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HEADER HYDROLASE/HYDROLASE INHIBITOR 13-JAN-16 5HKA
TITLE CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF BOUND TO AN AMIDE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN UCBPP-PA14);
SOURCE 3 ORGANISM_TAXID: 208963;
SOURCE 4 STRAIN: UCBPP-PA14;
SOURCE 5 GENE: PA14_26090;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDPM73
KEYWDS BACTERIAL EPOXIDE HYDROLASE, INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.HVORECNY,D.R.MADDEN
REVDAT 1 18-MAY-16 5HKA 0
JRNL AUTH S.KITAMURA,K.L.HVORECNY,J.NIU,B.D.HAMMOCK,D.R.MADDEN,
JRNL AUTH 2 C.MORISSEAU
JRNL TITL RATIONAL DESIGN OF POTENT AND SELECTIVE INHIBITORS OF AN
JRNL TITL 2 EPOXIDE HYDROLASE VIRULENCE FACTOR FROM PSEUDOMONAS
JRNL TITL 3 AERUGINOSA.
JRNL REF J.MED.CHEM. 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 27120257
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00173
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.3_928
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 75318
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3764
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 19.9677 - 6.0934 1.00 2723 191 0.1754 0.2026
REMARK 3 2 6.0934 - 4.8595 0.99 2662 190 0.1686 0.1429
REMARK 3 3 4.8595 - 4.2520 0.99 2822 0 0.1223 0.0000
REMARK 3 4 4.2520 - 3.8663 0.99 2645 190 0.1401 0.1549
REMARK 3 5 3.8663 - 3.5909 0.99 2614 191 0.1553 0.1841
REMARK 3 6 3.5909 - 3.3802 0.99 2678 136 0.1567 0.1991
REMARK 3 7 3.3802 - 3.2117 0.99 2755 53 0.1546 0.1805
REMARK 3 8 3.2117 - 3.0724 0.99 2627 190 0.1588 0.2168
REMARK 3 9 3.0724 - 2.9545 0.99 2580 189 0.1754 0.2149
REMARK 3 10 2.9545 - 2.8529 0.99 2800 0 0.1675 0.0000
REMARK 3 11 2.8529 - 2.7639 0.99 2614 190 0.1592 0.1888
REMARK 3 12 2.7639 - 2.6851 0.99 2590 189 0.1491 0.1757
REMARK 3 13 2.6851 - 2.6145 0.99 2578 189 0.1588 0.2188
REMARK 3 14 2.6145 - 2.5509 0.99 2801 0 0.1685 0.0000
REMARK 3 15 2.5509 - 2.4930 0.99 2607 187 0.1750 0.1993
REMARK 3 16 2.4930 - 2.4400 0.99 2601 188 0.1633 0.1976
REMARK 3 17 2.4400 - 2.3913 0.98 2578 188 0.1655 0.2075
REMARK 3 18 2.3913 - 2.3463 0.99 2775 0 0.1743 0.0000
REMARK 3 19 2.3463 - 2.3044 0.98 2581 187 0.1716 0.2296
REMARK 3 20 2.3044 - 2.2654 0.98 2576 188 0.1771 0.2539
REMARK 3 21 2.2654 - 2.2289 0.98 2577 183 0.1687 0.2249
REMARK 3 22 2.2289 - 2.1947 0.98 2764 0 0.1767 0.0000
REMARK 3 23 2.1947 - 2.1624 0.98 2592 186 0.1835 0.2518
REMARK 3 24 2.1624 - 2.1320 0.98 2550 186 0.1855 0.2583
REMARK 3 25 2.1320 - 2.1032 0.98 2563 189 0.1859 0.2268
REMARK 3 26 2.1032 - 2.0759 0.98 2760 0 0.1978 0.0000
REMARK 3 27 2.0759 - 2.0500 0.97 2541 184 0.2005 0.2168
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 33.27
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.68540
REMARK 3 B22 (A**2) : -2.31750
REMARK 3 B33 (A**2) : 3.00290
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.39620
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 : 0.007 9914
REMARK 3 ANGLE : 1.129 13473
REMARK 3 CHIRALITY : 0.076 1367
REMARK 3 PLANARITY : 0.005 1771
REMARK 3 DIHEDRAL : 14.602 3631
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0448 11.6744 27.1790
REMARK 3 T TENSOR
REMARK 3 T11: 0.1041 T22: 0.0941
REMARK 3 T33: 0.0812 T12: 0.0109
REMARK 3 T13: 0.0154 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.7711 L22: 1.0027
REMARK 3 L33: 0.9645 L12: 0.1765
REMARK 3 L13: -0.0021 L23: -0.0038
REMARK 3 S TENSOR
REMARK 3 S11: -0.0294 S12: -0.0811 S13: -0.0789
REMARK 3 S21: 0.0883 S22: -0.0199 S23: 0.0297
REMARK 3 S31: 0.1180 S32: 0.0016 S33: 0.0487
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.0945 50.9938 15.4655
REMARK 3 T TENSOR
REMARK 3 T11: 0.0826 T22: 0.0938
REMARK 3 T33: 0.1192 T12: 0.0118
REMARK 3 T13: -0.0226 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 1.0197 L22: 1.2219
REMARK 3 L33: 0.6266 L12: -0.3592
REMARK 3 L13: -0.1670 L23: -0.0694
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: 0.0142 S13: 0.1522
REMARK 3 S21: -0.0316 S22: 0.0160 S23: 0.0347
REMARK 3 S31: -0.0830 S32: -0.0358 S33: -0.0100
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESID 25:317)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6445 44.4982 26.8302
REMARK 3 T TENSOR
REMARK 3 T11: 0.0936 T22: 0.0924
REMARK 3 T33: 0.1061 T12: 0.0099
REMARK 3 T13: -0.0040 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.6972 L22: 1.2829
REMARK 3 L33: 1.0194 L12: 0.0848
REMARK 3 L13: 0.0746 L23: 0.1661
REMARK 3 S TENSOR
REMARK 3 S11: -0.0110 S12: -0.0315 S13: 0.0880
REMARK 3 S21: 0.0733 S22: -0.0279 S23: -0.0828
REMARK 3 S31: -0.1020 S32: 0.0221 S33: 0.0387
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESID 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8356 5.1093 15.5722
REMARK 3 T TENSOR
REMARK 3 T11: 0.0889 T22: 0.0991
REMARK 3 T33: 0.0741 T12: 0.0220
REMARK 3 T13: 0.0157 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.8146 L22: 0.9897
REMARK 3 L33: 0.5766 L12: -0.1202
REMARK 3 L13: 0.1212 L23: 0.1698
REMARK 3 S TENSOR
REMARK 3 S11: 0.0270 S12: 0.0256 S13: -0.0638
REMARK 3 S21: -0.0522 S22: -0.0051 S23: -0.0867
REMARK 3 S31: 0.0352 S32: 0.0109 S33: -0.0173
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5HKA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000217150.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9770
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JANUARY 10, 2014
REMARK 200 DATA SCALING SOFTWARE : XSCALE JANUARY 10, 2014
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75324
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.44500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.7.3_928
REMARK 200 STARTING MODEL: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CALCIUM CHLORIDE, SODIUM
REMARK 280 ACETATE, DIMETHYLSULFOXIDE, PH 5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 84.48550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.85550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.48550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.85550
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
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: 2770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 GLY B 318
REMARK 465 ARG B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 GLY C 318
REMARK 465 ARG C 319
REMARK 465 HIS C 320
REMARK 465 HIS C 321
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
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 ASP A 129 -132.77 60.09
REMARK 500 ALA A 154 149.16 -172.24
REMARK 500 ASP B 129 -136.58 62.64
REMARK 500 ALA B 154 142.09 -171.94
REMARK 500 ASP B 184 -159.19 -86.83
REMARK 500 ASP C 129 -131.52 58.90
REMARK 500 ALA C 154 146.65 -175.86
REMARK 500 ASP C 184 -178.42 -68.65
REMARK 500 CYS C 303 51.88 -140.31
REMARK 500 ASP D 129 -136.08 61.60
REMARK 500 ALA D 154 142.60 -174.23
REMARK 500 ARG D 319 120.95 -33.35
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 64N A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 64N B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 64N C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 64N D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 3KD2 CONTAINS THE SAME PROTEIN IN ITS APO STATE
REMARK 900 RELATED ID: 4YX9 RELATED DB: PDB
REMARK 900 4YX9 CONTAINS THE SAME PROTEIN COMPLEXED WITH TIRATRICOL
REMARK 900 RELATED ID: 5HKB RELATED DB: PDB
REMARK 900 RELATED ID: 5HK9 RELATED DB: PDB
DBREF1 5HKA A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5HKA A A0A0M3KL26 1 301
DBREF1 5HKA B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5HKA B A0A0M3KL26 1 301
DBREF1 5HKA C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5HKA C A0A0M3KL26 1 301
DBREF1 5HKA D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5HKA D A0A0M3KL26 1 301
SEQRES 1 A 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 A 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 A 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 A 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 A 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 A 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 A 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 A 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 A 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 A 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 A 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 A 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 A 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 A 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 A 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 A 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 A 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 A 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 A 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 A 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 A 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 A 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 A 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 A 301 HIS HIS
SEQRES 1 B 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 B 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 B 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 B 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 B 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 B 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 B 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 B 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 B 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 B 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 B 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 B 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 B 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 B 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 B 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 B 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 B 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 B 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 B 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 B 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 B 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 B 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 B 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 B 301 HIS HIS
SEQRES 1 C 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 C 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 C 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 C 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 C 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 C 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 C 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 C 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 C 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 C 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 C 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 C 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 C 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 C 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 C 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 C 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 C 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 C 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 C 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 C 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 C 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 C 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 C 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 C 301 HIS HIS
SEQRES 1 D 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 D 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 D 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 D 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 D 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 D 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 D 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 D 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 D 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 D 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA
SEQRES 11 D 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 D 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 D 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 D 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 D 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 D 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 D 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 D 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 D 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 D 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 D 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 D 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 D 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 D 301 HIS HIS
HET 64N A 401 30
HET 64N B 401 30
HET 64N C 401 30
HET 64N D 401 30
HETNAM 64N 5'-[2,6-DICHLORO-4-(PROPANOYLAMINO)PHENOXY]-2'-
HETNAM 2 64N HYDROXYBIPHENYL-4-CARBOXAMIDE
FORMUL 5 64N 4(C22 H18 CL2 N2 O4)
FORMUL 9 HOH *753(H2 O)
HELIX 1 AA1 THR A 66 HIS A 71 5 6
HELIX 2 AA2 LEU A 73 ALA A 78 1 6
HELIX 3 AA3 SER A 102 SER A 118 1 17
HELIX 4 AA4 ASP A 129 ASN A 134 1 6
HELIX 5 AA5 THR A 135 ASN A 142 1 8
HELIX 6 AA6 ASP A 158 PHE A 164 5 7
HELIX 7 AA7 TRP A 176 ALA A 183 1 8
HELIX 8 AA8 ARG A 186 ALA A 193 1 8
HELIX 9 AA9 LYS A 195 HIS A 207 1 13
HELIX 10 AB1 ASN A 210 PHE A 214 5 5
HELIX 11 AB2 SER A 215 ALA A 227 1 13
HELIX 12 AB3 LYS A 228 ALA A 241 1 14
HELIX 13 AB4 ALA A 241 ALA A 253 1 13
HELIX 14 AB5 THR A 274 ALA A 282 1 9
HELIX 15 AB6 TRP A 298 CYS A 303 1 6
HELIX 16 AB7 CYS A 303 SER A 316 1 14
HELIX 17 AB8 THR B 66 HIS B 71 5 6
HELIX 18 AB9 GLN B 72 ALA B 78 1 7
HELIX 19 AC1 SER B 102 SER B 118 1 17
HELIX 20 AC2 ASP B 129 ASN B 134 1 6
HELIX 21 AC3 THR B 135 ASN B 142 1 8
HELIX 22 AC4 ASP B 158 PHE B 164 5 7
HELIX 23 AC5 TRP B 176 ALA B 183 1 8
HELIX 24 AC6 ARG B 186 ALA B 193 1 8
HELIX 25 AC7 LYS B 195 HIS B 207 1 13
HELIX 26 AC8 ASN B 210 PHE B 214 5 5
HELIX 27 AC9 SER B 215 ALA B 227 1 13
HELIX 28 AD1 LYS B 228 ALA B 241 1 14
HELIX 29 AD2 ALA B 241 ALA B 253 1 13
HELIX 30 AD3 THR B 274 ALA B 284 1 11
HELIX 31 AD4 TRP B 298 CYS B 303 1 6
HELIX 32 AD5 CYS B 303 ARG B 317 1 15
HELIX 33 AD6 THR C 66 HIS C 71 5 6
HELIX 34 AD7 GLN C 72 ALA C 78 1 7
HELIX 35 AD8 SER C 102 SER C 118 1 17
HELIX 36 AD9 ASP C 129 ASN C 134 1 6
HELIX 37 AE1 THR C 135 ASN C 142 1 8
HELIX 38 AE2 ASP C 158 PHE C 164 5 7
HELIX 39 AE3 TRP C 176 ALA C 183 1 8
HELIX 40 AE4 ARG C 186 ALA C 193 1 8
HELIX 41 AE5 LYS C 195 HIS C 207 1 13
HELIX 42 AE6 ASN C 210 PHE C 214 5 5
HELIX 43 AE7 SER C 215 ALA C 227 1 13
HELIX 44 AE8 LYS C 228 ALA C 241 1 14
HELIX 45 AE9 ALA C 241 ALA C 253 1 13
HELIX 46 AF1 THR C 274 ALA C 282 1 9
HELIX 47 AF2 TRP C 298 CYS C 303 1 6
HELIX 48 AF3 CYS C 303 ARG C 317 1 15
HELIX 49 AF4 THR D 66 HIS D 71 5 6
HELIX 50 AF5 LEU D 73 ALA D 78 1 6
HELIX 51 AF6 SER D 102 SER D 118 1 17
HELIX 52 AF7 ASP D 129 ASN D 134 1 6
HELIX 53 AF8 THR D 135 ASN D 142 1 8
HELIX 54 AF9 ASP D 158 PHE D 164 5 7
HELIX 55 AG1 TRP D 176 ALA D 183 1 8
HELIX 56 AG2 ARG D 186 ALA D 193 1 8
HELIX 57 AG3 LYS D 195 HIS D 207 1 13
HELIX 58 AG4 ASN D 210 PHE D 214 5 5
HELIX 59 AG5 SER D 215 ALA D 227 1 13
HELIX 60 AG6 LYS D 228 ALA D 241 1 14
HELIX 61 AG7 ALA D 241 ALA D 253 1 13
HELIX 62 AG8 THR D 274 ALA D 284 1 11
HELIX 63 AG9 TRP D 298 CYS D 303 1 6
HELIX 64 AH1 CYS D 303 ARG D 317 1 15
SHEET 1 AA1 8 GLU A 35 VAL A 41 0
SHEET 2 AA1 8 VAL A 44 GLY A 52 -1 O LYS A 50 N GLU A 35
SHEET 3 AA1 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51
SHEET 4 AA1 8 LEU A 56 VAL A 60 1 N LEU A 59 O ILE A 84
SHEET 5 AA1 8 PHE A 123 HIS A 128 1 O ASP A 124 N LEU A 56
SHEET 6 AA1 8 ILE A 146 MET A 152 1 O VAL A 150 N LEU A 125
SHEET 7 AA1 8 THR A 261 GLY A 266 1 O MET A 262 N LEU A 149
SHEET 8 AA1 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265
SHEET 1 AA2 2 PHE A 167 THR A 168 0
SHEET 2 AA2 2 GLY A 171 GLU A 172 -1 O GLY A 171 N THR A 168
SHEET 1 AA3 8 GLU B 35 VAL B 41 0
SHEET 2 AA3 8 VAL B 44 GLY B 52 -1 O LEU B 46 N ARG B 39
SHEET 3 AA3 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 AA3 8 LEU B 56 VAL B 60 1 N LEU B 59 O ILE B 84
SHEET 5 AA3 8 PHE B 123 HIS B 128 1 O VAL B 126 N VAL B 60
SHEET 6 AA3 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 AA3 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 AA3 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 AA4 2 PHE B 167 THR B 168 0
SHEET 2 AA4 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SHEET 1 AA5 8 GLU C 35 VAL C 41 0
SHEET 2 AA5 8 VAL C 44 GLY C 52 -1 O TYR C 48 N ALA C 37
SHEET 3 AA5 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 AA5 8 LEU C 56 VAL C 60 1 N LEU C 59 O ILE C 84
SHEET 5 AA5 8 PHE C 123 HIS C 128 1 O ASP C 124 N LEU C 56
SHEET 6 AA5 8 ILE C 146 MET C 152 1 O VAL C 150 N LEU C 125
SHEET 7 AA5 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 AA5 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 AA6 2 PHE C 167 THR C 168 0
SHEET 2 AA6 2 GLY C 171 GLU C 172 -1 O GLY C 171 N THR C 168
SHEET 1 AA7 8 GLU D 35 VAL D 41 0
SHEET 2 AA7 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
SHEET 3 AA7 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA7 8 LEU D 56 VAL D 60 1 N VAL D 57 O THR D 82
SHEET 5 AA7 8 PHE D 123 HIS D 128 1 O ASP D 124 N LEU D 56
SHEET 6 AA7 8 ILE D 146 MET D 152 1 O VAL D 150 N ALA D 127
SHEET 7 AA7 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA7 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA8 2 PHE D 167 THR D 168 0
SHEET 2 AA8 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SSBOND 1 CYS A 295 CYS A 303 1555 1555 2.01
SSBOND 2 CYS B 295 CYS B 303 1555 1555 2.01
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.01
SSBOND 4 CYS D 295 CYS D 303 1555 1555 2.00
SITE 1 AC1 16 ASP A 129 ILE A 130 TRP A 133 GLU A 153
SITE 2 AC1 16 PHE A 164 PRO A 165 LEU A 174 VAL A 175
SITE 3 AC1 16 HIS A 177 TYR A 239 GLY A 270 GLY A 271
SITE 4 AC1 16 MET A 272 HIS A 297 HOH A 586 HOH A 601
SITE 1 AC2 15 ASP B 129 PHE B 164 LEU B 174 VAL B 175
SITE 2 AC2 15 HIS B 177 PHE B 178 HIS B 207 TYR B 239
SITE 3 AC2 15 GLY B 270 GLY B 271 MET B 272 PHE B 275
SITE 4 AC2 15 HIS B 297 HOH B 612 HOH B 677
SITE 1 AC3 16 GLU A 278 ASP C 129 ILE C 130 TRP C 133
SITE 2 AC3 16 GLU C 153 PHE C 164 LEU C 174 VAL C 175
SITE 3 AC3 16 HIS C 177 TYR C 239 GLY C 270 GLY C 271
SITE 4 AC3 16 MET C 272 PHE C 275 HIS C 297 HOH C 602
SITE 1 AC4 13 ASP D 129 PHE D 164 LEU D 174 VAL D 175
SITE 2 AC4 13 HIS D 177 PHE D 178 HIS D 207 TYR D 239
SITE 3 AC4 13 GLY D 270 GLY D 271 MET D 272 PHE D 275
SITE 4 AC4 13 HIS D 297
CRYST1 168.971 83.711 88.879 90.00 100.68 90.00 C 1 2 1 16
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 0.005918 0.000000 0.001116 0.00000
SCALE2 0.000000 0.011946 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011449 0.00000
TER 2395 HIS A 321
TER 4738 ARG B 317
TER 7111 ARG C 317
TER 9485 HIS D 321
MASTER 376 0 4 64 40 0 16 610295 4 128 96
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