HEADER TRANSFERASE 11-NOV-09 2WY2
TITLE NMR STRUCTURE OF THE IIACHITOBIOSE-IIBCHITOBIOSE PHOSPHORYL TRANSITION
TITLE 2 STATE COMPLEX OF THE N,N'-DIACETYLCHITOBOISE BRANCE OF THE E. COLI
TITLE 3 PHOSPHOTRANSFERASE SYSTEM.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N\,N'-DIACETYLCHITOBIOSE-SPECIFIC PHOSPHOTRANSFERASE ENZYME
COMPND 3 IIA COMPONENT;
COMPND 4 CHAIN: A, B, C;
COMPND 5 FRAGMENT: RESIDUES 14-116;
COMPND 6 SYNONYM: IIACHB, PTS SYSTEM N\,N'-DIACETYLCHITOBIOSE-SPECIFIC EIIA
COMPND 7 COMPONENT, EIIA-CHB, EIII-CHB;
COMPND 8 EC: 2.7.1.-;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: N\,N'-DIACETYLCHITOBIOSE-SPECIFIC PHOSPHOTRANSFERASE ENZYME
COMPND 13 IIB COMPONENT;
COMPND 14 CHAIN: D;
COMPND 15 SYNONYM: IIBCHB, PTS SYSTEM N\,N'-DIACETYLCHITOBIOSE-SPECIFIC EIIB
COMPND 16 COMPONENT;
COMPND 17 EC: 2.7.1.69;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 496008;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 8 ORGANISM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS KINASE, PHOSPHOTRANSFERASE SYSTEM, CHITOBIOSE, TRANSFERASE, SUGAR
KEYWDS 2 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 64
MDLTYP RESTRAINED MINIMIZED AVERAGE, MODEL 1
AUTHOR Y.S.SANG,M.CAI,G.M.CLORE
REVDAT 5 16-OCT-19 2WY2 1 COMPND SOURCE REMARK
REVDAT 4 19-APR-17 2WY2 1 REMARK
REVDAT 3 25-JUL-12 2WY2 1 REMARK VERSN DBREF MASTER
REVDAT 2 09-FEB-10 2WY2 1 JRNL
REVDAT 1 08-DEC-09 2WY2 0
JRNL AUTH Y.S.JUNG,M.CAI,G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF THE IIACHITOBOSE-IIBCHITOBIOSE COMPLEX
JRNL TITL 2 OF THE N,N'-DIACETYLCHITOBIOSE BRANCH OF THE ESCHERICHIA
JRNL TITL 3 COLI PHOSPHOTRANSFER SYSTEM
JRNL REF J.BIOL.CHEM. V. 285 4173 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 19959833
JRNL DOI 10.1074/JBC.M109.080937
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.TANG,D.C.J.WILLIAMS,R.GHIRLANDO,G.M.CLORE
REMARK 1 TITL SOLUTION STRUCTURE OF ENZYME IIA(CHITOBIOSE) FROM THE
REMARK 1 TITL 2 N,N'-DIACETYLCHITOBIOSE BRANCH OF THE ESCHERICHIA COLI
REMARK 1 TITL 3 PHOSPHOTRANSFERASE SYSTEM.
REMARK 1 REF J.BIOL.CHEM. V. 280 11770 2005
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 15654077
REMARK 1 DOI 10.1074/JBC.M414300200
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.L.VAN MONTFORT,T.PIJNING,K.H.KALK,J.REIZER,M.H.J.SAIER,
REMARK 1 AUTH 2 M.M.THUNNISSEN,G.T.ROBILLARD,B.W.DIJKSTRA
REMARK 1 TITL THE STRUCTURE OF AN ENERGY-COUPLING PROTEIN FROM BACTERIA,
REMARK 1 TITL 2 IIBCELLOBIOSE, REVEALS SIMILARITY TO EUKARYOTIC PROTEIN
REMARK 1 TITL 3 TYROSINE PHOSPHATASES.
REMARK 1 REF STRUCTURE V. 5 217 1997
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 9032081
REMARK 1 DOI 10.1016/S0969-2126(97)00180-9
REMARK 1 REFERENCE 3
REMARK 1 AUTH E.AB,G.K.SCHUURMAN-WOLTERS,D.NIJLANT,K.DIJKSTRA,M.H.SAIER,
REMARK 1 AUTH 2 G.T.ROBILLARD,R.M.SCHEEK
REMARK 1 TITL NMR STRUCTURE OF CYSTEINYL-PHOSPHORYLATED ENZYME IIB OF THE
REMARK 1 TITL 2 N,N'-DIACETYLCHITOBIOSE-SPECIFIC
REMARK 1 TITL 3 PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM OF
REMARK 1 TITL 4 ESCHERICHIA COLI.
REMARK 1 REF J.MOL.BIOL. V. 308 993 2001
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 11352587
REMARK 1 DOI 10.1006/JMBI.2001.4623
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.23
REMARK 3 AUTHORS : SCHWIETERS,KUSZEWSKI,CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS SOLVED ON THE BASIS
REMARK 3 OF THE COORDINATES OF THE UNPHOSPHORYLATED COMPLEX 2WWV. TO
REMARK 3 SOLVE THE TRANSITION STATE COMPLEX, THE COORDINATES OF THE
REMARK 3 UNPHOSPHORYLATED COMPLEX 2WWV ARE HELD FIXED WITH THE EXCEPTION
REMARK 3 OF THE ACTIVE SITE LOOP OF IIBCHB, THE ACTIVE SITE OF IIACHB,
REMARK 3 THE PHOSPHORYL GROUP, AND INTERFACIAL SIDE CHAINS IN THE
REMARK 3 IMMEDIATE VICINITY OF THE ACTIVE SITE AND THE PHOSPHORYL GROUP
REMARK 3 WHICH ARE GIVEN TORSION DEGREES OF FREEDOM. THE ACTIVE SITE LOOP
REMARK 3 OF IIBCHB COMPRISES RESIDUES 9-16 OF CHAIN D. THE ACTIVE SITE
REMARK 3 REGION OF IIACHB COMPRISES RESIDUES 74 TO 79 OF CHAINS A, B AND
REMARK 3 C. THE EXPERIMENTAL NMR RESTRAINTS ARE IDENTICAL TO THOSE USED
REMARK 3 TO CALCULATE 2WWV EXCEPT FOR THE DIPOLAR COUPLINGS WHICH WERE
REMARK 3 OBTAINED FROM FREE PHOSPHORYLATED IIBCHB. FOR FURTHER DETAILS
REMARK 3 SEE THE JNRL CITATION ABOVE.
REMARK 4
REMARK 4 2WY2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1290041701.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308.0
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ; 900
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 64
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 64
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NONE
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASP 92 TO LEU
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASP 92 TO LEU
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, ASP 92 TO LEU
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 O GLU B 3 H VAL B 7 1.45
REMARK 500 O GLU A 3 H VAL A 7 1.46
REMARK 500 O GLU C 3 H VAL C 7 1.46
REMARK 500 O CYS D 10 H GLU D 41 1.48
REMARK 500 O ALA B 1 H GLU B 5 1.49
REMARK 500 O ALA C 1 H GLU C 5 1.50
REMARK 500 O ALA A 1 H GLU A 5 1.50
REMARK 500 O MET D 14 H SER D 17 1.53
REMARK 500 O LEU A 48 H HIS A 52 1.59
REMARK 500 O VAL C 75 H LEU C 79 1.60
REMARK 500 O LEU A 94 HD1 HIS A 98 1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 HIS A 76 CG HIS A 76 CD2 0.057
REMARK 500 2 VAL A 75 C HIS A 76 N 0.308
REMARK 500 3 VAL A 75 C HIS A 76 N 0.308
REMARK 500 4 VAL A 75 C HIS A 76 N 0.308
REMARK 500 5 VAL A 75 C HIS A 76 N 0.309
REMARK 500 6 VAL A 75 C HIS A 76 N 0.308
REMARK 500 7 VAL A 75 C HIS A 76 N 0.308
REMARK 500 8 VAL A 75 C HIS A 76 N 0.308
REMARK 500 9 VAL A 75 C HIS A 76 N 0.309
REMARK 500 10 VAL A 75 C HIS A 76 N 0.308
REMARK 500 11 VAL A 75 C HIS A 76 N 0.308
REMARK 500 12 VAL A 75 C HIS A 76 N 0.308
REMARK 500 13 VAL A 75 C HIS A 76 N 0.307
REMARK 500 14 VAL A 75 C HIS A 76 N 0.309
REMARK 500 15 VAL A 75 C HIS A 76 N 0.308
REMARK 500 16 VAL A 75 C HIS A 76 N 0.308
REMARK 500 17 VAL A 75 C HIS A 76 N 0.308
REMARK 500 18 VAL A 75 C HIS A 76 N 0.309
REMARK 500 19 VAL A 75 C HIS A 76 N 0.309
REMARK 500 20 VAL A 75 C HIS A 76 N 0.308
REMARK 500 21 VAL A 75 C HIS A 76 N 0.308
REMARK 500 22 VAL A 75 C HIS A 76 N 0.308
REMARK 500 23 VAL A 75 C HIS A 76 N 0.308
REMARK 500 24 VAL A 75 C HIS A 76 N 0.307
REMARK 500 25 VAL A 75 C HIS A 76 N 0.308
REMARK 500 26 VAL A 75 C HIS A 76 N 0.309
REMARK 500 27 VAL A 75 C HIS A 76 N 0.308
REMARK 500 28 VAL A 75 C HIS A 76 N 0.309
REMARK 500 29 VAL A 75 C HIS A 76 N 0.308
REMARK 500 30 VAL A 75 C HIS A 76 N 0.309
REMARK 500 31 VAL A 75 C HIS A 76 N 0.308
REMARK 500 32 VAL A 75 C HIS A 76 N 0.308
REMARK 500 33 VAL A 75 C HIS A 76 N 0.308
REMARK 500 34 VAL A 75 C HIS A 76 N 0.308
REMARK 500 35 VAL A 75 C HIS A 76 N 0.308
REMARK 500 36 VAL A 75 C HIS A 76 N 0.309
REMARK 500 37 VAL A 75 C HIS A 76 N 0.308
REMARK 500 38 VAL A 75 C HIS A 76 N 0.308
REMARK 500 39 VAL A 75 C HIS A 76 N 0.308
REMARK 500 40 VAL A 75 C HIS A 76 N 0.308
REMARK 500 41 VAL A 75 C HIS A 76 N 0.308
REMARK 500 42 VAL A 75 C HIS A 76 N 0.308
REMARK 500 43 VAL A 75 C HIS A 76 N 0.308
REMARK 500 44 VAL A 75 C HIS A 76 N 0.308
REMARK 500 45 VAL A 75 C HIS A 76 N 0.308
REMARK 500 46 VAL A 75 C HIS A 76 N 0.309
REMARK 500 47 VAL A 75 C HIS A 76 N 0.309
REMARK 500 48 VAL A 75 C HIS A 76 N 0.309
REMARK 500 49 VAL A 75 C HIS A 76 N 0.308
REMARK 500 50 VAL A 75 C HIS A 76 N 0.308
REMARK 500
REMARK 500 THIS ENTRY HAS 64 BOND DEVIATIONS.
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 1 GLU A 2 -86.05 -24.58
REMARK 500 1 LYS A 67 -81.72 -67.41
REMARK 500 1 LEU A 101 2.76 -63.90
REMARK 500 1 LYS A 102 -60.87 81.31
REMARK 500 1 GLU B 2 -86.04 -24.80
REMARK 500 1 LYS B 67 -81.63 -67.45
REMARK 500 1 LEU B 101 3.42 -64.09
REMARK 500 1 LYS B 102 -60.80 80.29
REMARK 500 1 GLU C 2 -85.87 -24.15
REMARK 500 1 LYS C 67 -81.68 -67.45
REMARK 500 1 LEU C 101 2.13 -63.43
REMARK 500 1 LYS C 102 -61.00 82.09
REMARK 500 1 MET D 14 -71.98 -107.52
REMARK 500 2 GLU A 2 -86.05 -24.58
REMARK 500 2 LYS A 67 -81.72 -67.41
REMARK 500 2 LEU A 101 2.76 -63.90
REMARK 500 2 LYS A 102 -60.87 81.31
REMARK 500 2 GLU B 2 -86.04 -24.80
REMARK 500 2 LYS B 67 -81.63 -67.45
REMARK 500 2 LEU B 101 3.42 -64.09
REMARK 500 2 LYS B 102 -60.80 80.29
REMARK 500 2 GLU C 2 -85.87 -24.15
REMARK 500 2 LYS C 67 -81.68 -67.45
REMARK 500 2 LEU C 101 2.13 -63.43
REMARK 500 2 LYS C 102 -61.00 82.09
REMARK 500 2 MET D 14 -72.21 -105.26
REMARK 500 3 GLU A 2 -86.05 -24.58
REMARK 500 3 LYS A 67 -81.72 -67.41
REMARK 500 3 LEU A 101 2.76 -63.90
REMARK 500 3 LYS A 102 -60.87 81.31
REMARK 500 3 GLU B 2 -86.04 -24.80
REMARK 500 3 LYS B 67 -81.63 -67.45
REMARK 500 3 LEU B 101 3.42 -64.09
REMARK 500 3 LYS B 102 -60.80 80.29
REMARK 500 3 GLU C 2 -85.87 -24.15
REMARK 500 3 LYS C 67 -81.68 -67.45
REMARK 500 3 LEU C 101 2.13 -63.43
REMARK 500 3 LYS C 102 -61.00 82.09
REMARK 500 3 MET D 14 -72.37 -105.38
REMARK 500 4 GLU A 2 -86.05 -24.58
REMARK 500 4 LYS A 67 -81.72 -67.41
REMARK 500 4 LEU A 101 2.76 -63.90
REMARK 500 4 LYS A 102 -60.87 81.31
REMARK 500 4 GLU B 2 -86.04 -24.80
REMARK 500 4 LYS B 67 -81.63 -67.45
REMARK 500 4 LEU B 101 3.42 -64.09
REMARK 500 4 LYS B 102 -60.80 80.29
REMARK 500 4 GLU C 2 -85.87 -24.15
REMARK 500 4 LYS C 67 -81.68 -67.45
REMARK 500 4 LEU C 101 2.13 -63.43
REMARK 500
REMARK 500 THIS ENTRY HAS 845 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 PHOSPHORYL GROUP (PO3): THIS IS A PLANAR PHOSPHORYL GROUP
REMARK 600 IN A PENTACOORDINATE TRANSITION STATE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO3 D 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WWV RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE IIACHITOBIOSE- IIBCHITOBIOSE COMPLEX OF THE N,
REMARK 900 N'- DIACETYLCHITOBOISE BRANCE OF THE E. COLI PHOSPHOTRANSFERASE
REMARK 900 SYSTEM.
REMARK 900 RELATED ID: 1WCR RELATED DB: PDB
REMARK 900 TRIMERIC STRUCTURE OF THE ENZYME IIA FROM ESCHERICHIA COLI
REMARK 900 PHOSPHOTRANSFERASE SYSTEM SPECIFIC FOR N,N'-DIACETYLCHITOBIOSE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 1 IN CHAINS A, B AND C CORRESPONDS TO RESIDUE 14
REMARK 999 OF WILD TYPE IIACHB, RESIDUE 76 IS A HIS.
REMARK 999 TO OBTAIN WILD TYPE NUMBERING ADD 14. IN THE CONSTRUCT
REMARK 999 EMPLOYED THE 1ST 13 RESIDUES OF THE WILD TYPE HAVE BEEN
REMARK 999 DELETED.
REMARK 999 CHAIN D SEQUENCE STARTS AT RESIDUE 3
REMARK 999 CHAIN D BEST MATCH AGAINST UNIPROT SEQUENCE DATABASE WAS
REMARK 999 FOUND TO BE C3T7F7. CHAIN D IS CHEMICALLY SYNTHESIZED.
DBREF 2WY2 A 1 103 UNP P69791 PTQA_ECOLI 14 116
DBREF 2WY2 B 1 103 UNP P69791 PTQA_ECOLI 14 116
DBREF 2WY2 C 1 103 UNP P69791 PTQA_ECOLI 14 116
DBREF 2WY2 D 3 105 UNP C3T7F7 C3T7F7_ECOLX 3 105
SEQADV 2WY2 LEU A 79 UNP P69791 ASP 92 ENGINEERED MUTATION
SEQADV 2WY2 LEU B 79 UNP P69791 ASP 92 ENGINEERED MUTATION
SEQADV 2WY2 LEU C 79 UNP P69791 ASP 92 ENGINEERED MUTATION
SEQRES 1 A 103 ALA GLU GLU LEU GLU GLU VAL VAL MET GLY LEU ILE ILE
SEQRES 2 A 103 ASN SER GLY GLN ALA ARG SER LEU ALA TYR ALA ALA LEU
SEQRES 3 A 103 LYS GLN ALA LYS GLN GLY ASP PHE ALA ALA ALA LYS ALA
SEQRES 4 A 103 MET MET ASP GLN SER ARG MET ALA LEU ASN GLU ALA HIS
SEQRES 5 A 103 LEU VAL GLN THR LYS LEU ILE GLU GLY ASP ALA GLY GLU
SEQRES 6 A 103 GLY LYS MET LYS VAL SER LEU VAL LEU VAL HIS ALA GLN
SEQRES 7 A 103 LEU HIS LEU MET THR SER MET LEU ALA ARG GLU LEU ILE
SEQRES 8 A 103 THR GLU LEU ILE GLU LEU HIS GLU LYS LEU LYS ALA
SEQRES 1 B 103 ALA GLU GLU LEU GLU GLU VAL VAL MET GLY LEU ILE ILE
SEQRES 2 B 103 ASN SER GLY GLN ALA ARG SER LEU ALA TYR ALA ALA LEU
SEQRES 3 B 103 LYS GLN ALA LYS GLN GLY ASP PHE ALA ALA ALA LYS ALA
SEQRES 4 B 103 MET MET ASP GLN SER ARG MET ALA LEU ASN GLU ALA HIS
SEQRES 5 B 103 LEU VAL GLN THR LYS LEU ILE GLU GLY ASP ALA GLY GLU
SEQRES 6 B 103 GLY LYS MET LYS VAL SER LEU VAL LEU VAL HIS ALA GLN
SEQRES 7 B 103 LEU HIS LEU MET THR SER MET LEU ALA ARG GLU LEU ILE
SEQRES 8 B 103 THR GLU LEU ILE GLU LEU HIS GLU LYS LEU LYS ALA
SEQRES 1 C 103 ALA GLU GLU LEU GLU GLU VAL VAL MET GLY LEU ILE ILE
SEQRES 2 C 103 ASN SER GLY GLN ALA ARG SER LEU ALA TYR ALA ALA LEU
SEQRES 3 C 103 LYS GLN ALA LYS GLN GLY ASP PHE ALA ALA ALA LYS ALA
SEQRES 4 C 103 MET MET ASP GLN SER ARG MET ALA LEU ASN GLU ALA HIS
SEQRES 5 C 103 LEU VAL GLN THR LYS LEU ILE GLU GLY ASP ALA GLY GLU
SEQRES 6 C 103 GLY LYS MET LYS VAL SER LEU VAL LEU VAL HIS ALA GLN
SEQRES 7 C 103 LEU HIS LEU MET THR SER MET LEU ALA ARG GLU LEU ILE
SEQRES 8 C 103 THR GLU LEU ILE GLU LEU HIS GLU LYS LEU LYS ALA
SEQRES 1 D 103 LYS LYS HIS ILE TYR LEU PHE CYS SER ALA GLY MET SER
SEQRES 2 D 103 THR SER LEU LEU VAL SER LYS MET ARG ALA GLN ALA GLU
SEQRES 3 D 103 LYS TYR GLU VAL PRO VAL ILE ILE GLU ALA PHE PRO GLU
SEQRES 4 D 103 THR LEU ALA GLY GLU LYS GLY GLN ASN ALA ASP VAL VAL
SEQRES 5 D 103 LEU LEU GLY PRO GLN ILE ALA TYR MET LEU PRO GLU ILE
SEQRES 6 D 103 GLN ARG LEU LEU PRO ASN LYS PRO VAL GLU VAL ILE ASP
SEQRES 7 D 103 SER LEU LEU TYR GLY LYS VAL ASP GLY LEU GLY VAL LEU
SEQRES 8 D 103 LYS ALA ALA VAL ALA ALA ILE LYS LYS ALA ALA ALA
HET PO3 D 200 4
HETNAM PO3 PHOSPHITE ION
FORMUL 5 PO3 O3 P 3-
HELIX 1 1 ALA A 1 GLN A 31 1 31
HELIX 2 2 ASP A 33 GLY A 61 1 29
HELIX 3 3 LEU A 72 LEU A 101 1 30
HELIX 4 4 ALA B 1 GLN B 31 1 31
HELIX 5 5 ASP B 33 GLY B 61 1 29
HELIX 6 6 LEU B 72 LEU B 101 1 30
HELIX 7 7 ALA C 1 GLN C 31 1 31
HELIX 8 8 ASP C 33 GLY C 61 1 29
HELIX 9 9 LEU C 72 LEU C 101 1 30
HELIX 10 10 MET D 14 TYR D 30 1 17
HELIX 11 11 LEU D 43 GLN D 49 1 7
HELIX 12 12 PRO D 58 TYR D 62 5 5
HELIX 13 13 MET D 63 LEU D 71 1 9
HELIX 14 14 ASP D 80 LYS D 86 1 7
HELIX 15 15 ASP D 88 ALA D 105 1 18
SHEET 1 DA 4 VAL D 34 PRO D 40 0
SHEET 2 DA 4 LYS D 4 CYS D 10 1 O LYS D 4 N ILE D 35
SHEET 3 DA 4 VAL D 53 LEU D 56 1 O VAL D 53 N TYR D 7
SHEET 4 DA 4 VAL D 76 VAL D 78 1 O GLU D 77 N LEU D 56
SITE 1 AC1 8 ILE A 12 HIS A 76 CYS D 10 SER D 11
SITE 2 AC1 8 ALA D 12 GLY D 13 MET D 14 SER D 15
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END