Header list of 2cqu.pdb file
Complete list - r 9 2 Bytes
HEADER ISOMERASE 20-MAY-05 2CQU TITLE SOLUTION STRUCTURE OF RSGI RUH-045, A HUMAN ACYL-COA BINDING PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PEROXISOMAL D3,D2-ENOYL-COA ISOMERASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ACBP DOMAIN; COMPND 5 SYNONYM: RSGI RUH-045, ACYL-COA BINDING PROTEIN; COMPND 6 EC: 5.3.3.8; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P040329-47; SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS (E.COLI) KEYWDS ACYL-COA BINDING PROTEIN, HOMO SAPIENS, STRUCTURAL GENOMICS, NPPSFA, KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, ISOMERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR Y.TSUBOTA,A.Z.M.RUHUL MOMEN,H.ONUKI,H.HIROTA,K.SAITO,S.KOSHIBA, AUTHOR 2 T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE AUTHOR 3 (RSGI) REVDAT 3 09-MAR-22 2CQU 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CQU 1 VERSN REVDAT 1 20-NOV-05 2CQU 0 JRNL AUTH Y.TSUBOTA,A.Z.M.RUHUL MOMEN,H.ONUKI,H.HIROTA,K.SAITO, JRNL AUTH 2 S.KOSHIBA,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF RSGI RUH-045, A HUMAN ACYL-COA BINDING JRNL TITL 2 PROTEIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 2.0.17 REMARK 3 AUTHORS : GUNTERT, P. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2CQU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024521. 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 : 100MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.60MM ACYL-COA BINDING PROTEIN REMARK 210 U-15N, 13C; 20MM D-TRIS-HCL(PH REMARK 210 7.0), 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 : XWINNMR 3.6, NMRPIPE 20031121, REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.9295, REMARK 210 CYANA 2.0.17 REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH REMARK 210 THE LOWEST ENERGY,STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 VIOLATIONS 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 ARG A 10 -58.40 -122.68 REMARK 500 1 CYS A 54 105.29 -48.50 REMARK 500 1 SER A 78 31.59 -96.54 REMARK 500 1 SER A 101 84.67 -62.18 REMARK 500 1 PRO A 113 93.45 -69.76 REMARK 500 2 ARG A 14 131.31 -34.32 REMARK 500 2 CYS A 54 105.56 -49.36 REMARK 500 2 ASP A 63 42.04 -90.98 REMARK 500 2 LEU A 64 -34.60 -38.45 REMARK 500 2 SER A 78 33.93 -84.36 REMARK 500 2 GLU A 106 141.85 -39.32 REMARK 500 3 SER A 3 42.23 -101.72 REMARK 500 3 MET A 8 113.03 -166.68 REMARK 500 3 ASP A 33 107.04 -35.97 REMARK 500 3 THR A 50 -46.19 -134.98 REMARK 500 3 CYS A 54 103.78 -44.60 REMARK 500 3 SER A 78 36.61 -83.72 REMARK 500 4 ASN A 36 -19.43 -48.34 REMARK 500 4 CYS A 54 104.88 -46.93 REMARK 500 4 SER A 78 31.41 -87.17 REMARK 500 5 THR A 11 -34.12 -35.97 REMARK 500 5 ASN A 36 -18.48 -49.42 REMARK 500 5 THR A 50 -41.12 -135.00 REMARK 500 5 CYS A 54 105.27 -43.23 REMARK 500 5 ASP A 63 45.65 -92.88 REMARK 500 5 SER A 78 31.91 -95.18 REMARK 500 5 GLU A 100 168.53 -45.95 REMARK 500 5 THR A 109 35.09 34.11 REMARK 500 5 SER A 111 48.04 39.05 REMARK 500 6 CYS A 54 104.47 -48.06 REMARK 500 6 SER A 78 31.76 -87.68 REMARK 500 6 SER A 103 -57.01 -128.99 REMARK 500 7 MET A 8 89.83 -63.66 REMARK 500 7 THR A 11 32.45 -95.05 REMARK 500 7 THR A 50 -46.87 -134.76 REMARK 500 7 CYS A 54 105.28 -46.98 REMARK 500 7 ASP A 63 74.07 -105.36 REMARK 500 7 SER A 78 31.83 -89.09 REMARK 500 7 GLU A 100 95.92 -63.27 REMARK 500 8 SER A 16 -67.21 -123.83 REMARK 500 8 GLN A 17 -47.74 -131.66 REMARK 500 8 THR A 50 -45.56 -131.43 REMARK 500 8 CYS A 54 104.76 -41.68 REMARK 500 8 PRO A 59 -178.34 -69.76 REMARK 500 8 ILE A 65 -72.59 -70.56 REMARK 500 8 SER A 78 39.58 -82.56 REMARK 500 8 GLU A 100 101.18 -46.47 REMARK 500 8 VAL A 105 91.78 -66.68 REMARK 500 9 SER A 2 -51.10 -121.18 REMARK 500 9 SER A 5 108.07 -51.83 REMARK 500 REMARK 500 THIS ENTRY HAS 129 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSS001000550.1 RELATED DB: TARGETDB DBREF 2CQU A 8 110 UNP O75521 PECI_HUMAN 1 103 SEQADV 2CQU GLY A 1 UNP O75521 CLONING ARTIFACT SEQADV 2CQU SER A 2 UNP O75521 CLONING ARTIFACT SEQADV 2CQU SER A 3 UNP O75521 CLONING ARTIFACT SEQADV 2CQU GLY A 4 UNP O75521 CLONING ARTIFACT SEQADV 2CQU SER A 5 UNP O75521 CLONING ARTIFACT SEQADV 2CQU SER A 6 UNP O75521 CLONING ARTIFACT SEQADV 2CQU GLY A 7 UNP O75521 CLONING ARTIFACT SEQADV 2CQU SER A 111 UNP O75521 CLONING ARTIFACT SEQADV 2CQU GLY A 112 UNP O75521 CLONING ARTIFACT SEQADV 2CQU PRO A 113 UNP O75521 CLONING ARTIFACT SEQADV 2CQU SER A 114 UNP O75521 CLONING ARTIFACT SEQADV 2CQU SER A 115 UNP O75521 CLONING ARTIFACT SEQADV 2CQU GLY A 116 UNP O75521 CLONING ARTIFACT SEQRES 1 A 116 GLY SER SER GLY SER SER GLY MET ASN ARG THR ALA MET SEQRES 2 A 116 ARG ALA SER GLN LYS ASP PHE GLU ASN SER MET ASN GLN SEQRES 3 A 116 VAL LYS LEU LEU LYS LYS ASP PRO GLY ASN GLU VAL LYS SEQRES 4 A 116 LEU LYS LEU TYR ALA LEU TYR LYS GLN ALA THR GLU GLY SEQRES 5 A 116 PRO CYS ASN MET PRO LYS PRO GLY VAL PHE ASP LEU ILE SEQRES 6 A 116 ASN LYS ALA LYS TRP ASP ALA TRP ASN ALA LEU GLY SER SEQRES 7 A 116 LEU PRO LYS GLU ALA ALA ARG GLN ASN TYR VAL ASP LEU SEQRES 8 A 116 VAL SER SER LEU SER PRO SER LEU GLU SER SER SER GLN SEQRES 9 A 116 VAL GLU PRO GLY THR ASP SER GLY PRO SER SER GLY HELIX 1 1 SER A 16 LEU A 30 1 15 HELIX 2 2 GLY A 35 LYS A 47 1 13 HELIX 3 3 ASP A 63 GLY A 77 1 15 HELIX 4 4 PRO A 80 SER A 96 1 17 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