Header list of 1ezd.pdb file
Complete list - r 25 2 Bytes
HEADER PHOSPHOTRANSFERASE 01-JAN-97 1EZD TITLE AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI NMR, 16 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 16 AUTHOR D.S.GARRETT,A.M.GRONENBORN,G.M.CLORE REVDAT 3 24-NOV-10 1EZD 1 REMARK REVDAT 2 24-FEB-09 1EZD 1 VERSN REVDAT 1 07-JAN-98 1EZD 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 1EZD 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 : 16 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 HH22 ARG A 47 O LEU A 80 1.40 REMARK 500 H LYS A 213 OD2 ASP A 216 1.49 REMARK 500 O ALA A 91 H ASP A 95 1.57 REMARK 500 O VAL A 40 H LEU A 44 1.58 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 35 LEU A 6 96.34 49.28 REMARK 500 35 GLU A 198 8.86 52.93 REMARK 500 35 ASP A 215 -0.27 80.45 REMARK 500 35 ALA A 222 17.37 38.88 REMARK 500 36 LEU A 6 92.85 52.43 REMARK 500 36 ASP A 182 50.44 -99.20 REMARK 500 36 GLU A 198 8.72 55.12 REMARK 500 36 VAL A 203 -27.70 -140.83 REMARK 500 36 ALA A 222 19.03 38.63 REMARK 500 36 ASP A 258 -69.40 -91.68 REMARK 500 37 LEU A 6 91.79 48.96 REMARK 500 37 ASP A 119 47.39 -97.61 REMARK 500 37 ASP A 182 55.22 -95.65 REMARK 500 37 THR A 187 40.46 -109.01 REMARK 500 37 GLU A 198 7.18 53.47 REMARK 500 37 VAL A 203 -30.49 -133.04 REMARK 500 37 ASP A 215 -2.35 81.02 REMARK 500 37 ALA A 222 19.55 38.36 REMARK 500 38 LEU A 6 101.27 49.32 REMARK 500 38 ASP A 119 45.59 -102.06 REMARK 500 38 GLU A 198 12.51 54.28 REMARK 500 38 VAL A 203 -33.83 -136.48 REMARK 500 38 ASP A 215 -1.14 81.88 REMARK 500 38 ALA A 222 16.13 37.91 REMARK 500 39 LEU A 6 96.51 49.40 REMARK 500 39 ASP A 119 40.92 -99.94 REMARK 500 39 ASP A 182 47.78 -102.58 REMARK 500 39 GLU A 198 13.70 52.48 REMARK 500 39 ALA A 254 30.98 -81.51 REMARK 500 40 LEU A 6 97.98 51.93 REMARK 500 40 ASP A 119 44.67 -101.87 REMARK 500 40 ASP A 162 145.87 -173.21 REMARK 500 40 ASP A 182 51.26 -104.19 REMARK 500 40 GLU A 198 12.40 55.86 REMARK 500 40 VAL A 203 -31.83 -134.22 REMARK 500 40 ASP A 215 -1.29 81.88 REMARK 500 40 ALA A 222 12.44 40.29 REMARK 500 40 LYS A 255 37.86 -84.08 REMARK 500 40 LEU A 256 44.37 -80.00 REMARK 500 41 LEU A 6 93.53 50.39 REMARK 500 41 ASP A 119 40.67 -99.44 REMARK 500 41 ASP A 162 148.42 -173.20 REMARK 500 41 ASP A 182 56.88 -102.10 REMARK 500 41 THR A 187 35.89 -141.02 REMARK 500 41 GLU A 198 9.36 52.67 REMARK 500 41 ASP A 215 2.10 80.42 REMARK 500 41 ALA A 222 23.15 38.65 REMARK 500 41 VAL A 223 -59.45 -122.80 REMARK 500 42 LEU A 6 96.01 53.81 REMARK 500 42 ASP A 162 149.47 -173.03 REMARK 500 REMARK 500 THIS ENTRY HAS 123 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: 1EZC RELATED DB: PDB REMARK 900 CONTAINS MODELS 18 - 34 OF 50 DBREF 1EZD 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 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 LEU A 197 1 9 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 VAL A 156 ALA A 160 1 N ILE A 157 O LEU A 17 SHEET 3 B 3 VAL A 176 THR A 181 1 N LEU A 177 O VAL A 156 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 35
Complete list - r 25 2 Bytes