Header list of 1zu2.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSPORT PROTEIN 30-MAY-05 1ZU2 TITLE SOLUTION NMR STRUCTURE OF THE PLANT TOM20 MITOCHONDRIAL IMPORT TITLE 2 RECEPTOR FROM ARABIDOPSIS THALIANA COMPND MOL_ID: 1; COMPND 2 MOLECULE: MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM20-3; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ISOFORM-3 CYTOSOLIC RECEPTOR DOMAIN; COMPND 5 SYNONYM: TRANSLOCASE OF OUTER MEMBRANE 20 KDA ISOFORM 3; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 GENE: TOM20-3; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA [BL21(DE3) DERIVED]; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-3 KEYWDS TPR, TETRATRICOPEPTIDE REPEAT LIKE, TPR-LIKE, TRANSPORT PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.J.PERRY,J.M.HULETT,T.LITHGOW,P.R.GOOLEY REVDAT 4 02-MAR-22 1ZU2 1 REMARK SEQADV REVDAT 3 24-FEB-09 1ZU2 1 VERSN REVDAT 2 21-FEB-06 1ZU2 1 JRNL REVDAT 1 06-DEC-05 1ZU2 0 JRNL AUTH A.J.PERRY,J.M.HULETT,V.A.LIKIC,T.LITHGOW,P.R.GOOLEY JRNL TITL CONVERGENT EVOLUTION OF RECEPTORS FOR PROTEIN IMPORT INTO JRNL TITL 2 MITOCHONDRIA JRNL REF CURR.BIOL. V. 16 221 2006 JRNL REFN ISSN 0960-9822 JRNL PMID 16461275 JRNL DOI 10.1016/J.CUB.2005.12.034 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.J.PERRY,J.M.HULETT,T.LITHGOW,P.R.GOOLEY REMARK 1 TITL LETTER TO THE EDITOR: 1H, 13C AND 15N RESONANCE ASSIGNMENTS REMARK 1 TITL 2 OF THE CYTOSOLIC DOMAIN OF TOM20 FROM ARABIDOPSIS THALIANA REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 4.1C, CYANA 1.0.7 REMARK 3 AUTHORS : VARIAN INC. (VNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE CANDID SOFTWARE WAS USED FOR REMARK 3 INITIAL AUTOMATIC NOE ASSIGNMENT. STRUCTURES ARE BASED ON 1629 REMARK 3 NOE-DERIVED UPPER DISTANCE CONSTRAINTS (47 INTRA RESIDUE), 136 REMARK 3 DISTANCE RESTRAINTS FROM HYDROGEN BONDS, REFINEMENT AGAINST 129 REMARK 3 J(HNHA) COUPLING CONSTANTS AND 234 PHI/PSI DIHEDRAL ANGLE REMARK 3 CONSTRAINTS FROM TALOS. REMARK 4 REMARK 4 1ZU2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-05. REMARK 100 THE DEPOSITION ID IS D_1000033118. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 150MM SODIUM CHLORIDE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM TOM20 U-15N,13C, 20MM SODIUM REMARK 210 PHOSPHATE BUFFER, 150MM SODIUM REMARK 210 CHLORIDE, 0.02 %(W/V) SODIUM REMARK 210 AZIDE, 1MM DITHIOTHREITOL, 1MM REMARK 210 EDTA, 3MM REMARK 210 PHENYLMETHYLSULPHONYLFLUORIDE, REMARK 210 90 % H2O, 10 % D2O; 1MM TOM20 U- REMARK 210 15N, 20MM SODIUM PHOSPHATE REMARK 210 BUFFER, 150MM SODIUM CHLORIDE, REMARK 210 0.02 %(W/V) SODIUM AZIDE, 1MM REMARK 210 DITHIOTHREITOL, 1MM EDTA, 3MM REMARK 210 PHENYLMETHYLSULPHONYLFLUORIDE, REMARK 210 90 % H2O, 10 % D2O; 1MM TOM20 U- REMARK 210 15N,13C, 20MM SODIUM PHOSPHATE REMARK 210 BUFFER, 150MM SODIUM CHLORIDE, REMARK 210 0.02 %(W/V) SODIUM AZIDE, 1MM REMARK 210 DITHIOTHREITOL, 1MM EDTA, 3MM REMARK 210 PHENYLMETHYLSULPHONYLFLUORIDE, REMARK 210 95 % D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; 3D-13C- REMARK 210 SEPARATED_NOESY (AROMATICS) REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.1, SPARKY 3.111, CYANA REMARK 210 1.0.7, CANDID 1.0 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: STRUCTURE CONTAINS 5 NON-NATIVE RESIDUES AT THE N-TERMINUS REMARK 210 (FROM FUSION SYSTEM PROTEASE SITE) AND 8 NON-NATIVE RESIDUES AT REMARK 210 THE C-TERMINUS FROM A POLYHISTIDINE TAG. 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 O GLU A 76 H CYS A 80 1.44 REMARK 500 O GLU A 95 H LYS A 99 1.49 REMARK 500 O LYS A 131 H LEU A 135 1.50 REMARK 500 O ARG A 17 H GLU A 21 1.51 REMARK 500 O ILE A 16 H ALA A 20 1.52 REMARK 500 O ILE A 50 H LYS A 54 1.54 REMARK 500 O GLN A 134 H GLU A 138 1.54 REMARK 500 O TRP A 79 H ASN A 83 1.58 REMARK 500 O VAL A 40 H LEU A 44 1.58 REMARK 500 O ASP A 94 H ALA A 98 1.58 REMARK 500 O ALA A 137 H LYS A 141 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 -2 176.55 62.29 REMARK 500 1 MET A 1 90.29 55.33 REMARK 500 1 ASP A 2 -51.21 -173.53 REMARK 500 1 THR A 3 -41.45 -166.18 REMARK 500 1 GLU A 4 154.06 65.00 REMARK 500 1 GLU A 6 -42.48 86.05 REMARK 500 1 ASN A 27 90.39 -169.46 REMARK 500 1 ASP A 30 98.75 -64.26 REMARK 500 1 SER A 49 150.32 -44.34 REMARK 500 1 LYS A 74 77.51 -67.91 REMARK 500 1 ASP A 94 85.30 -59.48 REMARK 500 1 LEU A 144 86.37 -154.16 REMARK 500 1 SER A 147 157.16 -41.52 REMARK 500 1 HIS A 148 -64.68 -103.76 REMARK 500 2 MET A 1 144.31 63.62 REMARK 500 2 ASP A 2 51.19 74.23 REMARK 500 2 THR A 5 18.09 -145.74 REMARK 500 2 GLU A 6 -23.86 89.33 REMARK 500 2 ASN A 27 86.12 -169.24 REMARK 500 2 ASP A 30 99.55 -68.48 REMARK 500 2 SER A 49 154.33 -47.43 REMARK 500 2 LYS A 74 73.27 -66.93 REMARK 500 2 ASP A 94 85.34 -59.36 REMARK 500 2 LEU A 144 -59.55 74.16 REMARK 500 2 SER A 147 131.68 67.55 REMARK 500 2 HIS A 148 87.77 58.66 REMARK 500 2 HIS A 149 159.45 60.49 REMARK 500 2 HIS A 150 -65.45 -120.58 REMARK 500 2 HIS A 151 -64.37 -138.24 REMARK 500 3 LEU A -2 -66.24 -156.61 REMARK 500 3 ASP A 2 179.61 59.28 REMARK 500 3 GLU A 4 135.82 61.83 REMARK 500 3 THR A 5 -60.72 -158.98 REMARK 500 3 GLU A 6 -48.64 -169.97 REMARK 500 3 ASN A 27 91.80 -169.38 REMARK 500 3 ASP A 30 99.13 -64.16 REMARK 500 3 HIS A 48 -92.39 -78.78 REMARK 500 3 SER A 49 148.83 172.04 REMARK 500 3 LYS A 74 74.90 -65.72 REMARK 500 3 ASP A 94 85.63 -60.87 REMARK 500 3 GLN A 116 90.69 -160.06 REMARK 500 3 LEU A 144 -62.09 -148.84 REMARK 500 3 HIS A 148 -76.74 65.29 REMARK 500 4 LEU A -2 86.80 41.25 REMARK 500 4 MET A 1 98.87 58.88 REMARK 500 4 THR A 5 -56.46 -145.61 REMARK 500 4 GLU A 6 -24.78 89.51 REMARK 500 4 ASN A 27 82.58 -169.66 REMARK 500 4 ASP A 94 86.39 -59.06 REMARK 500 4 GLN A 116 89.24 -156.16 REMARK 500 REMARK 500 THIS ENTRY HAS 262 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1ZU2 A 1 145 UNP P82874 TO203_ARATH 1 145 SEQADV 1ZU2 GLY A -4 UNP P82874 CLONING ARTIFACT SEQADV 1ZU2 PRO A -3 UNP P82874 CLONING ARTIFACT SEQADV 1ZU2 LEU A -2 UNP P82874 CLONING ARTIFACT SEQADV 1ZU2 GLY A -1 UNP P82874 CLONING ARTIFACT SEQADV 1ZU2 SER A 0 UNP P82874 CLONING ARTIFACT SEQADV 1ZU2 GLY A 146 UNP P82874 EXPRESSION TAG SEQADV 1ZU2 SER A 147 UNP P82874 EXPRESSION TAG SEQADV 1ZU2 HIS A 148 UNP P82874 EXPRESSION TAG SEQADV 1ZU2 HIS A 149 UNP P82874 EXPRESSION TAG SEQADV 1ZU2 HIS A 150 UNP P82874 EXPRESSION TAG SEQADV 1ZU2 HIS A 151 UNP P82874 EXPRESSION TAG SEQADV 1ZU2 HIS A 152 UNP P82874 EXPRESSION TAG SEQADV 1ZU2 HIS A 153 UNP P82874 EXPRESSION TAG SEQRES 1 A 158 GLY PRO LEU GLY SER MET ASP THR GLU THR GLU PHE ASP SEQRES 2 A 158 ARG ILE LEU LEU PHE GLU GLN ILE ARG GLN ASP ALA GLU SEQRES 3 A 158 ASN THR TYR LYS SER ASN PRO LEU ASP ALA ASP ASN LEU SEQRES 4 A 158 THR ARG TRP GLY GLY VAL LEU LEU GLU LEU SER GLN PHE SEQRES 5 A 158 HIS SER ILE SER ASP ALA LYS GLN MET ILE GLN GLU ALA SEQRES 6 A 158 ILE THR LYS PHE GLU GLU ALA LEU LEU ILE ASP PRO LYS SEQRES 7 A 158 LYS ASP GLU ALA VAL TRP CYS ILE GLY ASN ALA TYR THR SEQRES 8 A 158 SER PHE ALA PHE LEU THR PRO ASP GLU THR GLU ALA LYS SEQRES 9 A 158 HIS ASN PHE ASP LEU ALA THR GLN PHE PHE GLN GLN ALA SEQRES 10 A 158 VAL ASP GLU GLN PRO ASP ASN THR HIS TYR LEU LYS SER SEQRES 11 A 158 LEU GLU MET THR ALA LYS ALA PRO GLN LEU HIS ALA GLU SEQRES 12 A 158 ALA TYR LYS GLN GLY LEU GLY GLY SER HIS HIS HIS HIS SEQRES 13 A 158 HIS HIS HELIX 1 1 GLU A 6 ASN A 27 1 22 HELIX 2 2 ASP A 30 HIS A 48 1 19 HELIX 3 3 SER A 49 ASP A 71 1 23 HELIX 4 4 LYS A 74 THR A 92 1 19 HELIX 5 5 ASP A 94 GLN A 116 1 23 HELIX 6 6 ASN A 119 LYS A 131 1 13 HELIX 7 7 LYS A 131 GLN A 142 1 12 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 - r 2 2 Bytes