HEADER TRANSFERASE 04-NOV-98 3EZE
TITLE COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-
TITLE 2 CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR,
TITLE 3 RESTRAINED REGULARIZED MEAN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PHOSPHOTRANSFERASE SYSTEM, ENZYME I);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AMINO-TERMINAL DOMAIN RESIDUES 1 - 259;
COMPND 5 EC: 2.7.3.9;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN (PHOSPHOTRANSFERASE SYSTEM, HPR);
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: GI698;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PLP2;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 10 ORGANISM_TAXID: 562;
SOURCE 11 STRAIN: GI698;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PSP100
KEYWDS PHOSPHOTRANSFERASE, TRANSFERASE, KINASE, SUGAR TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,D.S.GARRETT,A.M.GRONENBORN
REVDAT 5 27-DEC-23 3EZE 1 REMARK
REVDAT 4 16-MAR-22 3EZE 1 REMARK
REVDAT 3 24-FEB-09 3EZE 1 VERSN
REVDAT 2 29-DEC-99 3EZE 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 16-DEC-98 3EZE 0
JRNL AUTH D.S.GARRETT,Y.J.SEOK,A.PETERKOFSKY,A.M.GRONENBORN,G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF THE 40,000 MR PHOSPHORYL TRANSFER
JRNL TITL 2 COMPLEX BETWEEN THE N-TERMINAL DOMAIN OF ENZYME I AND HPR.
JRNL REF NAT.STRUCT.BIOL. V. 6 166 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10048929
JRNL DOI 10.1038/5854
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.S.GARRETT,Y.J.SEOK,A.PETERKOFSKY,G.M.CLORE,A.M.GRONENBORN
REMARK 1 TITL TAUTOMERIC STATE AND PKA OF THE PHOSPHORYLATED ACTIVE SITE
REMARK 1 TITL 2 HISTIDINE IN THE N-TERMINAL DOMAIN OF ENZYME I OF THE
REMARK 1 TITL 3 ESCHERICHIA COLI PHOSPHOENOLPYRUVATE: SUGAR
REMARK 1 TITL 4 PHOSPHOTRANSFERASE SYSTEM
REMARK 1 REF PROTEIN SCI. V. 7 789 1998
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.S.GARRETT,Y.J.SEOK,D.I.LIAO,A.PETERKOFSKY,A.M.GRONENBORN,
REMARK 1 AUTH 2 G.M.CLORE
REMARK 1 TITL SOLUTION STRUCTURE OF THE 30 KDA N-TERMINAL DOMAIN OF ENZYME
REMARK 1 TITL 2 I OF THE ESCHERICHIA COLI PHOSPHOENOLPYRUVATE:SUGAR
REMARK 1 TITL 3 PHOSPHOTRANSFERASE SYSTEM BY MULTIDIMENSIONAL NMR
REMARK 1 REF BIOCHEMISTRY V. 36 2517 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.S.GARRETT,Y.J.SEOK,A.PETERKOFSKY,G.M.CLORE,A.M.GRONENBORN
REMARK 1 TITL IDENTIFICATION BY NMR OF THE BINDING SURFACE FOR THE
REMARK 1 TITL 2 HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR ON THE
REMARK 1 TITL 3 N-TERMINAL DOMAIN OF ENZYME I OF THE ESCHERICHIA COLI
REMARK 1 TITL 4 PHOSPHOTRANSFERASE SYSTEM
REMARK 1 REF BIOCHEMISTRY V. 36 4393 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING
REMARK 3 PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE
REMARK 3 PROGRAM CNS MODIFIED TO INCORPORATE COUPLING CONSTANT RESTRAINTS
REMARK 3 (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104, 99-103),
REMARK 3 CARBON CHEMICAL SHIFT RESTRAINTS, (KUSZEWSKI ET AL. (1995) J.
REMARK 3 MAGN. RESON. SERIES B 106, 92-96) RESTRAINTS, AND RESIDUAL DIPOLAR
REMARK 3 COUPLING RESTRAINTS (CLORE ET AL. J. MAGN. RESON 131, 159-162
REMARK 3 (1998); J. MAGN 133, 216-221 (1998)).
REMARK 3
REMARK 3 IN THIS ENTRY THE LAST COLUMN REPRESENTS THE AVERAGE RMS
REMARK 3 DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING
REMARK 3 STRUCTURES AND THE MEAN COORDINATE POSITIONS. THE LAST
REMARK 3 COLUMN IN THE INDIVIDUAL SA STRUCTURES HAS NO MEANING. BEST
REMARK 3 FITTING TO GENERATE THE AVERAGE STRUCTURE IS WITH RESPECT
REMARK 3 TO RESIDUES 1 - 250
REMARK 3 (RESIDUES 251 - 259 ARE DISORDERED IN SOLUTION) OF ENZYME I
REMARK 3 AND RESIDUES 301-385 OF HPR. RESIDUES 251-259 ARE OMITTED
REMARK 3 FROM THE MEAN STRUCTURE
REMARK 4
REMARK 4 3EZE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-98.
REMARK 100 THE DEPOSITION ID IS D_1000000219.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 7.00
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; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS (SEE ABOVE)
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : REGULARIZED MEAN STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE 3D STRUCTURE OF THE EIN-HPR COMPLEX WAS SOLVED BY
REMARK 210 MULTI HETERONUCLEAR NMR AND IS BASED ON 5475
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 LYS A 250
REMARK 465 ALA A 251
REMARK 465 GLU A 252
REMARK 465 LEU A 253
REMARK 465 ALA A 254
REMARK 465 LYS A 255
REMARK 465 LEU A 256
REMARK 465 LYS A 257
REMARK 465 ASP A 258
REMARK 465 ARG A 259
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 LEU B 350 H LEU B 353 1.44
REMARK 500 O ALA A 91 H ASP A 95 1.55
REMARK 500 OG SER A 188 HG1 THR A 190 1.56
REMARK 500 O PRO B 318 H PHE B 322 1.59
REMARK 500 NE2 HIS A 189 P PO3 B 600 2.08
REMARK 500 ND1 HIS B 315 P PO3 B 600 2.12
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 LEU A 6 102.07 52.45
REMARK 500 LYS A 49 -74.90 -64.62
REMARK 500 ALA A 50 -36.86 -38.57
REMARK 500 ASP A 148 96.34 69.03
REMARK 500 PRO A 165 -34.57 -39.25
REMARK 500 GLN A 170 37.66 -92.92
REMARK 500 ALA A 183 -160.40 -58.00
REMARK 500 SER A 207 32.09 -155.50
REMARK 500 ASP A 215 6.99 80.65
REMARK 500 ALA A 222 15.64 47.20
REMARK 500 VAL A 223 -43.41 -131.83
REMARK 500 ASN B 338 70.80 41.64
REMARK 500 GLN B 351 -21.02 -37.68
REMARK 500 ALA B 373 -77.68 -45.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO3 B 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EZA RELATED DB: PDB
REMARK 900 RELATED ID: 3EZB RELATED DB: PDB
DBREF 3EZE A 1 259 UNP P08839 PT1_ECOLI 1 259
DBREF 3EZE B 301 385 UNP P0AA04 PTHP_ECOLI 1 85
SEQRES 1 A 259 MET ILE SER GLY ILE LEU ALA SER PRO GLY ILE ALA PHE
SEQRES 2 A 259 GLY LYS ALA LEU LEU LEU LYS GLU ASP GLU ILE VAL ILE
SEQRES 3 A 259 ASP ARG LYS LYS ILE SER ALA ASP GLN VAL ASP GLN GLU
SEQRES 4 A 259 VAL GLU ARG PHE LEU SER GLY ARG ALA LYS ALA SER ALA
SEQRES 5 A 259 GLN LEU GLU THR ILE LYS THR LYS ALA GLY GLU THR PHE
SEQRES 6 A 259 GLY GLU GLU LYS GLU ALA ILE PHE GLU GLY HIS ILE MET
SEQRES 7 A 259 LEU LEU GLU ASP GLU GLU LEU GLU GLN GLU ILE ILE ALA
SEQRES 8 A 259 LEU ILE LYS ASP LYS HIS MET THR ALA ASP ALA ALA ALA
SEQRES 9 A 259 HIS GLU VAL ILE GLU GLY GLN ALA SER ALA LEU GLU GLU
SEQRES 10 A 259 LEU ASP ASP GLU TYR LEU LYS GLU ARG ALA ALA ASP VAL
SEQRES 11 A 259 ARG ASP ILE GLY LYS ARG LEU LEU ARG ASN ILE LEU GLY
SEQRES 12 A 259 LEU LYS ILE ILE ASP LEU SER ALA ILE GLN ASP GLU VAL
SEQRES 13 A 259 ILE LEU VAL ALA ALA ASP LEU THR PRO SER GLU THR ALA
SEQRES 14 A 259 GLN LEU ASN LEU LYS LYS VAL LEU GLY PHE ILE THR ASP
SEQRES 15 A 259 ALA GLY GLY ARG THR SER HIS THR SER ILE MET ALA ARG
SEQRES 16 A 259 SER LEU GLU LEU PRO ALA ILE VAL GLY THR GLY SER VAL
SEQRES 17 A 259 THR SER GLN VAL LYS ASN ASP ASP TYR LEU ILE LEU ASP
SEQRES 18 A 259 ALA VAL ASN ASN GLN VAL TYR VAL ASN PRO THR ASN GLU
SEQRES 19 A 259 VAL ILE ASP LYS MET ARG ALA VAL GLN GLU GLN VAL ALA
SEQRES 20 A 259 SER GLU LYS ALA GLU LEU ALA LYS LEU LYS ASP ARG
SEQRES 1 B 85 MET PHE GLN GLN GLU VAL THR ILE THR ALA PRO ASN GLY
SEQRES 2 B 85 LEU HIS THR ARG PRO ALA ALA GLN PHE VAL LYS GLU ALA
SEQRES 3 B 85 LYS GLY PHE THR SER GLU ILE THR VAL THR SER ASN GLY
SEQRES 4 B 85 LYS SER ALA SER ALA LYS SER LEU PHE LYS LEU GLN THR
SEQRES 5 B 85 LEU GLY LEU THR GLN GLY THR VAL VAL THR ILE SER ALA
SEQRES 6 B 85 GLU GLY GLU ASP GLU GLN LYS ALA VAL GLU HIS LEU VAL
SEQRES 7 B 85 LYS LEU MET ALA GLU LEU GLU
HET PO3 B 600 4
HETNAM PO3 PHOSPHITE ION
FORMUL 3 PO3 O3 P 3-
HELIX 1 1 ALA A 33 THR A 64 1 32
HELIX 2 2 GLU A 67 LEU A 80 1 14
HELIX 3 3 GLU A 83 LYS A 96 1 14
HELIX 4 4 ALA A 100 GLU A 116 1 17
HELIX 5 5 GLU A 121 LEU A 142 1 22
HELIX 6 6 LEU A 149 ALA A 151 5 3
HELIX 7 7 PRO A 165 ALA A 169 1 5
HELIX 8 8 HIS A 189 LEU A 197 1 9
HELIX 9 9 VAL A 208 GLN A 211 1 4
HELIX 10 10 ASN A 233 SER A 248 1 16
HELIX 11 11 THR B 316 GLY B 328 1 13
HELIX 12 12 LEU B 347 THR B 352 1 6
HELIX 13 13 GLU B 370 GLU B 383 1 14
SHEET 1 A 5 PHE A 179 THR A 181 0
SHEET 2 A 5 ILE A 157 ALA A 160 1 N LEU A 158 O ILE A 180
SHEET 3 A 5 ALA A 12 LEU A 18 1 N LEU A 17 O ILE A 157
SHEET 4 A 5 ASP A 216 LEU A 220 -1 N LEU A 220 O ALA A 12
SHEET 5 A 5 VAL A 227 VAL A 229 -1 N TYR A 228 O ILE A 219
SHEET 1 B 4 PHE B 302 THR B 307 0
SHEET 2 B 4 VAL B 360 GLU B 366 -1 N ALA B 365 O PHE B 302
SHEET 3 B 4 GLU B 332 SER B 337 -1 N THR B 336 O THR B 362
SHEET 4 B 4 LYS B 340 SER B 343 -1 N ALA B 342 O VAL B 335
SITE 1 AC1 3 HIS A 189 HIS B 315 THR B 316
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
(ATOM LINES ARE NOT SHOWN.)
END