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HEADER HYDROLASE 10-JUN-21 7OTS
TITLE CRYSTAL STRUCTURE OF HUMAN MONOACYLGLYCEROL LIPASE ABHD6 IN COMPLEX
TITLE 2 WITH OLEIC ACID AND OCTYL GLUCOSIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOACYLGLYCEROL LIPASE ABHD6;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 2-ARACHIDONOYLGLYCEROL HYDROLASE,ABHYDROLASE DOMAIN-
COMPND 5 CONTAINING PROTEIN 6;
COMPND 6 EC: 3.1.1.23;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ABHD6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA-HYDROLASE DOMAIN CONTAINING 6; 2-ARACHIDONOYLGLYCEROL
KEYWDS 2 HYDROLASE; MONOACYLGLYCEROL LIPASE ABHD6; ENDOCANNABINOID SYSTEM; 2-
KEYWDS 3 AG SIGNALLING, NERVOUS SYSTEM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.NAWROTEK,A.TALAGAS,L.VUILLARD,L.MIALLAU
REVDAT 1 23-JUN-21 7OTS 0
JRNL AUTH A.NAWROTEK,A.TALAGAS,L.VUILLARD
JRNL TITL CRYSTAL STRUCTURE OF HUMAN MONOACYLGLYCEROL LIPASE ABHD6 IN
JRNL TITL 2 COMPLEX WITH OLEIC ACID AND OCTYL GLUCOSIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.8
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 66.6
REMARK 3 NUMBER OF REFLECTIONS : 39001
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1921
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 8.47
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2686
REMARK 3 BIN FREE R VALUE : 0.4203
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 44
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4587
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 93
REMARK 3 SOLVENT ATOMS : 293
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.83880
REMARK 3 B22 (A**2) : 0.90600
REMARK 3 B33 (A**2) : 0.93280
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.53950
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.300
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.238
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.195
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.237
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.196
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4928 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6706 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1785 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 817 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4871 ; 10.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 608 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4238 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 0.98
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.06
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.68
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7OTS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-JUN-21.
REMARK 100 THE DEPOSITION ID IS D_1292116414.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41378
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.766
REMARK 200 RESOLUTION RANGE LOW (A) : 72.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.92300
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
REMARK 200 STARTING MODEL: 4OPM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 35 % PEG 3350,
REMARK 280 0.1 M MES PH 6.5, 0.5% BETA-OG, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.74700
REMARK 290 SMTRY3 2 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 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 SER A 41
REMARK 465 MET A 42
REMARK 465 ARG A 43
REMARK 465 ARG A 44
REMARK 465 ASP A 337
REMARK 465 GLY B 193
REMARK 465 SER B 194
REMARK 465 ALA B 195
REMARK 465 ALA B 196
REMARK 465 VAL B 197
REMARK 465 THR B 330
REMARK 465 ASP B 331
REMARK 465 ASN B 332
REMARK 465 ASN B 333
REMARK 465 LYS B 334
REMARK 465 LYS B 335
REMARK 465 LEU B 336
REMARK 465 ASP B 337
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER B 41 OG
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 LEU A 46 15.86 57.30
REMARK 500 GLU A 56 -120.31 59.22
REMARK 500 ALA A 82 -150.68 -98.76
REMARK 500 GLU A 109 -119.64 49.70
REMARK 500 ALA A 148 -115.04 51.89
REMARK 500 CYS A 172 56.66 32.25
REMARK 500 VAL A 280 -63.95 -97.88
REMARK 500 GLU B 56 -128.02 61.81
REMARK 500 ALA B 82 -152.54 -101.52
REMARK 500 ASN B 97 26.06 -79.63
REMARK 500 PRO B 106 123.13 -37.23
REMARK 500 GLU B 109 -117.53 48.81
REMARK 500 ALA B 148 -115.60 53.32
REMARK 500 CYS B 172 56.00 33.84
REMARK 500 VAL B 280 -60.34 -99.60
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7OTS A 43 337 UNP Q9BV23 ABHD6_HUMAN 43 337
DBREF 7OTS B 43 337 UNP Q9BV23 ABHD6_HUMAN 43 337
SEQADV 7OTS SER A 41 UNP Q9BV23 EXPRESSION TAG
SEQADV 7OTS MET A 42 UNP Q9BV23 EXPRESSION TAG
SEQADV 7OTS ALA A 148 UNP Q9BV23 SER 148 ENGINEERED MUTATION
SEQADV 7OTS SER B 41 UNP Q9BV23 EXPRESSION TAG
SEQADV 7OTS MET B 42 UNP Q9BV23 EXPRESSION TAG
SEQADV 7OTS ALA B 148 UNP Q9BV23 SER 148 ENGINEERED MUTATION
SEQRES 1 A 297 SER MET ARG ARG THR LEU GLY MET GLN VAL ARG TYR VAL
SEQRES 2 A 297 HIS HIS GLU ASP TYR GLN PHE CYS TYR SER PHE ARG GLY
SEQRES 3 A 297 ARG PRO GLY HIS LYS PRO SER ILE LEU MET LEU HIS GLY
SEQRES 4 A 297 PHE SER ALA HIS LYS ASP MET TRP LEU SER VAL VAL LYS
SEQRES 5 A 297 PHE LEU PRO LYS ASN LEU HIS LEU VAL CYS VAL ASP MET
SEQRES 6 A 297 PRO GLY HIS GLU GLY THR THR ARG SER SER LEU ASP ASP
SEQRES 7 A 297 LEU SER ILE ASP GLY GLN VAL LYS ARG ILE HIS GLN PHE
SEQRES 8 A 297 VAL GLU CYS LEU LYS LEU ASN LYS LYS PRO PHE HIS LEU
SEQRES 9 A 297 VAL GLY THR ALA MET GLY GLY GLN VAL ALA GLY VAL TYR
SEQRES 10 A 297 ALA ALA TYR TYR PRO SER ASP VAL SER SER LEU CYS LEU
SEQRES 11 A 297 VAL CYS PRO ALA GLY LEU GLN TYR SER THR ASP ASN GLN
SEQRES 12 A 297 PHE VAL GLN ARG LEU LYS GLU LEU GLN GLY SER ALA ALA
SEQRES 13 A 297 VAL GLU LYS ILE PRO LEU ILE PRO SER THR PRO GLU GLU
SEQRES 14 A 297 MET SER GLU MET LEU GLN LEU CYS SER TYR VAL ARG PHE
SEQRES 15 A 297 LYS VAL PRO GLN GLN ILE LEU GLN GLY LEU VAL ASP VAL
SEQRES 16 A 297 ARG ILE PRO HIS ASN ASN PHE TYR ARG LYS LEU PHE LEU
SEQRES 17 A 297 GLU ILE VAL SER GLU LYS SER ARG TYR SER LEU HIS GLN
SEQRES 18 A 297 ASN MET ASP LYS ILE LYS VAL PRO THR GLN ILE ILE TRP
SEQRES 19 A 297 GLY LYS GLN ASP GLN VAL LEU ASP VAL SER GLY ALA ASP
SEQRES 20 A 297 MET LEU ALA LYS SER ILE ALA ASN CYS GLN VAL GLU LEU
SEQRES 21 A 297 LEU GLU ASN CYS GLY HIS SER VAL VAL MET GLU ARG PRO
SEQRES 22 A 297 ARG LYS THR ALA LYS LEU ILE ILE ASP PHE LEU ALA SER
SEQRES 23 A 297 VAL HIS ASN THR ASP ASN ASN LYS LYS LEU ASP
SEQRES 1 B 297 SER MET ARG ARG THR LEU GLY MET GLN VAL ARG TYR VAL
SEQRES 2 B 297 HIS HIS GLU ASP TYR GLN PHE CYS TYR SER PHE ARG GLY
SEQRES 3 B 297 ARG PRO GLY HIS LYS PRO SER ILE LEU MET LEU HIS GLY
SEQRES 4 B 297 PHE SER ALA HIS LYS ASP MET TRP LEU SER VAL VAL LYS
SEQRES 5 B 297 PHE LEU PRO LYS ASN LEU HIS LEU VAL CYS VAL ASP MET
SEQRES 6 B 297 PRO GLY HIS GLU GLY THR THR ARG SER SER LEU ASP ASP
SEQRES 7 B 297 LEU SER ILE ASP GLY GLN VAL LYS ARG ILE HIS GLN PHE
SEQRES 8 B 297 VAL GLU CYS LEU LYS LEU ASN LYS LYS PRO PHE HIS LEU
SEQRES 9 B 297 VAL GLY THR ALA MET GLY GLY GLN VAL ALA GLY VAL TYR
SEQRES 10 B 297 ALA ALA TYR TYR PRO SER ASP VAL SER SER LEU CYS LEU
SEQRES 11 B 297 VAL CYS PRO ALA GLY LEU GLN TYR SER THR ASP ASN GLN
SEQRES 12 B 297 PHE VAL GLN ARG LEU LYS GLU LEU GLN GLY SER ALA ALA
SEQRES 13 B 297 VAL GLU LYS ILE PRO LEU ILE PRO SER THR PRO GLU GLU
SEQRES 14 B 297 MET SER GLU MET LEU GLN LEU CYS SER TYR VAL ARG PHE
SEQRES 15 B 297 LYS VAL PRO GLN GLN ILE LEU GLN GLY LEU VAL ASP VAL
SEQRES 16 B 297 ARG ILE PRO HIS ASN ASN PHE TYR ARG LYS LEU PHE LEU
SEQRES 17 B 297 GLU ILE VAL SER GLU LYS SER ARG TYR SER LEU HIS GLN
SEQRES 18 B 297 ASN MET ASP LYS ILE LYS VAL PRO THR GLN ILE ILE TRP
SEQRES 19 B 297 GLY LYS GLN ASP GLN VAL LEU ASP VAL SER GLY ALA ASP
SEQRES 20 B 297 MET LEU ALA LYS SER ILE ALA ASN CYS GLN VAL GLU LEU
SEQRES 21 B 297 LEU GLU ASN CYS GLY HIS SER VAL VAL MET GLU ARG PRO
SEQRES 22 B 297 ARG LYS THR ALA LYS LEU ILE ILE ASP PHE LEU ALA SER
SEQRES 23 B 297 VAL HIS ASN THR ASP ASN ASN LYS LYS LEU ASP
HET BOG A 601 20
HET OLA A 602 20
HET SO4 A 603 5
HET SO4 A 604 5
HET OLA B 401 20
HET GOL B 402 6
HET GOL B 403 6
HET GOL B 404 6
HET SO4 B 405 5
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETNAM OLA OLEIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN BOG BETA-OCTYLGLUCOSIDE; OCTYL BETA-D-GLUCOSIDE; OCTYL D-
HETSYN 2 BOG GLUCOSIDE; OCTYL GLUCOSIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 BOG C14 H28 O6
FORMUL 4 OLA 2(C18 H34 O2)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 8 GOL 3(C3 H8 O3)
FORMUL 12 HOH *293(H2 O)
HELIX 1 AA1 HIS A 83 MET A 86 5 4
HELIX 2 AA2 TRP A 87 LYS A 92 1 6
HELIX 3 AA3 SER A 120 LYS A 136 1 17
HELIX 4 AA4 LEU A 137 LYS A 140 5 4
HELIX 5 AA5 ALA A 148 TYR A 161 1 14
HELIX 6 AA6 ASN A 182 GLY A 193 1 12
HELIX 7 AA7 ALA A 196 ILE A 200 5 5
HELIX 8 AA8 THR A 206 SER A 218 1 13
HELIX 9 AA9 PRO A 225 VAL A 235 1 11
HELIX 10 AB1 ARG A 236 PRO A 238 5 3
HELIX 11 AB2 HIS A 239 VAL A 251 1 13
HELIX 12 AB3 TYR A 257 MET A 263 1 7
HELIX 13 AB4 ASP A 264 ILE A 266 5 3
HELIX 14 AB5 SER A 284 ILE A 293 1 10
HELIX 15 AB6 SER A 307 ARG A 312 1 6
HELIX 16 AB7 ARG A 312 LYS A 335 1 24
HELIX 17 AB8 MET B 42 LEU B 46 1 5
HELIX 18 AB9 HIS B 83 MET B 86 5 4
HELIX 19 AC1 TRP B 87 LYS B 92 1 6
HELIX 20 AC2 SER B 120 LYS B 136 1 17
HELIX 21 AC3 LEU B 137 LYS B 140 5 4
HELIX 22 AC4 ALA B 148 TYR B 161 1 14
HELIX 23 AC5 ASN B 182 GLN B 192 1 11
HELIX 24 AC6 THR B 206 SER B 218 1 13
HELIX 25 AC7 PRO B 225 ILE B 237 1 13
HELIX 26 AC8 HIS B 239 SER B 252 1 14
HELIX 27 AC9 SER B 252 TYR B 257 1 6
HELIX 28 AD1 TYR B 257 MET B 263 1 7
HELIX 29 AD2 ASP B 264 ILE B 266 5 3
HELIX 30 AD3 VAL B 283 ILE B 293 1 11
HELIX 31 AD4 SER B 307 ARG B 312 1 6
HELIX 32 AD5 ARG B 312 ASN B 329 1 18
SHEET 1 AA1 8 GLN A 49 HIS A 55 0
SHEET 2 AA1 8 TYR A 58 ARG A 65 -1 O TYR A 58 N HIS A 55
SHEET 3 AA1 8 LEU A 100 VAL A 103 -1 O CYS A 102 N SER A 63
SHEET 4 AA1 8 ILE A 74 LEU A 77 1 N MET A 76 O VAL A 101
SHEET 5 AA1 8 PHE A 142 THR A 147 1 O VAL A 145 N LEU A 75
SHEET 6 AA1 8 VAL A 165 VAL A 171 1 O VAL A 171 N GLY A 146
SHEET 7 AA1 8 THR A 270 GLY A 275 1 O GLN A 271 N LEU A 170
SHEET 8 AA1 8 CYS A 296 LEU A 301 1 O LEU A 301 N TRP A 274
SHEET 1 AA2 8 GLN B 49 HIS B 55 0
SHEET 2 AA2 8 TYR B 58 ARG B 65 -1 O PHE B 60 N VAL B 53
SHEET 3 AA2 8 LEU B 100 VAL B 103 -1 O CYS B 102 N SER B 63
SHEET 4 AA2 8 ILE B 74 LEU B 77 1 N MET B 76 O VAL B 101
SHEET 5 AA2 8 PHE B 142 THR B 147 1 O VAL B 145 N LEU B 75
SHEET 6 AA2 8 VAL B 165 VAL B 171 1 O VAL B 171 N GLY B 146
SHEET 7 AA2 8 THR B 270 GLY B 275 1 O GLN B 271 N LEU B 170
SHEET 8 AA2 8 CYS B 296 LEU B 301 1 O GLU B 299 N ILE B 272
CRYST1 60.815 71.494 77.830 90.00 111.11 90.00 P 1 21 1 4
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 0.016443 0.000000 0.006348 0.00000
SCALE2 0.000000 0.013987 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013773 0.00000
TER 2354 LEU A 336
TER 4673 ASN B 329
MASTER 275 0 9 32 16 0 0 6 4973 2 93 46
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