Header list of 1uk5.pdb file
Complete list - r 2 2 Bytes
HEADER CHAPERONE 19-AUG-03 1UK5 TITLE SOLUTION STRUCTURE OF THE MURINE BAG DOMAIN OF BCL2-ASSOCIATED TITLE 2 ATHANOGENE 3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BAG-FAMILY MOLECULAR CHAPERONE REGULATOR-3; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: BAG DOMAIN; COMPND 5 SYNONYM: BCL2-ASSOCIATED ATHANOGENE 3, BCL-2 BINDING ATHANOGENE-3, COMPND 6 BAG-3, BCL-2-BINDING PROTEIN BIS; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: FANTOM 2 CDNA 4931440G06; SOURCE 6 EXPRESSION_SYSTEM: CELL-FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P020122-09 KEYWDS TRIPLE HELIX BANDLE, CAIR-1, BIS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, CHAPERONE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR R.HATTA,M.YOSHIDA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 4 02-MAR-22 1UK5 1 REMARK SEQADV REVDAT 3 31-MAR-10 1UK5 1 JRNL REVDAT 2 24-FEB-09 1UK5 1 VERSN REVDAT 1 19-FEB-04 1UK5 0 JRNL AUTH A.ARAKAWA,N.HANDA,N.OHSAWA,M.SHIDA,T.KIGAWA,F.HAYASHI, JRNL AUTH 2 M.SHIROUZU,S.YOKOYAMA JRNL TITL THE C-TERMINAL BAG DOMAIN OF BAG5 INDUCES CONFORMATIONAL JRNL TITL 2 CHANGES OF THE HSP70 NUCLEOTIDE-BINDING DOMAIN FOR ADP-ATP JRNL TITL 3 EXCHANGE JRNL REF STRUCTURE V. 18 309 2010 JRNL REFN ISSN 0969-2126 JRNL PMID 20223214 JRNL DOI 10.1016/J.STR.2010.01.004 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 1.0.7 REMARK 3 AUTHORS : GUENTERT, P. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1UK5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-AUG-03. REMARK 100 THE DEPOSITION ID IS D_1000005917. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 250MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.7MM 13C, 15N-LABELED PROTEIN, REMARK 210 20MM PHOSPHATE BUFFER, 90MM NACL, REMARK 210 40MM MGSO4, 0.4MM NAN3, 8% D2O 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 : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 6.1C, NMRPIPE 20020425, REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.823, REMARK 210 CYANA 1.0.7 REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, TARGET REMARK 210 FUNCTION 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 O TYR A 58 H GLU A 62 1.54 REMARK 500 O ALA A 86 H GLY A 90 1.58 REMARK 500 O ARG A 80 H ARG A 84 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 SER A 3 168.25 58.64 REMARK 500 1 SER A 5 116.47 -173.82 REMARK 500 1 ALA A 8 81.33 -176.53 REMARK 500 1 ALA A 10 84.98 -159.48 REMARK 500 1 ALA A 13 112.67 -160.78 REMARK 500 1 ALA A 14 68.89 -156.00 REMARK 500 1 SER A 17 78.93 -103.65 REMARK 500 1 GLU A 19 154.85 -39.05 REMARK 500 1 ALA A 20 172.23 63.56 REMARK 500 1 GLU A 21 176.44 68.32 REMARK 500 1 GLU A 50 132.11 -170.14 REMARK 500 1 GLU A 78 -59.17 69.00 REMARK 500 1 SER A 109 98.13 -173.06 REMARK 500 1 SER A 110 106.30 -169.62 REMARK 500 2 SER A 3 128.45 65.30 REMARK 500 2 SER A 5 139.56 -177.05 REMARK 500 2 ALA A 14 -53.95 166.81 REMARK 500 2 GLU A 19 145.61 175.96 REMARK 500 2 GLU A 21 155.43 -43.78 REMARK 500 2 LYS A 25 -123.75 -142.71 REMARK 500 2 LYS A 52 -164.43 -121.88 REMARK 500 2 GLU A 78 -62.13 68.52 REMARK 500 2 VAL A 83 -62.82 -94.78 REMARK 500 2 ARG A 84 -30.96 -37.72 REMARK 500 2 GLN A 85 -74.58 -75.25 REMARK 500 2 SER A 110 118.30 62.82 REMARK 500 3 ALA A 13 133.81 67.32 REMARK 500 3 ALA A 14 114.04 -169.57 REMARK 500 3 LYS A 16 -37.90 -179.99 REMARK 500 3 GLU A 19 96.90 49.12 REMARK 500 3 GLU A 21 155.08 -38.93 REMARK 500 3 LYS A 25 -133.67 -111.40 REMARK 500 3 GLU A 62 -39.51 -39.33 REMARK 500 3 LEU A 65 -78.14 -65.31 REMARK 500 3 LYS A 93 -75.26 -56.13 REMARK 500 3 GLU A 102 -78.08 -47.84 REMARK 500 3 SER A 110 100.53 55.16 REMARK 500 4 SER A 2 -69.35 74.17 REMARK 500 4 SER A 3 166.08 67.56 REMARK 500 4 ALA A 8 75.58 69.77 REMARK 500 4 GLU A 11 91.23 178.14 REMARK 500 4 LYS A 16 -93.48 -83.32 REMARK 500 4 GLU A 19 -175.38 47.80 REMARK 500 4 LYS A 25 -134.45 -110.68 REMARK 500 4 LYS A 52 -151.66 -123.32 REMARK 500 4 LEU A 65 -75.67 -54.26 REMARK 500 4 GLU A 78 -61.18 71.18 REMARK 500 4 SER A 109 -58.76 -151.07 REMARK 500 5 SER A 2 163.19 64.08 REMARK 500 5 SER A 5 95.93 54.39 REMARK 500 REMARK 500 THIS ENTRY HAS 247 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007013830.1 RELATED DB: TARGETDB DBREF 1UK5 A 8 105 UNP Q9JLV1 BAG3_MOUSE 406 503 SEQADV 1UK5 GLY A 1 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 SER A 2 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 SER A 3 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 GLY A 4 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 SER A 5 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 SER A 6 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 GLY A 7 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 SER A 106 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 GLY A 107 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 PRO A 108 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 SER A 109 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 SER A 110 UNP Q9JLV1 EXPRESSION TAG SEQADV 1UK5 GLY A 111 UNP Q9JLV1 EXPRESSION TAG SEQRES 1 A 111 GLY SER SER GLY SER SER GLY ALA PRO ALA GLU PRO ALA SEQRES 2 A 111 ALA PRO LYS SER GLY GLU ALA GLU THR PRO PRO LYS HIS SEQRES 3 A 111 PRO GLY VAL LEU LYS VAL GLU ALA ILE LEU GLU LYS VAL SEQRES 4 A 111 GLN GLY LEU GLU GLN ALA VAL ASP SER PHE GLU GLY LYS SEQRES 5 A 111 LYS THR ASP LYS LYS TYR LEU MET ILE GLU GLU TYR LEU SEQRES 6 A 111 THR LYS GLU LEU LEU ALA LEU ASP SER VAL ASP PRO GLU SEQRES 7 A 111 GLY ARG ALA ASP VAL ARG GLN ALA ARG ARG ASP GLY VAL SEQRES 8 A 111 ARG LYS VAL GLN THR ILE LEU GLU LYS LEU GLU GLN LYS SEQRES 9 A 111 ALA SER GLY PRO SER SER GLY HELIX 1 1 PRO A 27 ASP A 47 1 21 HELIX 2 2 LYS A 56 SER A 74 1 19 HELIX 3 3 ALA A 81 ALA A 105 1 25 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