Header list of 1wib.pdb file
Complete list - r 2 2 Bytes
HEADER RIBOSOME 28-MAY-04 1WIB TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN FROM MOUSE HYPOTHETICAL TITLE 2 PROTEIN BAB22488 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 60S RIBOSOMAL PROTEIN L12; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: RIKEN CDNA 0710001M22; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030414-86; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS N-TERMINAL DOMAIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, RIBOSOME EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WIB 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WIB 1 VERSN REVDAT 1 28-NOV-04 1WIB 0 JRNL AUTH S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN FROM MOUSE JRNL TITL 2 HYPOTHETICAL PROTEIN BAB22488 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WIB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023610. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 100MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.7MM 13C/15N-PROTEIN 20MM D REMARK 210 -TRIS-HCL; 100MM NACL; 1MM D-DTT; REMARK 210 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.3, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.901, OLIVIA 1.9.12, REMARK 210 CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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: 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 PRO A 3 -172.74 -69.82 REMARK 500 1 LEU A 37 178.14 -53.17 REMARK 500 1 ALA A 79 97.41 -57.00 REMARK 500 2 SER A -1 44.31 39.12 REMARK 500 2 ASP A 6 79.84 -107.68 REMARK 500 2 ASN A 8 -54.19 -122.19 REMARK 500 2 SER A 26 53.14 72.96 REMARK 500 2 LEU A 37 162.63 -47.81 REMARK 500 2 SER A 76 133.06 -173.15 REMARK 500 2 ALA A 77 135.91 -36.93 REMARK 500 3 SER A -2 43.27 38.50 REMARK 500 3 GLU A 21 45.24 -92.72 REMARK 500 3 LEU A 37 177.72 -52.48 REMARK 500 3 LYS A 54 84.14 -64.19 REMARK 500 3 PRO A 83 -177.66 -69.72 REMARK 500 3 SER A 84 83.77 -68.23 REMARK 500 4 LEU A 37 175.67 -52.35 REMARK 500 4 LYS A 54 85.83 -68.97 REMARK 500 4 PRO A 83 90.83 -69.83 REMARK 500 4 SER A 85 53.38 -90.75 REMARK 500 5 ASP A 6 79.42 -118.33 REMARK 500 5 ASN A 8 -73.97 -129.91 REMARK 500 5 SER A 26 48.50 -78.88 REMARK 500 5 LEU A 37 170.13 -52.79 REMARK 500 5 SER A 76 111.32 -168.95 REMARK 500 5 ALA A 79 108.04 -55.82 REMARK 500 6 SER A -4 109.26 -50.41 REMARK 500 6 LEU A 37 169.62 -46.65 REMARK 500 6 SER A 78 -62.28 -133.33 REMARK 500 6 SER A 85 108.67 -55.99 REMARK 500 7 PRO A 3 -173.36 -69.72 REMARK 500 7 ASN A 8 -70.39 -81.62 REMARK 500 7 GLU A 9 164.37 -44.42 REMARK 500 7 GLU A 21 44.61 -92.75 REMARK 500 7 VAL A 22 151.76 -37.49 REMARK 500 7 SER A 26 99.25 -54.51 REMARK 500 7 LEU A 37 175.03 -51.19 REMARK 500 7 PRO A 75 -166.86 -69.75 REMARK 500 7 ALA A 79 93.17 -56.94 REMARK 500 8 PHE A 5 118.60 -164.09 REMARK 500 8 ASP A 6 144.02 -170.64 REMARK 500 8 ASN A 8 -54.60 -122.45 REMARK 500 8 SER A 26 41.72 38.77 REMARK 500 8 LYS A 54 89.53 -67.75 REMARK 500 8 SER A 78 73.76 -105.10 REMARK 500 8 SER A 85 41.72 38.12 REMARK 500 9 PHE A 5 65.88 -107.60 REMARK 500 9 ASP A 6 143.97 -36.33 REMARK 500 9 ASN A 8 -70.61 -134.37 REMARK 500 9 ALA A 24 46.12 -83.05 REMARK 500 REMARK 500 THIS ENTRY HAS 133 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 AUTHOR DETERMINATION METHOD: AUTHOR DETERMINED REMARK 700 REMARK 700 SHEET REMARK 700 AUTHOR DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMK001000344.1 RELATED DB: TARGETDB DBREF 1WIB A 1 79 UNP P35979 RL12_MOUSE 2 80 SEQADV 1WIB GLY A -6 UNP P35979 CLONING ARTIFACT SEQADV 1WIB SER A -5 UNP P35979 CLONING ARTIFACT SEQADV 1WIB SER A -4 UNP P35979 CLONING ARTIFACT SEQADV 1WIB GLY A -3 UNP P35979 CLONING ARTIFACT SEQADV 1WIB SER A -2 UNP P35979 CLONING ARTIFACT SEQADV 1WIB SER A -1 UNP P35979 CLONING ARTIFACT SEQADV 1WIB GLY A 1 UNP P35979 CLONING ARTIFACT SEQADV 1WIB SER A 81 UNP P35979 CLONING ARTIFACT SEQADV 1WIB GLY A 82 UNP P35979 CLONING ARTIFACT SEQADV 1WIB PRO A 83 UNP P35979 CLONING ARTIFACT SEQADV 1WIB SER A 84 UNP P35979 CLONING ARTIFACT SEQADV 1WIB SER A 84 UNP P35979 CLONING ARTIFACT SEQADV 1WIB GLY A 86 UNP P35979 CLONING ARTIFACT SEQRES 1 A 92 GLY SER SER GLY SER SER GLY PRO PRO LYS PHE ASP PRO SEQRES 2 A 92 ASN GLU VAL LYS VAL VAL TYR LEU ARG CYS THR GLY GLY SEQRES 3 A 92 GLU VAL GLY ALA THR SER ALA LEU ALA PRO LYS ILE GLY SEQRES 4 A 92 PRO LEU GLY LEU SER PRO LYS LYS VAL GLY ASP ASP ILE SEQRES 5 A 92 ALA LYS ALA THR GLY ASP TRP LYS GLY LEU ARG ILE THR SEQRES 6 A 92 VAL LYS LEU THR ILE GLN ASN ARG GLN ALA GLN ILE GLU SEQRES 7 A 92 VAL VAL PRO SER ALA SER ALA LEU SER GLY PRO SER SER SEQRES 8 A 92 GLY HELIX 1 1 LEU A 28 LEU A 35 1 8 HELIX 2 2 PRO A 39 THR A 50 1 12 SHEET 1 A 3 LYS A 11 THR A 18 0 SHEET 2 A 3 LEU A 56 GLN A 65 -1 O LEU A 62 N VAL A 13 SHEET 3 A 3 GLN A 68 VAL A 74 -1 O GLN A 68 N GLN A 65 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