Header list of 1ezc.pdb file
Complete list - r 25 2 Bytes
HEADER PHOSPHOTRANSFERASE 01-JAN-97 1EZC
TITLE AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI, NMR, 17
TITLE 2 STRUCTURES
SPLIT 1EZB 1EZC 1EZD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 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, KINASE, SUGAR TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR D.S.GARRETT,A.M.GRONENBORN,G.M.CLORE
REVDAT 3 24-NOV-10 1EZC 1 REMARK
REVDAT 2 24-FEB-09 1EZC 1 VERSN
REVDAT 1 07-JAN-98 1EZC 0
JRNL AUTH D.S.GARRETT,Y.J.SEOK,D.I.LIAO,A.PETERKOFSKY,A.M.GRONENBORN,
JRNL AUTH 2 G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF THE 30 KDA N-TERMINAL DOMAIN OF ENZYME
JRNL TITL 2 I OF THE ESCHERICHIA COLI PHOSPHOENOLPYRUVATE:SUGAR
JRNL TITL 3 PHOSPHOTRANSFERASE SYSTEM BY MULTIDIMENSIONAL NMR.
JRNL REF BIOCHEMISTRY V. 36 2517 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9054557
JRNL DOI 10.1021/BI962924Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR (SEE ABOVE) ABOVE)
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE 3D STRUCTURE OF THE EIN WAS SOLVED BY
REMARK 3 MULTI-DIMENSIONAL HETERONUCLEAR NMR AND
REMARK 3 IS BASED ON 4251 EXPERIMENTAL NMR RESTRAINTS:
REMARK 3 (A) INTRAPROTEIN: 952 SEQUENTIAL (|I- J|=1), 809 MEDIUM
REMARK 3 RANGE (1 < |I-J| <=5) AND 586 LONG RANGE (|I-J| >5)
REMARK 3 INTERRESIDUES AND 471 INTRARESIDUE APPROXIMATE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS; 230 DISTANCES FOR 115 BACKBONE
REMARK 3 HYDROGEN BONDS; 140 TORSION ANGLE RESTRAINTS; 163
REMARK 3 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; AND 498
REMARK 3 (258 CALPHA AND 241 CBETA) 13C SHIFT RESTRAINTS. (NUMBERS
REMARK 3 OF RESIDUES 1 - 259).
REMARK 3
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
REMARK 3 TO 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 A CONFORMATIONAL DATABASE
REMARK 3 POTENTIAL (KUSZEWSKI ET AL.(1996) PROTEIN SCI. 5, 1067-1080
REMARK 3
REMARK 3 IN THE RESTRAINED REGULARIZED MEAN COORDINATES THE
REMARK 3 TEMPERATURE FACTOR FIELD 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) NOTE THE OCCUPANCY FIELD HAS NO
REMARK 3 MEANING.
REMARK 4
REMARK 4 1EZC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 : TRIPLE RESONANCE FOR ASSIGNMENT
REMARK 210 OF PROTEIN; QUANTITATIVE J
REMARK 210 CORRELATION FOR COUPLING
REMARK 210 CONSTANTS 3D; 4D HETERONUCLEAR
REMARK 210 SEPARATED NOE EXPERIMENTS. 3D 13C
REMARK 210 -SEPARATED/12C-FILTERED NOE
REMARK 210 EXPERIMENTS FOR REVERSE LABELED
REMARK 210 AROMATIC SAMPLES
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 : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 HH21 ARG A 240 HE21 GLN A 243 1.54
REMARK 500 O ALA A 91 H ASP A 95 1.54
REMARK 500 O GLY A 4 HD22 ASN A 225 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 18 LEU A 6 93.39 51.80
REMARK 500 18 ASP A 119 40.78 -98.10
REMARK 500 18 ASP A 182 56.33 -104.02
REMARK 500 18 GLU A 198 8.31 54.82
REMARK 500 18 ASP A 215 2.52 80.61
REMARK 500 18 ALA A 222 19.13 38.65
REMARK 500 18 LEU A 256 -98.82 -88.42
REMARK 500 18 LYS A 257 -94.00 -127.03
REMARK 500 19 LEU A 6 95.62 49.49
REMARK 500 19 ASP A 182 53.43 -101.67
REMARK 500 19 GLU A 198 9.78 54.43
REMARK 500 19 VAL A 203 -31.67 -140.94
REMARK 500 19 ASP A 215 -3.42 81.07
REMARK 500 19 ALA A 222 19.34 37.64
REMARK 500 19 VAL A 223 -60.14 -108.42
REMARK 500 20 LEU A 6 98.73 50.06
REMARK 500 20 ASP A 182 65.36 -104.09
REMARK 500 20 GLU A 198 12.46 49.60
REMARK 500 20 ALA A 222 17.75 39.78
REMARK 500 20 LEU A 256 44.15 -87.24
REMARK 500 21 LEU A 6 97.43 50.91
REMARK 500 21 ASP A 119 55.26 -99.41
REMARK 500 21 GLU A 198 8.15 53.72
REMARK 500 21 VAL A 203 -28.43 -141.54
REMARK 500 21 ASP A 215 0.54 80.10
REMARK 500 21 ALA A 222 18.56 37.94
REMARK 500 21 VAL A 223 -60.30 -108.14
REMARK 500 21 LYS A 255 32.17 -80.90
REMARK 500 22 LEU A 6 101.99 50.71
REMARK 500 22 ASP A 119 47.49 -102.61
REMARK 500 22 ASP A 182 55.52 -102.43
REMARK 500 22 GLU A 198 12.50 52.29
REMARK 500 22 VAL A 203 -32.80 -137.90
REMARK 500 22 ASP A 215 0.11 81.18
REMARK 500 22 ALA A 222 14.25 39.11
REMARK 500 23 LEU A 6 93.97 51.80
REMARK 500 23 ASP A 119 35.77 -98.21
REMARK 500 23 GLU A 198 8.53 53.36
REMARK 500 23 ASP A 215 2.75 81.72
REMARK 500 23 ALA A 222 12.94 40.06
REMARK 500 23 VAL A 223 -61.49 -108.53
REMARK 500 23 LEU A 256 33.07 -83.46
REMARK 500 24 ILE A 2 73.22 51.01
REMARK 500 24 LEU A 6 100.41 50.61
REMARK 500 24 ASP A 162 148.00 -172.45
REMARK 500 24 PRO A 165 -38.72 -39.93
REMARK 500 24 ASP A 182 49.56 -103.03
REMARK 500 24 GLU A 198 8.78 54.11
REMARK 500 24 VAL A 203 -32.69 -134.11
REMARK 500 24 ASP A 215 -1.76 81.07
REMARK 500
REMARK 500 THIS ENTRY HAS 126 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EZA RELATED DB: PDB
REMARK 900 CONTAINS THE RESTRAINED REGULARIZED MEAN STRUCTURE
REMARK 900 RELATED ID: 1EZB RELATED DB: PDB
REMARK 900 CONTAINS MODELS 1 - 17 OF 50
REMARK 900 RELATED ID: 1EZD RELATED DB: PDB
REMARK 900 CONTAINS MODELS 35 - 50 OF 50
DBREF 1EZC 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 PHE A 65 1 33
HELIX 2 2 GLU A 67 GLU A 81 1 15
HELIX 3 3 GLU A 83 LYS A 96 1 14
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 ALA A 169 1 5
HELIX 8 8 HIS A 189 LEU A 197 1 9
HELIX 9 9 VAL A 208 SER A 210 5 3
HELIX 10 10 ASN A 233 LEU A 253 1 21
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
MODEL 18
Complete list - r 25 2 Bytes