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HEADER HYDROLASE 27-JUL-20 6ZVY
TITLE X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7-Q165H-P174R
TITLE 2 LABELED WITH A CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE
TITLE 3 SUBSTRATE
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HALO, TAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS 2 FLUOROPHORE, TETRAMETHYLRHODAMINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON
REVDAT 1 04-AUG-21 6ZVY 0
JRNL AUTH M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON
JRNL TITL X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE
JRNL TITL 2 HALOTAG7-Q165H-P174R LABELED WITH A
JRNL TITL 3 CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.40 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.020
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 3 NUMBER OF REFLECTIONS : 99379
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4970
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 40.4000 - 4.3500 0.95 3417 181 0.1571 0.1603
REMARK 3 2 4.3500 - 3.4500 0.95 3432 180 0.1444 0.1552
REMARK 3 3 3.4500 - 3.0200 0.94 3378 178 0.1505 0.1617
REMARK 3 4 3.0200 - 2.7400 0.93 3357 177 0.1721 0.1871
REMARK 3 5 2.7400 - 2.5400 0.93 3340 176 0.1699 0.1818
REMARK 3 6 2.5400 - 2.3900 0.92 3287 172 0.0000 0.1604
REMARK 3 7 2.3900 - 2.2700 0.92 3320 175 0.1676 0.2041
REMARK 3 8 2.2700 - 2.1700 0.92 3292 174 0.1612 0.1711
REMARK 3 9 2.1700 - 2.0900 0.91 3273 172 0.1649 0.1927
REMARK 3 10 2.0900 - 2.0200 0.92 3318 174 0.1628 0.1897
REMARK 3 11 2.0200 - 1.9600 0.91 3275 173 0.1610 0.1717
REMARK 3 12 1.9600 - 1.9000 0.91 3266 172 0.1668 0.1869
REMARK 3 13 1.9000 - 1.8500 0.92 3326 175 0.1738 0.2179
REMARK 3 14 1.8500 - 1.8000 0.91 3279 172 0.1747 0.1931
REMARK 3 15 1.8000 - 1.7600 0.92 3295 174 0.1666 0.1750
REMARK 3 16 1.7600 - 1.7300 0.92 3321 175 0.1594 0.1829
REMARK 3 17 1.7300 - 1.6900 0.92 3306 174 0.1581 0.1791
REMARK 3 18 1.6900 - 1.6600 0.92 3370 177 0.1612 0.1979
REMARK 3 19 1.6600 - 1.6300 0.92 3259 171 0.1614 0.2069
REMARK 3 20 1.6300 - 1.6000 0.92 3352 177 0.1650 0.1917
REMARK 3 21 1.6000 - 1.5800 0.93 3276 172 0.1655 0.2042
REMARK 3 22 1.5800 - 1.5500 0.93 3392 179 0.1651 0.1960
REMARK 3 23 1.5500 - 1.5300 0.92 3242 170 0.1677 0.1914
REMARK 3 24 1.5300 - 1.5100 0.91 3331 176 0.1633 0.2265
REMARK 3 25 1.5100 - 1.4900 0.89 3204 168 0.1704 0.2000
REMARK 3 26 1.4900 - 1.4700 0.85 3034 160 0.1761 0.2232
REMARK 3 27 1.4700 - 1.4500 0.71 2589 136 0.1846 0.2101
REMARK 3 28 1.4500 - 1.4300 0.61 2182 115 0.1816 0.2524
REMARK 3 29 1.4300 - 1.4200 0.54 1958 103 0.1878 0.2050
REMARK 3 30 1.4200 - 1.4000 0.49 1738 92 0.1817 0.2354
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) : 0.124
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.884
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.92
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 : 0.006 5006
REMARK 3 ANGLE : 0.882 6842
REMARK 3 CHIRALITY : 0.081 714
REMARK 3 PLANARITY : 0.008 956
REMARK 3 DIHEDRAL : 7.819 3018
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 6ZVY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1292110336.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-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) : 0.999878
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 : 99388
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
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 (%) : 87.5
REMARK 200 DATA REDUNDANCY : 1.910
REMARK 200 R MERGE (I) : 0.02600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.8200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.81
REMARK 200 R MERGE FOR SHELL (I) : 0.12500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.570
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 (%): 44.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0, 1.0 M LITHIUM
REMARK 280 CHLORIDE, 20% (M/V) PEG 6000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 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
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 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 48.46 -107.73
REMARK 500 THR A 43 -159.90 -104.56
REMARK 500 GLU A 98 -92.52 -107.67
REMARK 500 ASP A 106 -132.73 52.49
REMARK 500 ARG A 153 45.58 -88.14
REMARK 500 ASP A 156 -78.00 -98.63
REMARK 500 VAL A 245 -62.89 -131.75
REMARK 500 LEU A 271 -98.93 -115.21
REMARK 500 PRO B 42 49.08 -107.45
REMARK 500 THR B 43 -160.22 -102.68
REMARK 500 GLU B 98 -93.21 -107.81
REMARK 500 ASP B 106 -133.52 55.22
REMARK 500 ARG B 153 44.60 -87.36
REMARK 500 ASP B 156 -79.69 -98.06
REMARK 500 VAL B 245 -68.34 -131.57
REMARK 500 LEU B 271 -100.03 -116.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ZVU RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVV RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVX RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVW RELATED DB: PDB
DBREF 6ZVY A 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 6ZVY B 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
SEQADV 6ZVY GLY A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVY VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6ZVY THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6ZVY GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6ZVY PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6ZVY MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6ZVY PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6ZVY THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6ZVY LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6ZVY HIS A 165 UNP P0A3G3 GLN 165 ENGINEERED MUTATION
SEQADV 6ZVY VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6ZVY THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6ZVY ARG A 174 UNP P0A3G3 PRO 174 ENGINEERED MUTATION
SEQADV 6ZVY MET A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6ZVY GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6ZVY ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6ZVY GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6ZVY ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6ZVY LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6ZVY ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6ZVY ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6ZVY LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6ZVY SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6ZVY THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6ZVY GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVY ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVY GLY B 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVY VAL B 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6ZVY THR B 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6ZVY GLY B 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6ZVY PHE B 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6ZVY MET B 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6ZVY PHE B 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6ZVY THR B 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6ZVY LYS B 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6ZVY HIS B 165 UNP P0A3G3 GLN 165 ENGINEERED MUTATION
SEQADV 6ZVY VAL B 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6ZVY THR B 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6ZVY ARG B 174 UNP P0A3G3 PRO 174 ENGINEERED MUTATION
SEQADV 6ZVY MET B 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6ZVY GLY B 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6ZVY ASN B 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6ZVY GLU B 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6ZVY ASP B 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6ZVY LYS B 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6ZVY ALA B 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6ZVY ASN B 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6ZVY LEU B 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6ZVY SER B 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6ZVY THR B 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6ZVY GLU B 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVY ILE B 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 HIS ASN VAL PHE ILE GLU GLY
SEQRES 14 A 293 THR LEU ARG 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 HIS ASN VAL PHE ILE GLU GLY
SEQRES 14 B 293 THR LEU ARG 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
HET OEH A 301 44
HET CL A 302 1
HET GOL A 303 6
HET GOL A 304 6
HET GOL B 301 6
HET GOL B 302 6
HET OEH B 303 44
HET CL B 304 1
HETNAM OEH [9-[2-CARBOXY-5-[2-[2-(6-CHLORANYLHEXOXY)
HETNAM 2 OEH ETHOXY]ETHYLCARBAMOYL]PHENYL]-6-(DIMETHYLAMINO)
HETNAM 3 OEH XANTHEN-3-YLIDENE]-DIMETHYL-AZANIUM
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 OEH 2(C35 H43 CL N3 O6 1+)
FORMUL 4 CL 2(CL 1-)
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 11 HOH *648(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 SER A 232 1 18
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
HELIX 19 AC1 SER B 44 ARG B 49 5 6
HELIX 20 AC2 ILE B 51 ALA B 56 1 6
HELIX 21 AC3 PHE B 80 LEU B 95 1 16
HELIX 22 AC4 ASP B 106 ASN B 119 1 14
HELIX 23 AC5 THR B 137 TRP B 141 5 5
HELIX 24 AC6 PRO B 142 PHE B 144 5 3
HELIX 25 AC7 ALA B 145 ARG B 153 1 9
HELIX 26 AC8 ASP B 156 ILE B 163 1 8
HELIX 27 AC9 ASN B 166 GLY B 171 1 6
HELIX 28 AD1 GLY B 171 GLY B 176 1 6
HELIX 29 AD2 THR B 182 GLU B 191 1 10
HELIX 30 AD3 PRO B 192 LEU B 194 5 3
HELIX 31 AD4 ASN B 195 ASP B 198 5 4
HELIX 32 AD5 ARG B 199 LEU B 209 1 11
HELIX 33 AD6 PRO B 215 HIS B 230 1 16
HELIX 34 AD7 PRO B 248 LEU B 259 1 12
HELIX 35 AD8 LEU B 273 ASN B 278 1 6
HELIX 36 AD9 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 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 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 LYS B 124 N VAL B 100
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 VAL B 265 N LEU B 238
LINK OD2 ASP A 106 C20 OEH A 301 1555 1555 1.38
LINK OD2 ASP B 106 C20 OEH B 303 1555 1555 1.38
CISPEP 1 ASN A 41 PRO A 42 0 1.35
CISPEP 2 GLU A 214 PRO A 215 0 -7.32
CISPEP 3 THR A 242 PRO A 243 0 6.64
CISPEP 4 ASN B 41 PRO B 42 0 -0.45
CISPEP 5 GLU B 214 PRO B 215 0 -8.10
CISPEP 6 THR B 242 PRO B 243 0 5.12
CRYST1 44.150 47.340 78.470 97.67 90.19 113.54 P 1 2
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 0.022650 0.009866 0.001543 0.00000
SCALE2 0.000000 0.023041 0.003424 0.00000
SCALE3 0.000000 0.000000 0.012884 0.00000
TER 2371 ILE A 295
TER 4732 ILE B 295
MASTER 251 0 8 36 16 0 0 6 5472 2 114 46
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