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HEADER HYDROLASE 12-OCT-17 6BA8
TITLE YBTT - TYPE II THIOESTERASE FROM YERSINIABACTIN NRPS/PKS BIOSYNTHETIC
TITLE 2 PATHWAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IRON AQUISITION YERSINIABACTIN SYNTHESIS ENZYME, YBTT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SURFACTIN SYNTHASE THIOESTERASE SUBUNIT, THIOESTERASE,
COMPND 5 YERSINIABACTIN SIDEROPHORE BIOSYNTHETIC PROTEIN, YERSINIABACTIN
COMPND 6 SYNTHETASE, THIOESTERASE COMPONENT;
COMPND 7 EC: 3.1.2.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: IRP4, SRFAD, A4T40_14730, AML07_28155, AUS26_21405,
SOURCE 5 AW106_20985, ECONIH1_11380, ERS085406_04094, ERS150876_03959,
SOURCE 6 FORC28_2175, MS6198_22290, SK85_02209, WM48_10340;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: ROSETTA2 (DE3)
KEYWDS THIOESTERASE, NON-RIBOSOMAL PEPTIDE SYNTHESIS, SIDERAPHORE SYNTHESIS,
KEYWDS 2 YERSINIABACTIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.J.BRETT,D.L.KOBER,S.I.OHLEMACHER,J.P.HENDERSON
REVDAT 2 07-NOV-18 6BA8 1 JRNL
REVDAT 1 31-OCT-18 6BA8 0
JRNL AUTH S.I.OHLEMACHER,Y.XU,D.L.KOBER,M.MALIK,J.C.NIX,T.J.BRETT,
JRNL AUTH 2 J.P.HENDERSON
JRNL TITL YBTT IS A LOW-SPECIFICITY TYPE II THIOESTERASE THAT
JRNL TITL 2 MAINTAINS PRODUCTION OF THE METALLOPHORE YERSINIABACTIN IN
JRNL TITL 3 PATHOGENIC ENTEROBACTERIA.
JRNL REF J. BIOL. CHEM. 2018
JRNL REFN ESSN 1083-351X
JRNL PMID 30355735
JRNL DOI 10.1074/JBC.RA118.005752
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 22676
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 1116
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 58.0929 - 3.7997 1.00 2915 142 0.1596 0.1850
REMARK 3 2 3.7997 - 3.0160 1.00 2736 147 0.1760 0.2298
REMARK 3 3 3.0160 - 2.6347 1.00 2683 160 0.2070 0.2470
REMARK 3 4 2.6347 - 2.3938 1.00 2707 126 0.2087 0.2407
REMARK 3 5 2.3938 - 2.2222 1.00 2684 127 0.2179 0.2832
REMARK 3 6 2.2222 - 2.0912 1.00 2690 106 0.2265 0.2837
REMARK 3 7 2.0912 - 1.9865 1.00 2653 148 0.2552 0.2643
REMARK 3 8 1.9865 - 1.9000 0.96 2492 160 0.3158 0.3506
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 2014
REMARK 3 ANGLE : 0.876 2748
REMARK 3 CHIRALITY : 0.053 297
REMARK 3 PLANARITY : 0.006 363
REMARK 3 DIHEDRAL : 2.739 1193
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 6BA8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1000230526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-17
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 : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CMOS
REMARK 200 DETECTOR MANUFACTURER : RDI CMOS_8M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22829
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 58.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.80
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.90
REMARK 200 R MERGE FOR SHELL (I) : 3.89600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.600
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: PDB ENTRY 3QMW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM TRI-SODIUM CITRATE, 1% PEG3350,
REMARK 280 0.5% N-DODECYL-B-D-MALTOSIDE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
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+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.15050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.15050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.15050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.15050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.15050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.15050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.15050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.15050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: 11190 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 325 LIES ON A SPECIAL POSITION.
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 -4
REMARK 465 MET A -3
REMARK 465 GLN A -2
REMARK 465 SER A -1
REMARK 465 ALA A 249
REMARK 465 MET A 250
REMARK 465 THR A 251
REMARK 465 ALA A 252
REMARK 465 TRP A 253
REMARK 465 GLN A 254
REMARK 465 LYS A 255
REMARK 465 GLN A 256
REMARK 465 PRO A 257
REMARK 465 SER A 258
REMARK 465 THR A 259
REMARK 465 SER A 260
REMARK 465 GLU A 261
REMARK 465 ARG A 262
REMARK 465 LYS A 263
REMARK 465 LEU A 264
REMARK 465 GLY A 265
REMARK 465 PRO A 266
REMARK 465 GLU A 267
REMARK 465 GLN A 268
REMARK 465 LYS A 269
REMARK 465 LEU A 270
REMARK 465 ILE A 271
REMARK 465 SER A 272
REMARK 465 GLU A 273
REMARK 465 GLU A 274
REMARK 465 ASP A 275
REMARK 465 LEU A 276
REMARK 465 ASN A 277
REMARK 465 SER A 278
REMARK 465 ALA A 279
REMARK 465 VAL A 280
REMARK 465 ASP A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 HIS A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
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 OG SER A 89 O HOH A 301 2.10
REMARK 500 O GLU A 57 O HOH A 302 2.14
REMARK 500 O HOH A 461 O HOH A 506 2.14
REMARK 500 O HOH A 382 O HOH A 450 2.18
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 NH2 ARG A 54 OE2 GLU A 74 4455 1.85
REMARK 500 O HOH A 332 O HOH A 361 3545 2.16
REMARK 500 O HOH A 486 O HOH A 497 4555 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 GLU A 35 117.21 -161.47
REMARK 500 ASP A 51 -137.19 46.09
REMARK 500 HIS A 55 6.03 -67.93
REMARK 500 SER A 89 -124.16 55.26
REMARK 500 PRO A 109 172.31 -59.85
REMARK 500 ASP A 224 -164.64 -102.66
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 A 510 DISTANCE = 6.91 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6BA9 RELATED DB: PDB
DBREF1 6BA8 A -2 262 UNP A0A061LQM0_ECOLX
DBREF2 6BA8 A A0A061LQM0 3 267
SEQADV 6BA8 MET A -4 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 MET A -3 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 LYS A 263 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 LEU A 264 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 GLY A 265 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 PRO A 266 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 GLU A 267 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 GLN A 268 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 LYS A 269 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 LEU A 270 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 ILE A 271 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 SER A 272 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 GLU A 273 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 GLU A 274 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 ASP A 275 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 LEU A 276 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 ASN A 277 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 SER A 278 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 ALA A 279 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 VAL A 280 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 ASP A 281 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 HIS A 282 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 HIS A 283 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 HIS A 284 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 HIS A 285 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 HIS A 286 UNP A0A061LQM EXPRESSION TAG
SEQADV 6BA8 HIS A 287 UNP A0A061LQM EXPRESSION TAG
SEQRES 1 A 292 MET MET GLN SER ALA MET CYS ILE PRO LEU TRP PRO ALA
SEQRES 2 A 292 ARG ASN GLY ASN THR ALA HIS LEU VAL MET CYS PRO PHE
SEQRES 3 A 292 ALA GLY GLY SER SER SER ALA PHE ARG HIS TRP GLN ALA
SEQRES 4 A 292 GLU GLN LEU ALA ASP CYS ALA LEU SER LEU VAL THR TRP
SEQRES 5 A 292 PRO GLY ARG ASP ARG LEU ARG HIS LEU GLU PRO LEU ARG
SEQRES 6 A 292 SER ILE THR GLN LEU ALA ALA LEU LEU ALA ASN GLU LEU
SEQRES 7 A 292 GLU ALA SER VAL SER PRO ASP THR PRO LEU LEU LEU ALA
SEQRES 8 A 292 GLY HIS SER MET GLY ALA GLN VAL ALA PHE GLU THR CYS
SEQRES 9 A 292 ARG LEU LEU GLU GLN ARG GLY LEU ALA PRO GLN GLY LEU
SEQRES 10 A 292 ILE ILE SER GLY CYS HIS ALA PRO HIS LEU HIS SER GLU
SEQRES 11 A 292 ARG GLN LEU SER HIS ARG ASP ASP ALA ASP PHE ILE ALA
SEQRES 12 A 292 GLU LEU ILE ASP ILE GLY GLY CYS SER PRO GLU LEU ARG
SEQRES 13 A 292 GLU ASN GLN GLU LEU MET SER LEU PHE LEU PRO LEU LEU
SEQRES 14 A 292 ARG ALA ASP PHE TYR ALA THR GLU SER TYR HIS TYR ASP
SEQRES 15 A 292 SER PRO ASP VAL CYS PRO PRO LEU ARG THR PRO ALA LEU
SEQRES 16 A 292 LEU LEU CYS GLY SER HIS ASP ARG GLU ALA SER TRP GLN
SEQRES 17 A 292 GLN VAL ASP ALA TRP ARG GLN TRP LEU SER HIS VAL THR
SEQRES 18 A 292 GLY PRO VAL VAL ILE ASP GLY ASP HIS PHE TYR PRO ILE
SEQRES 19 A 292 GLN GLN ALA ARG SER PHE PHE THR GLN ILE VAL ARG HIS
SEQRES 20 A 292 PHE PRO HIS ALA PHE SER ALA MET THR ALA TRP GLN LYS
SEQRES 21 A 292 GLN PRO SER THR SER GLU ARG LYS LEU GLY PRO GLU GLN
SEQRES 22 A 292 LYS LEU ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP
SEQRES 23 A 292 HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *210(H2 O)
HELIX 1 AA1 SER A 25 ALA A 28 5 4
HELIX 2 AA2 PHE A 29 ALA A 34 1 6
HELIX 3 AA3 ARG A 50 ARG A 54 5 5
HELIX 4 AA4 SER A 61 VAL A 77 1 17
HELIX 5 AA5 SER A 89 ARG A 105 1 17
HELIX 6 AA6 ASP A 132 GLY A 144 1 13
HELIX 7 AA7 SER A 147 GLU A 152 5 6
HELIX 8 AA8 ASN A 153 TYR A 174 1 22
HELIX 9 AA9 SER A 178 CYS A 182 5 5
HELIX 10 AB1 SER A 201 ALA A 207 1 7
HELIX 11 AB2 TRP A 208 LEU A 212 5 5
HELIX 12 AB3 PHE A 226 GLN A 231 1 6
HELIX 13 AB4 GLN A 231 PHE A 243 1 13
SHEET 1 AA1 7 CYS A 2 TRP A 6 0
SHEET 2 AA1 7 ALA A 41 VAL A 45 -1 O LEU A 42 N LEU A 5
SHEET 3 AA1 7 HIS A 15 CYS A 19 1 N LEU A 16 O ALA A 41
SHEET 4 AA1 7 LEU A 83 HIS A 88 1 O LEU A 84 N VAL A 17
SHEET 5 AA1 7 GLY A 111 SER A 115 1 O ILE A 113 N LEU A 85
SHEET 6 AA1 7 ALA A 189 GLY A 194 1 O LEU A 190 N ILE A 114
SHEET 7 AA1 7 VAL A 215 ILE A 221 1 O ILE A 221 N CYS A 193
CISPEP 1 GLY A 217 PRO A 218 0 3.98
CRYST1 82.301 82.301 81.935 90.00 90.00 90.00 P 4 21 2 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 0.012151 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012151 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012205 0.00000
TER 1957 SER A 248
MASTER 347 0 0 13 7 0 0 6 2166 1 0 23
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