Header list of 2dbg.pdb file
Complete list - r 9 2 Bytes
HEADER IMMUNE SYSTEM 15-DEC-05 2DBG TITLE SOLUTION STRUCTURE OF THE PYRIN (PAAD-DAPIN) DOMAIN IN HUMAN MYELOID TITLE 2 CELL NUCLEAR DIFFERENTIATION ANTIGEN COMPND MOL_ID: 1; COMPND 2 MOLECULE: MYELOID CELL NUCLEAR DIFFERENTIATION ANTIGEN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PYRIN DOMAIN; COMPND 5 SYNONYM: MNDA; 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 GENE: AB1735_E12; SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050613-16; SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS INTERFERON INDUCTION, DNA-BINDING, STRUCTURAL GENOMICS, NPPSFA, KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, IMMUNE SYSTEM EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.SAITO,M.INOUE,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2DBG 1 REMARK SEQADV REVDAT 2 24-FEB-09 2DBG 1 VERSN REVDAT 1 15-JUN-06 2DBG 0 JRNL AUTH K.SAITO,M.INOUE,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE PYRIN (PAAD-DAPIN) DOMAIN IN HUMAN JRNL TITL 2 MYELOID CELL NUCLEAR DIFFERENTIATION ANTIGEN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, AT (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2DBG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000025216. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN, 20MM D-TRIS-HCL, REMARK 210 PH7.0, 100MM NACL, 1MM D-DTT, REMARK 210 0.02% NAN3, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C 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 2002, NMRVIEW 5, CNS 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING 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: 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: 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 ASN A 10 84.03 60.77 REMARK 500 1 LYS A 19 61.40 -114.03 REMARK 500 1 LEU A 82 44.54 -95.91 REMARK 500 1 SER A 102 96.50 60.40 REMARK 500 2 SER A 3 37.22 -99.02 REMARK 500 2 SER A 5 -54.16 -145.78 REMARK 500 2 ASN A 10 150.34 64.55 REMARK 500 2 LYS A 19 50.92 -90.78 REMARK 500 2 ALA A 76 31.43 -98.45 REMARK 500 2 LEU A 82 32.92 -96.68 REMARK 500 2 ALA A 97 33.09 -143.73 REMARK 500 2 SER A 102 94.95 58.70 REMARK 500 3 SER A 2 101.16 60.46 REMARK 500 3 MET A 8 31.84 -163.43 REMARK 500 3 LYS A 19 47.08 -93.37 REMARK 500 3 ALA A 76 32.35 -98.16 REMARK 500 3 ASP A 78 40.08 -102.08 REMARK 500 3 LEU A 82 30.95 -98.21 REMARK 500 3 LYS A 95 45.82 -92.64 REMARK 500 3 SER A 98 -46.67 -151.19 REMARK 500 4 SER A 3 104.01 60.43 REMARK 500 4 SER A 5 -53.40 -123.23 REMARK 500 4 SER A 6 -50.94 -132.76 REMARK 500 4 MET A 8 111.45 60.86 REMARK 500 4 LYS A 19 58.94 -101.64 REMARK 500 4 ASP A 78 30.96 -98.10 REMARK 500 4 LEU A 82 35.08 -98.19 REMARK 500 5 SER A 3 -61.99 -147.98 REMARK 500 5 SER A 5 34.06 -167.40 REMARK 500 5 MET A 8 -60.85 -135.02 REMARK 500 5 ALA A 76 50.72 -93.20 REMARK 500 5 ASP A 78 48.55 -93.06 REMARK 500 5 LYS A 95 53.80 -100.64 REMARK 500 5 ALA A 97 120.30 62.12 REMARK 500 6 SER A 2 -46.92 -150.40 REMARK 500 6 SER A 5 -54.20 -149.67 REMARK 500 6 SER A 6 -74.19 -76.61 REMARK 500 6 LYS A 19 55.93 -94.66 REMARK 500 6 ASN A 51 -167.16 -110.13 REMARK 500 6 ALA A 76 31.35 -98.50 REMARK 500 6 ALA A 97 -172.24 61.09 REMARK 500 6 SER A 101 78.52 -110.26 REMARK 500 7 SER A 2 -46.28 -156.18 REMARK 500 7 SER A 6 168.53 60.28 REMARK 500 7 MET A 8 30.96 -99.07 REMARK 500 7 VAL A 9 -66.73 -133.04 REMARK 500 7 LYS A 19 55.16 -93.21 REMARK 500 7 ASP A 78 30.68 -98.78 REMARK 500 7 LEU A 82 40.01 -96.86 REMARK 500 7 VAL A 96 74.50 -67.32 REMARK 500 REMARK 500 THIS ENTRY HAS 141 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSO003001042.1 RELATED DB: TARGETDB DBREF 2DBG A 8 97 UNP P41218 MNDA_HUMAN 1 90 SEQADV 2DBG GLY A 1 UNP P41218 CLONING ARTIFACT SEQADV 2DBG SER A 2 UNP P41218 CLONING ARTIFACT SEQADV 2DBG SER A 3 UNP P41218 CLONING ARTIFACT SEQADV 2DBG GLY A 4 UNP P41218 CLONING ARTIFACT SEQADV 2DBG SER A 5 UNP P41218 CLONING ARTIFACT SEQADV 2DBG SER A 6 UNP P41218 CLONING ARTIFACT SEQADV 2DBG GLY A 7 UNP P41218 CLONING ARTIFACT SEQADV 2DBG SER A 98 UNP P41218 CLONING ARTIFACT SEQADV 2DBG GLY A 99 UNP P41218 CLONING ARTIFACT SEQADV 2DBG PRO A 100 UNP P41218 CLONING ARTIFACT SEQADV 2DBG SER A 101 UNP P41218 CLONING ARTIFACT SEQADV 2DBG SER A 102 UNP P41218 CLONING ARTIFACT SEQADV 2DBG GLY A 103 UNP P41218 CLONING ARTIFACT SEQRES 1 A 103 GLY SER SER GLY SER SER GLY MET VAL ASN GLU TYR LYS SEQRES 2 A 103 LYS ILE LEU LEU LEU LYS GLY PHE GLU LEU MET ASP ASP SEQRES 3 A 103 TYR HIS PHE THR SER ILE LYS SER LEU LEU ALA TYR ASP SEQRES 4 A 103 LEU GLY LEU THR THR LYS MET GLN GLU GLU TYR ASN ARG SEQRES 5 A 103 ILE LYS ILE THR ASP LEU MET GLU LYS LYS PHE GLN GLY SEQRES 6 A 103 VAL ALA CYS LEU ASP LYS LEU ILE GLU LEU ALA LYS ASP SEQRES 7 A 103 MET PRO SER LEU LYS ASN LEU VAL ASN ASN LEU ARG LYS SEQRES 8 A 103 GLU LYS SER LYS VAL ALA SER GLY PRO SER SER GLY HELIX 1 1 ASN A 10 LYS A 19 1 10 HELIX 2 2 ASP A 25 GLY A 41 1 17 HELIX 3 3 THR A 43 TYR A 50 1 8 HELIX 4 4 ASN A 51 PHE A 63 1 13 HELIX 5 5 VAL A 66 ALA A 76 1 11 HELIX 6 6 MET A 79 SER A 81 5 3 HELIX 7 7 LEU A 82 ALA A 97 1 16 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 9 2 Bytes