Header list of 1t23.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 20-APR-04 1T23 TITLE NMR SOLUTION STRUCTURE OF THE ARCHAEBACTERIAL CHROMOSOMAL PROTEIN MC1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHROMOSOMAL PROTEIN MC1; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: METHANOSARCINA THERMOPHILA; SOURCE 3 ORGANISM_TAXID: 2210; SOURCE 4 STRAIN: CHTI55 KEYWDS ALPHA/BETA BARREL, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 8 AUTHOR F.PAQUET,F.CULARD,F.BARBAULT,J.C.MAURIZOT,G.LANCELOT REVDAT 3 02-MAR-22 1T23 1 REMARK REVDAT 2 24-FEB-09 1T23 1 VERSN REVDAT 1 07-DEC-04 1T23 0 SPRSDE 07-DEC-04 1T23 1KOM JRNL AUTH F.PAQUET,F.CULARD,F.BARBAULT,J.C.MAURIZOT,G.LANCELOT JRNL TITL NMR SOLUTION STRUCTURE OF THE ARCHAEBACTERIAL CHROMOSOMAL JRNL TITL 2 PROTEIN MC1 REVEALS A NEW PROTEIN FOLD JRNL REF BIOCHEMISTRY V. 43 14971 2004 JRNL REFN ISSN 0006-2960 JRNL PMID 15554704 JRNL DOI 10.1021/BI048382Z REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1B, X-PLOR 3.851 REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1T23 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-04. REMARK 100 THE DEPOSITION ID IS D_1000022214. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 5.3 REMARK 210 IONIC STRENGTH : 800MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.74 MM MC1, 70 MM SODIUM REMARK 210 ACETATE BUFFER, 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; AMX REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : UXNMR, DYANA 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 8 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR SPECTRA 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 HZ1 LYS A 22 OE1 GLN A 26 1.35 REMARK 500 OD1 ASN A 33 HZ3 LYS A 81 1.35 REMARK 500 OE1 GLU A 49 HZ3 LYS A 54 1.38 REMARK 500 HZ2 LYS A 91 O LEU A 92 1.38 REMARK 500 OG1 THR A 52 HZ1 LYS A 54 1.39 REMARK 500 HZ3 LYS A 91 OE2 GLU A 93 1.41 REMARK 500 OD1 ASP A 66 HZ2 LYS A 78 1.44 REMARK 500 O ARG A 9 H ASN A 14 1.46 REMARK 500 O GLU A 49 HH21 ARG A 50 1.48 REMARK 500 HH11 ARG A 88 OE2 GLU A 90 1.48 REMARK 500 OD2 ASP A 10 H THR A 38 1.51 REMARK 500 H GLU A 11 O ASN A 41 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 ASP A 10 -155.14 -75.07 REMARK 500 1 ASP A 12 8.80 58.07 REMARK 500 1 ASN A 14 -78.06 -118.40 REMARK 500 1 GLU A 15 133.82 -179.23 REMARK 500 1 PHE A 19 -173.32 -176.24 REMARK 500 1 ARG A 34 -70.84 -99.70 REMARK 500 1 LYS A 39 -56.60 76.59 REMARK 500 1 ASN A 41 68.49 -158.43 REMARK 500 1 ALA A 67 100.41 -58.39 REMARK 500 1 MET A 75 123.55 -176.21 REMARK 500 1 ILE A 79 170.54 177.87 REMARK 500 1 LYS A 81 -155.54 -165.02 REMARK 500 2 ASP A 10 -153.19 -73.49 REMARK 500 2 GLU A 11 50.95 71.90 REMARK 500 2 ASP A 12 6.60 59.14 REMARK 500 2 ASN A 14 -81.67 -117.49 REMARK 500 2 GLU A 15 129.84 -170.12 REMARK 500 2 PHE A 19 -172.11 -175.42 REMARK 500 2 ARG A 34 -72.31 -97.04 REMARK 500 2 LYS A 39 -59.16 72.84 REMARK 500 2 ASN A 41 67.77 -159.05 REMARK 500 2 TRP A 61 -166.13 -128.49 REMARK 500 2 LYS A 69 62.02 -69.44 REMARK 500 2 LYS A 81 -152.58 -169.81 REMARK 500 2 LYS A 91 95.23 -163.69 REMARK 500 3 ASP A 10 -156.16 -73.48 REMARK 500 3 GLU A 11 51.66 70.92 REMARK 500 3 ASP A 12 7.95 59.45 REMARK 500 3 ASN A 14 -77.24 -117.11 REMARK 500 3 GLU A 15 138.08 -178.05 REMARK 500 3 PHE A 19 -173.49 -175.17 REMARK 500 3 ARG A 34 -73.44 -94.98 REMARK 500 3 LYS A 39 -56.57 72.01 REMARK 500 3 ASN A 41 67.73 -156.75 REMARK 500 3 ASP A 43 -168.71 -165.11 REMARK 500 3 LEU A 47 93.32 -69.71 REMARK 500 3 ARG A 48 -165.41 -113.12 REMARK 500 3 ALA A 67 98.60 -66.18 REMARK 500 3 LYS A 69 54.03 38.99 REMARK 500 3 MET A 75 132.20 -170.42 REMARK 500 3 LYS A 81 -162.41 -164.16 REMARK 500 4 ASP A 10 -144.09 -98.61 REMARK 500 4 GLU A 11 57.54 72.63 REMARK 500 4 ASP A 12 -5.15 74.14 REMARK 500 4 ASN A 14 -74.49 -129.19 REMARK 500 4 PHE A 19 -170.65 -174.81 REMARK 500 4 ARG A 34 -75.16 -92.47 REMARK 500 4 LYS A 39 -55.87 67.67 REMARK 500 4 TRP A 61 -165.07 -128.11 REMARK 500 4 VAL A 65 -167.94 -102.00 REMARK 500 REMARK 500 THIS ENTRY HAS 108 RAMACHANDRAN OUTLIERS. 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 1 ARG A 4 0.29 SIDE CHAIN REMARK 500 1 ARG A 9 0.31 SIDE CHAIN REMARK 500 1 ARG A 25 0.26 SIDE CHAIN REMARK 500 1 ARG A 34 0.31 SIDE CHAIN REMARK 500 1 ARG A 46 0.31 SIDE CHAIN REMARK 500 1 ARG A 48 0.28 SIDE CHAIN REMARK 500 1 ARG A 50 0.30 SIDE CHAIN REMARK 500 1 ARG A 71 0.26 SIDE CHAIN REMARK 500 1 ARG A 88 0.31 SIDE CHAIN REMARK 500 2 ARG A 4 0.32 SIDE CHAIN REMARK 500 2 ARG A 9 0.32 SIDE CHAIN REMARK 500 2 ARG A 25 0.18 SIDE CHAIN REMARK 500 2 ARG A 34 0.32 SIDE CHAIN REMARK 500 2 ARG A 46 0.31 SIDE CHAIN REMARK 500 2 ARG A 48 0.32 SIDE CHAIN REMARK 500 2 ARG A 50 0.32 SIDE CHAIN REMARK 500 2 ARG A 71 0.31 SIDE CHAIN REMARK 500 2 ARG A 88 0.32 SIDE CHAIN REMARK 500 3 ARG A 4 0.29 SIDE CHAIN REMARK 500 3 ARG A 9 0.30 SIDE CHAIN REMARK 500 3 ARG A 25 0.20 SIDE CHAIN REMARK 500 3 ARG A 34 0.32 SIDE CHAIN REMARK 500 3 ARG A 46 0.29 SIDE CHAIN REMARK 500 3 ARG A 48 0.32 SIDE CHAIN REMARK 500 3 ARG A 50 0.26 SIDE CHAIN REMARK 500 3 ARG A 71 0.32 SIDE CHAIN REMARK 500 3 ARG A 88 0.30 SIDE CHAIN REMARK 500 4 ARG A 4 0.32 SIDE CHAIN REMARK 500 4 ARG A 9 0.29 SIDE CHAIN REMARK 500 4 ARG A 25 0.30 SIDE CHAIN REMARK 500 4 ARG A 34 0.30 SIDE CHAIN REMARK 500 4 ARG A 46 0.30 SIDE CHAIN REMARK 500 4 ARG A 48 0.32 SIDE CHAIN REMARK 500 4 ARG A 50 0.30 SIDE CHAIN REMARK 500 4 ARG A 71 0.28 SIDE CHAIN REMARK 500 4 ARG A 88 0.11 SIDE CHAIN REMARK 500 5 ARG A 4 0.23 SIDE CHAIN REMARK 500 5 ARG A 9 0.32 SIDE CHAIN REMARK 500 5 ARG A 25 0.28 SIDE CHAIN REMARK 500 5 ARG A 34 0.31 SIDE CHAIN REMARK 500 5 ARG A 46 0.25 SIDE CHAIN REMARK 500 5 ARG A 48 0.20 SIDE CHAIN REMARK 500 5 ARG A 50 0.30 SIDE CHAIN REMARK 500 5 ARG A 71 0.28 SIDE CHAIN REMARK 500 5 ARG A 88 0.31 SIDE CHAIN REMARK 500 6 ARG A 4 0.29 SIDE CHAIN REMARK 500 6 ARG A 9 0.30 SIDE CHAIN REMARK 500 6 ARG A 25 0.30 SIDE CHAIN REMARK 500 6 ARG A 34 0.32 SIDE CHAIN REMARK 500 6 ARG A 46 0.29 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 72 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1T23 A 1 93 UNP P12770 HMC1_METTE 1 93 SEQRES 1 A 93 SER ASN THR ARG ASN PHE VAL LEU ARG ASP GLU ASP GLY SEQRES 2 A 93 ASN GLU HIS GLY VAL PHE THR GLY LYS GLN PRO ARG GLN SEQRES 3 A 93 ALA ALA LEU LYS ALA ALA ASN ARG GLY SER GLY THR LYS SEQRES 4 A 93 ALA ASN PRO ASP ILE ILE ARG LEU ARG GLU ARG GLY THR SEQRES 5 A 93 LYS LYS VAL HIS VAL PHE LYS ALA TRP LYS GLU ILE VAL SEQRES 6 A 93 ASP ALA PRO LYS ASN ARG PRO ALA TRP MET PRO GLU LYS SEQRES 7 A 93 ILE SER LYS PRO PHE VAL LYS LYS GLU ARG ILE GLU LYS SEQRES 8 A 93 LEU GLU HELIX 1 1 ARG A 25 GLY A 35 1 11 SHEET 1 A 2 ARG A 4 LEU A 8 0 SHEET 2 A 2 GLY A 17 GLY A 21 -1 O GLY A 21 N ARG A 4 SHEET 1 B 3 ILE A 44 GLU A 49 0 SHEET 2 B 3 LYS A 54 ALA A 60 -1 O HIS A 56 N LEU A 47 SHEET 3 B 3 VAL A 84 LYS A 91 -1 O GLU A 90 N VAL A 55 SHEET 1 C 2 GLU A 63 VAL A 65 0 SHEET 2 C 2 ILE A 79 LYS A 81 -1 O LYS A 81 N GLU A 63 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