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HEADER HYDROLASE 14-OCT-16 5TNH
TITLE CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR
TITLE 2 CIF CONTAINING THE ADDUCTED 17,18-EPETE HYDROLYSIS INTERMEDIATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR;
COMPND 3 CHAIN: C, D, A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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
KEYWDS EPOXIDE HYDROLASE, HYDROXYALKYL-ENZYME INTERMEDIATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.HVORECNY,D.R.MADDEN
REVDAT 1 11-OCT-17 5TNH 0
JRNL AUTH K.L.HVORECNY,C.D.BAHL,S.KITAMURA,K.S.S.LEE,B.D.HAMMOCK,
JRNL AUTH 2 C.MORISSEAU,D.R.MADDEN
JRNL TITL ACTIVE-SITE FLEXIBILITY AND SUBSTRATE SPECIFICITY IN A
JRNL TITL 2 BACTERIAL VIRULENCE FACTOR: CRYSTALLOGRAPHIC SNAPSHOTS OF AN
JRNL TITL 3 EPOXIDE HYDROLASE.
JRNL REF STRUCTURE V. 25 697 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 28392259
JRNL DOI 10.1016/J.STR.2017.03.002
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 71620
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3576
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 19.8411 - 6.1610 1.00 2676 179 0.1869 0.2105
REMARK 3 2 6.1610 - 4.9146 1.00 2598 179 0.1819 0.2000
REMARK 3 3 4.9146 - 4.3006 1.00 2784 0 0.1525 0.0000
REMARK 3 4 4.3006 - 3.9107 1.00 2564 179 0.1657 0.1961
REMARK 3 5 3.9107 - 3.6322 1.00 2620 179 0.1761 0.2157
REMARK 3 6 3.6322 - 3.4192 1.00 2561 179 0.1718 0.2316
REMARK 3 7 3.4192 - 3.2487 1.00 2759 0 0.1788 0.0000
REMARK 3 8 3.2487 - 3.1079 1.00 2567 179 0.1799 0.2063
REMARK 3 9 3.1079 - 2.9886 1.00 2595 179 0.1903 0.2625
REMARK 3 10 2.9886 - 2.8858 1.00 2592 179 0.1970 0.2331
REMARK 3 11 2.8858 - 2.7958 1.00 2540 156 0.1916 0.2504
REMARK 3 12 2.7958 - 2.7161 1.00 2757 23 0.1890 0.2522
REMARK 3 13 2.7161 - 2.6448 1.00 2569 179 0.2004 0.2464
REMARK 3 14 2.6448 - 2.5804 1.00 2591 179 0.1888 0.2376
REMARK 3 15 2.5804 - 2.5219 1.00 2573 179 0.1969 0.2620
REMARK 3 16 2.5219 - 2.4683 1.00 2725 0 0.1986 0.0000
REMARK 3 17 2.4683 - 2.4190 1.00 2548 179 0.2032 0.2691
REMARK 3 18 2.4190 - 2.3734 1.00 2580 179 0.2003 0.2835
REMARK 3 19 2.3734 - 2.3311 1.00 2544 179 0.1939 0.2422
REMARK 3 20 2.3311 - 2.2917 1.00 2724 0 0.1974 0.0000
REMARK 3 21 2.2917 - 2.2547 1.00 2616 178 0.2003 0.2554
REMARK 3 22 2.2547 - 2.2201 1.00 2547 179 0.1955 0.2583
REMARK 3 23 2.2201 - 2.1875 1.00 2530 179 0.1937 0.2494
REMARK 3 24 2.1875 - 2.1567 1.00 2767 0 0.2014 0.0000
REMARK 3 25 2.1567 - 2.1276 1.00 2547 176 0.2126 0.2716
REMARK 3 26 2.1276 - 2.1000 1.00 2570 179 0.2210 0.2988
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.000
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 9778
REMARK 3 ANGLE : 0.821 13266
REMARK 3 CHIRALITY : 0.049 1362
REMARK 3 PLANARITY : 0.006 1734
REMARK 3 DIHEDRAL : 15.764 5766
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN C AND RESID 25:317 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9935 29.7947 -27.0027
REMARK 3 T TENSOR
REMARK 3 T11: 0.1047 T22: 0.1183
REMARK 3 T33: 0.1546 T12: -0.0074
REMARK 3 T13: -0.0028 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.0926 L22: 1.0829
REMARK 3 L33: 0.8551 L12: -0.1455
REMARK 3 L13: -0.0874 L23: -0.1766
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0429 S13: 0.1517
REMARK 3 S21: -0.0468 S22: -0.0227 S23: 0.0264
REMARK 3 S31: -0.1181 S32: -0.0354 S33: 0.0240
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN D AND RESID 25:317 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7316 -9.4892 -15.7260
REMARK 3 T TENSOR
REMARK 3 T11: 0.1220 T22: 0.1413
REMARK 3 T33: 0.1142 T12: -0.0258
REMARK 3 T13: 0.0049 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 1.1106 L22: 1.3005
REMARK 3 L33: 0.4958 L12: 0.4319
REMARK 3 L13: -0.1454 L23: -0.0929
REMARK 3 S TENSOR
REMARK 3 S11: -0.0098 S12: -0.0431 S13: -0.0861
REMARK 3 S21: 0.0489 S22: 0.0154 S23: 0.0970
REMARK 3 S31: 0.0902 S32: -0.0124 S33: -0.0066
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 25:318 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0116 -2.7354 -27.1755
REMARK 3 T TENSOR
REMARK 3 T11: 0.0955 T22: 0.1173
REMARK 3 T33: 0.1419 T12: -0.0095
REMARK 3 T13: 0.0024 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 1.1543 L22: 1.0551
REMARK 3 L33: 0.8432 L12: -0.0132
REMARK 3 L13: 0.1883 L23: 0.0252
REMARK 3 S TENSOR
REMARK 3 S11: 0.0044 S12: 0.0799 S13: -0.1040
REMARK 3 S21: -0.0602 S22: -0.0062 S23: -0.0304
REMARK 3 S31: 0.0999 S32: 0.0238 S33: 0.0040
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN B AND RESID 25:318 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7894 36.5750 -15.6674
REMARK 3 T TENSOR
REMARK 3 T11: 0.1084 T22: 0.1310
REMARK 3 T33: 0.1551 T12: -0.0243
REMARK 3 T13: -0.0164 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 1.3075 L22: 1.4665
REMARK 3 L33: 0.7739 L12: 0.5832
REMARK 3 L13: 0.0821 L23: 0.2553
REMARK 3 S TENSOR
REMARK 3 S11: -0.0132 S12: -0.0121 S13: 0.1224
REMARK 3 S21: 0.0603 S22: 0.0214 S23: -0.0724
REMARK 3 S31: -0.0824 S32: 0.0003 S33: -0.0058
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 5TNH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000222803.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
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) : 0.8856
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 NOVEMBER 1, 2011
REMARK 200 DATA SCALING SOFTWARE : XDS NOVEMBER 1, 2011
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71625
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 19.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.650
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.2100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.69
REMARK 200 R MERGE FOR SHELL (I) : 0.63400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.760
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (1.10_2155: ???)
REMARK 200 STARTING MODEL: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PH5 CALCIUM CHLORIDE
REMARK 280 PEG 8000, 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 84.06600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.04150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.06600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.04150
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: 2800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 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: 2850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 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 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 GLY D 318
REMARK 465 ARG D 319
REMARK 465 HIS D 320
REMARK 465 HIS D 321
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
REMARK 465 ARG A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
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 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 C 129 -128.52 58.58
REMARK 500 ALA C 154 147.80 -170.28
REMARK 500 CYS C 303 59.25 -142.34
REMARK 500 ASP D 129 -127.96 58.15
REMARK 500 ALA D 154 138.58 178.98
REMARK 500 ASP D 185 16.63 59.89
REMARK 500 TRP D 298 56.44 -90.96
REMARK 500 ASP A 129 -128.85 57.10
REMARK 500 ASN A 142 58.06 -140.29
REMARK 500 ALA A 154 146.72 -170.20
REMARK 500 ASP B 129 -129.24 63.67
REMARK 500 ALA B 154 142.58 176.91
REMARK 500 LYS B 195 28.48 -142.43
REMARK 500 TRP B 298 59.17 -92.20
REMARK 500 CYS B 303 52.56 -142.45
REMARK 500 ARG B 317 96.45 -63.07
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 C 659 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH C 660 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH C 661 DISTANCE = 7.76 ANGSTROMS
REMARK 525 HOH D 650 DISTANCE = 5.85 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7MS C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7MS A 401 and ASP A
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7MS B 401 and ASP B
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7MS D 401 and ASP D
REMARK 800 129
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KD2, 4DMC RELATED DB: PDB
REMARK 900 3KD2 - WILD TYPE VERSION OF THE CURRENT SUBMISSION 4DMC - APO
REMARK 900 VERSION OF SAME PROTEIN AS CURRENT SUBMISSION (CIF WITH E153Q
REMARK 900 MUTATION)
DBREF1 5TNH C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNH C A0A0M3KL26 1 301
DBREF1 5TNH D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNH D A0A0M3KL26 1 301
DBREF1 5TNH A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNH A A0A0M3KL26 1 301
DBREF1 5TNH B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5TNH B A0A0M3KL26 1 301
SEQADV 5TNH GLN C 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNH GLN D 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNH GLN A 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5TNH GLN B 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
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 GLN 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 GLN 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
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 GLN 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 GLN 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
HET 7MS C 401 23
HET 7MS D 401 23
HET 7MS A 401 23
HET 7MS B 401 23
HETNAM 7MS (5Z,8Z,11Z,14Z,17R,18R)-17,18-DIHYDROXYICOSA-5,8,11,14-
HETNAM 2 7MS TETRAENOIC ACID
FORMUL 5 7MS 4(C20 H32 O4)
FORMUL 9 HOH *600(H2 O)
HELIX 1 AA1 THR C 66 HIS C 71 5 6
HELIX 2 AA2 GLN C 72 LYS C 79 1 8
HELIX 3 AA3 SER C 102 SER C 118 1 17
HELIX 4 AA4 ASP C 129 ASN C 134 1 6
HELIX 5 AA5 THR C 135 ASN C 142 1 8
HELIX 6 AA6 ASP C 158 PHE C 164 5 7
HELIX 7 AA7 TRP C 176 ALA C 183 1 8
HELIX 8 AA8 ARG C 186 ALA C 193 1 8
HELIX 9 AA9 LYS C 195 HIS C 207 1 13
HELIX 10 AB1 ASN C 210 PHE C 214 5 5
HELIX 11 AB2 SER C 215 ALA C 227 1 13
HELIX 12 AB3 LYS C 228 ALA C 241 1 14
HELIX 13 AB4 ALA C 241 ALA C 253 1 13
HELIX 14 AB5 THR C 274 ALA C 284 1 11
HELIX 15 AB6 TRP C 298 CYS C 303 1 6
HELIX 16 AB7 CYS C 303 SER C 316 1 14
HELIX 17 AB8 THR D 66 HIS D 71 5 6
HELIX 18 AB9 GLN D 72 ALA D 78 1 7
HELIX 19 AC1 SER D 102 SER D 118 1 17
HELIX 20 AC2 ASP D 129 ASN D 134 1 6
HELIX 21 AC3 THR D 135 ASN D 142 1 8
HELIX 22 AC4 ASP D 158 PHE D 164 5 7
HELIX 23 AC5 TRP D 176 ALA D 183 1 8
HELIX 24 AC6 ARG D 186 ALA D 193 1 8
HELIX 25 AC7 LYS D 195 HIS D 207 1 13
HELIX 26 AC8 ASN D 210 PHE D 214 5 5
HELIX 27 AC9 SER D 215 ALA D 227 1 13
HELIX 28 AD1 LYS D 228 ALA D 241 1 14
HELIX 29 AD2 ALA D 241 ALA D 253 1 13
HELIX 30 AD3 THR D 274 ALA D 282 1 9
HELIX 31 AD4 TRP D 298 CYS D 303 1 6
HELIX 32 AD5 CYS D 303 ARG D 317 1 15
HELIX 33 AD6 THR A 66 HIS A 71 5 6
HELIX 34 AD7 LEU A 73 ALA A 78 1 6
HELIX 35 AD8 SER A 102 SER A 118 1 17
HELIX 36 AD9 ASP A 129 ASN A 134 1 6
HELIX 37 AE1 THR A 135 ASN A 142 1 8
HELIX 38 AE2 ASP A 158 ARG A 163 5 6
HELIX 39 AE3 TRP A 176 ALA A 183 1 8
HELIX 40 AE4 ARG A 186 ALA A 193 1 8
HELIX 41 AE5 LYS A 195 HIS A 207 1 13
HELIX 42 AE6 ASN A 210 PHE A 214 5 5
HELIX 43 AE7 SER A 215 ALA A 227 1 13
HELIX 44 AE8 LYS A 228 ALA A 241 1 14
HELIX 45 AE9 ALA A 241 ALA A 253 1 13
HELIX 46 AF1 THR A 274 ALA A 284 1 11
HELIX 47 AF2 TRP A 298 CYS A 303 1 6
HELIX 48 AF3 CYS A 303 SER A 316 1 14
HELIX 49 AF4 THR B 66 HIS B 71 5 6
HELIX 50 AF5 GLN B 72 ALA B 78 1 7
HELIX 51 AF6 SER B 102 SER B 118 1 17
HELIX 52 AF7 ASP B 129 ASN B 134 1 6
HELIX 53 AF8 THR B 135 ASN B 142 1 8
HELIX 54 AF9 ASP B 158 PHE B 164 5 7
HELIX 55 AG1 TRP B 176 ALA B 183 1 8
HELIX 56 AG2 ARG B 186 ALA B 193 1 8
HELIX 57 AG3 LYS B 195 HIS B 207 1 13
HELIX 58 AG4 SER B 215 ALA B 227 1 13
HELIX 59 AG5 LYS B 228 ALA B 241 1 14
HELIX 60 AG6 ALA B 241 ALA B 253 1 13
HELIX 61 AG7 THR B 274 ALA B 282 1 9
HELIX 62 AG8 TRP B 298 CYS B 303 1 6
HELIX 63 AG9 CYS B 303 ARG B 317 1 15
SHEET 1 AA1 8 PHE C 34 VAL C 41 0
SHEET 2 AA1 8 VAL C 44 GLY C 52 -1 O VAL C 44 N VAL C 41
SHEET 3 AA1 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 AA1 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 AA1 8 PHE C 123 HIS C 128 1 O VAL C 126 N MET C 58
SHEET 6 AA1 8 ILE C 146 MET C 152 1 O ALA C 147 N PHE C 123
SHEET 7 AA1 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 AA1 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 AA2 8 GLU D 35 VAL D 41 0
SHEET 2 AA2 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
SHEET 3 AA2 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA2 8 LEU D 56 VAL D 60 1 N VAL D 57 O THR D 82
SHEET 5 AA2 8 PHE D 123 HIS D 128 1 O ASP D 124 N LEU D 56
SHEET 6 AA2 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 AA2 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA2 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA3 2 PHE D 167 THR D 168 0
SHEET 2 AA3 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SHEET 1 AA4 8 PHE A 34 VAL A 41 0
SHEET 2 AA4 8 VAL A 44 GLY A 52 -1 O VAL A 44 N VAL A 41
SHEET 3 AA4 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51
SHEET 4 AA4 8 LEU A 56 VAL A 60 1 N VAL A 57 O THR A 82
SHEET 5 AA4 8 PHE A 123 HIS A 128 1 O ASP A 124 N MET A 58
SHEET 6 AA4 8 ILE A 146 MET A 152 1 O ALA A 147 N PHE A 123
SHEET 7 AA4 8 THR A 261 GLY A 266 1 O MET A 262 N TYR A 151
SHEET 8 AA4 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265
SHEET 1 AA5 2 PHE A 167 THR A 168 0
SHEET 2 AA5 2 GLY A 171 GLU A 172 -1 O GLY A 171 N THR A 168
SHEET 1 AA6 8 GLU B 35 VAL B 41 0
SHEET 2 AA6 8 VAL B 44 GLY B 52 -1 O LYS B 50 N GLU B 35
SHEET 3 AA6 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 AA6 8 LEU B 56 VAL B 60 1 N VAL B 57 O THR B 82
SHEET 5 AA6 8 PHE B 123 HIS B 128 1 O VAL B 126 N VAL B 60
SHEET 6 AA6 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 AA6 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 AA6 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 AA7 2 PHE B 167 THR B 168 0
SHEET 2 AA7 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SSBOND 1 CYS C 295 CYS C 303 1555 1555 2.01
SSBOND 2 CYS D 295 CYS D 303 1555 1555 2.01
SSBOND 3 CYS A 295 CYS A 303 1555 1555 2.02
SSBOND 4 CYS B 295 CYS B 303 1555 1555 2.00
LINK OD1 ASP C 129 C3 7MS C 401 1555 1555 1.41
LINK OD1 ASP D 129 C3 7MS D 401 1555 1555 1.41
LINK OD1 ASP A 129 C3 7MS A 401 1555 1555 1.41
LINK OD1 ASP B 129 C3 7MS B 401 1555 1555 1.41
SITE 1 AC1 13 ASP C 129 GLN C 153 PHE C 164 PRO C 165
SITE 2 AC1 13 LEU C 174 HIS C 177 PHE C 178 PHE C 203
SITE 3 AC1 13 TYR C 239 GLY C 270 GLY C 271 MET C 272
SITE 4 AC1 13 HIS C 297
SITE 1 AC2 19 GLY A 62 PHE A 63 HIS A 128 ILE A 130
SITE 2 AC2 19 GLY A 131 ILE A 132 MET A 152 GLN A 153
SITE 3 AC2 19 ALA A 154 LEU A 174 HIS A 177 PHE A 178
SITE 4 AC2 19 PHE A 203 HIS A 207 TYR A 239 GLY A 270
SITE 5 AC2 19 MET A 272 HIS A 297 HOH A 581
SITE 1 AC3 20 PHE B 63 HIS B 128 ILE B 130 GLY B 131
SITE 2 AC3 20 ILE B 132 MET B 152 GLN B 153 ALA B 154
SITE 3 AC3 20 PHE B 164 LEU B 174 VAL B 175 HIS B 177
SITE 4 AC3 20 PHE B 178 PHE B 203 TYR B 239 GLY B 270
SITE 5 AC3 20 MET B 272 PHE B 275 HIS B 297 HOH B 606
SITE 1 AC4 17 PHE D 63 HIS D 128 ILE D 130 GLY D 131
SITE 2 AC4 17 ILE D 132 MET D 152 GLN D 153 ALA D 154
SITE 3 AC4 17 PRO D 165 SER D 173 LEU D 174 HIS D 177
SITE 4 AC4 17 PHE D 178 PHE D 203 TYR D 239 GLY D 270
SITE 5 AC4 17 HIS D 297
CRYST1 168.132 84.083 89.564 90.00 100.28 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 0.005948 0.000000 0.001078 0.00000
SCALE2 0.000000 0.011893 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011347 0.00000
TER 2351 ARG C 317
TER 4702 ARG D 317
TER 7045 GLY A 318
TER 9395 GLY B 318
MASTER 401 0 4 63 38 0 19 610052 4 104 96
END |