Header list of 2hm2.pdb file
Complete list - r 9 2 Bytes
HEADER APOPTOSIS 11-JUL-06 2HM2 TITLE SOLUTION STRUCTURE OF ASC2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PYRIN-ONLY PROTEIN 1; COMPND 3 CHAIN: Q; COMPND 4 FRAGMENT: PYRIN DOMAIN; COMPND 5 SYNONYM: ASC2; PYRIN DOMAIN CONTAINING 1; PAAD-ONLY PROTEIN; 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: POP1, PYDC1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE-30 KEYWDS PYRIN DOMAIN, SIX HELIX BUNDLE, APOPTOSIS EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.NATARAJAN,R.GHOSE,J.M.HILL REVDAT 5 09-MAR-22 2HM2 1 REMARK REVDAT 4 24-FEB-09 2HM2 1 VERSN REVDAT 3 12-DEC-06 2HM2 1 JRNL REVDAT 2 28-NOV-06 2HM2 1 JRNL REVDAT 1 25-JUL-06 2HM2 0 JRNL AUTH A.NATARAJAN,R.GHOSE,J.M.HILL JRNL TITL STRUCTURE AND DYNAMICS OF ASC2, A PYRIN DOMAIN-ONLY PROTEIN JRNL TITL 2 THAT REGULATES INFLAMMATORY SIGNALING JRNL REF J.BIOL.CHEM. V. 281 31863 2006 JRNL REFN ISSN 0021-9258 JRNL PMID 16905547 JRNL DOI 10.1074/JBC.M605458200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH 2.11.2 REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 1778 NMR-DERIVED RESTRAINTS, INCLUDING 1338 NOES, 197 DIHEDRAL REMARK 3 ANGLE RESTRAINTS, 73 3J(NH-HA) COUPLING CONSTANTS AND 170 13CA/ REMARK 3 CB SECONDARY SHIFT RESTRAINTS REMARK 4 REMARK 4 2HM2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-06. REMARK 100 THE DEPOSITION ID IS D_1000038502. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.3 REMARK 210 IONIC STRENGTH : 10 MM SODIUM PHOSPHATE AND 140 REMARK 210 MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1 MM ASC2 U-15N,13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : VARIOUS DOUBLE AND TRIPLE REMARK 210 RESONANCE EXPERIMENTS REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: Q 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 HZ3 LYS Q 24 O LEU Q 44 1.39 REMARK 500 O ALA Q 65 H VAL Q 69 1.47 REMARK 500 O ASP Q 48 H LEU Q 52 1.48 REMARK 500 O LYS Q 22 H LYS Q 26 1.50 REMARK 500 O ASP Q 54 H ALA Q 58 1.51 REMARK 500 O THR Q 53 H VAL Q 57 1.54 REMARK 500 O LYS Q 4 H ILE Q 8 1.55 REMARK 500 O LYS Q 26 HG1 THR Q 29 1.57 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 PRO Q 17 -37.29 -32.20 REMARK 500 1 GLU Q 34 -95.24 -32.86 REMARK 500 1 PRO Q 40 146.08 -39.95 REMARK 500 1 TYR Q 61 152.37 77.56 REMARK 500 1 ALA Q 88 48.26 -73.53 REMARK 500 2 THR Q 29 -50.76 -125.67 REMARK 500 2 PRO Q 31 147.52 -39.34 REMARK 500 2 ARG Q 33 -178.37 -69.36 REMARK 500 2 GLU Q 34 -94.10 25.29 REMARK 500 2 PRO Q 40 116.61 -37.77 REMARK 500 2 LEU Q 44 4.50 -68.34 REMARK 500 2 GLN Q 46 7.04 -49.70 REMARK 500 2 ILE Q 49 -16.63 -48.35 REMARK 500 2 TYR Q 61 147.77 80.54 REMARK 500 2 MET Q 78 64.33 -113.81 REMARK 500 2 GLN Q 86 -9.41 -58.18 REMARK 500 2 ALA Q 88 40.80 -73.93 REMARK 500 3 LEU Q 44 6.48 -69.30 REMARK 500 3 GLN Q 46 5.51 -45.55 REMARK 500 3 ILE Q 49 -19.13 -47.83 REMARK 500 3 TYR Q 61 152.63 76.90 REMARK 500 3 ALA Q 88 41.01 -73.32 REMARK 500 4 PRO Q 17 -39.21 -33.99 REMARK 500 4 GLU Q 34 92.68 -65.61 REMARK 500 4 PRO Q 40 125.36 -37.82 REMARK 500 4 LEU Q 44 6.81 -69.37 REMARK 500 4 GLN Q 46 12.20 -51.16 REMARK 500 4 TYR Q 61 152.90 77.73 REMARK 500 4 ALA Q 88 -81.66 -71.28 REMARK 500 5 ARG Q 33 -172.70 -69.27 REMARK 500 5 PRO Q 40 113.12 -38.52 REMARK 500 5 LEU Q 44 1.33 -64.81 REMARK 500 5 GLN Q 46 2.30 -47.99 REMARK 500 5 TYR Q 61 155.23 75.05 REMARK 500 5 MET Q 76 32.25 -86.37 REMARK 500 5 ALA Q 88 47.61 -72.28 REMARK 500 6 GLU Q 34 -88.92 -39.00 REMARK 500 6 PRO Q 40 112.65 -39.67 REMARK 500 6 GLN Q 46 11.34 -50.88 REMARK 500 6 ILE Q 49 -18.97 -48.69 REMARK 500 6 TYR Q 61 153.44 50.72 REMARK 500 6 ARG Q 77 40.85 70.64 REMARK 500 6 ALA Q 88 46.79 -73.53 REMARK 500 7 ARG Q 33 -179.43 -67.81 REMARK 500 7 GLU Q 34 -92.17 20.22 REMARK 500 7 ARG Q 38 170.62 -59.69 REMARK 500 7 PRO Q 40 108.87 -40.89 REMARK 500 7 GLN Q 46 8.19 -50.67 REMARK 500 7 ILE Q 49 -18.09 -47.91 REMARK 500 7 TYR Q 61 150.07 78.80 REMARK 500 REMARK 500 THIS ENTRY HAS 144 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2HM2 Q 1 89 UNP Q8WXC3 Q8WXC3_HUMAN 1 89 SEQRES 1 Q 89 MET GLY THR LYS ARG GLU ALA ILE LEU LYS VAL LEU GLU SEQRES 2 Q 89 ASN LEU THR PRO GLU GLU LEU LYS LYS PHE LYS MET LYS SEQRES 3 Q 89 LEU GLY THR VAL PRO LEU ARG GLU GLY PHE GLU ARG ILE SEQRES 4 Q 89 PRO ARG GLY ALA LEU GLY GLN LEU ASP ILE VAL ASP LEU SEQRES 5 Q 89 THR ASP LYS LEU VAL ALA SER TYR TYR GLU ASP TYR ALA SEQRES 6 Q 89 ALA GLU LEU VAL VAL ALA VAL LEU ARG ASP MET ARG MET SEQRES 7 Q 89 LEU GLU GLU ALA ALA ARG LEU GLN ARG ALA ALA HELIX 1 1 THR Q 3 GLU Q 13 1 11 HELIX 2 2 THR Q 16 LEU Q 27 1 12 HELIX 3 3 PRO Q 40 LEU Q 44 5 5 HELIX 4 4 ASP Q 48 MET Q 76 1 29 HELIX 5 5 MET Q 78 ARG Q 87 1 10 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