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HEADER HYDROLASE 23-MAR-22 7ZBB
TITLE HALOTAG WITH TRAQ-G-CTRL LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HALOTAG, HALOALKANE DEHALOGENASE, SILICON RHODAMINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HUBNER,P.RIVERA-FUENTES,F.POJER,K.LAU
REVDAT 1 01-FEB-23 7ZBB 0
JRNL AUTH S.HUBNER,G.QUARGNALI,S.THALLMAIR,P.RIVERA-FUENTES
JRNL TITL A LOCALLY ACTIVATABLE SENSOR FOR ROBUST QUANTIFICATION OF
JRNL TITL 2 ORGANELLAR GLUTATHIONE
JRNL REF BIORXIV 2022
JRNL REFN ISSN 2692-8205
JRNL DOI 10.1101/2022.04.01.486692
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,
REMARK 1 AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,
REMARK 1 AUTH 3 P.H.ZWART,P.D.ADAMS
REMARK 1 TITL TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH
REMARK 1 TITL 2 PHENIX.REFINE.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 68 352 2012
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 22505256
REMARK 1 DOI 10.1107/S0907444912001308
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN,
REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY,
REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON,
REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL,
REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS,
REMARK 1 AUTH 6 P.D.ADAMS
REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS,
REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX.
REMARK 1 REF ACTA CRYSTALLOGR D STRUCT V. 75 861 2019
REMARK 1 REF 2 BIOL
REMARK 1 REFN ISSN 2059-7983
REMARK 1 PMID 31588918
REMARK 1 DOI 10.1107/S2059798319011471
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 94488
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.170
REMARK 3 FREE R VALUE TEST SET COUNT : 3939
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 44.3000 - 5.9100 1.00 3293 131 0.1667 0.1754
REMARK 3 2 5.9000 - 4.6900 0.99 3239 148 0.1451 0.2137
REMARK 3 3 4.6900 - 4.1000 0.98 3234 131 0.1284 0.1409
REMARK 3 4 4.1000 - 3.7200 0.99 3275 145 0.1382 0.1642
REMARK 3 5 3.7200 - 3.4600 0.99 3252 145 0.1404 0.1952
REMARK 3 6 3.4600 - 3.2500 0.99 3246 150 0.1492 0.1777
REMARK 3 7 3.2500 - 3.0900 1.00 3299 133 0.1561 0.2061
REMARK 3 8 3.0900 - 2.9600 0.99 3215 138 0.1584 0.2109
REMARK 3 9 2.9500 - 2.8400 0.99 3292 133 0.1678 0.2119
REMARK 3 10 2.8400 - 2.7400 0.99 3277 141 0.1828 0.2121
REMARK 3 11 2.7400 - 2.6600 0.99 3219 145 0.1866 0.2252
REMARK 3 12 2.6600 - 2.5800 0.96 3157 141 0.1984 0.2350
REMARK 3 13 2.5800 - 2.5100 0.98 3256 141 0.1950 0.2393
REMARK 3 14 2.5100 - 2.4500 0.99 3242 147 0.2030 0.2306
REMARK 3 15 2.4500 - 2.4000 0.99 3255 146 0.2006 0.1994
REMARK 3 16 2.4000 - 2.3500 0.99 3224 147 0.2092 0.2817
REMARK 3 17 2.3500 - 2.3000 0.99 3260 143 0.2175 0.2743
REMARK 3 18 2.3000 - 2.2600 0.99 3230 148 0.2186 0.2460
REMARK 3 19 2.2600 - 2.2200 0.99 3297 144 0.2275 0.3024
REMARK 3 20 2.2200 - 2.1800 0.99 3267 138 0.2293 0.2781
REMARK 3 21 2.1800 - 2.1400 0.99 3204 142 0.2321 0.2783
REMARK 3 22 2.1400 - 2.1100 0.99 3296 151 0.2353 0.2825
REMARK 3 23 2.1100 - 2.0800 0.98 3225 140 0.2612 0.2828
REMARK 3 24 2.0800 - 2.0500 0.96 3183 130 0.2746 0.3371
REMARK 3 25 2.0500 - 2.0200 0.98 3209 135 0.2747 0.3152
REMARK 3 26 2.0200 - 2.0000 0.98 3208 139 0.2701 0.2841
REMARK 3 27 2.0000 - 1.9700 0.98 3239 135 0.2756 0.3232
REMARK 3 28 1.9700 - 1.9500 0.91 2956 132 0.3113 0.3362
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.251
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.998
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.36
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 : 0.008 5001
REMARK 3 ANGLE : 1.004 6844
REMARK 3 CHIRALITY : 0.060 709
REMARK 3 PLANARITY : 0.008 896
REMARK 3 DIHEDRAL : 7.883 673
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7ZBB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-22.
REMARK 100 THE DEPOSITION ID IS D_1292121618.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94488
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 44.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 1.20.1_4487
REMARK 200 STARTING MODEL: 6U32
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% V/V PEG 6000, 0.1 M LITHIUM
REMARK 280 CHLORIDE, 0.1 M SODIUM CITRATE, PH 4, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 280K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 44.18733
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 88.37467
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 66.28100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 110.46833
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 22.09367
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: 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 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 294
REMARK 465 ILE A 295
REMARK 465 SER A 296
REMARK 465 GLY A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ILE B 295
REMARK 465 SER B 296
REMARK 465 GLY B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 42 44.70 -104.76
REMARK 500 THR A 43 -159.36 -99.00
REMARK 500 GLU A 98 -86.95 -113.96
REMARK 500 ASP A 106 -130.38 57.14
REMARK 500 ARG A 153 31.73 -90.40
REMARK 500 VAL A 245 -68.06 -130.41
REMARK 500 LEU A 271 -99.49 -121.12
REMARK 500 PRO B 42 46.78 -103.48
REMARK 500 THR B 43 -159.66 -101.86
REMARK 500 GLU B 98 -83.42 -108.26
REMARK 500 ASP B 106 -135.91 56.66
REMARK 500 GLU B 130 64.02 38.76
REMARK 500 ASP B 156 -60.52 77.55
REMARK 500 VAL B 245 -67.90 -128.86
REMARK 500 LEU B 271 -89.52 -117.94
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 B 719 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH B 720 DISTANCE = 6.26 ANGSTROMS
DBREF 7ZBB A 1 290 UNP P0A3G3 DHAA_RHOSO 1 290
DBREF 7ZBB B 1 290 UNP P0A3G3 DHAA_RHOSO 1 290
SEQADV 7ZBB ALA A 2 UNP P0A3G3 SER 2 ENGINEERED MUTATION
SEQADV 7ZBB VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7ZBB THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7ZBB GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7ZBB PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7ZBB MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7ZBB PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7ZBB THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7ZBB LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7ZBB VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7ZBB THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7ZBB MET A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7ZBB GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7ZBB ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7ZBB GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7ZBB ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7ZBB LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7ZBB ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7ZBB ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7ZBB LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7ZBB SER A 291 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB THR A 292 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB LEU A 293 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB SER A 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB GLY A 297 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS A 298 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS A 299 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS A 300 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS A 301 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS A 302 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS A 303 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB ALA B 2 UNP P0A3G3 SER 2 ENGINEERED MUTATION
SEQADV 7ZBB VAL B 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7ZBB THR B 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7ZBB GLY B 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7ZBB PHE B 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7ZBB MET B 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7ZBB PHE B 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7ZBB THR B 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7ZBB LYS B 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7ZBB VAL B 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7ZBB THR B 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7ZBB MET B 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7ZBB GLY B 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7ZBB ASN B 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7ZBB GLU B 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7ZBB ASP B 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7ZBB LYS B 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7ZBB ALA B 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7ZBB ASN B 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7ZBB LEU B 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7ZBB SER B 291 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB THR B 292 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB LEU B 293 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB GLU B 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB ILE B 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB SER B 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB GLY B 297 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS B 298 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS B 299 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS B 300 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS B 301 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS B 302 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBB HIS B 303 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 303 MET ALA GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 303 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 303 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 303 GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE
SEQRES 5 A 303 PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 303 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY
SEQRES 7 A 303 TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE
SEQRES 8 A 303 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 303 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 303 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 A 303 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 303 PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP
SEQRES 13 A 303 VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE
SEQRES 14 A 303 GLU GLY THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR
SEQRES 15 A 303 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN
SEQRES 16 A 303 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 303 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 A 303 VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 303 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 303 PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO
SEQRES 21 A 303 ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU
SEQRES 22 A 303 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 303 ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY HIS HIS
SEQRES 24 A 303 HIS HIS HIS HIS
SEQRES 1 B 303 MET ALA GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 B 303 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 B 303 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 B 303 GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE
SEQRES 5 B 303 PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 B 303 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY
SEQRES 7 B 303 TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE
SEQRES 8 B 303 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 B 303 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 B 303 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 B 303 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 B 303 PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP
SEQRES 13 B 303 VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE
SEQRES 14 B 303 GLU GLY THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR
SEQRES 15 B 303 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN
SEQRES 16 B 303 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 B 303 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 B 303 VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL
SEQRES 19 B 303 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 B 303 PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO
SEQRES 21 B 303 ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU
SEQRES 22 B 303 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 B 303 ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY HIS HIS
SEQRES 24 B 303 HIS HIS HIS HIS
HET ILJ A 401 86
HET GOL A 402 14
HET GOL A 403 14
HET GOL A 404 14
HET CL A 405 1
HET ILJ B 401 86
HET CL B 402 1
HETNAM ILJ (E)-[7-AZANYL-10-[2-CARBOXY-5-[2-[2-(6-
HETNAM 2 ILJ CHLORANYLHEXOXY)ETHOXY]ETHYLCARBAMOYL]PHENYL]-5,5-
HETNAM 3 ILJ DIMETHYL-BENZO[B][1]BENZOSILIN-3-YLIDENE]-METHYL-
HETNAM 4 ILJ AZANIUM
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETSYN ILJ HALOTAG WITH TRAQ-G-CTRL LIGAND
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ILJ 2(C34 H43 CL N3 O5 SI 1+)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 7 CL 2(CL 1-)
FORMUL 10 HOH *436(H2 O)
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 SER A 232 1 18
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 LEU A 293 1 16
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 ARG B 153 1 12
HELIX 24 AC6 ASP B 156 ILE B 163 1 8
HELIX 25 AC7 ASN B 166 GLY B 171 1 6
HELIX 26 AC8 LEU B 173 VAL B 177 5 5
HELIX 27 AC9 THR B 182 GLU B 191 1 10
HELIX 28 AD1 PRO B 192 LEU B 194 5 3
HELIX 29 AD2 ASN B 195 ASP B 198 5 4
HELIX 30 AD3 ARG B 199 PHE B 205 1 7
HELIX 31 AD4 PRO B 206 LEU B 209 5 4
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
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 VAL A 35 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 VAL A 265 N LEU A 238
SHEET 1 AA2 8 HIS B 13 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 101 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
LINK OD2 ASP A 106 C40 ILJ A 401 1555 1555 1.38
LINK OD2 ASP B 106 C40 ILJ B 401 1555 1555 1.37
CISPEP 1 ASN A 41 PRO A 42 0 -1.33
CISPEP 2 GLU A 214 PRO A 215 0 -3.37
CISPEP 3 THR A 242 PRO A 243 0 1.40
CISPEP 4 ASN B 41 PRO B 42 0 -0.55
CISPEP 5 GLU B 214 PRO B 215 0 -4.61
CISPEP 6 THR B 242 PRO B 243 0 0.72
CRYST1 94.010 94.010 132.562 90.00 90.00 120.00 P 61 12
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 0.010637 0.006141 0.000000 0.00000
SCALE2 0.000000 0.012283 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007544 0.00000
TER 2360 LEU A 293
TER 4732 GLU B 294
MASTER 331 0 7 35 16 0 0 6 5225 2 214 48
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