Header list of 3ezb.pdb file
Complete list - ar 16 Bytes
HEADER TRANSFERASE 03-NOV-98 3EZB
TITLE COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-
TITLE 2 CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PHOSPHOTRANSFER 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 (PHOSPHOCARRIER PROTEIN 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_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PLP2;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 11 ORGANISM_TAXID: 562;
SOURCE 12 STRAIN: GI698;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PSP100
KEYWDS PHOSPHOTRANSFERASE, KINASE, SUGAR TRANSPORT, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR G.M.CLORE,D.S.GARRETT,A.M.GRONENBORN
REVDAT 4 16-MAR-22 3EZB 1 REMARK SEQADV
REVDAT 3 24-FEB-09 3EZB 1 VERSN
REVDAT 2 29-DEC-99 3EZB 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 16-DEC-99 3EZB 0
SPRSDE 29-DEC-99 3EZB 3EZD
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 ACTI
REMARK 1 TITL 2 HISTIDINE IN THE N- TERMINAL DOMAIN OF ENZYME I OF T
REMARK 1 TITL 3 ESCHRICHIA COLI PHOSPHOENOLPYRUVATE:SUGAR PHOSPHOTR 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 TH
REMARK 1 TITL 2 HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR ON
REMARK 1 TITL 3 N-TERMINAL DOMAIN OF ENZYME I OF THE ESCHERICHIA CO
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,ADAMS, CLORE, DELANO, GROS, GROSSE
REMARK 3 -KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU, READ,
REMARK 3 RICE WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE CALCULATED USING
REMARK 3 THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS
REMARK 3 LETT. 229, 129-136 USING THE PROGRAM CNS MODIFIED TO INCORPORATE
REMARK 3 COUPLING CONSTANT RESTRAINTS (GARRETT ET AL. (1984) J. MAGN.
REMARK 3 RESON. SERIES B 104, 99-103), CARBON CHEMICAL SHIFT RESTRAINTS,
REMARK 3 (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B 106, 92-96)
REMARK 3 RESTRAINTS, AND RESIDUAL DIPOLAR COUPLING RESTRAINTS (CLORE ET
REMARK 3 AL. J. MAGN. RESON 131, 159-162 (1998); J. MAGN 133, 216-221
REMARK 3 (1998)).
REMARK 4
REMARK 4 3EZB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000008052.
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 : 1) TRIPLE RESONANCE FOR
REMARK 210 ASSIGNMENT OF PROTEIN. (2)
REMARK 210 QUANTITATIVE J CORRELATION FOR
REMARK 210 COUPLING CONSTANTS. (3) 3D; 4D
REMARK 210 HETERONUCLEAR SEPARATED;
REMARK 210 FILTERED NOE E (4) IPAP EXPTS
REMARK 210 FOR DIPOLAR COUPLINGS DIPOLAR
REMARK 210 COUPLINGS WERE MEASURED IN A
REMARK 210 NEMATIC PHASE OF A CO SUSPENSION
REMARK 210 OF PHAGE FD (CLORE ET AL. 1998
REMARK 210 J. AM. CHEM. SOC
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
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-40
REMARK 470 RES CSSEQI ATOMS
REMARK 470 MET A 1 N
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 H GLY A 4 HD22 ASN A 225 1.27
REMARK 500 O LEU B 350 H LEU B 353 1.43
REMARK 500 O ALA A 91 H ASP A 95 1.54
REMARK 500 O LYS A 15 H ILE A 157 1.55
REMARK 500 O LYS A 60 HG1 THR A 64 1.55
REMARK 500 O GLU A 74 H MET A 78 1.59
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 LEU A 6 98.14 53.30
REMARK 500 1 LYS A 49 -73.70 -72.46
REMARK 500 1 ASP A 119 48.98 -99.33
REMARK 500 1 ASP A 148 103.36 63.76
REMARK 500 1 GLN A 170 38.52 -85.02
REMARK 500 1 ALA A 183 -159.67 -57.44
REMARK 500 1 SER A 207 35.01 -157.34
REMARK 500 1 ASP A 215 -2.53 89.30
REMARK 500 1 ALA A 222 11.67 46.76
REMARK 500 1 HIS B 315 -159.97 -97.69
REMARK 500 1 GLN B 351 -22.68 -38.33
REMARK 500 1 GLN B 357 157.44 -48.62
REMARK 500 1 ALA B 373 -76.03 -47.27
REMARK 500 2 LEU A 6 103.60 51.51
REMARK 500 2 LYS A 49 -73.43 -72.33
REMARK 500 2 ALA A 50 -34.70 -38.53
REMARK 500 2 GLU A 117 -17.92 -49.26
REMARK 500 2 ASP A 119 44.15 -93.94
REMARK 500 2 ASP A 148 113.91 62.62
REMARK 500 2 GLN A 170 39.75 -82.27
REMARK 500 2 ALA A 183 -172.14 -47.85
REMARK 500 2 SER A 207 38.36 -156.92
REMARK 500 2 ASP A 215 -0.03 82.59
REMARK 500 2 ALA A 222 16.14 45.71
REMARK 500 2 ASN A 230 70.17 68.55
REMARK 500 2 LYS A 250 42.55 -85.80
REMARK 500 2 LYS A 257 -172.23 45.94
REMARK 500 2 ASP A 258 -123.05 -150.72
REMARK 500 2 GLN B 351 -12.56 -43.16
REMARK 500 2 ALA B 373 -75.13 -46.61
REMARK 500 3 LEU A 6 96.41 54.94
REMARK 500 3 LYS A 49 -72.97 -63.50
REMARK 500 3 ALA A 50 -34.00 -37.88
REMARK 500 3 ASP A 119 41.51 -85.76
REMARK 500 3 ASP A 148 125.58 60.17
REMARK 500 3 ALA A 151 27.97 -79.72
REMARK 500 3 ASP A 162 146.48 -170.51
REMARK 500 3 GLN A 170 38.08 -86.99
REMARK 500 3 ALA A 183 -162.92 -55.37
REMARK 500 3 ASP A 215 10.72 83.53
REMARK 500 3 ALA A 222 15.80 48.89
REMARK 500 3 VAL A 223 -46.12 -132.19
REMARK 500 3 ASN A 230 69.92 69.25
REMARK 500 3 ALA A 254 6.94 48.39
REMARK 500 3 LYS A 255 8.46 49.52
REMARK 500 3 HIS B 315 -159.78 -96.54
REMARK 500 3 LYS B 327 -17.34 -49.96
REMARK 500 3 GLN B 351 -23.69 -38.37
REMARK 500 3 ALA B 373 -74.80 -50.18
REMARK 500 4 LEU A 6 103.93 51.02
REMARK 500
REMARK 500 THIS ENTRY HAS 698 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EZA RELATED DB: PDB
REMARK 900 RESTRAINED REGULARIZED MEAN STRUCTURE
REMARK 900 RELATED ID: 3EZE RELATED DB: PDB
REMARK 900 RESTRAINED REGULARIZED MEAN STRUCTURE OF THE TRANSITION STATE
DBREF 3EZB A 1 259 UNP P08839 PT1_ECOLI 1 259
DBREF 3EZB B 301 385 UNP P0AA04 PTHP_ECOLI 1 85
SEQADV 3EZB ARG A 259 UNP P08839 LEU 259 CONFLICT
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
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 ALA A 251 1 19
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
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
Complete list - ar 16 Bytes