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HEADER HYDROLASE/HYDROLASE INHIBITOR 13-JAN-16 5HKB
TITLE CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF BOUND TO THE
TITLE 2 INHIBITOR KB2115
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR (CIF);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA UCBPP-PA14;
SOURCE 3 ORGANISM_TAXID: 208963;
SOURCE 4 GENE: PA14_26090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 8 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 5HKB 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. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 150014
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 7518
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 19.9229 - 5.0991 0.99 4870 376 0.2540 0.2511
REMARK 3 2 5.0991 - 4.0585 1.00 5102 0 0.1625 0.0000
REMARK 3 3 4.0585 - 3.5488 1.00 4698 376 0.1715 0.1888
REMARK 3 4 3.5488 - 3.2258 1.00 4673 376 0.1718 0.1922
REMARK 3 5 3.2258 - 2.9954 1.00 5064 0 0.1798 0.0000
REMARK 3 6 2.9954 - 2.8193 1.00 4639 376 0.1801 0.1858
REMARK 3 7 2.8193 - 2.6785 1.00 4653 376 0.1743 0.1970
REMARK 3 8 2.6785 - 2.5621 1.00 4983 0 0.1809 0.0000
REMARK 3 9 2.5621 - 2.4637 1.00 4652 376 0.1883 0.2106
REMARK 3 10 2.4637 - 2.3788 1.00 4616 376 0.1824 0.1912
REMARK 3 11 2.3788 - 2.3045 1.00 4991 0 0.1798 0.0000
REMARK 3 12 2.3045 - 2.2388 1.00 4624 376 0.1912 0.2244
REMARK 3 13 2.2388 - 2.1799 1.00 4622 376 0.1876 0.2175
REMARK 3 14 2.1799 - 2.1268 1.00 4997 0 0.1878 0.0000
REMARK 3 15 2.1268 - 2.0785 1.00 4578 375 0.1891 0.1971
REMARK 3 16 2.0785 - 2.0343 1.00 4615 375 0.1879 0.2157
REMARK 3 17 2.0343 - 1.9936 1.00 4973 0 0.1891 0.0000
REMARK 3 18 1.9936 - 1.9560 1.00 4604 376 0.1879 0.2242
REMARK 3 19 1.9560 - 1.9211 1.00 4601 376 0.1877 0.2246
REMARK 3 20 1.9211 - 1.8886 1.00 4937 0 0.2001 0.0000
REMARK 3 21 1.8886 - 1.8582 1.00 4594 376 0.1879 0.2310
REMARK 3 22 1.8582 - 1.8296 1.00 4574 376 0.1940 0.2285
REMARK 3 23 1.8296 - 1.8027 1.00 5016 0 0.1990 0.0000
REMARK 3 24 1.8027 - 1.7773 1.00 4596 376 0.2023 0.2450
REMARK 3 25 1.7773 - 1.7533 1.00 4529 376 0.2119 0.2633
REMARK 3 26 1.7533 - 1.7306 1.00 4998 0 0.2146 0.0000
REMARK 3 27 1.7306 - 1.7089 1.00 4589 376 0.2242 0.2679
REMARK 3 28 1.7089 - 1.6884 1.00 4541 376 0.2248 0.2672
REMARK 3 29 1.6884 - 1.6687 1.00 5009 0 0.2198 0.0000
REMARK 3 30 1.6687 - 1.6500 1.00 4558 376 0.2358 0.2453
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.60
REMARK 3 K_SOL : 0.42
REMARK 3 B_SOL : 46.33
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.510
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) : -2.36070
REMARK 3 B22 (A**2) : -1.46360
REMARK 3 B33 (A**2) : 3.82430
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 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 10041
REMARK 3 ANGLE : 1.161 13661
REMARK 3 CHIRALITY : 0.079 1392
REMARK 3 PLANARITY : 0.006 1801
REMARK 3 DIHEDRAL : 13.741 3693
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): 16.6010 -22.0094 202.8195
REMARK 3 T TENSOR
REMARK 3 T11: 0.0387 T22: 0.0315
REMARK 3 T33: 0.0240 T12: -0.0084
REMARK 3 T13: -0.0007 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 0.4949 L22: 0.4677
REMARK 3 L33: 0.5805 L12: -0.0313
REMARK 3 L13: 0.0250 L23: 0.1486
REMARK 3 S TENSOR
REMARK 3 S11: -0.0107 S12: -0.0207 S13: -0.0255
REMARK 3 S21: 0.0460 S22: 0.0118 S23: -0.0386
REMARK 3 S31: 0.0318 S32: 0.0545 S33: 0.0029
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.1570 -31.3901 191.1672
REMARK 3 T TENSOR
REMARK 3 T11: 0.0326 T22: 0.0391
REMARK 3 T33: 0.0419 T12: -0.0166
REMARK 3 T13: 0.0041 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.8419 L22: 0.9572
REMARK 3 L33: 0.3500 L12: 0.3491
REMARK 3 L13: 0.0264 L23: -0.0828
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: 0.0376 S13: 0.0124
REMARK 3 S21: -0.0283 S22: -0.0053 S23: 0.1290
REMARK 3 S31: 0.0126 S32: -0.0407 S33: 0.0020
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESID 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4984 5.4778 202.7093
REMARK 3 T TENSOR
REMARK 3 T11: 0.0263 T22: 0.0311
REMARK 3 T33: 0.0353 T12: -0.0101
REMARK 3 T13: 0.0131 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.6142 L22: 0.5066
REMARK 3 L33: 0.5222 L12: -0.1534
REMARK 3 L13: 0.0014 L23: 0.0296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0181 S12: -0.0186 S13: 0.0536
REMARK 3 S21: 0.0307 S22: 0.0053 S23: 0.0531
REMARK 3 S31: -0.0159 S32: -0.0499 S33: -0.0027
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESID 25:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3381 14.9332 191.1087
REMARK 3 T TENSOR
REMARK 3 T11: 0.0304 T22: 0.0239
REMARK 3 T33: -0.0064 T12: -0.0208
REMARK 3 T13: 0.0129 T23: 0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 0.6869 L22: 0.8958
REMARK 3 L33: 0.3820 L12: 0.3374
REMARK 3 L13: -0.1074 L23: 0.1826
REMARK 3 S TENSOR
REMARK 3 S11: -0.0049 S12: 0.0057 S13: 0.1088
REMARK 3 S21: -0.0285 S22: 0.0294 S23: -0.0434
REMARK 3 S31: -0.0113 S32: 0.0220 S33: -0.0051
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 5HKB 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_1000217114.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-12
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 : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
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 : 150068
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 19.921
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.60
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.220
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: 3KB2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
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 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 87.78400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 87.78400
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 42.08400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.74700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.08400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.74700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 87.78400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.08400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 84.74700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 87.78400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.08400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 84.74700
REMARK 290 SMTRY3 8 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: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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: 3220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH D 720 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 855 LIES ON A SPECIAL POSITION.
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 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
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 -133.37 61.18
REMARK 500 ALA A 154 147.54 -173.58
REMARK 500 CYS A 303 56.29 -143.52
REMARK 500 THR B 99 -67.80 -91.29
REMARK 500 ASP B 129 -134.76 58.68
REMARK 500 ASP B 184 -162.75 -79.95
REMARK 500 ASP B 185 16.55 59.04
REMARK 500 CYS B 303 52.56 -142.93
REMARK 500 ASP C 129 -133.59 61.00
REMARK 500 ALA C 154 147.19 -174.83
REMARK 500 CYS C 303 56.10 -143.40
REMARK 500 THR D 99 -66.59 -90.89
REMARK 500 ASP D 129 -134.20 58.22
REMARK 500 ASP D 185 18.91 59.24
REMARK 500 CYS D 303 54.68 -141.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 851 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 852 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A 853 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A 854 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 855 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH B 836 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH C 862 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH C 863 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH C 864 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH C 865 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH C 866 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH C 867 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH D 855 DISTANCE = 6.09 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 64L A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 64L B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 64L C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 64L D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 3KD2 IS THE SAME PROTEIN WITHOUT LIGAND
REMARK 900 RELATED ID: 4YX9 RELATED DB: PDB
REMARK 900 4XY9 CONTAINS THE SAME PROTEIN COMPLEXED WITH THE INHIBITOR
REMARK 900 TIRATRICOL
REMARK 900 RELATED ID: 5HKA RELATED DB: PDB
REMARK 900 RELATED ID: 5HK9 RELATED DB: PDB
DBREF1 5HKB A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5HKB A A0A0M3KL26 1 301
DBREF1 5HKB B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5HKB B A0A0M3KL26 1 301
DBREF1 5HKB C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5HKB C A0A0M3KL26 1 301
DBREF1 5HKB D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5HKB 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 64L A 401 26
HET ACT A 402 4
HET 64L B 401 26
HET ACT B 402 4
HET 64L C 401 26
HET ACT C 402 4
HET 64L D 401 26
HET ACT D 402 4
HETNAM 64L KB2115
HETNAM ACT ACETATE ION
HETSYN 64L 3-({3,5-DIBROMO-4-[4-HYDROXY-3-(PROPAN-2-YL)
HETSYN 2 64L PHENOXY]PHENYL}AMINO)-3-OXOPROPANOIC ACID
FORMUL 5 64L 4(C18 H17 BR2 N O5)
FORMUL 6 ACT 4(C2 H3 O2 1-)
FORMUL 13 HOH *1413(H2 O)
HELIX 1 AA1 THR A 66 HIS A 71 5 6
HELIX 2 AA2 GLN A 72 ALA A 78 1 7
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 LYS A 281 1 8
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 LYS B 228 1 14
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 282 1 9
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 284 1 11
HELIX 47 AF2 TRP C 298 CYS C 303 1 6
HELIX 48 AF3 CYS C 303 SER C 316 1 14
HELIX 49 AF4 THR D 66 HIS D 71 5 6
HELIX 50 AF5 GLN D 72 ALA D 78 1 7
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 LYS D 228 1 14
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 282 1 9
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 VAL A 44 N VAL A 41
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 TYR A 151
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 LYS B 50 N GLU B 35
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 VAL B 57 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 LEU C 46 N ARG C 39
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 VAL C 126 N VAL C 60
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 PHE D 34 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 VAL D 126 N VAL D 60
SHEET 6 AA7 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
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 14 GLU A 153 ARG A 163 PHE A 164 PRO A 165
SITE 2 AC1 14 LEU A 174 VAL A 175 HIS A 177 GLY A 270
SITE 3 AC1 14 GLY A 271 MET A 272 PHE A 275 HIS A 297
SITE 4 AC1 14 ACT A 402 HOH A 506
SITE 1 AC2 6 ASP A 129 TRP A 133 HIS A 177 PHE A 178
SITE 2 AC2 6 TYR A 239 64L A 401
SITE 1 AC3 11 GLU B 153 PHE B 164 LEU B 174 VAL B 175
SITE 2 AC3 11 GLY B 270 GLY B 271 MET B 272 PHE B 275
SITE 3 AC3 11 HIS B 297 ACT B 402 HOH B 718
SITE 1 AC4 5 ASP B 129 HIS B 177 PHE B 178 TYR B 239
SITE 2 AC4 5 64L B 401
SITE 1 AC5 14 GLU C 153 PHE C 164 PRO C 165 LEU C 174
SITE 2 AC5 14 VAL C 175 HIS C 177 GLY C 270 GLY C 271
SITE 3 AC5 14 MET C 272 PHE C 275 HIS C 297 ACT C 402
SITE 4 AC5 14 HOH C 535 HOH C 552
SITE 1 AC6 5 ASP C 129 TRP C 133 HIS C 177 TYR C 239
SITE 2 AC6 5 64L C 401
SITE 1 AC7 12 GLU D 153 PHE D 164 LEU D 174 VAL D 175
SITE 2 AC7 12 HIS D 177 GLY D 270 GLY D 271 MET D 272
SITE 3 AC7 12 PHE D 275 HIS D 297 HOH D 511 HOH D 687
SITE 1 AC8 4 ASP D 129 HIS D 177 PHE D 178 TYR D 239
CRYST1 84.168 169.494 175.568 90.00 90.00 90.00 C 2 2 21 32
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 0.011881 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005900 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005696 0.00000
TER 2411 HIS A 321
TER 4804 HIS B 321
TER 7206 HIS C 321
TER 9606 HIS D 321
MASTER 441 0 8 64 40 0 21 611025 4 128 96
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