Header list of 2coo.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSFERASE 18-MAY-05 2COO TITLE SOLUTION STRUCTURE OF THE E3_BINDING DOMAIN OF DIHYDROLIPOAMIDE TITLE 2 BRANCHED CHAINTRANSACYLASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN COMPND 3 ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: E3_BINDING DOMAIN; COMPND 6 SYNONYM: DIHYDROLIPOYLLYSINE-RESIDUE 2-METHYLPROPANOYL, TRANSFERASE, COMPND 7 E2, DIHYDROLIPOAMIDE BRANCHED CHAIN TRANSACYLASE, BCKAD E2 SUBUNIT; COMPND 8 EC: 2.3.1.168; COMPND 9 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: DBT, BCATE2; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040510-10; SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS E3_BINDING DOMAIN, LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED- KEYWDS 2 CHAIN ALPHA-KETO ACID, DIHYDROLIPOYLLYSINE-RESIDUE (2- KEYWDS 3 METHYLPROPANOYL)TRANSFERASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL KEYWDS 4 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN KEYWDS 5 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.P.ZHANG,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS AUTHOR 2 INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2COO 1 REMARK SEQADV REVDAT 2 24-FEB-09 2COO 1 VERSN REVDAT 1 18-NOV-05 2COO 0 JRNL AUTH H.P.ZHANG,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE E3_BINDING DOMAIN OF JRNL TITL 2 DIHYDROLIPOAMIDE BRANCHED CHAINTRANSACYLASE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17 REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT,P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2COO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024456. 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 : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.11MM 13C, 15N-LABELED PROTEIN; REMARK 210 20MM D-TRIS-HCL (PH7.0); 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3 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 : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.04, REMARK 210 KUJIRA 0.9296, CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS 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 LYS A 12 161.17 -41.63 REMARK 500 1 VAL A 37 101.58 -58.21 REMARK 500 1 SER A 65 39.59 37.02 REMARK 500 2 ALA A 18 149.32 -175.04 REMARK 500 2 ASP A 42 31.71 -86.73 REMARK 500 2 ILE A 61 38.42 -82.41 REMARK 500 2 SER A 68 -70.92 -34.63 REMARK 500 3 ALA A 18 144.86 -170.83 REMARK 500 3 SER A 65 151.43 -47.50 REMARK 500 4 HIS A 8 40.27 -85.28 REMARK 500 4 ALA A 18 136.84 -174.57 REMARK 500 4 THR A 19 160.63 -47.27 REMARK 500 4 ASP A 42 47.03 -80.30 REMARK 500 4 SER A 65 89.12 -60.22 REMARK 500 5 LEU A 25 -19.06 -48.61 REMARK 500 5 VAL A 37 98.30 -66.84 REMARK 500 5 THR A 58 113.39 -34.20 REMARK 500 5 ALA A 60 97.46 -49.41 REMARK 500 5 ILE A 61 49.09 36.98 REMARK 500 5 PRO A 67 90.37 -69.79 REMARK 500 6 ILE A 11 149.96 -37.18 REMARK 500 6 VAL A 37 96.95 -54.77 REMARK 500 6 ALA A 60 96.97 -50.87 REMARK 500 6 PRO A 64 -175.28 -69.76 REMARK 500 7 VAL A 37 97.83 -61.20 REMARK 500 7 ASP A 42 31.95 -84.68 REMARK 500 7 ARG A 44 108.22 -53.12 REMARK 500 7 THR A 58 128.05 -34.56 REMARK 500 7 ILE A 61 40.45 -105.65 REMARK 500 7 SER A 69 106.44 -169.52 REMARK 500 8 ALA A 18 149.92 -175.04 REMARK 500 8 LEU A 25 -19.14 -49.14 REMARK 500 8 THR A 58 -31.49 -35.29 REMARK 500 8 PRO A 64 0.75 -69.78 REMARK 500 8 SER A 65 -39.80 -38.71 REMARK 500 9 SER A 5 117.88 -163.02 REMARK 500 9 THR A 19 160.77 -44.81 REMARK 500 9 LYS A 41 -70.56 -36.52 REMARK 500 9 SER A 65 118.43 -38.87 REMARK 500 10 SER A 3 -53.26 -129.28 REMARK 500 10 HIS A 8 148.23 -170.93 REMARK 500 10 GLN A 9 106.24 -167.06 REMARK 500 10 ALA A 60 -176.25 -56.94 REMARK 500 11 SER A 5 107.13 -170.64 REMARK 500 11 LEU A 25 -30.08 -36.22 REMARK 500 11 VAL A 36 97.54 -69.66 REMARK 500 11 VAL A 37 104.29 -54.80 REMARK 500 11 ASP A 42 47.74 -80.88 REMARK 500 11 PRO A 64 95.53 -69.76 REMARK 500 11 SER A 65 104.33 -35.05 REMARK 500 REMARK 500 THIS ENTRY HAS 102 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: HSS001000683.1 RELATED DB: TARGETDB DBREF 2COO A 8 65 UNP P11182 ODB2_HUMAN 163 220 SEQADV 2COO GLY A 1 UNP P11182 CLONING ARTIFACT SEQADV 2COO SER A 2 UNP P11182 CLONING ARTIFACT SEQADV 2COO SER A 3 UNP P11182 CLONING ARTIFACT SEQADV 2COO GLY A 4 UNP P11182 CLONING ARTIFACT SEQADV 2COO SER A 5 UNP P11182 CLONING ARTIFACT SEQADV 2COO SER A 6 UNP P11182 CLONING ARTIFACT SEQADV 2COO GLY A 7 UNP P11182 CLONING ARTIFACT SEQADV 2COO GLY A 66 UNP P11182 CLONING ARTIFACT SEQADV 2COO PRO A 67 UNP P11182 CLONING ARTIFACT SEQADV 2COO SER A 68 UNP P11182 CLONING ARTIFACT SEQADV 2COO SER A 69 UNP P11182 CLONING ARTIFACT SEQADV 2COO GLY A 70 UNP P11182 CLONING ARTIFACT SEQRES 1 A 70 GLY SER SER GLY SER SER GLY HIS GLN GLU ILE LYS GLY SEQRES 2 A 70 ARG LYS THR LEU ALA THR PRO ALA VAL ARG ARG LEU ALA SEQRES 3 A 70 MET GLU ASN ASN ILE LYS LEU SER GLU VAL VAL GLY SER SEQRES 4 A 70 GLY LYS ASP GLY ARG ILE LEU LYS GLU ASP ILE LEU ASN SEQRES 5 A 70 TYR LEU GLU LYS GLN THR GLY ALA ILE LEU PRO PRO SER SEQRES 6 A 70 GLY PRO SER SER GLY HELIX 1 1 PRO A 20 ASN A 29 1 10 HELIX 2 2 LEU A 33 GLU A 35 5 3 HELIX 3 3 LYS A 47 LEU A 54 1 8 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