Header list of 1ly7.pdb file
Complete list - c 21 2 Bytes
HEADER UNKNOWN FUNCTION 07-JUN-02 1LY7 TITLE THE SOLUTION STRUCTURE OF THE THE C-TERMINAL DOMAIN OF FRATAXIN, THE TITLE 2 PROTEIN RESPONSIBLE FOR FRIEDREICH ATAXIA COMPND MOL_ID: 1; COMPND 2 MOLECULE: FRATAXIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (91-210); COMPND 5 SYNONYM: FRIEDREICH'S ATAXIA PROTEIN, FXN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET KEYWDS ALPHA-BETA, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR G.MUSCO,G.STIER,B.KOLMERER,S.ADINOLFI,S.MARTIN,T.FRENKIEL,T.GIBSON, AUTHOR 2 A.PASTORE REVDAT 4 21-DEC-22 1LY7 1 SEQADV REVDAT 3 23-FEB-22 1LY7 1 REMARK REVDAT 2 24-FEB-09 1LY7 1 VERSN REVDAT 1 26-JUN-02 1LY7 0 SPRSDE 26-JUN-02 1LY7 1DLX JRNL AUTH G.MUSCO,G.STIER,B.KOLMERER,S.ADINOLFI,S.MARTIN,T.FRENKIEL, JRNL AUTH 2 T.GIBSON,A.PASTORE JRNL TITL TOWARDS A STRUCTURAL UNDERSTANDING OF FRIEDREICH'S ATAXIA: JRNL TITL 2 THE SOLUTION STRUCTURE OF FRATAXIN JRNL REF STRUCTURE FOLD.DES. V. 8 695 2000 JRNL REFN ISSN 0969-2126 JRNL PMID 10903947 JRNL DOI 10.1016/S0969-2126(00)00158-1 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.MUSCO,T.DE TOMMASI,G.STIER,B.KOLMERER,M.BOTTOMLEY, REMARK 1 AUTH 2 S.ADINOLFI,F.W.MUSKETT,T.J.GIBSON,T.A.FRENKIEL,A.PASTORE REMARK 1 TITL ASSIGNMENT OF THE 1H, 15N, AND 13C RESONANCES OF THE REMARK 1 TITL 2 C-TERMINAL DOMAIN OF FRATAXIN, THE PROTEIN RESPONSIBLE FOR REMARK 1 TITL 3 FRIEDREICH ATAXIA REMARK 1 REF J.BIOMOL.NMR V. 15 87 1999 REMARK 1 REFN ISSN 0925-2738 REMARK 1 DOI 10.1023/A:1008398832619 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 1.7, ARIA 1.0 REMARK 3 AUTHORS : DELAGLIO ET AL. (NMRPIPE), NILGES ET AL. (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ARIA REMARK 4 REMARK 4 1LY7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-02. REMARK 100 THE DEPOSITION ID IS D_1000016403. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 10 MM PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM FRATAXIN. U-15N 10 MM REMARK 210 PHOSPHATE BUFFER (PH 6.8)90% H2O, REMARK 210 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS; DMX REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.2, ARIA 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON REMARK 210 -BOND ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 H THR A 149 HD2 PRO A 150 1.34 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 ASP A 91 -27.16 -168.86 REMARK 500 1 LEU A 132 73.67 -160.21 REMARK 500 1 LEU A 140 -79.10 -70.98 REMARK 500 1 GLN A 148 -145.00 58.85 REMARK 500 1 THR A 149 -47.42 -162.50 REMARK 500 1 PRO A 150 -80.15 -26.89 REMARK 500 1 LYS A 152 77.92 46.68 REMARK 500 1 PRO A 159 0.40 -67.14 REMARK 500 1 SER A 160 -71.41 -88.11 REMARK 500 1 LYS A 171 24.55 -142.10 REMARK 500 1 TYR A 175 -157.46 -81.39 REMARK 500 1 SER A 176 -17.63 -145.15 REMARK 500 1 ASP A 178 -60.49 -121.59 REMARK 500 1 ALA A 187 -71.84 -60.97 REMARK 500 1 ASP A 199 84.77 -174.66 REMARK 500 1 LEU A 203 -171.92 -68.64 REMARK 500 2 ASP A 91 -170.12 56.26 REMARK 500 2 GLU A 92 -99.78 54.10 REMARK 500 2 THR A 93 -89.33 48.40 REMARK 500 2 THR A 119 -168.52 -70.78 REMARK 500 2 ASP A 139 -31.85 -172.02 REMARK 500 2 LEU A 140 -74.96 -58.68 REMARK 500 2 GLN A 148 -145.12 -118.13 REMARK 500 2 THR A 149 -49.41 -153.61 REMARK 500 2 PRO A 150 -78.14 -36.38 REMARK 500 2 LYS A 152 87.04 48.59 REMARK 500 2 SER A 160 -68.74 -124.21 REMARK 500 2 SER A 176 52.21 -115.17 REMARK 500 2 HIS A 177 -52.46 -153.39 REMARK 500 2 LEU A 182 -79.15 -65.36 REMARK 500 2 ALA A 187 -73.57 -59.03 REMARK 500 2 GLU A 189 -70.55 -63.13 REMARK 500 2 ASP A 199 85.60 55.52 REMARK 500 2 LYS A 208 50.79 33.35 REMARK 500 3 THR A 93 -70.06 -116.23 REMARK 500 3 THR A 119 -176.14 -65.09 REMARK 500 3 ASP A 122 52.50 -116.92 REMARK 500 3 LEU A 140 -78.27 -97.99 REMARK 500 3 GLN A 148 -138.02 -96.94 REMARK 500 3 THR A 149 -49.81 -155.05 REMARK 500 3 ASN A 151 65.67 -160.14 REMARK 500 3 LYS A 152 77.75 47.94 REMARK 500 3 SER A 176 94.72 -69.02 REMARK 500 3 HIS A 177 -57.83 -179.11 REMARK 500 3 ASP A 178 36.20 179.31 REMARK 500 3 VAL A 180 153.38 61.63 REMARK 500 3 ALA A 187 -70.29 -57.35 REMARK 500 3 GLU A 189 -71.40 -64.28 REMARK 500 3 LYS A 195 49.28 32.25 REMARK 500 3 ASP A 199 92.44 58.48 REMARK 500 REMARK 500 THIS ENTRY HAS 247 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1DLX RELATED DB: PDB REMARK 900 RELATED ID: 4342 RELATED DB: BMRB DBREF 1LY7 A 91 210 UNP Q16595 FRDA_HUMAN 91 210 SEQADV 1LY7 MET A 90 UNP Q16595 INITIATING METHIONINE SEQRES 1 A 121 MET ASP GLU THR THR TYR GLU ARG LEU ALA GLU GLU THR SEQRES 2 A 121 LEU ASP SER LEU ALA GLU PHE PHE GLU ASP LEU ALA ASP SEQRES 3 A 121 LYS PRO TYR THR PHE GLU ASP TYR ASP VAL SER PHE GLY SEQRES 4 A 121 SER GLY VAL LEU THR VAL LYS LEU GLY GLY ASP LEU GLY SEQRES 5 A 121 THR TYR VAL ILE ASN LYS GLN THR PRO ASN LYS GLN ILE SEQRES 6 A 121 TRP LEU SER SER PRO SER SER GLY PRO LYS ARG TYR ASP SEQRES 7 A 121 TRP THR GLY LYS ASN TRP VAL TYR SER HIS ASP GLY VAL SEQRES 8 A 121 SER LEU HIS GLU LEU LEU ALA ALA GLU LEU THR LYS ALA SEQRES 9 A 121 LEU LYS THR LYS LEU ASP LEU SER SER LEU ALA TYR SER SEQRES 10 A 121 GLY LYS ASP ALA HELIX 1 1 THR A 94 ALA A 114 1 21 HELIX 2 2 SER A 181 LEU A 194 1 14 SHEET 1 A 6 ASP A 122 SER A 126 0 SHEET 2 A 6 THR A 133 GLY A 137 -1 O GLY A 137 N ASP A 122 SHEET 3 A 6 GLY A 141 ASN A 146 -1 O TYR A 143 N VAL A 134 SHEET 4 A 6 ILE A 154 SER A 157 -1 O SER A 157 N VAL A 144 SHEET 5 A 6 ARG A 165 THR A 169 -1 O TYR A 166 N ILE A 154 SHEET 6 A 6 ASN A 172 VAL A 174 -1 O ASN A 172 N THR A 169 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 - c 21 2 Bytes