Header list of 2eza.pdb file
Complete list - 9 20 Bytes
HEADER PHOSPHOTRANSFERASE 07-MAY-97 2EZA
TITLE AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR,
TITLE 2 RESTRAINED REGULARIZED MEAN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 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
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
KEYWDS PHOSPHOTRANSFERASE, TRANSFERASE, KINASE, SUGAR TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,N.TJANDRA,D.S.GARRETT,A.M.GRONENBORN
REVDAT 3 09-MAR-22 2EZA 1 REMARK
REVDAT 2 24-FEB-09 2EZA 1 VERSN
REVDAT 1 20-AUG-97 2EZA 0
JRNL AUTH N.TJANDRA,D.S.GARRETT,A.M.GRONENBORN,A.BAX,G.M.CLORE
JRNL TITL DEFINING LONG RANGE ORDER IN NMR STRUCTURE DETERMINATION
JRNL TITL 2 FROM THE DEPENDENCE OF HETERONUCLEAR RELAXATION TIMES ON
JRNL TITL 3 ROTATIONAL DIFFUSION ANISOTROPY.
JRNL REF NAT.STRUCT.BIOL. V. 4 443 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9187651
JRNL DOI 10.1038/NSB0697-443
REMARK 1
REMARK 1 REFERENCE 1
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 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229,
REMARK 3 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO
REMARK 3 INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J.
REMARK 3 MAGN. RESON. SERIES B 104, 99-103) AND CARBON CHEMICAL
REMARK 3 SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B
REMARK 3 106, 92-96) RESTRAINTS, AND T1/T2 RESTRAINTS
REMARK 3 (TJANDRA ET AL. NATURE STRUCT. BIOL. 4, 443-449, 1997).
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.
REMARK 3 BEST FITTING TO GENERATE THE AVERAGE STRUCTURE IS WITH
REMARK 3 RESPECT TO RESIDUES 1 - 246 (RESIDUES 250 - 259 ARE
REMARK 3 DISORDERED IN SOLUTION).
REMARK 3
REMARK 3 THE DIFFUSION AXIS IS REPRESENTED BY A LINE CONNECTING THE
REMARK 3 FOLLOWING POINTS:
REMARK 3 P1 99.732 -1.172 2.902
REMARK 3 P2 101.246 -1.242 3.113
REMARK 4
REMARK 4 2EZA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178052.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 7
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
REMARK 210 SPECTROMETER MODEL : AMX500; AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR (SEE ABOVE) ABOVE)
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
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:
REMARK 210 THE 3D STRUCTURE OF THE EIN WAS SOLVED BY MULTI-DIMENSIONAL
REMARK 210 HETERONUCLEAR NMR AND IS BASED ON 4369 EXPERIMENTAL NMR
REMARK 210 RESTRAINTS: 117 T1/T2 RESTRAINTS; 952 SEQUENTIAL
REMARK 210 (|I- J|=1), 809 MEDIUM RANGE (1 < |I-J| <=5) AND 586 LONG
REMARK 210 RANGE (|I-J| >5) INTERRESIDUES AND 471 INTRARESIDUE
REMARK 210 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 230 DISTANCES
REMARK 210 FOR 115 BACKBONE HYDROGEN BONDS; 543 TORSION ANGLE
REMARK 210 RESTRAINTS; 163 THREE-BOND HN-HA COUPLING CONSTANT
REMARK 210 RESTRAINTS; AND 498 (257 CALPHA AND 241 CBETA) 13C SHIFT.
REMARK 210 RESTRAINTS. (NUMBERS OF RESIDUES 1 - 259)
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: MONOMERIC
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 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 H1 MET A 1 H ILE A 2 1.26
REMARK 500 O ALA A 91 H ASP A 95 1.42
REMARK 500 O VAL A 40 H LEU A 44 1.47
REMARK 500 O ALA A 16 H ASP A 215 1.51
REMARK 500 O LYS A 250 H LEU A 253 1.53
REMARK 500 O LYS A 255 HH22 ARG A 259 1.57
REMARK 500 O ALA A 254 HZ1 LYS A 257 1.58
REMARK 500 O LYS A 255 H LYS A 257 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 ILE A 2 93.42 -61.18
REMARK 500 LEU A 6 109.08 58.83
REMARK 500 GLU A 68 -15.18 -46.40
REMARK 500 ASP A 119 56.07 -97.41
REMARK 500 LEU A 144 156.13 -49.93
REMARK 500 ASP A 182 50.28 -94.55
REMARK 500 GLU A 198 6.74 52.66
REMARK 500 VAL A 203 -31.29 -139.30
REMARK 500 ASP A 215 -13.37 72.84
REMARK 500 ALA A 222 20.55 41.15
REMARK 500 ASN A 230 70.17 53.47
REMARK 500 LEU A 256 39.16 -73.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 259 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EZB RELATED DB: PDB
REMARK 900 MODELS 1 - 14 OF 28
REMARK 900 RELATED ID: 2EZC RELATED DB: PDB
REMARK 900 MODELS 15 - 28 OF 28
DBREF 2EZA A 1 258 UNP P08839 PT1_ECOLI 1 258
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
HELIX 1 1 ALA A 33 THR A 64 1 32
HELIX 2 2 GLU A 67 LEU A 80 5 14
HELIX 3 3 GLU A 83 ASP A 95 1 13
HELIX 4 4 ALA A 100 GLU A 117 1 18
HELIX 5 5 GLU A 121 ILE A 141 1 21
HELIX 6 6 LEU A 149 ALA A 151 5 3
HELIX 7 7 PRO A 165 GLN A 170 1 6
HELIX 8 8 HIS A 189 SER A 196 1 8
HELIX 9 9 VAL A 208 SER A 210 5 3
HELIX 10 10 ASN A 233 ALA A 254 1 22
SHEET 1 A 3 ALA A 12 LYS A 15 0
SHEET 2 A 3 TYR A 217 LEU A 220 -1 N LEU A 220 O ALA A 12
SHEET 3 A 3 VAL A 227 VAL A 229 -1 N TYR A 228 O ILE A 219
SHEET 1 B 3 ALA A 16 LEU A 18 0
SHEET 2 B 3 ILE A 157 ALA A 160 1 N ILE A 157 O LEU A 17
SHEET 3 B 3 PHE A 179 THR A 181 1 N ILE A 180 O LEU A 158
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
Complete list - 9 20 Bytes