYDRATASE, CYTOSOLIC
COMPND 6 EPOXIDE HYDROLASE, CEH;
COMPND 7 EC: 3.3.2.10;
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: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.CHIYO,T.ISHII,S.HOURAI,K.YANAGI
REVDAT 1 19-JAN-11 3ANT 0
JRNL AUTH D.TANAKA,Y.TSUDA,T.SHIYAMA,T.NISHIMURA,N.CHIYO,Y.TOMINAGA,
JRNL AUTH 2 N.SAWADA,T.MIMOTO,N.KUSUNOSE
JRNL TITL A PRACTICAL USE OF LIGAND EFFICIENCY INDICES OUT OF THE
JRNL TITL 2 FRAGMENT-BASED APPROACH: LIGAND EFFICIENCY-GUIDED LEAD
JRNL TITL 3 IDENTIFICATION OF SOLUBLE EPOXIDE HYDROLASE INHIBITORS
JRNL REF J.MED.CHEM. 2010
JRNL REFN ISSN 0022-2623
JRNL PMID 21192659
JRNL DOI 10.1021/JM101273E
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 28433
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1439
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.47
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1792
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 108
REMARK 3 BIN FREE R VALUE : 0.2570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5066
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 121
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.257
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.180
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.610
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5276 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7160 ; 1.204 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 626 ; 5.603 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 244 ;35.819 ;23.934
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 880 ;15.335 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;12.905 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 732 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4100 ; 0.005 ; 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): 3142 ; 0.604 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5078 ; 1.164 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2134 ; 1.522 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2076 ; 2.594 ; 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 : NULL
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 U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3ANT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB029477.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28466
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.4000
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) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.17900
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3ANS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG 8000, 200MM SODIUM
REMARK 280 IODIDE, PH 7.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 64.69200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.14800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.69200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.14800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
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: 3
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 220
REMARK 465 LYS A 221
REMARK 465 LYS A 222
REMARK 465 GLY A 223
REMARK 465 HIS A 224
REMARK 465 HIS A 225
REMARK 465 HIS A 226
REMARK 465 HIS A 227
REMARK 465 HIS A 228
REMARK 465 HIS A 229
REMARK 465 THR A 230
REMARK 465 SER A 231
REMARK 465 ALA A 546
REMARK 465 ARG A 547
REMARK 465 ASN A 548
REMARK 465 PRO A 549
REMARK 465 PRO A 550
REMARK 465 VAL A 551
REMARK 465 VAL A 552
REMARK 465 SER A 553
REMARK 465 LYS A 554
REMARK 465 MET A 555
REMARK 465 MET B 220
REMARK 465 LYS B 221
REMARK 465 LYS B 222
REMARK 465 GLY B 223
REMARK 465 HIS B 224
REMARK 465 HIS B 225
REMARK 465 HIS B 226
REMARK 465 HIS B 227
REMARK 465 HIS B 228
REMARK 465 HIS B 229
REMARK 465 THR B 230
REMARK 465 SER B 231
REMARK 465 ALA B 546
REMARK 465 ARG B 547
REMARK 465 ASN B 548
REMARK 465 PRO B 549
REMARK 465 PRO B 550
REMARK 465 VAL B 551
REMARK 465 VAL B 552
REMARK 465 SER B 553
REMARK 465 LYS B 554
REMARK 465 MET B 555
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 -139.20 -112.13
REMARK 500 ASP A 335 -130.28 62.51
REMARK 500 ASN A 359 -44.16 80.51
REMARK 500 GLU A 435 76.41 -117.64
REMARK 500 GLU B 269 -149.91 -117.48
REMARK 500 ASP B 335 -127.65 61.05
REMARK 500 ASN B 359 -48.06 74.11
REMARK 500 LEU B 499 74.19 -101.14
REMARK 500 HIS B 513 38.24 -92.06
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 292 147.50
REMARK 500 MET B 291 ASP B 292 148.92
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 S82 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S82 B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ANS RELATED DB: PDB
DBREF 3ANT A 230 555 UNP P34913 HYES_HUMAN 230 555
DBREF 3ANT B 230 555 UNP P34913 HYES_HUMAN 230 555
SEQADV 3ANT MET A 220 UNP P34913 EXPRESSION TAG
SEQADV 3ANT LYS A 221 UNP P34913 EXPRESSION TAG
SEQADV 3ANT LYS A 222 UNP P34913 EXPRESSION TAG
SEQADV 3ANT GLY A 223 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS A 224 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS A 225 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS A 226 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS A 227 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS A 228 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS A 229 UNP P34913 EXPRESSION TAG
SEQADV 3ANT MET B 220 UNP P34913 EXPRESSION TAG
SEQADV 3ANT LYS B 221 UNP P34913 EXPRESSION TAG
SEQADV 3ANT LYS B 222 UNP P34913 EXPRESSION TAG
SEQADV 3ANT GLY B 223 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS B 224 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS B 225 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS B 226 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS B 227 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS B 228 UNP P34913 EXPRESSION TAG
SEQADV 3ANT HIS B 229 UNP P34913 EXPRESSION TAG
SEQRES 1 A 336 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS THR SER CYS
SEQRES 2 A 336 ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL LYS
SEQRES 3 A 336 PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY
SEQRES 4 A 336 PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP
SEQRES 5 A 336 TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA
SEQRES 6 A 336 GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY
SEQRES 7 A 336 GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET
SEQRES 8 A 336 GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS
SEQRES 9 A 336 LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP
SEQRES 10 A 336 GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO
SEQRES 11 A 336 GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE
SEQRES 12 A 336 ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE
SEQRES 13 A 336 LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN
SEQRES 14 A 336 GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU
SEQRES 15 A 336 SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU
SEQRES 16 A 336 SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY
SEQRES 17 A 336 LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG
SEQRES 18 A 336 MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN
SEQRES 19 A 336 PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR
SEQRES 20 A 336 ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER
SEQRES 21 A 336 LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR
SEQRES 22 A 336 ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN
SEQRES 23 A 336 HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS
SEQRES 24 A 336 ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO
SEQRES 25 A 336 THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER
SEQRES 26 A 336 ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET
SEQRES 1 B 336 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS THR SER CYS
SEQRES 2 B 336 ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL LYS
SEQRES 3 B 336 PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY
SEQRES 4 B 336 PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP
SEQRES 5 B 336 TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA
SEQRES 6 B 336 GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY
SEQRES 7 B 336 GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET
SEQRES 8 B 336 GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS
SEQRES 9 B 336 LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP
SEQRES 10 B 336 GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO
SEQRES 11 B 336 GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE
SEQRES 12 B 336 ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE
SEQRES 13 B 336 LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN
SEQRES 14 B 336 GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU
SEQRES 15 B 336 SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU
SEQRES 16 B 336 SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY
SEQRES 17 B 336 LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG
SEQRES 18 B 336 MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN
SEQRES 19 B 336 PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR
SEQRES 20 B 336 ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER
SEQRES 21 B 336 LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR
SEQRES 22 B 336 ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN
SEQRES 23 B 336 HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS
SEQRES 24 B 336 ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO
SEQRES 25 B 336 THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER
SEQRES 26 B 336 ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET
HET S82 A 601 26
HET S82 B 602 26
HETNAM S82 4-[3-(1-METHYLETHYL)-1,2,4-OXADIAZOL-5-YL]-N-[(1S,2R)-
HETNAM 2 S82 2-PHENYLCYCLOPROPYL]PIPERIDINE-1-CARBOXAMIDE
FORMUL 3 S82 2(C20 H26 N4 O2)
FORMUL 5 HOH *121(H2 O)
HELIX 1 1 ASN A 233 MET A 237 5 5
HELIX 2 2 SER A 270 ARG A 275 5 6
HELIX 3 3 TYR A 276 ALA A 284 1 9
HELIX 4 4 GLU A 304 TYR A 308 5 5
HELIX 5 5 CYS A 309 LEU A 324 1 16
HELIX 6 6 ASP A 335 TYR A 348 1 14
HELIX 7 7 SER A 370 LYS A 376 1 7
HELIX 8 8 ALA A 377 PHE A 381 5 5
HELIX 9 9 ASP A 382 PHE A 387 1 6
HELIX 10 10 GLY A 391 GLU A 398 1 8
HELIX 11 11 ASN A 400 PHE A 409 1 10
HELIX 12 12 ALA A 411 SER A 415 5 5
HELIX 13 13 THR A 443 LYS A 455 1 13
HELIX 14 14 PHE A 459 TRP A 465 1 7
HELIX 15 15 ASN A 468 LYS A 478 1 11
HELIX 16 16 VAL A 500 GLN A 505 5 6
HELIX 17 17 HIS A 506 TRP A 510 5 5
HELIX 18 18 TRP A 525 LYS A 530 1 6
HELIX 19 19 LYS A 530 ASP A 545 1 16
HELIX 20 20 ASN B 233 MET B 237 5 5
HELIX 21 21 SER B 270 ARG B 275 5 6
HELIX 22 22 TYR B 276 ALA B 284 1 9
HELIX 23 23 GLU B 304 TYR B 308 5 5
HELIX 24 24 CYS B 309 GLY B 325 1 17
HELIX 25 25 ASP B 335 TYR B 348 1 14
HELIX 26 26 SER B 370 ASN B 378 1 9
HELIX 27 27 PRO B 379 PHE B 381 5 3
HELIX 28 28 ASP B 382 PHE B 387 1 6
HELIX 29 29 GLY B 391 ASN B 400 1 10
HELIX 30 30 ASN B 400 PHE B 409 1 10
HELIX 31 31 ALA B 411 SER B 415 5 5
HELIX 32 32 THR B 443 LYS B 455 1 13
HELIX 33 33 PHE B 459 TRP B 465 1 7
HELIX 34 34 ASN B 468 LYS B 478 1 11
HELIX 35 35 VAL B 500 GLN B 505 5 6
HELIX 36 36 HIS B 506 TRP B 510 5 5
HELIX 37 37 TRP B 525 LYS B 530 1 6
HELIX 38 38 LYS B 530 ASP B 545 1 16
SHEET 1 A16 LYS A 515 ILE A 519 0
SHEET 2 A16 ALA A 488 ALA A 493 1 N THR A 492 O ILE A 519
SHEET 3 A16 VAL A 352 LEU A 358 1 N SER A 357 O VAL A 491
SHEET 4 A16 ALA A 329 HIS A 334 1 N GLY A 333 O LEU A 358
SHEET 5 A16 ALA A 260 CYS A 264 1 N CYS A 262 O VAL A 330
SHEET 6 A16 ARG A 287 MET A 291 1 O ARG A 287 N VAL A 261
SHEET 7 A16 VAL A 248 LEU A 255 -1 N LEU A 255 O VAL A 288
SHEET 8 A16 SER A 238 LYS A 245 -1 N GLY A 240 O PHE A 252
SHEET 9 A16 SER B 238 LYS B 245 -1 O TYR B 241 N HIS A 239
SHEET 10 A16 VAL B 248 LEU B 255 -1 O PHE B 252 N GLY B 240
SHEET 11 A16 ARG B 287 MET B 291 -1 O VAL B 288 N LEU B 255
SHEET 12 A16 ALA B 260 CYS B 264 1 N VAL B 261 O LEU B 289
SHEET 13 A16 ALA B 329 HIS B 334 1 O VAL B 330 N CYS B 262
SHEET 14 A16 VAL B 352 LEU B 358 1 O ALA B 356 N PHE B 331
SHEET 15 A16 ALA B 488 ALA B 493 1 O VAL B 491 N SER B 357
SHEET 16 A16 LEU B 514 ILE B 519 1 O LYS B 515 N ALA B 488
CISPEP 1 PHE A 267 PRO A 268 0 -11.32
CISPEP 2 PHE B 267 PRO B 268 0 -7.51
SITE 1 AC1 10 PHE A 267 ASP A 335 MET A 339 THR A 360
SITE 2 AC1 10 TYR A 383 GLN A 384 LEU A 408 TYR A 466
SITE 3 AC1 10 MET A 503 HIS A 524
SITE 1 AC2 12 PHE B 267 ASP B 335 TRP B 336 THR B 360
SITE 2 AC2 12 TYR B 383 GLN B 384 LEU B 408 MET B 419
SITE 3 AC2 12 TYR B 466 LEU B 499 MET B 503 HIS B 524
CRYST1 129.384 80.296 88.867 90.00 125.88 90.00 C 1 2 1 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 0.007729 0.000000 0.005590 0.00000
SCALE2 0.000000 0.012454 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013888 0.00000
TER 2534 ASP A 545
TER 5068 ASP B 545
MASTER 346 0 2 38 16 0 6 6 5239 2 52 52
END |