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HEADER HYDROLASE 03-MAY-24 9F7B
TITLE THIOESTERASE DOMAIN (GBND6 TE DOMAIN) FROM THE GLADIOLIN PKS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-HYDROXYACYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA GLADIOLI;
SOURCE 3 ORGANISM_TAXID: 28095;
SOURCE 4 GENE: A8H28_02115;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIOESTERASE, ALPHA/BETA-HYDROLASE, POLYKETIDE SYNTHASE, GLADIOLIN
KEYWDS 2 BIOSYNTHESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.ALKHALAF,F.PANG,C.FAGE
REVDAT 1 14-MAY-25 9F7B 0
JRNL AUTH L.M.ALKHALAF,F.PANG
JRNL TITL THIOESTERASE DOMAIN (GBND6 TE DOMAIN) FROM THE GLADIOLIN PKS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0415
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 19199
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.927
REMARK 3 FREE R VALUE TEST SET COUNT : 946
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1320
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2275
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05400
REMARK 3 B22 (A**2) : 0.00800
REMARK 3 B33 (A**2) : -0.06300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.01100
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.189
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.166
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.500
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2350 ; 0.006 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 2150 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3206 ; 1.341 ; 1.668
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4916 ; 0.446 ; 1.579
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 296 ; 6.785 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 22 ; 6.331 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 328 ;14.804 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 346 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2868 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 580 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 475 ; 0.218 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 40 ; 0.192 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1146 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 140 ; 0.150 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1185 ; 1.979 ; 2.338
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1184 ; 1.962 ; 2.335
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1479 ; 3.117 ; 4.184
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1480 ; 3.121 ; 4.186
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1165 ; 2.334 ; 2.478
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1166 ; 2.333 ; 2.479
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1726 ; 3.626 ; 4.459
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1727 ; 3.625 ; 4.461
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 9F7B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAY-24.
REMARK 100 THE DEPOSITION ID IS D_1292135614.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-21
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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 : DIALS
REMARK 200 DATA SCALING SOFTWARE : DIALS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19199
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 43.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.15510
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.8700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : 0.65180
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.380
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 8000 AND 0.1 M CHES (PH 8.5).,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 30.00450
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 GLY A 2
REMARK 465 GLU A 3
REMARK 465 ARG A 4
REMARK 465 VAL A 5
REMARK 465 SER A 6
REMARK 465 ASP A 7
REMARK 465 THR A 8
REMARK 465 PRO A 9
REMARK 465 THR A 10
REMARK 465 GLN A 11
REMARK 465 ARG A 12
REMARK 465 ASP A 166
REMARK 465 LEU A 167
REMARK 465 ALA A 168
REMARK 465 GLU A 169
REMARK 465 VAL A 170
REMARK 465 SER A 313
REMARK 465 GLY A 314
REMARK 465 SER A 315
REMARK 465 THR A 316
REMARK 465 THR A 317
REMARK 465 ASP A 318
REMARK 465 GLN A 319
REMARK 465 ALA A 320
REMARK 465 GLY A 321
REMARK 465 ALA A 322
REMARK 465 LEU A 323
REMARK 465 LEU A 324
REMARK 465 VAL A 325
REMARK 465 SER A 326
REMARK 465 GLY A 327
REMARK 465 PRO A 328
REMARK 465 ALA A 329
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 ASP A 13 CG OD1 OD2
REMARK 470 ARG A 63 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 65 CG CD OE1 OE2
REMARK 470 ARG A 92 NE CZ NH1 NH2
REMARK 470 ARG A 95 CZ NH1 NH2
REMARK 470 LYS A 138 CG CD CE NZ
REMARK 470 ASP A 163 CG OD1 OD2
REMARK 470 ARG A 172 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 ARG A 191 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 212 CD NE CZ NH1 NH2
REMARK 470 ARG A 250 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 274 CZ NH1 NH2
REMARK 470 GLU A 308 CG CD OE1 OE2
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 SER A 100 -131.17 61.43
REMARK 500 PRO A 248 26.66 -79.49
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9F7B A 1 329 UNP A0A808VW73_BURGA
DBREF2 9F7B A A0A808VW73 5568 5896
SEQADV 9F7B MET A -20 UNP A0A808VW7 INITIATING METHIONINE
SEQADV 9F7B GLY A -19 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B SER A -18 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B SER A -17 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B HIS A -16 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B HIS A -15 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B HIS A -14 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B HIS A -13 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B HIS A -12 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B HIS A -11 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B SER A -10 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B SER A -9 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B GLY A -8 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B LEU A -7 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B VAL A -6 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B PRO A -5 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B ARG A -4 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B GLY A -3 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B SER A -2 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B HIS A -1 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B MET A 0 UNP A0A808VW7 EXPRESSION TAG
SEQADV 9F7B THR A 278 UNP A0A808VW7 ALA 5845 CONFLICT
SEQRES 1 A 350 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 350 LEU VAL PRO ARG GLY SER HIS MET ALA GLY GLU ARG VAL
SEQRES 3 A 350 SER ASP THR PRO THR GLN ARG ASP PRO VAL PHE GLU ILE
SEQRES 4 A 350 LEU GLN SER ARG GLY ARG ARG SER PRO ALA VAL TRP PHE
SEQRES 5 A 350 HIS GLY SER MET GLY THR VAL GLN ALA TYR LEU GLY LEU
SEQRES 6 A 350 ALA ARG ALA ILE GLY ASP GLU VAL PRO PHE HIS ALA PHE
SEQRES 7 A 350 GLN SER ARG GLY LEU ARG GLY GLU ASP ALA PRO LEU ALA
SEQRES 8 A 350 ASP LEU GLY GLU MET ALA ALA LEU TYR THR ARG ARG LEU
SEQRES 9 A 350 LEU ALA ARG GLN PRO ASP GLU SER ARG ALA PHE ARG LEU
SEQRES 10 A 350 GLY GLY TYR SER GLN GLY GLY LEU LEU ALA TYR GLU VAL
SEQRES 11 A 350 THR ARG GLN LEU GLN LEU ALA GLY ARG ARG VAL GLU SER
SEQRES 12 A 350 LEU VAL MET VAL ASP THR PRO TYR ALA TYR GLY ASP MET
SEQRES 13 A 350 ALA LEU LYS ASP ASP ASP ASP THR ASP SER LEU ARG LEU
SEQRES 14 A 350 ALA ILE VAL TYR VAL ASN LEU LEU LEU MET ASN GLY LEU
SEQRES 15 A 350 GLY ASP PHE SER ASP LEU ALA GLU VAL HIS ARG PRO GLY
SEQRES 16 A 350 ILE ASP PRO ALA GLU LEU LEU PRO ALA LEU VAL ARG ALA
SEQRES 17 A 350 GLY ILE ASP ARG GLY LEU PRO TYR THR PRO GLN ALA LEU
SEQRES 18 A 350 GLY GLN LEU ILE GLU ARG HIS HIS ARG VAL ALA ARG ALA
SEQRES 19 A 350 ASN GLU THR ALA ALA ARG THR TYR LEU PRO ALA ASP LEU
SEQRES 20 A 350 PRO HIS PRO GLY GLN PRO VAL VAL HIS TYR PHE ALA ARG
SEQRES 21 A 350 ARG HIS PRO GLN VAL TYR PHE ASP PRO ALA ARG PHE SER
SEQRES 22 A 350 GLY PRO MET VAL GLU TRP THR ASN ARG TYR PHE ALA ASP
SEQRES 23 A 350 LYS ASP CYS ALA SER ARG TRP GLN ARG HIS LEU PRO THR
SEQRES 24 A 350 TRP HIS HIS HIS ALA THR PRO ALA VAL ASP HIS PHE ALA
SEQRES 25 A 350 MET LEU THR ASP SER ALA SER PHE ALA ALA ILE VAL ARG
SEQRES 26 A 350 THR CYS ARG GLU LEU TYR LEU GLY SER GLY SER THR THR
SEQRES 27 A 350 ASP GLN ALA GLY ALA LEU LEU VAL SER GLY PRO ALA
FORMUL 2 HOH *173(H2 O)
HELIX 1 AA1 VAL A 38 ALA A 40 5 3
HELIX 2 AA2 TYR A 41 GLY A 49 1 9
HELIX 3 AA3 ASP A 71 GLN A 87 1 17
HELIX 4 AA4 SER A 100 ALA A 116 1 17
HELIX 5 AA5 ASP A 140 MET A 158 1 19
HELIX 6 AA6 ASP A 176 ARG A 191 1 16
HELIX 7 AA7 THR A 196 TYR A 221 1 26
HELIX 8 AA8 GLY A 253 ASP A 265 1 13
HELIX 9 AA9 ASP A 267 LEU A 276 1 10
HELIX 10 AB1 ASP A 288 MET A 292 5 5
HELIX 11 AB2 ASP A 295 LEU A 311 1 17
SHEET 1 AA1 7 PHE A 16 GLN A 20 0
SHEET 2 AA1 7 PHE A 54 PHE A 57 -1 O ALA A 56 N GLU A 17
SHEET 3 AA1 7 ALA A 28 PHE A 31 1 N ALA A 28 O HIS A 55
SHEET 4 AA1 7 PHE A 94 TYR A 99 1 O ARG A 95 N VAL A 29
SHEET 5 AA1 7 VAL A 120 VAL A 126 1 O VAL A 126 N GLY A 98
SHEET 6 AA1 7 VAL A 233 ALA A 238 1 O HIS A 235 N MET A 125
SHEET 7 AA1 7 TRP A 279 ALA A 283 1 O HIS A 282 N TYR A 236
CRYST1 37.745 60.009 63.472 90.00 95.79 90.00 P 1 21 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 0.026494 0.000000 0.002688 0.00000
SCALE2 0.000000 0.016664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015836 0.00000
TER 2285 GLY A 312
MASTER 332 0 0 11 7 0 0 6 2448 1 0 27
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