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HEADER HYDROLASE 27-SEP-22 8B6R
TITLE X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7 LABELED WITH A
TITLE 2 CHLOROALKANE CYANINE3 FLUOROPHORE SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
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, HALOTAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS 2 FLUOROPHORE, CYANINE 3, CY3, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,L.HELLWEG,J.HIBLOT
REVDAT 1 26-JUL-23 8B6R 0
JRNL AUTH L.HELLWEG,A.EDENHOFER,L.BARCK,M.C.HUPPERTZ,M.S.FREI,
JRNL AUTH 2 M.TARNAWSKI,A.BERGNER,B.KOCH,K.JOHNSSON,J.HIBLOT
JRNL TITL A GENERAL METHOD FOR THE DEVELOPMENT OF MULTICOLOR
JRNL TITL 2 BIOSENSORS WITH LARGE DYNAMIC RANGES.
JRNL REF NAT.CHEM.BIOL. 2023
JRNL REFN ESSN 1552-4469
JRNL PMID 37291200
JRNL DOI 10.1038/S41589-023-01350-1
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 46120
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2306
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 41.2500 - 3.7800 1.00 2961 156 0.1517 0.1812
REMARK 3 2 3.7800 - 3.0000 1.00 2808 148 0.1523 0.1817
REMARK 3 3 3.0000 - 2.6200 1.00 2771 146 0.1598 0.1755
REMARK 3 4 2.6200 - 2.3800 1.00 2770 146 0.1593 0.1655
REMARK 3 5 2.3800 - 2.2100 1.00 2730 143 0.1528 0.1720
REMARK 3 6 2.2100 - 2.0800 1.00 2741 145 0.1527 0.1931
REMARK 3 7 2.0800 - 1.9800 1.00 2728 143 0.1550 0.1738
REMARK 3 8 1.9800 - 1.8900 1.00 2714 143 0.1507 0.1633
REMARK 3 9 1.8900 - 1.8200 1.00 2719 143 0.1434 0.2085
REMARK 3 10 1.8200 - 1.7500 1.00 2704 143 0.1619 0.2031
REMARK 3 11 1.7500 - 1.7000 1.00 2686 141 0.1738 0.2323
REMARK 3 12 1.7000 - 1.6500 1.00 2705 142 0.1880 0.2489
REMARK 3 13 1.6500 - 1.6100 1.00 2705 143 0.1872 0.2323
REMARK 3 14 1.6100 - 1.5700 1.00 2689 141 0.1919 0.2383
REMARK 3 15 1.5700 - 1.5300 1.00 2674 141 0.2320 0.2893
REMARK 3 16 1.5300 - 1.5000 1.00 2709 142 0.3540 0.3937
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) : 0.181
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.608
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.08
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 : 0.013 2516
REMARK 3 ANGLE : 1.229 3438
REMARK 3 CHIRALITY : 0.081 359
REMARK 3 PLANARITY : 0.011 466
REMARK 3 DIHEDRAL : 9.220 375
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 8B6R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1292125781.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-20
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) : 0.999884
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46121
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.2100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.65700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.360
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: 6Y7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM ACETATE, 19% (M/V) PEG
REMARK 280 3350, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 56.28000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 56.28000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.16500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 56.28000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 56.28000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 22.16500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 56.28000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.28000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 22.16500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 56.28000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.28000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 22.16500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 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 A 514 LIES ON A SPECIAL POSITION.
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 31 -159.94 -91.94
REMARK 500 PRO A 42 45.80 -108.37
REMARK 500 THR A 43 -158.09 -102.41
REMARK 500 GLU A 98 -92.47 -110.91
REMARK 500 ASP A 106 -129.13 52.63
REMARK 500 ARG A 153 50.27 -90.31
REMARK 500 VAL A 245 -69.31 -132.77
REMARK 500 LEU A 271 -96.84 -117.64
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 697 DISTANCE = 6.41 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 306 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 20 OE2
REMARK 620 2 HOH A 426 O 91.0
REMARK 620 3 HOH A 462 O 91.2 88.4
REMARK 620 4 HOH A 466 O 90.4 176.9 88.9
REMARK 620 5 HOH A 547 O 87.7 93.6 177.7 89.1
REMARK 620 6 HOH A 655 O 173.1 86.5 95.2 92.4 86.1
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8B6S RELATED DB: PDB
REMARK 900 RELATED ID: 8B6T RELATED DB: PDB
DBREF 8B6R A 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
SEQADV 8B6R GLY A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6R VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 8B6R THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 8B6R GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 8B6R PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 8B6R MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 8B6R PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 8B6R THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 8B6R LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 8B6R VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 8B6R THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 8B6R MET A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 8B6R GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 8B6R ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 8B6R GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 8B6R ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 8B6R LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 8B6R ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 8B6R ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 8B6R LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 8B6R SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 8B6R THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 8B6R GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6R ILE A 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
HET PJI A 301 46
HET CL A 302 1
HET GOL A 303 6
HET GOL A 304 6
HET GOL A 305 6
HET MG A 306 1
HET GOL A 307 6
HETNAM PJI ~{N}-[2-[2-(6-CHLORANYLHEXOXY)ETHOXY]ETHYL]-6-[3,3-
HETNAM 2 PJI DIMETHYL-2-[(~{E})-3-(1,3,3-TRIMETHYLINDOL-2-YLIDENE)
HETNAM 3 PJI PROP-1-ENYL]INDOL-1-IUM-1-YL]HEXANAMIDE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 PJI C40 H57 CL N3 O3 1+
FORMUL 3 CL CL 1-
FORMUL 4 GOL 4(C3 H8 O3)
FORMUL 7 MG MG 2+
FORMUL 9 HOH *297(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 PHE A 144 5 3
HELIX 7 AA7 ALA A 145 ARG A 153 1 9
HELIX 8 AA8 ASP A 156 ILE A 163 1 8
HELIX 9 AA9 ASN A 166 GLY A 171 1 6
HELIX 10 AB1 LEU A 173 VAL A 177 5 5
HELIX 11 AB2 THR A 182 GLU A 191 1 10
HELIX 12 AB3 PRO A 192 LEU A 194 5 3
HELIX 13 AB4 ASN A 195 ASP A 198 5 4
HELIX 14 AB5 ARG A 199 LEU A 209 1 11
HELIX 15 AB6 PRO A 215 GLN A 231 1 17
HELIX 16 AB7 PRO A 248 LEU A 259 1 12
HELIX 17 AB8 LEU A 273 ASN A 278 1 6
HELIX 18 AB9 ASN A 278 SER A 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
LINK OD2 ASP A 106 C10 PJI A 301 1555 1555 1.39
LINK OE2 GLU A 20 MG MG A 306 1555 1555 2.07
LINK MG MG A 306 O HOH A 426 1555 1555 2.07
LINK MG MG A 306 O HOH A 462 1555 7554 1.99
LINK MG MG A 306 O HOH A 466 1555 7554 2.11
LINK MG MG A 306 O HOH A 547 1555 1555 2.02
LINK MG MG A 306 O HOH A 655 1555 7554 2.18
CISPEP 1 ASN A 41 PRO A 42 0 1.89
CISPEP 2 GLU A 214 PRO A 215 0 -9.07
CISPEP 3 THR A 242 PRO A 243 0 4.61
CRYST1 112.560 112.560 44.330 90.00 90.00 90.00 P 42 21 2 8
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 0.008884 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008884 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022558 0.00000
TER 2366 ILE A 295
MASTER 283 0 7 18 8 0 0 6 2719 1 75 23
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