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HEADER HYDROLASE 30-JUN-24 9CGO
TITLE TYLOSIN THIOESTERASE DOMAIN (TYLG5 TE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYLACTONE SYNTHASE MODULE 7;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES FRADIAE;
SOURCE 3 ORGANISM_TAXID: 1906;
SOURCE 4 GENE: TYLG;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIOESTERASE, NATURAL PRODUCTS, PKS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.SMITH,V.CHOUDHARY
REVDAT 1 18-SEP-24 9CGO 0
JRNL AUTH T.M.MCCULLOUGH,V.CHOUDHARY,D.L.AKEY,M.A.SKIBA,S.M.BERNARD,
JRNL AUTH 2 J.D.KITTENDORF,J.J.SCHMIDT,D.H.SHERMAN,J.L.SMITH
JRNL TITL SUBSTRATE TRAPPING IN POLYKETIDE SYNTHASE THIOESTERASE
JRNL TITL 2 DOMAINS: STRUCTURAL BASIS FOR MACROLACTONE FORMATION
JRNL REF ACS CATALYSIS V. 14 2024
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.4C03637
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21_5207
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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 39846
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 2042
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 49.2600 - 4.7600 1.00 2541 122 0.1932 0.2221
REMARK 3 2 4.7600 - 3.7800 1.00 2521 126 0.1721 0.1953
REMARK 3 3 3.7800 - 3.3000 1.00 2550 132 0.1747 0.2036
REMARK 3 4 3.3000 - 3.0000 1.00 2478 160 0.1760 0.1963
REMARK 3 5 3.0000 - 2.7900 1.00 2542 151 0.1884 0.2420
REMARK 3 6 2.7900 - 2.6200 1.00 2544 117 0.1866 0.2199
REMARK 3 7 2.6200 - 2.4900 1.00 2482 153 0.1817 0.2074
REMARK 3 8 2.4900 - 2.3800 1.00 2485 147 0.1704 0.2032
REMARK 3 9 2.3800 - 2.2900 1.00 2511 150 0.1719 0.2323
REMARK 3 10 2.2900 - 2.2100 1.00 2539 140 0.1576 0.1820
REMARK 3 11 2.2100 - 2.1400 1.00 2516 125 0.1520 0.2042
REMARK 3 12 2.1400 - 2.0800 1.00 2536 141 0.1493 0.1976
REMARK 3 13 2.0800 - 2.0300 1.00 2498 123 0.1575 0.2094
REMARK 3 14 2.0300 - 1.9800 1.00 2539 121 0.1601 0.2410
REMARK 3 15 1.9800 - 1.9300 1.00 2522 134 0.1653 0.2302
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.569
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.34
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 : 0.007 4125
REMARK 3 ANGLE : 0.992 5647
REMARK 3 CHIRALITY : 0.052 606
REMARK 3 PLANARITY : 0.010 750
REMARK 3 DIHEDRAL : 14.062 1433
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 9CGO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-24.
REMARK 100 THE DEPOSITION ID IS D_1000285422.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-12
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 : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39846
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 49.260
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M SODIUM CITRATE, 100 MM SODIUM
REMARK 280 MALONATE, 100 MM BISTRISPROPANE PH 6.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 194.98000
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 97.49000
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 146.23500
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 48.74500
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 243.72500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 THR A 1540
REMARK 465 GLY A 1541
REMARK 465 ALA A 1542
REMARK 465 ALA A 1543
REMARK 465 PRO A 1544
REMARK 465 ALA A 1545
REMARK 465 ASP A 1546
REMARK 465 ALA A 1547
REMARK 465 GLY A 1548
REMARK 465 GLU A 1599
REMARK 465 ASP A 1600
REMARK 465 ASP A 1734
REMARK 465 ILE A 1735
REMARK 465 GLY B 1597
REMARK 465 ALA B 1598
REMARK 465 GLU B 1599
REMARK 465 ASP B 1600
REMARK 465 THR B 1601
REMARK 465 ASP B 1734
REMARK 465 ILE B 1735
REMARK 465 PRO B 1736
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG1 THR B 1711 O HOH B 1901 1.75
REMARK 500 O HOH A 1990 O HOH A 1992 2.07
REMARK 500 OE2 GLU B 1695 O HOH B 1902 2.09
REMARK 500 O HOH B 1957 O HOH B 1987 2.10
REMARK 500 O HOH A 2001 O HOH B 2000 2.13
REMARK 500 O HOH A 1941 O HOH A 1975 2.13
REMARK 500 O HOH A 1978 O HOH A 1988 2.15
REMARK 500 O PRO B 1647 O HOH B 1903 2.16
REMARK 500 O HOH A 1949 O HOH A 1954 2.18
REMARK 500 OE2 GLU B 1664 O HOH B 1904 2.19
REMARK 500 O HOH A 1938 O HOH A 1946 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 1909 O HOH B 1984 6554 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 A1585 60.77 -107.99
REMARK 500 SER A1681 -139.38 57.84
REMARK 500 ASP A1780 -164.59 -114.50
REMARK 500 THR A1805 -91.85 -97.96
REMARK 500 ALA B1543 85.59 -152.48
REMARK 500 SER B1549 -14.83 -150.42
REMARK 500 ARG B1563 53.48 -118.67
REMARK 500 ASP B1585 57.88 -116.46
REMARK 500 ASP B1630 7.71 -68.27
REMARK 500 ALA B1671 -141.25 59.10
REMARK 500 SER B1681 -120.30 61.65
REMARK 500 ASP B1738 -169.34 -105.27
REMARK 500 ASP B1780 -166.90 -111.48
REMARK 500 ASN B1799 -167.59 -109.25
REMARK 500 THR B1805 -79.66 -133.83
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 A2009 DISTANCE = 7.15 ANGSTROMS
DBREF 9CGO A 1540 1820 UNP O33958 O33958_STRFR 1540 1820
DBREF 9CGO B 1540 1820 UNP O33958 O33958_STRFR 1540 1820
SEQRES 1 A 281 THR GLY ALA ALA PRO ALA ASP ALA GLY SER GLY LEU PRO
SEQRES 2 A 281 ALA LEU TYR ARG GLU ALA VAL ARG THR GLY ARG ALA ALA
SEQRES 3 A 281 GLU MSE ALA GLU LEU LEU ALA ALA ALA SER ARG PHE ARG
SEQRES 4 A 281 PRO ALA PHE GLY THR ALA ASP ARG GLN PRO VAL ALA LEU
SEQRES 5 A 281 VAL PRO LEU ALA ASP GLY ALA GLU ASP THR GLY LEU PRO
SEQRES 6 A 281 LEU LEU VAL GLY CYS ALA GLY THR ALA VAL ALA SER GLY
SEQRES 7 A 281 PRO VAL GLU PHE THR ALA PHE ALA GLY ALA LEU ALA ASP
SEQRES 8 A 281 LEU PRO ALA ALA ALA PRO MSE ALA ALA LEU PRO GLN PRO
SEQRES 9 A 281 GLY PHE LEU PRO GLY GLU ARG VAL PRO ALA THR PRO GLU
SEQRES 10 A 281 ALA LEU PHE GLU ALA GLN ALA GLU ALA LEU LEU ARG TYR
SEQRES 11 A 281 ALA ALA GLY ARG PRO PHE VAL LEU LEU GLY HIS SER ALA
SEQRES 12 A 281 GLY ALA ASN MSE ALA HIS ALA LEU THR ARG HIS LEU GLU
SEQRES 13 A 281 ALA ASN GLY GLY GLY PRO ALA GLY LEU VAL LEU MSE ASP
SEQRES 14 A 281 ILE TYR THR PRO ALA ASP PRO GLY ALA MSE GLY VAL TRP
SEQRES 15 A 281 ARG ASN ASP MSE PHE GLN TRP VAL TRP ARG ARG SER ASP
SEQRES 16 A 281 ILE PRO PRO ASP ASP HIS ARG LEU THR ALA MSE GLY ALA
SEQRES 17 A 281 TYR HIS ARG LEU LEU LEU ASP TRP SER PRO THR PRO VAL
SEQRES 18 A 281 ARG ALA PRO VAL LEU HIS LEU ARG ALA ALA GLU PRO MSE
SEQRES 19 A 281 GLY ASP TRP PRO PRO GLY ASP THR GLY TRP GLN SER HIS
SEQRES 20 A 281 TRP ASP GLY ALA HIS THR THR ALA GLY ILE PRO GLY ASN
SEQRES 21 A 281 HIS PHE THR MSE MSE THR GLU HIS ALA SER ALA ALA ALA
SEQRES 22 A 281 ARG LEU VAL HIS GLY TRP LEU ALA
SEQRES 1 B 281 THR GLY ALA ALA PRO ALA ASP ALA GLY SER GLY LEU PRO
SEQRES 2 B 281 ALA LEU TYR ARG GLU ALA VAL ARG THR GLY ARG ALA ALA
SEQRES 3 B 281 GLU MSE ALA GLU LEU LEU ALA ALA ALA SER ARG PHE ARG
SEQRES 4 B 281 PRO ALA PHE GLY THR ALA ASP ARG GLN PRO VAL ALA LEU
SEQRES 5 B 281 VAL PRO LEU ALA ASP GLY ALA GLU ASP THR GLY LEU PRO
SEQRES 6 B 281 LEU LEU VAL GLY CYS ALA GLY THR ALA VAL ALA SER GLY
SEQRES 7 B 281 PRO VAL GLU PHE THR ALA PHE ALA GLY ALA LEU ALA ASP
SEQRES 8 B 281 LEU PRO ALA ALA ALA PRO MSE ALA ALA LEU PRO GLN PRO
SEQRES 9 B 281 GLY PHE LEU PRO GLY GLU ARG VAL PRO ALA THR PRO GLU
SEQRES 10 B 281 ALA LEU PHE GLU ALA GLN ALA GLU ALA LEU LEU ARG TYR
SEQRES 11 B 281 ALA ALA GLY ARG PRO PHE VAL LEU LEU GLY HIS SER ALA
SEQRES 12 B 281 GLY ALA ASN MSE ALA HIS ALA LEU THR ARG HIS LEU GLU
SEQRES 13 B 281 ALA ASN GLY GLY GLY PRO ALA GLY LEU VAL LEU MSE ASP
SEQRES 14 B 281 ILE TYR THR PRO ALA ASP PRO GLY ALA MSE GLY VAL TRP
SEQRES 15 B 281 ARG ASN ASP MSE PHE GLN TRP VAL TRP ARG ARG SER ASP
SEQRES 16 B 281 ILE PRO PRO ASP ASP HIS ARG LEU THR ALA MSE GLY ALA
SEQRES 17 B 281 TYR HIS ARG LEU LEU LEU ASP TRP SER PRO THR PRO VAL
SEQRES 18 B 281 ARG ALA PRO VAL LEU HIS LEU ARG ALA ALA GLU PRO MSE
SEQRES 19 B 281 GLY ASP TRP PRO PRO GLY ASP THR GLY TRP GLN SER HIS
SEQRES 20 B 281 TRP ASP GLY ALA HIS THR THR ALA GLY ILE PRO GLY ASN
SEQRES 21 B 281 HIS PHE THR MSE MSE THR GLU HIS ALA SER ALA ALA ALA
SEQRES 22 B 281 ARG LEU VAL HIS GLY TRP LEU ALA
MODRES 9CGO MSE A 1567 MET MODIFIED RESIDUE
MODRES 9CGO MSE A 1637 MET MODIFIED RESIDUE
MODRES 9CGO MSE A 1686 MET MODIFIED RESIDUE
MODRES 9CGO MSE A 1707 MET MODIFIED RESIDUE
MODRES 9CGO MSE A 1718 MET MODIFIED RESIDUE
MODRES 9CGO MSE A 1725 MET MODIFIED RESIDUE
MODRES 9CGO MSE A 1745 MET MODIFIED RESIDUE
MODRES 9CGO MSE A 1773 MET MODIFIED RESIDUE
MODRES 9CGO MSE A 1803 MET MODIFIED RESIDUE
MODRES 9CGO MSE A 1804 MET MODIFIED RESIDUE
MODRES 9CGO MSE B 1567 MET MODIFIED RESIDUE
MODRES 9CGO MSE B 1637 MET MODIFIED RESIDUE
MODRES 9CGO MSE B 1686 MET MODIFIED RESIDUE
MODRES 9CGO MSE B 1707 MET MODIFIED RESIDUE
MODRES 9CGO MSE B 1718 MET MODIFIED RESIDUE
MODRES 9CGO MSE B 1725 MET MODIFIED RESIDUE
MODRES 9CGO MSE B 1745 MET MODIFIED RESIDUE
MODRES 9CGO MSE B 1773 MET MODIFIED RESIDUE
MODRES 9CGO MSE B 1803 MET MODIFIED RESIDUE
MODRES 9CGO MSE B 1804 MET MODIFIED RESIDUE
HET MSE A1567 8
HET MSE A1637 8
HET MSE A1686 8
HET MSE A1707 8
HET MSE A1718 8
HET MSE A1725 8
HET MSE A1745 8
HET MSE A1773 8
HET MSE A1803 8
HET MSE A1804 8
HET MSE B1567 8
HET MSE B1637 8
HET MSE B1686 8
HET MSE B1707 8
HET MSE B1718 8
HET MSE B1725 8
HET MSE B1745 8
HET MSE B1773 8
HET MSE B1803 8
HET MSE B1804 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 HOH *210(H2 O)
HELIX 1 AA1 SER A 1549 THR A 1561 1 13
HELIX 2 AA2 ARG A 1563 ARG A 1576 1 14
HELIX 3 AA3 GLY A 1617 GLU A 1620 5 4
HELIX 4 AA4 PHE A 1621 ASP A 1630 1 10
HELIX 5 AA5 THR A 1654 ALA A 1671 1 18
HELIX 6 AA6 SER A 1681 ASN A 1697 1 17
HELIX 7 AA7 GLY A 1716 TRP A 1721 1 6
HELIX 8 AA8 TRP A 1721 SER A 1733 1 13
HELIX 9 AA9 ASP A 1738 ASP A 1754 1 17
HELIX 10 AB1 PHE A 1801 THR A 1805 5 5
HELIX 11 AB2 HIS A 1807 ALA A 1820 1 14
HELIX 12 AB3 GLY B 1550 THR B 1561 1 12
HELIX 13 AB4 ARG B 1563 SER B 1575 1 13
HELIX 14 AB5 ARG B 1576 ARG B 1578 5 3
HELIX 15 AB6 GLY B 1617 GLU B 1620 5 4
HELIX 16 AB7 PHE B 1621 ASP B 1630 1 10
HELIX 17 AB8 THR B 1654 ALA B 1671 1 18
HELIX 18 AB9 SER B 1681 ASN B 1697 1 17
HELIX 19 AC1 GLY B 1716 TRP B 1721 1 6
HELIX 20 AC2 TRP B 1721 SER B 1733 1 13
HELIX 21 AC3 ASP B 1738 LEU B 1752 1 15
HELIX 22 AC4 PHE B 1801 THR B 1805 5 5
HELIX 23 AC5 HIS B 1807 LEU B 1819 1 13
SHEET 1 AA1 2 ALA A1580 PHE A1581 0
SHEET 2 AA1 2 VAL A1651 PRO A1652 1 O VAL A1651 N PHE A1581
SHEET 1 AA2 7 VAL A1592 ALA A1595 0
SHEET 2 AA2 7 MSE A1637 LEU A1640 -1 O MSE A1637 N ALA A1595
SHEET 3 AA2 7 LEU A1605 CYS A1609 1 N GLY A1608 O LEU A1640
SHEET 4 AA2 7 PHE A1675 HIS A1680 1 O LEU A1678 N CYS A1609
SHEET 5 AA2 7 GLY A1703 MSE A1707 1 O VAL A1705 N LEU A1677
SHEET 6 AA2 7 VAL A1764 ALA A1769 1 O LEU A1767 N LEU A1706
SHEET 7 AA2 7 THR A1792 ILE A1796 1 O ILE A1796 N ARG A1768
SHEET 1 AA3 2 ALA B1580 PHE B1581 0
SHEET 2 AA3 2 VAL B1651 PRO B1652 1 O VAL B1651 N PHE B1581
SHEET 1 AA4 6 MSE B1637 LEU B1640 0
SHEET 2 AA4 6 LEU B1605 CYS B1609 1 N LEU B1606 O ALA B1638
SHEET 3 AA4 6 PHE B1675 HIS B1680 1 O LEU B1678 N CYS B1609
SHEET 4 AA4 6 LEU B1704 MSE B1707 1 O VAL B1705 N LEU B1677
SHEET 5 AA4 6 VAL B1764 ALA B1769 1 O LEU B1765 N LEU B1706
SHEET 6 AA4 6 THR B1792 ILE B1796 1 O ALA B1794 N HIS B1766
LINK C GLU A1566 N MSE A1567 1555 1555 1.33
LINK C MSE A1567 N ALA A1568 1555 1555 1.34
LINK C PRO A1636 N MSE A1637 1555 1555 1.34
LINK C MSE A1637 N ALA A1638 1555 1555 1.34
LINK C ASN A1685 N MSE A1686 1555 1555 1.34
LINK C MSE A1686 N ALA A1687 1555 1555 1.33
LINK C LEU A1706 N MSE A1707 1555 1555 1.33
LINK C MSE A1707 N ASP A1708 1555 1555 1.33
LINK C ALA A1717 N MSE A1718 1555 1555 1.33
LINK C MSE A1718 N GLY A1719 1555 1555 1.33
LINK C ASP A1724 N MSE A1725 1555 1555 1.33
LINK C MSE A1725 N PHE A1726 1555 1555 1.34
LINK C ALA A1744 N MSE A1745 1555 1555 1.33
LINK C MSE A1745 N GLY A1746 1555 1555 1.34
LINK C PRO A1772 N MSE A1773 1555 1555 1.33
LINK C MSE A1773 N GLY A1774 1555 1555 1.34
LINK C THR A1802 N MSE A1803 1555 1555 1.33
LINK C MSE A1803 N MSE A1804 1555 1555 1.33
LINK C MSE A1804 N THR A1805 1555 1555 1.33
LINK C GLU B1566 N MSE B1567 1555 1555 1.33
LINK C MSE B1567 N ALA B1568 1555 1555 1.34
LINK C PRO B1636 N MSE B1637 1555 1555 1.33
LINK C MSE B1637 N ALA B1638 1555 1555 1.33
LINK C ASN B1685 N MSE B1686 1555 1555 1.34
LINK C MSE B1686 N ALA B1687 1555 1555 1.34
LINK C LEU B1706 N MSE B1707 1555 1555 1.33
LINK C MSE B1707 N ASP B1708 1555 1555 1.34
LINK C ALA B1717 N MSE B1718 1555 1555 1.33
LINK C MSE B1718 N GLY B1719 1555 1555 1.33
LINK C ASP B1724 N MSE B1725 1555 1555 1.33
LINK C MSE B1725 N PHE B1726 1555 1555 1.34
LINK C ALA B1744 N MSE B1745 1555 1555 1.34
LINK C MSE B1745 N GLY B1746 1555 1555 1.33
LINK C PRO B1772 N MSE B1773 1555 1555 1.33
LINK C MSE B1773 N GLY B1774 1555 1555 1.33
LINK C THR B1802 N MSE B1803 1555 1555 1.33
LINK C MSE B1803 N MSE B1804 1555 1555 1.33
LINK C MSE B1804 N THR B1805 1555 1555 1.33
CISPEP 1 THR A 1601 GLY A 1602 0 -12.77
CISPEP 2 PRO B 1647 GLY B 1648 0 -22.65
CRYST1 56.880 56.880 292.470 90.00 90.00 120.00 P 65 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 0.017581 0.010150 0.000000 0.00000
SCALE2 0.000000 0.020301 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003419 0.00000
TER 1987 ALA A1820
TER 4001 ALA B1820
MASTER 327 0 20 23 17 0 0 6 4209 2 196 44
END |