| content |
HEADER HYDROLASE 12-OCT-17 6BA9
TITLE YBTT - TYPE II THIOESTERASE FROM YERSINIABACTIN NRPS/PKS BIOSYNTHETIC
TITLE 2 PATHWAY- S89A MUTANT
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;
COMPND 9 MUTATION: 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 6BA9 1 JRNL
REVDAT 1 31-OCT-18 6BA9 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. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 55425
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2790
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 47.5512 - 3.7996 1.00 2906 157 0.1642 0.1736
REMARK 3 2 3.7996 - 3.0160 1.00 2748 150 0.1551 0.1597
REMARK 3 3 3.0160 - 2.6348 1.00 2679 178 0.1594 0.1720
REMARK 3 4 2.6348 - 2.3939 1.00 2698 147 0.1488 0.1736
REMARK 3 5 2.3939 - 2.2223 1.00 2689 129 0.1430 0.1488
REMARK 3 6 2.2223 - 2.0913 1.00 2629 191 0.1385 0.1520
REMARK 3 7 2.0913 - 1.9866 1.00 2680 138 0.1459 0.1652
REMARK 3 8 1.9866 - 1.9001 1.00 2633 148 0.1503 0.1678
REMARK 3 9 1.9001 - 1.8269 1.00 2683 112 0.1560 0.1572
REMARK 3 10 1.8269 - 1.7639 1.00 2668 113 0.1689 0.2251
REMARK 3 11 1.7639 - 1.7087 1.00 2637 149 0.1730 0.1801
REMARK 3 12 1.7087 - 1.6599 1.00 2660 131 0.1728 0.2131
REMARK 3 13 1.6599 - 1.6162 1.00 2630 131 0.1740 0.1969
REMARK 3 14 1.6162 - 1.5768 1.00 2691 105 0.1880 0.2141
REMARK 3 15 1.5768 - 1.5409 1.00 2623 163 0.2073 0.2154
REMARK 3 16 1.5409 - 1.5081 1.00 2618 131 0.2178 0.2804
REMARK 3 17 1.5081 - 1.4780 0.99 2610 138 0.2490 0.2645
REMARK 3 18 1.4780 - 1.4501 0.97 2541 127 0.2794 0.2750
REMARK 3 19 1.4501 - 1.4242 0.92 2398 150 0.3010 0.3053
REMARK 3 20 1.4242 - 1.4000 0.84 2214 102 0.3331 0.3765
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.80
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 : 0.008 2013
REMARK 3 ANGLE : 0.974 2747
REMARK 3 CHIRALITY : 0.077 297
REMARK 3 PLANARITY : 0.007 363
REMARK 3 DIHEDRAL : 14.687 722
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 6BA9 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_1000230532.
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 : 55628
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 58.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 11.90
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 1.86500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.700
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 (%): 48.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM DI-AMMONIUM HYDROGEN CITRATE,
REMARK 280 21% PEG3350, VAPOR DIFFUSION, HANGING DROP, 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 41.22500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.22500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.22500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.22500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.22500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.22500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.22500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.22500
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: 11210 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 305 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 441 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 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 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 C ALA A 0 H MET A 1 1.24
REMARK 500 HG SER A 124 O HOH A 302 1.57
REMARK 500 O HOH A 485 O HOH A 559 1.84
REMARK 500 O HOH A 577 O HOH A 590 1.93
REMARK 500 SG CYS A 182 O HOH A 519 2.01
REMARK 500 O HOH A 541 O HOH A 559 2.08
REMARK 500 O HOH A 313 O HOH A 481 2.08
REMARK 500 O HOH A 486 O HOH A 527 2.08
REMARK 500 O HOH A 302 O HOH A 445 2.11
REMARK 500 OE1 GLN A 110 O HOH A 301 2.11
REMARK 500 O HOH A 389 O HOH A 512 2.14
REMARK 500 O HOH A 457 O HOH A 516 2.15
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 A 323 O HOH A 323 7556 1.48
REMARK 500 O HOH A 527 O HOH A 527 2665 1.77
REMARK 500 O HOH A 314 O HOH A 518 7555 1.94
REMARK 500 O HOH A 570 O HOH A 578 3545 2.03
REMARK 500 O HOH A 449 O HOH A 573 4455 2.07
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 A 51 -133.92 55.24
REMARK 500 ALA A 89 -123.75 58.03
REMARK 500 HIS A 175 139.78 -170.32
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 598 DISTANCE = 6.97 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6BA8 RELATED DB: PDB
DBREF1 6BA9 A 0 262 UNP A0A061LQM0_ECOLX
DBREF2 6BA9 A A0A061LQM0 5 267
SEQADV 6BA9 ALA A 89 UNP A0A061LQM SER 94 ENGINEERED MUTATION
SEQRES 1 A 263 ALA MET CYS ILE PRO LEU TRP PRO ALA ARG ASN GLY ASN
SEQRES 2 A 263 THR ALA HIS LEU VAL MET CYS PRO PHE ALA GLY GLY SER
SEQRES 3 A 263 SER SER ALA PHE ARG HIS TRP GLN ALA GLU GLN LEU ALA
SEQRES 4 A 263 ASP CYS ALA LEU SER LEU VAL THR TRP PRO GLY ARG ASP
SEQRES 5 A 263 ARG LEU ARG HIS LEU GLU PRO LEU ARG SER ILE THR GLN
SEQRES 6 A 263 LEU ALA ALA LEU LEU ALA ASN GLU LEU GLU ALA SER VAL
SEQRES 7 A 263 SER PRO ASP THR PRO LEU LEU LEU ALA GLY HIS ALA MET
SEQRES 8 A 263 GLY ALA GLN VAL ALA PHE GLU THR CYS ARG LEU LEU GLU
SEQRES 9 A 263 GLN ARG GLY LEU ALA PRO GLN GLY LEU ILE ILE SER GLY
SEQRES 10 A 263 CYS HIS ALA PRO HIS LEU HIS SER GLU ARG GLN LEU SER
SEQRES 11 A 263 HIS ARG ASP ASP ALA ASP PHE ILE ALA GLU LEU ILE ASP
SEQRES 12 A 263 ILE GLY GLY CYS SER PRO GLU LEU ARG GLU ASN GLN GLU
SEQRES 13 A 263 LEU MET SER LEU PHE LEU PRO LEU LEU ARG ALA ASP PHE
SEQRES 14 A 263 TYR ALA THR GLU SER TYR HIS TYR ASP SER PRO ASP VAL
SEQRES 15 A 263 CYS PRO PRO LEU ARG THR PRO ALA LEU LEU LEU CYS GLY
SEQRES 16 A 263 SER HIS ASP ARG GLU ALA SER TRP GLN GLN VAL ASP ALA
SEQRES 17 A 263 TRP ARG GLN TRP LEU SER HIS VAL THR GLY PRO VAL VAL
SEQRES 18 A 263 ILE ASP GLY ASP HIS PHE TYR PRO ILE GLN GLN ALA ARG
SEQRES 19 A 263 SER PHE PHE THR GLN ILE VAL ARG HIS PHE PRO HIS ALA
SEQRES 20 A 263 PHE SER ALA MET THR ALA TRP GLN LYS GLN PRO SER THR
SEQRES 21 A 263 SER GLU ARG
FORMUL 2 HOH *298(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 ALA 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
HELIX 14 AB5 PHE A 243 SER A 248 1 6
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 MET A 18 O SER A 43
SHEET 4 AA1 7 LEU A 83 HIS A 88 1 O ALA A 86 N CYS A 19
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 5.52
CRYST1 82.450 82.450 82.043 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 0.012129 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012129 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012189 0.00000
TER 3830 SER A 248
MASTER 337 0 0 14 7 0 0 6 2253 1 0 21
END |