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HEADER HYDROLASE 28-FEB-20 6Y7B
TITLE X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7 LABELED WITH A
TITLE 2 CHLOROALKANE-CARBOPYRONINE FLUOROPHORE SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HALO, TAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS 2 FLUOROPHORE, CARBOPYRONINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,K.JOHNSSON,J.HIBLOT
REVDAT 1 31-MAR-21 6Y7B 0
JRNL AUTH M.TARNAWSKI,K.JOHNSSON,J.HIBLOT
JRNL TITL X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7
JRNL TITL 2 LABELED WITH A CHLOROALKANE-CARBOPYRONINE FLUOROPHORE
JRNL TITL 3 SUBSTRATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34290
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1715
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 49.3100 - 7.0900 1.00 2860 151 0.1653 0.1929
REMARK 3 2 7.0900 - 5.6300 1.00 2761 145 0.1959 0.2608
REMARK 3 3 5.6300 - 4.9200 1.00 2734 144 0.1778 0.1976
REMARK 3 4 4.9200 - 4.4700 1.00 2699 142 0.1722 0.2249
REMARK 3 5 4.4700 - 4.1500 1.00 2703 143 0.1789 0.2471
REMARK 3 6 4.1500 - 3.9100 1.00 2692 141 0.1981 0.2530
REMARK 3 7 3.9100 - 3.7100 1.00 2701 143 0.2254 0.2656
REMARK 3 8 3.7100 - 3.5500 1.00 2697 141 0.2447 0.3130
REMARK 3 9 3.5500 - 3.4100 1.00 2685 142 0.2617 0.3164
REMARK 3 10 3.4100 - 3.2900 1.00 2659 140 0.2642 0.3482
REMARK 3 11 3.2900 - 3.1900 1.00 2704 142 0.2645 0.3412
REMARK 3 12 3.1900 - 3.1000 1.00 2680 141 0.2822 0.3348
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.395
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.916
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.23
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 : 0.004 12390
REMARK 3 ANGLE : 0.788 16955
REMARK 3 CHIRALITY : 0.053 1770
REMARK 3 PLANARITY : 0.006 2360
REMARK 3 DIHEDRAL : 14.990 7340
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'B'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'C'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'D'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'E'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6Y7B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-FEB-20.
REMARK 100 THE DEPOSITION ID IS D_1292106997.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-19
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00006
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34294
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.750
REMARK 200 R MERGE (I) : 0.19600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.5300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.99
REMARK 200 R MERGE FOR SHELL (I) : 0.59600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: D_1292106996
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE PH 9.0, 1.7 M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 98 -70.41 -96.17
REMARK 500 ASP A 106 -127.31 52.94
REMARK 500 ARG A 153 48.77 -90.23
REMARK 500 ASP A 156 -66.59 -100.94
REMARK 500 VAL A 245 -69.78 -126.28
REMARK 500 LEU A 271 -88.29 -124.71
REMARK 500 ASN A 278 71.77 -150.21
REMARK 500 GLU B 98 -76.70 -91.96
REMARK 500 ASP B 106 -127.54 51.99
REMARK 500 ARG B 153 49.92 -91.47
REMARK 500 ASP B 156 -67.56 -100.87
REMARK 500 VAL B 245 -68.70 -126.53
REMARK 500 LEU B 271 -86.34 -125.86
REMARK 500 GLU C 98 -77.04 -93.82
REMARK 500 ASP C 106 -127.66 53.75
REMARK 500 ARG C 153 48.21 -90.23
REMARK 500 ASP C 156 -60.83 -102.24
REMARK 500 VAL C 245 -68.43 -126.87
REMARK 500 LEU C 271 -88.27 -124.42
REMARK 500 GLU D 98 -76.33 -93.58
REMARK 500 ASP D 106 -127.91 51.99
REMARK 500 ARG D 153 48.77 -90.91
REMARK 500 ASP D 156 -64.15 -98.81
REMARK 500 VAL D 245 -71.24 -127.05
REMARK 500 LEU D 271 -87.39 -126.38
REMARK 500 ASN D 278 72.36 -150.89
REMARK 500 GLU E 98 -75.25 -91.73
REMARK 500 ASP E 106 -128.27 54.03
REMARK 500 ARG E 153 46.43 -88.27
REMARK 500 ASP E 156 -69.03 -101.04
REMARK 500 VAL E 245 -68.45 -127.29
REMARK 500 LEU E 271 -87.64 -125.02
REMARK 500 ASN E 278 70.62 -150.95
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 OEK A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide OEK B 301 and ASP B
REMARK 800 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide OEK C 301 and ASP C
REMARK 800 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide OEK D 301 and ASP D
REMARK 800 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide OEK E 301 and ASP E
REMARK 800 106
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6Y7A RELATED DB: PDB
DBREF 6Y7B A 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 6Y7B B 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 6Y7B C 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 6Y7B D 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 6Y7B E 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
SEQADV 6Y7B GLY A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6Y7B THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6Y7B GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6Y7B PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6Y7B MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6Y7B PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6Y7B THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6Y7B LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6Y7B VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6Y7B THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6Y7B MET A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6Y7B GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6Y7B ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6Y7B GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6Y7B ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6Y7B LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6Y7B ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6Y7B ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6Y7B LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6Y7B SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6Y7B THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6Y7B GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B GLY B 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B VAL B 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6Y7B THR B 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6Y7B GLY B 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6Y7B PHE B 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6Y7B MET B 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6Y7B PHE B 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6Y7B THR B 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6Y7B LYS B 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6Y7B VAL B 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6Y7B THR B 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6Y7B MET B 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6Y7B GLY B 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6Y7B ASN B 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6Y7B GLU B 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6Y7B ASP B 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6Y7B LYS B 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6Y7B ALA B 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6Y7B ASN B 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6Y7B LEU B 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6Y7B SER B 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6Y7B THR B 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6Y7B GLU B 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B ILE B 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B GLY C 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B VAL C 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6Y7B THR C 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6Y7B GLY C 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6Y7B PHE C 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6Y7B MET C 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6Y7B PHE C 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6Y7B THR C 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6Y7B LYS C 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6Y7B VAL C 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6Y7B THR C 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6Y7B MET C 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6Y7B GLY C 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6Y7B ASN C 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6Y7B GLU C 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6Y7B ASP C 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6Y7B LYS C 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6Y7B ALA C 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6Y7B ASN C 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6Y7B LEU C 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6Y7B SER C 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6Y7B THR C 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6Y7B GLU C 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B ILE C 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B GLY D 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B VAL D 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6Y7B THR D 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6Y7B GLY D 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6Y7B PHE D 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6Y7B MET D 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6Y7B PHE D 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6Y7B THR D 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6Y7B LYS D 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6Y7B VAL D 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6Y7B THR D 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6Y7B MET D 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6Y7B GLY D 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6Y7B ASN D 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6Y7B GLU D 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6Y7B ASP D 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6Y7B LYS D 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6Y7B ALA D 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6Y7B ASN D 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6Y7B LEU D 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6Y7B SER D 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6Y7B THR D 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6Y7B GLU D 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B ILE D 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B GLY E 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B VAL E 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6Y7B THR E 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6Y7B GLY E 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6Y7B PHE E 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6Y7B MET E 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6Y7B PHE E 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6Y7B THR E 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6Y7B LYS E 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6Y7B VAL E 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6Y7B THR E 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6Y7B MET E 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6Y7B GLY E 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6Y7B ASN E 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6Y7B GLU E 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6Y7B ASP E 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6Y7B LYS E 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6Y7B ALA E 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6Y7B ASN E 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6Y7B LEU E 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6Y7B SER E 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6Y7B THR E 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6Y7B GLU E 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6Y7B ILE E 295 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 A 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 A 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 A 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 A 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 A 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 A 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 A 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 A 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 A 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 A 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 A 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 A 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 A 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 A 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 A 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 A 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 A 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 A 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 A 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 A 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 A 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 A 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 B 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 B 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 B 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 B 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 B 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 B 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 B 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 B 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 B 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 B 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 B 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 B 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 B 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 B 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 B 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 B 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 B 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 B 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 B 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 B 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 B 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 B 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 B 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 C 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 C 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 C 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 C 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 C 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 C 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 C 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 C 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 C 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 C 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 C 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 C 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 C 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 C 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 C 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 C 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 C 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 C 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 C 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 C 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 C 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 C 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 C 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 D 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 D 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 D 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 D 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 D 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 D 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 D 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 D 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 D 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 D 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 D 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 D 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 D 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 D 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 D 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 D 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 D 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 D 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 D 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 D 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 D 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 D 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 D 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 E 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 E 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 E 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 E 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 E 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 E 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 E 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 E 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 E 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 E 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 E 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 E 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 E 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 E 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 E 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 E 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 E 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 E 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 E 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 E 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 E 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 E 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 E 293 TRP LEU SER THR LEU GLU ILE
HET OEK A 301 46
HET CL A 302 1
HET OEK B 301 46
HET CL B 302 1
HET OEK C 301 46
HET CL C 302 1
HET OEK D 301 46
HET CL D 302 1
HET OEK E 301 46
HET CL E 302 1
HETNAM OEK 4-[2-[2-(6-CHLORANYLHEXOXY)ETHOXY]ETHYLCARBAMOYL]-2-[3-
HETNAM 2 OEK (DIMETHYLAMINO)-6-(DIMETHYL-$L^{4}-AZANYLIDENE)-10,10-
HETNAM 3 OEK DIMETHYL-ANTHRACEN-9-YL]BENZOIC ACID
HETNAM CL CHLORIDE ION
FORMUL 6 OEK 5( 1+)
FORMUL 7 CL 5(CL 1-)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 ASP A 156 ILE A 163 1 8
HELIX 8 AA8 ASN A 166 GLY A 171 1 6
HELIX 9 AA9 GLY A 171 GLY A 176 1 6
HELIX 10 AB1 THR A 182 GLU A 191 1 10
HELIX 11 AB2 PRO A 192 LEU A 194 5 3
HELIX 12 AB3 ASN A 195 ASP A 198 5 4
HELIX 13 AB4 ARG A 199 LEU A 209 1 11
HELIX 14 AB5 PRO A 215 GLN A 231 1 17
HELIX 15 AB6 PRO A 248 LEU A 259 1 12
HELIX 16 AB7 LEU A 273 ASN A 278 1 6
HELIX 17 AB8 ASN A 278 THR A 292 1 15
HELIX 18 AB9 SER B 44 ARG B 49 5 6
HELIX 19 AC1 ILE B 51 ALA B 56 1 6
HELIX 20 AC2 PHE B 80 LEU B 95 1 16
HELIX 21 AC3 ASP B 106 ASN B 119 1 14
HELIX 22 AC4 THR B 137 TRP B 141 5 5
HELIX 23 AC5 PRO B 142 PHE B 144 5 3
HELIX 24 AC6 ALA B 145 ARG B 153 1 9
HELIX 25 AC7 ASP B 156 ILE B 163 1 8
HELIX 26 AC8 ASN B 166 GLY B 171 1 6
HELIX 27 AC9 GLY B 171 GLY B 176 1 6
HELIX 28 AD1 THR B 182 GLU B 191 1 10
HELIX 29 AD2 PRO B 192 LEU B 194 5 3
HELIX 30 AD3 ASN B 195 ASP B 198 5 4
HELIX 31 AD4 ARG B 199 PHE B 205 1 7
HELIX 32 AD5 PRO B 215 SER B 232 1 18
HELIX 33 AD6 PRO B 248 LEU B 259 1 12
HELIX 34 AD7 LEU B 273 ASN B 278 1 6
HELIX 35 AD8 ASN B 278 SER B 291 1 14
HELIX 36 AD9 SER C 44 ARG C 49 5 6
HELIX 37 AE1 ILE C 51 ALA C 56 1 6
HELIX 38 AE2 PHE C 80 LEU C 95 1 16
HELIX 39 AE3 ASP C 106 ASN C 119 1 14
HELIX 40 AE4 THR C 137 TRP C 141 5 5
HELIX 41 AE5 PRO C 142 PHE C 144 5 3
HELIX 42 AE6 ALA C 145 ARG C 153 1 9
HELIX 43 AE7 ASP C 156 ILE C 163 1 8
HELIX 44 AE8 ASN C 166 GLY C 171 1 6
HELIX 45 AE9 GLY C 171 GLY C 176 1 6
HELIX 46 AF1 THR C 182 GLU C 191 1 10
HELIX 47 AF2 PRO C 192 LEU C 194 5 3
HELIX 48 AF3 ASN C 195 ASP C 198 5 4
HELIX 49 AF4 ARG C 199 PHE C 205 1 7
HELIX 50 AF5 PRO C 215 SER C 232 1 18
HELIX 51 AF6 PRO C 248 LEU C 259 1 12
HELIX 52 AF7 LEU C 273 ASN C 278 1 6
HELIX 53 AF8 ASN C 278 THR C 292 1 15
HELIX 54 AF9 SER D 44 ARG D 49 5 6
HELIX 55 AG1 ILE D 51 ALA D 56 1 6
HELIX 56 AG2 PHE D 80 LEU D 95 1 16
HELIX 57 AG3 ASP D 106 ASN D 119 1 14
HELIX 58 AG4 THR D 137 TRP D 141 5 5
HELIX 59 AG5 PRO D 142 PHE D 144 5 3
HELIX 60 AG6 ALA D 145 ARG D 153 1 9
HELIX 61 AG7 ASP D 156 ILE D 163 1 8
HELIX 62 AG8 ASN D 166 GLY D 171 1 6
HELIX 63 AG9 GLY D 171 GLY D 176 1 6
HELIX 64 AH1 THR D 182 GLU D 191 1 10
HELIX 65 AH2 PRO D 192 LEU D 194 5 3
HELIX 66 AH3 ASN D 195 ASP D 198 5 4
HELIX 67 AH4 ARG D 199 PHE D 205 1 7
HELIX 68 AH5 PRO D 215 SER D 232 1 18
HELIX 69 AH6 PRO D 248 LEU D 259 1 12
HELIX 70 AH7 LEU D 273 ASN D 278 1 6
HELIX 71 AH8 ASN D 278 SER D 291 1 14
HELIX 72 AH9 SER E 44 ARG E 49 5 6
HELIX 73 AI1 ILE E 51 ALA E 56 1 6
HELIX 74 AI2 PHE E 80 LEU E 95 1 16
HELIX 75 AI3 ASP E 106 ASN E 119 1 14
HELIX 76 AI4 THR E 137 TRP E 141 5 5
HELIX 77 AI5 PRO E 142 ARG E 153 1 12
HELIX 78 AI6 ASP E 156 ILE E 163 1 8
HELIX 79 AI7 ASN E 166 GLY E 171 1 6
HELIX 80 AI8 GLY E 171 GLY E 176 1 6
HELIX 81 AI9 THR E 182 GLU E 191 1 10
HELIX 82 AJ1 PRO E 192 LEU E 194 5 3
HELIX 83 AJ2 ASN E 195 ARG E 199 5 5
HELIX 84 AJ3 GLU E 200 PHE E 205 1 6
HELIX 85 AJ4 PRO E 215 SER E 232 1 18
HELIX 86 AJ5 PRO E 248 LEU E 259 1 12
HELIX 87 AJ6 LEU E 273 ASN E 278 1 6
HELIX 88 AJ7 ASN E 278 SER E 291 1 14
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O LYS A 263 N LEU A 238
SHEET 1 AA2 8 PRO B 12 VAL B 17 0
SHEET 2 AA2 8 GLU B 20 VAL B 27 -1 O GLU B 20 N VAL B 17
SHEET 3 AA2 8 CYS B 61 PRO B 64 -1 O CYS B 61 N VAL B 27
SHEET 4 AA2 8 VAL B 35 LEU B 38 1 N PHE B 37 O ILE B 62
SHEET 5 AA2 8 VAL B 100 HIS B 105 1 O VAL B 103 N LEU B 36
SHEET 6 AA2 8 VAL B 123 MET B 129 1 O ALA B 127 N LEU B 102
SHEET 7 AA2 8 LYS B 236 PRO B 243 1 O LEU B 237 N PHE B 128
SHEET 8 AA2 8 CYS B 262 GLY B 270 1 O LYS B 263 N LEU B 238
SHEET 1 AA3 8 HIS C 13 VAL C 17 0
SHEET 2 AA3 8 GLU C 20 VAL C 27 -1 O GLU C 20 N VAL C 17
SHEET 3 AA3 8 ARG C 60 PRO C 64 -1 O CYS C 61 N VAL C 27
SHEET 4 AA3 8 PRO C 34 LEU C 38 1 N VAL C 35 O ARG C 60
SHEET 5 AA3 8 VAL C 100 HIS C 105 1 O VAL C 103 N LEU C 36
SHEET 6 AA3 8 VAL C 123 MET C 129 1 O ALA C 127 N LEU C 102
SHEET 7 AA3 8 LYS C 236 PRO C 243 1 O LEU C 237 N PHE C 128
SHEET 8 AA3 8 CYS C 262 GLY C 270 1 O ILE C 267 N TRP C 240
SHEET 1 AA4 8 HIS D 13 VAL D 17 0
SHEET 2 AA4 8 GLU D 20 VAL D 27 -1 O GLU D 20 N VAL D 17
SHEET 3 AA4 8 ARG D 60 PRO D 64 -1 O CYS D 61 N VAL D 27
SHEET 4 AA4 8 PRO D 34 LEU D 38 1 N VAL D 35 O ARG D 60
SHEET 5 AA4 8 VAL D 100 HIS D 105 1 O VAL D 103 N LEU D 36
SHEET 6 AA4 8 VAL D 123 MET D 129 1 O ALA D 127 N LEU D 102
SHEET 7 AA4 8 LYS D 236 PRO D 243 1 O LEU D 237 N PHE D 128
SHEET 8 AA4 8 CYS D 262 GLY D 270 1 O LYS D 263 N LYS D 236
SHEET 1 AA5 8 HIS E 13 VAL E 17 0
SHEET 2 AA5 8 GLU E 20 VAL E 27 -1 O GLU E 20 N VAL E 17
SHEET 3 AA5 8 ARG E 60 PRO E 64 -1 O CYS E 61 N VAL E 27
SHEET 4 AA5 8 PRO E 34 LEU E 38 1 N VAL E 35 O ARG E 60
SHEET 5 AA5 8 VAL E 100 HIS E 105 1 O VAL E 101 N LEU E 36
SHEET 6 AA5 8 VAL E 123 MET E 129 1 O ALA E 127 N LEU E 102
SHEET 7 AA5 8 LYS E 236 PRO E 243 1 O LEU E 237 N PHE E 128
SHEET 8 AA5 8 CYS E 262 GLY E 270 1 O VAL E 265 N LEU E 238
LINK OD2 ASP A 106 C24 OEK A 301 1555 1555 1.38
LINK OD2 ASP B 106 C24 OEK B 301 1555 1555 1.37
LINK OD2 ASP C 106 C24 OEK C 301 1555 1555 1.38
LINK OD2 ASP D 106 C24 OEK D 301 1555 1555 1.38
LINK OD2 ASP E 106 C24 OEK E 301 1555 1555 1.38
CISPEP 1 ASN A 41 PRO A 42 0 -4.52
CISPEP 2 GLU A 214 PRO A 215 0 -2.75
CISPEP 3 THR A 242 PRO A 243 0 2.93
CISPEP 4 ASN B 41 PRO B 42 0 -5.49
CISPEP 5 GLU B 214 PRO B 215 0 -0.87
CISPEP 6 THR B 242 PRO B 243 0 4.06
CISPEP 7 ASN C 41 PRO C 42 0 -5.60
CISPEP 8 GLU C 214 PRO C 215 0 -3.67
CISPEP 9 THR C 242 PRO C 243 0 4.31
CISPEP 10 ASN D 41 PRO D 42 0 -5.28
CISPEP 11 GLU D 214 PRO D 215 0 -5.40
CISPEP 12 THR D 242 PRO D 243 0 3.41
CISPEP 13 ASN E 41 PRO E 42 0 -4.07
CISPEP 14 GLU E 214 PRO E 215 0 -8.16
CISPEP 15 THR E 242 PRO E 243 0 3.26
SITE 1 AC1 9 ASP A 106 ALA A 145 THR A 148 PHE A 149
SITE 2 AC1 9 GLN A 165 GLY A 171 THR A 172 MET A 175
SITE 3 AC1 9 ASN A 272
SITE 1 AC2 4 ASN A 41 TRP A 107 PHE A 205 PRO A 206
SITE 1 AC3 3 ASN B 41 TRP B 107 PRO B 206
SITE 1 AC4 3 ASN C 41 TRP C 107 OEK C 301
SITE 1 AC5 3 ASN D 41 TRP D 107 PRO D 206
SITE 1 AC6 2 TRP E 107 PHE E 205
SITE 1 AC7 17 GLY B 40 ASN B 41 HIS B 105 TRP B 107
SITE 2 AC7 17 GLY B 108 SER B 109 ALA B 110 GLU B 130
SITE 3 AC7 17 ILE B 132 THR B 148 GLN B 165 GLU B 170
SITE 4 AC7 17 GLY B 171 THR B 172 MET B 175 ASN B 272
SITE 5 AC7 17 THR E 58
SITE 1 AC8 18 ASN C 41 HIS C 105 TRP C 107 GLY C 108
SITE 2 AC8 18 SER C 109 ALA C 110 GLU C 130 ILE C 132
SITE 3 AC8 18 ALA C 145 THR C 148 PHE C 149 GLN C 165
SITE 4 AC8 18 GLU C 170 THR C 172 MET C 175 LEU C 246
SITE 5 AC8 18 ASN C 272 CL C 302
SITE 1 AC9 23 THR C 137 TRP C 138 ASP C 139 GLN C 150
SITE 2 AC9 23 ALA C 212 ASN D 41 HIS D 105 TRP D 107
SITE 3 AC9 23 GLY D 108 SER D 109 ALA D 110 GLU D 130
SITE 4 AC9 23 ILE D 132 PHE D 144 ALA D 145 THR D 148
SITE 5 AC9 23 GLN D 165 VAL D 167 GLU D 170 GLY D 171
SITE 6 AC9 23 THR D 172 LEU D 246 ASN D 272
SITE 1 AD1 15 ASN E 41 HIS E 105 TRP E 107 GLY E 108
SITE 2 AD1 15 SER E 109 ALA E 110 GLU E 130 ILE E 132
SITE 3 AD1 15 PHE E 144 ALA E 145 THR E 148 PHE E 149
SITE 4 AD1 15 GLN E 165 THR E 172 ASN E 272
CRYST1 161.270 161.270 124.660 90.00 90.00 120.00 P 3 2 1 30
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 0.006201 0.003580 0.000000 0.00000
SCALE2 0.000000 0.007160 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008022 0.00000
TER 2351 ILE A 295
TER 4702 ILE B 295
TER 7053 ILE C 295
TER 9404 ILE D 295
TER 11755 ILE E 295
MASTER 353 0 10 88 40 0 28 611985 5 235 115
END |