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HEADER HYDROLASE/HYDROLASE INHIBITOR 09-MAR-21 7EBA
TITLE CO-CRYSTAL OF KURARINONE WITH SEH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.3.2.10,3.1.3.76;
COMPND 5 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
KEYWDS SEH, INHIBITOR, KURARINONE, HYDROLASE, INTERACTION, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.P.SUN,X.C.MA
REVDAT 1 09-MAR-22 7EBA 0
JRNL AUTH C.P.SUN,J.J.ZHOU,Z.L.YU,X.K.HUO,J.ZHANG,C.MORISSEAU,
JRNL AUTH 2 B.D.HAMMOCK,X.C.MA
JRNL TITL KURARINONE ALLEVIATED PARKINSON'S DISEASE VIA STABILIZATION
JRNL TITL 2 OF EPOXYEICOSATRIENOIC ACIDS IN ANIMAL MODEL.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 119 18119 2022
JRNL REFN ESSN 1091-6490
JRNL PMID 35217618
JRNL DOI 10.1073/PNAS.2118818119
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 30233
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1514
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 2.3590 - 2.3000 0.76 1717 110 0.2390 0.2910
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.164
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
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 7EBA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-21.
REMARK 100 THE DEPOSITION ID IS D_1300021099.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JAN-20
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 : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33021
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
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: HKL-3000
REMARK 200 STARTING MODEL: 5G12
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM PHOSPHATE, POTASSIUM PHOSPHATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 66.85050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.21850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 66.85050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.21850
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: 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 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 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 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 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 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CB PRO B 371 SD MET B 469 1.91
REMARK 500 NZ LYS A 376 O HOH A 701 2.01
REMARK 500 CB PRO B 371 CG MET B 469 2.11
REMARK 500 O HOH B 811 O HOH B 820 2.11
REMARK 500 SG CYS A 232 O HOH A 817 2.13
REMARK 500 CD PRO A 512 O HOH A 795 2.14
REMARK 500 O HOH B 787 O HOH B 810 2.15
REMARK 500 O HOH A 822 O HOH B 805 2.17
REMARK 500 O PRO A 436 O HOH A 702 2.17
REMARK 500 O HOH B 788 O HOH B 799 2.18
REMARK 500 O HOH A 735 O HOH A 819 2.18
REMARK 500 O HOH A 814 O HOH A 815 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 440 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 440 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 246 -64.05 -23.89
REMARK 500 GLU A 269 -147.29 -126.76
REMARK 500 ASP A 335 -128.48 63.51
REMARK 500 ALA A 354 149.02 -173.10
REMARK 500 ASN A 359 -45.62 82.45
REMARK 500 HIS A 420 -75.01 -42.21
REMARK 500 LYS A 421 63.85 -114.37
REMARK 500 LYS A 478 -4.85 -58.24
REMARK 500 LEU A 480 -121.34 39.43
REMARK 500 LEU A 499 77.02 -103.47
REMARK 500 ILE A 511 79.78 -155.70
REMARK 500 LEU A 514 123.14 -26.08
REMARK 500 SER A 544 -81.79 -94.37
REMARK 500 SER B 231 -109.37 -94.01
REMARK 500 CYS B 232 -85.45 -33.13
REMARK 500 GLU B 269 -146.84 -127.76
REMARK 500 ASP B 335 -126.81 63.28
REMARK 500 ASN B 359 -42.79 80.03
REMARK 500 GLU B 435 76.44 -116.44
REMARK 500 LYS B 478 -6.30 -53.49
REMARK 500 HIS B 513 32.03 -85.17
REMARK 500 ALA B 546 34.27 -154.54
REMARK 500 ARG B 547 122.72 77.56
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 292 140.12
REMARK 500 GLY A 481 ARG A 482 -146.78
REMARK 500 CYS B 232 ASN B 233 -142.78
REMARK 500 MET B 291 ASP B 292 140.78
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 J0U A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J0U B 601
DBREF 7EBA A 230 555 UNP P34913 HYES_HUMAN 230 555
DBREF 7EBA B 230 555 UNP P34913 HYES_HUMAN 230 555
SEQADV 7EBA HIS A 224 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS A 225 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS A 226 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS A 227 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS A 228 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS A 229 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS B 224 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS B 225 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS B 226 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS B 227 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS B 228 UNP P34913 EXPRESSION TAG
SEQADV 7EBA HIS B 229 UNP P34913 EXPRESSION TAG
SEQRES 1 A 332 HIS HIS HIS HIS HIS HIS THR SER CYS ASN PRO SER ASP
SEQRES 2 A 332 MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG
SEQRES 3 A 332 LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS
SEQRES 4 A 332 LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG
SEQRES 5 A 332 TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL
SEQRES 6 A 332 LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA
SEQRES 7 A 332 PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS
SEQRES 8 A 332 LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER
SEQRES 9 A 332 GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU
SEQRES 10 A 332 VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG
SEQRES 11 A 332 ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN
SEQRES 12 A 332 PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO
SEQRES 13 A 332 VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL
SEQRES 14 A 332 ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE
SEQRES 15 A 332 LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER
SEQRES 16 A 332 MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN
SEQRES 17 A 332 SER PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU
SEQRES 18 A 332 GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER
SEQRES 19 A 332 GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU
SEQRES 20 A 332 ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS
SEQRES 21 A 332 ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP
SEQRES 22 A 332 PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP
SEQRES 23 A 332 TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS
SEQRES 24 A 332 GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN
SEQRES 25 A 332 GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN
SEQRES 26 A 332 PRO PRO VAL VAL SER LYS MET
SEQRES 1 B 332 HIS HIS HIS HIS HIS HIS THR SER CYS ASN PRO SER ASP
SEQRES 2 B 332 MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG
SEQRES 3 B 332 LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS
SEQRES 4 B 332 LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG
SEQRES 5 B 332 TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL
SEQRES 6 B 332 LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA
SEQRES 7 B 332 PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS
SEQRES 8 B 332 LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER
SEQRES 9 B 332 GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU
SEQRES 10 B 332 VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG
SEQRES 11 B 332 ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN
SEQRES 12 B 332 PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO
SEQRES 13 B 332 VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL
SEQRES 14 B 332 ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE
SEQRES 15 B 332 LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER
SEQRES 16 B 332 MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN
SEQRES 17 B 332 SER PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU
SEQRES 18 B 332 GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER
SEQRES 19 B 332 GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU
SEQRES 20 B 332 ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS
SEQRES 21 B 332 ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP
SEQRES 22 B 332 PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP
SEQRES 23 B 332 TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS
SEQRES 24 B 332 GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN
SEQRES 25 B 332 GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN
SEQRES 26 B 332 PRO PRO VAL VAL SER LYS MET
HET J0U A 601 32
HET J0U B 601 32
HETNAM J0U (2S)-2-[2,4-BIS(OXIDANYL)PHENYL]-5-METHOXY-8-[(2R)-5-
HETNAM 2 J0U METHYL-2-PROP-1-EN-2-YL-HEX-4-ENYL]-7-OXIDANYL-2,3-
HETNAM 3 J0U DIHYDROCHROMEN-4-ONE
HETSYN J0U KURARINONE
FORMUL 3 J0U 2(C26 H30 O6)
FORMUL 5 HOH *250(H2 O)
HELIX 1 AA1 ASN A 233 MET A 237 5 5
HELIX 2 AA2 SER A 270 ARG A 275 5 6
HELIX 3 AA3 TYR A 276 ALA A 284 1 9
HELIX 4 AA4 GLU A 304 TYR A 308 5 5
HELIX 5 AA5 CYS A 309 GLY A 325 1 17
HELIX 6 AA6 ASP A 335 TYR A 348 1 14
HELIX 7 AA7 SER A 370 ALA A 377 1 8
HELIX 8 AA8 ASN A 378 VAL A 380 5 3
HELIX 9 AA9 PHE A 381 PHE A 387 1 7
HELIX 10 AB1 GLY A 391 GLN A 399 1 9
HELIX 11 AB2 ASN A 400 PHE A 409 1 10
HELIX 12 AB3 ALA A 411 SER A 415 5 5
HELIX 13 AB4 THR A 443 LYS A 455 1 13
HELIX 14 AB5 PHE A 459 TRP A 465 1 7
HELIX 15 AB6 ASN A 468 LYS A 478 1 11
HELIX 16 AB7 VAL A 500 GLN A 505 5 6
HELIX 17 AB8 HIS A 506 ILE A 511 5 6
HELIX 18 AB9 TRP A 525 LYS A 530 1 6
HELIX 19 AC1 LYS A 530 ASP A 545 1 16
HELIX 20 AC2 ASN B 233 MET B 237 5 5
HELIX 21 AC3 SER B 270 ARG B 275 5 6
HELIX 22 AC4 TYR B 276 ALA B 284 1 9
HELIX 23 AC5 GLU B 304 TYR B 308 5 5
HELIX 24 AC6 CYS B 309 GLY B 325 1 17
HELIX 25 AC7 ASP B 335 TYR B 348 1 14
HELIX 26 AC8 SER B 370 ASN B 378 1 9
HELIX 27 AC9 PHE B 381 PHE B 387 1 7
HELIX 28 AD1 GLY B 391 ASN B 400 1 10
HELIX 29 AD2 ASN B 400 PHE B 409 1 10
HELIX 30 AD3 ALA B 411 SER B 415 5 5
HELIX 31 AD4 THR B 443 LYS B 456 1 14
HELIX 32 AD5 PHE B 459 TRP B 465 1 7
HELIX 33 AD6 ASN B 468 LYS B 478 1 11
HELIX 34 AD7 VAL B 500 GLN B 505 5 6
HELIX 35 AD8 MET B 507 ILE B 511 5 5
HELIX 36 AD9 TRP B 525 LYS B 530 1 6
HELIX 37 AE1 LYS B 530 ALA B 546 1 17
SHEET 1 AA116 LYS A 515 ILE A 519 0
SHEET 2 AA116 ALA A 488 ALA A 493 1 N ALA A 488 O LYS A 515
SHEET 3 AA116 VAL A 352 LEU A 358 1 N SER A 357 O VAL A 491
SHEET 4 AA116 ALA A 329 HIS A 334 1 N GLY A 333 O LEU A 358
SHEET 5 AA116 ALA A 260 CYS A 264 1 N CYS A 262 O VAL A 330
SHEET 6 AA116 ARG A 287 MET A 291 1 O ARG A 287 N VAL A 261
SHEET 7 AA116 VAL A 248 LEU A 255 -1 N LEU A 255 O VAL A 288
SHEET 8 AA116 SER A 238 LYS A 245 -1 N GLY A 240 O PHE A 252
SHEET 9 AA116 SER B 238 LYS B 245 -1 O HIS B 239 N TYR A 241
SHEET 10 AA116 VAL B 248 LEU B 255 -1 O LEU B 250 N VAL B 242
SHEET 11 AA116 ARG B 287 MET B 291 -1 O VAL B 288 N LEU B 255
SHEET 12 AA116 ALA B 260 CYS B 264 1 N VAL B 261 O ARG B 287
SHEET 13 AA116 ALA B 329 HIS B 334 1 O VAL B 330 N CYS B 262
SHEET 14 AA116 VAL B 352 LEU B 358 1 O ALA B 354 N PHE B 331
SHEET 15 AA116 ALA B 488 ALA B 493 1 O VAL B 491 N SER B 357
SHEET 16 AA116 LEU B 514 ILE B 519 1 O LYS B 515 N ALA B 488
CISPEP 1 PHE A 267 PRO A 268 0 -14.26
CISPEP 2 PHE B 267 PRO B 268 0 -18.44
SITE 1 AC1 16 ASP A 335 TRP A 336 MET A 339 TYR A 343
SITE 2 AC1 16 THR A 360 PRO A 361 ILE A 363 PRO A 364
SITE 3 AC1 16 ALA A 365 PHE A 381 GLN A 384 TYR A 466
SITE 4 AC1 16 MET A 469 ASN A 472 MET A 503 HOH A 740
SITE 1 AC2 13 ASP B 335 TRP B 336 MET B 339 TYR B 343
SITE 2 AC2 13 ILE B 363 PRO B 364 ALA B 365 PHE B 381
SITE 3 AC2 13 GLN B 384 TYR B 466 MET B 469 ASN B 472
SITE 4 AC2 13 HOH B 767
CRYST1 133.701 80.437 88.731 90.00 127.37 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 0.007479 0.000000 0.005713 0.00000
SCALE2 0.000000 0.012432 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014181 0.00000
TER 2545 ALA A 546
TER 5116 ASN B 548
MASTER 329 0 2 37 16 0 8 6 5428 2 64 52
END |