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HEADER HYDROLASE 02-FEB-22 7R0X
TITLE STRUCTURE OF THE BRANCHING THIOESTERASE FROM OOCYDIN BIOSYNTHESIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYKETIDE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OOCS TEB, THIOESTERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SERRATIA;
SOURCE 3 ORGANISM_TAXID: 613;
SOURCE 4 GENE: CT690_01900;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THIOESTERASE, POLYKETIDE, ACYLATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.FRALEY,J.PIEL
REVDAT 1 10-AUG-22 7R0X 0
JRNL AUTH A.E.FRALEY,C.DIETERICH,M.MABESOONE,H.A.MINAS,R.A.MEODED,
JRNL AUTH 2 F.HEMMERLING,J.PIEL
JRNL TITL STRUCTURE OF A PROMISCUOUS THIOESTERASE DOMAIN RESPONSIBLE
JRNL TITL 2 FOR BRANCHING ACYLATION IN POLYKETIDE BIOSYNTHESIS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 2022
JRNL REFN ESSN 1521-3773
JRNL PMID 35903999
JRNL DOI 10.1002/ANIE.202206385
REMARK 2
REMARK 2 RESOLUTION. 2.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19-4092
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) : 2.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 20593
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2041
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 40.7600 - 6.9700 1.00 1241 129 0.1878 0.2697
REMARK 3 2 6.9700 - 5.5300 1.00 1257 150 0.2304 0.2833
REMARK 3 3 5.5300 - 4.8400 1.00 1222 136 0.2011 0.2536
REMARK 3 4 4.8400 - 4.3900 1.00 1245 130 0.1802 0.2052
REMARK 3 5 4.3900 - 4.0800 1.00 1249 129 0.1753 0.2490
REMARK 3 6 4.0800 - 3.8400 1.00 1229 144 0.1864 0.2274
REMARK 3 7 3.8400 - 3.6500 1.00 1258 136 0.2120 0.2468
REMARK 3 8 3.6400 - 3.4900 1.00 1203 138 0.2265 0.2970
REMARK 3 9 3.4900 - 3.3500 1.00 1245 134 0.2509 0.3851
REMARK 3 10 3.3500 - 3.2400 1.00 1227 129 0.3085 0.3558
REMARK 3 11 3.2400 - 3.1400 1.00 1234 136 0.2925 0.2715
REMARK 3 12 3.1400 - 3.0500 1.00 1242 136 0.2969 0.3730
REMARK 3 13 3.0500 - 2.9700 1.00 1239 144 0.3139 0.3963
REMARK 3 14 2.9700 - 2.9000 1.00 1230 132 0.3236 0.3882
REMARK 3 15 2.8900 - 2.8300 0.99 1231 138 0.4031 0.3753
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) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.238
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 64.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.38
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 : 0.002 2480
REMARK 3 ANGLE : 0.512 3359
REMARK 3 CHIRALITY : 0.036 357
REMARK 3 PLANARITY : 0.005 435
REMARK 3 DIHEDRAL : 4.410 333
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 7R0X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292120701.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-21
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XDS, AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 144817
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.830
REMARK 200 RESOLUTION RANGE LOW (A) : 40.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.060
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.809M AMMONIUM SULFATE, 100MM HEPES
REMARK 280 PH 7.5, 4.14% PEG 8K (W/V), 3.95% PEG400 (V/V), VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293.1K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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,X,Z
REMARK 290 4555 Y,-X,Z
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+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 53.40900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.40900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 39.07000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 53.40900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.40900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.07000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 53.40900
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 53.40900
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 39.07000
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 53.40900
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 53.40900
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 39.07000
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: 15010 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 ALA A 1
REMARK 465 GLU A 2
REMARK 465 SER A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 PRO A 8
REMARK 465 THR A 9
REMARK 465 LEU A 10
REMARK 465 SER A 11
REMARK 465 ALA A 12
REMARK 465 GLU A 13
REMARK 465 GLN A 14
REMARK 465 GLY A 15
REMARK 465 ALA A 16
REMARK 465 THR A 17
REMARK 465 ALA A 18
REMARK 465 HIS A 19
REMARK 465 GLY A 20
REMARK 465 ARG A 21
REMARK 465 GLN A 22
REMARK 465 MET A 23
REMARK 465 GLY A 24
REMARK 465 LYS A 25
REMARK 465 ALA A 26
REMARK 465 TRP A 27
REMARK 465 LEU A 28
REMARK 465 LYS A 29
REMARK 465 GLN A 30
REMARK 465 SER A 189
REMARK 465 GLY A 190
REMARK 465 GLN A 191
REMARK 465 VAL A 192
REMARK 465 SER A 274
REMARK 465 SER A 275
REMARK 465 ASN A 276
REMARK 465 GLY A 277
REMARK 465 ALA A 278
REMARK 465 ARG A 279
REMARK 465 SER A 280
REMARK 465 ASP A 281
REMARK 465 LYS A 282
REMARK 465 GLY A 283
REMARK 465 ASN A 284
REMARK 465 THR A 285
REMARK 465 SER A 286
REMARK 465 SER A 287
REMARK 465 ALA A 288
REMARK 465 LEU A 289
REMARK 465 ALA A 290
REMARK 465 GLU A 291
REMARK 465 ASN A 292
REMARK 465 ALA A 354
REMARK 465 ARG A 355
REMARK 465 LYS A 356
REMARK 465 THR A 357
REMARK 465 THR A 358
REMARK 465 THR A 359
REMARK 465 ALA A 360
REMARK 465 ASP A 361
REMARK 465 ALA A 362
REMARK 465 GLU A 363
REMARK 465 GLU A 364
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 ARG A 42 35.51 -76.48
REMARK 500 ALA A 43 33.52 -95.64
REMARK 500 PRO A 58 -147.70 -81.35
REMARK 500 ARG A 90 35.69 -88.20
REMARK 500 SER A 123 -112.17 54.81
REMARK 500 ALA A 139 -157.22 -80.39
REMARK 500 GLU A 157 -70.35 -66.34
REMARK 500 GLU A 226 71.10 38.51
REMARK 500 ASN A 260 70.77 60.57
REMARK 500 ARG A 324 32.26 -97.02
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7R0X A 1 364 UNP A0A318P693_SERPL
DBREF2 7R0X A A0A318P693 3745 4108
SEQRES 1 A 364 ALA GLU SER THR GLU ALA ALA PRO THR LEU SER ALA GLU
SEQRES 2 A 364 GLN GLY ALA THR ALA HIS GLY ARG GLN MET GLY LYS ALA
SEQRES 3 A 364 TRP LEU LYS GLN TYR PRO GLU CYS ILE PRO LEU SER ARG
SEQRES 4 A 364 GLN LEU ARG ALA GLY ASP GLU ARG GLU HIS ASP ARG SER
SEQRES 5 A 364 ARG PHE TRP ILE HIS PRO LEU THR GLY SER THR GLY LEU
SEQRES 6 A 364 TYR LEU LYS VAL ALA GLU ASN LEU GLY ASP ASP TYR ALA
SEQRES 7 A 364 ILE TRP GLY ILE HIS SER ARG GLY PHE LEU THR ARG HIS
SEQRES 8 A 364 PRO PRO LEU LYS SER ILE GLU SER MSE ALA ASN TYR TYR
SEQRES 9 A 364 ILE GLU ILE LEU GLN ALA GLY ASN ALA THR GLY PRO TYR
SEQRES 10 A 364 GLU LEU ALA GLY TYR SER MSE GLY GLY ILE ILE ALA TYR
SEQRES 11 A 364 GLU MSE ALA ARG GLN LEU GLN LEU ALA GLY TYR ARG VAL
SEQRES 12 A 364 SER SER LEU ILE LEU LEU GLU PRO PRO PHE PRO HIS PRO
SEQRES 13 A 364 GLU HIS LEU HIS GLN SER SER PRO PHE TYR TYR HIS ASP
SEQRES 14 A 364 ALA LEU LEU MET SER ALA ASN PHE PHE LEU HIS TYR SER
SEQRES 15 A 364 LEU LYS ASP ILE VAL ALA SER GLY GLN VAL ALA PHE GLU
SEQRES 16 A 364 THR LEU ALA TYR ARG GLU GLN GLU LEU MET GLY ILE ASP
SEQRES 17 A 364 ALA ASP LYS GLN VAL THR TRP LEU ALA GLU GLY CYS LEU
SEQRES 18 A 364 ARG LYS GLY VAL GLU GLN PRO LEU SER VAL VAL LYS GLU
SEQRES 19 A 364 LYS ILE GLU ASN MSE ALA GLN ILE LEU LYS HIS ASN ARG
SEQRES 20 A 364 GLU ALA MET ALA ALA TYR VAL VAL LYS ALA LEU PRO ASN
SEQRES 21 A 364 ALA HIS ASP ILE ASP LEU HIS TYR MSE THR VAL SER GLN
SEQRES 22 A 364 SER SER ASN GLY ALA ARG SER ASP LYS GLY ASN THR SER
SEQRES 23 A 364 SER ALA LEU ALA GLU ASN ASN ARG HIS VAL LEU GLY GLU
SEQRES 24 A 364 ALA LEU THR HIS ASP GLU SER HIS CYS GLN ARG TRP LEU
SEQRES 25 A 364 ASP TYR LEU PRO GLY ALA GLN VAL PHE ARG THR ARG ALA
SEQRES 26 A 364 LYS ASP HIS PHE HIS LEU LEU SER GLU ARG GLU SER VAL
SEQRES 27 A 364 ALA MET ILE SER ASP ARG CYS ARG THR ILE TYR GLN ASN
SEQRES 28 A 364 ALA SER ALA ARG LYS THR THR THR ALA ASP ALA GLU GLU
MODRES 7R0X MSE A 100 MET MODIFIED RESIDUE
MODRES 7R0X MSE A 124 MET MODIFIED RESIDUE
MODRES 7R0X MSE A 132 MET MODIFIED RESIDUE
MODRES 7R0X MSE A 239 MET MODIFIED RESIDUE
MODRES 7R0X MSE A 269 MET MODIFIED RESIDUE
HET MSE A 100 8
HET MSE A 124 8
HET MSE A 132 8
HET MSE A 239 8
HET MSE A 269 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 2 HOH *39(H2 O)
HELIX 1 AA1 THR A 63 LEU A 65 5 3
HELIX 2 AA2 TYR A 66 ASN A 72 1 7
HELIX 3 AA3 SER A 96 ALA A 110 1 15
HELIX 4 AA4 SER A 123 ALA A 139 1 17
HELIX 5 AA5 HIS A 155 SER A 163 1 9
HELIX 6 AA6 TYR A 166 LEU A 183 1 18
HELIX 7 AA7 PHE A 194 ALA A 198 1 5
HELIX 8 AA8 ARG A 200 MET A 205 5 6
HELIX 9 AA9 LYS A 211 LYS A 223 1 13
HELIX 10 AB1 PRO A 228 ALA A 252 1 25
HELIX 11 AB2 ASN A 260 ILE A 264 5 5
HELIX 12 AB3 ASP A 304 ASP A 313 1 10
HELIX 13 AB4 GLU A 334 ASN A 351 1 18
SHEET 1 AA1 7 LEU A 37 ARG A 39 0
SHEET 2 AA1 7 TRP A 80 ILE A 82 -1 O GLY A 81 N SER A 38
SHEET 3 AA1 7 ARG A 53 ILE A 56 1 N TRP A 55 O TRP A 80
SHEET 4 AA1 7 TYR A 117 TYR A 122 1 O GLU A 118 N PHE A 54
SHEET 5 AA1 7 VAL A 143 LEU A 149 1 O LEU A 149 N GLY A 121
SHEET 6 AA1 7 ASP A 265 VAL A 271 1 O MSE A 269 N LEU A 148
SHEET 7 AA1 7 GLN A 319 THR A 323 1 O PHE A 321 N THR A 270
LINK C SER A 99 N MSE A 100 1555 1555 1.33
LINK C MSE A 100 N ALA A 101 1555 1555 1.33
LINK C SER A 123 N MSE A 124 1555 1555 1.33
LINK C MSE A 124 N GLY A 125 1555 1555 1.34
LINK C GLU A 131 N MSE A 132 1555 1555 1.33
LINK C MSE A 132 N ALA A 133 1555 1555 1.34
LINK C ASN A 238 N MSE A 239 1555 1555 1.33
LINK C MSE A 239 N ALA A 240 1555 1555 1.34
LINK C TYR A 268 N MSE A 269 1555 1555 1.33
LINK C MSE A 269 N THR A 270 1555 1555 1.33
CRYST1 106.818 106.818 78.140 90.00 90.00 90.00 I 4 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 0.009362 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009362 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012798 0.00000
TER 2419 SER A 353
MASTER 321 0 5 13 7 0 0 6 2457 1 50 28
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