Header list of 1j26.pdb file
Complete list - r 25 2 Bytes
HEADER TRANSLATION 25-DEC-02 1J26 TITLE SOLUTION STRUCTURE OF A PUTATIVE PEPTIDYL-TRNA HYDROLASE DOMAIN IN A TITLE 2 MOUSE HYPOTHETICAL PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMATURE COLON CARCINOMA TRANSCRIPT 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PEPTIDYL-TRNA HYDROLASE DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: NIA MOUSE 15K CDNA CLONE: H3024H01; SOURCE 6 EXPRESSION_SYSTEM: CELL-FREE PROTEIN SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P020715-17 KEYWDS PEPTIDE CHAIN RELEASE FACTORS, RF-1, THE GGQ MOTIF, IMMATURE COLON KEYWDS 2 CARCINOMA TRANSCRIPT 1, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 3 INITIATIVE, RSGI, STRUCTURAL GENOMICS, TRANSLATION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.NAMEKI,T.KIGAWA,S.KOSHIBA,N.KOBAYASHI,N.TOCHIO,M.INOUE,S.YOKOYAMA, AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 13-OCT-10 1J26 1 JRNL REVDAT 2 24-FEB-09 1J26 1 VERSN REVDAT 1 01-JUN-04 1J26 0 JRNL AUTH Y.HANDA,Y.HIKAWA,N.TOCHIO,H.KOGURE,M.INOUE,S.KOSHIBA, JRNL AUTH 2 P.GUNTERT,Y.INOUE,T.KIGAWA,S.YOKOYAMA,N.NAMEKI JRNL TITL SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF THE JRNL TITL 2 MITOCHONDRIAL PROTEIN ICT1 THAT IS ESSENTIAL FOR CELL JRNL TITL 3 VITALITY JRNL REF J.MOL.BIOL. 2010 JRNL REFN ESSN 1089-8638 JRNL PMID 20869366 JRNL DOI 10.1016/J.JMB.2010.09.033 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : OPALP REMARK 3 AUTHORS : GUENTERT, P. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1J26 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-DEC-02. REMARK 100 THE RCSB ID CODE IS RCSB005536. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.7MM PEPTIDYL-TRNA HYDROLASE REMARK 210 DOMAIN U-15N, 13C; 20MM PHOSPHATE REMARK 210 BUFFER NA; 100MM NACL; 1MM D-DTT; REMARK 210 0.02% NAN3; 90% H2O, 10% 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 : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.6, NMRPIPE 20020425, REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.704, REMARK 210 CYANA 1.0.7 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 MOLECULAR DYNAMICS 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, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY, 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 HG SER A 82 OE1 GLU A 94 1.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 5 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 7 TYR A 26 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES REMARK 500 13 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES 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 2 84.83 -69.64 REMARK 500 1 SER A 3 -139.86 50.14 REMARK 500 1 SER A 5 75.29 48.97 REMARK 500 1 GLN A 12 -75.67 -74.73 REMARK 500 1 SER A 15 -27.35 -148.20 REMARK 500 1 ILE A 17 95.72 50.11 REMARK 500 1 SER A 29 122.31 80.46 REMARK 500 1 ASN A 36 -71.25 -68.13 REMARK 500 1 VAL A 37 64.97 32.16 REMARK 500 1 LYS A 74 -49.57 141.17 REMARK 500 1 SER A 84 -6.99 -162.64 REMARK 500 1 GLN A 88 -71.73 -79.93 REMARK 500 1 SER A 110 -53.33 -156.45 REMARK 500 1 SER A 111 120.17 -175.61 REMARK 500 2 ALA A 10 -169.53 58.86 REMARK 500 2 LYS A 11 -3.84 65.79 REMARK 500 2 SER A 14 89.45 42.35 REMARK 500 2 ILE A 17 101.30 54.34 REMARK 500 2 SER A 29 138.00 58.25 REMARK 500 2 SER A 30 162.18 135.06 REMARK 500 2 PRO A 32 45.76 -78.44 REMARK 500 2 GLN A 35 59.14 153.09 REMARK 500 2 ASN A 36 -56.95 78.87 REMARK 500 2 ASN A 38 -52.93 61.94 REMARK 500 2 LYS A 39 -117.76 -139.74 REMARK 500 2 VAL A 40 -82.03 65.43 REMARK 500 2 ASN A 41 73.73 73.26 REMARK 500 2 SER A 42 52.35 -149.70 REMARK 500 2 ASP A 54 38.67 -84.84 REMARK 500 2 TRP A 55 -0.15 -141.49 REMARK 500 2 LYS A 74 -60.09 133.39 REMARK 500 2 SER A 84 -14.41 -148.66 REMARK 500 2 GLN A 88 -85.12 -90.60 REMARK 500 2 SER A 110 96.53 -66.38 REMARK 500 2 SER A 111 149.32 66.46 REMARK 500 3 SER A 5 177.95 63.54 REMARK 500 3 ALA A 13 157.90 122.12 REMARK 500 3 ILE A 17 103.90 54.81 REMARK 500 3 ARG A 28 -20.45 142.19 REMARK 500 3 SER A 29 147.05 56.69 REMARK 500 3 SER A 30 -33.09 -141.31 REMARK 500 3 GLN A 35 -119.02 -136.79 REMARK 500 3 ASN A 41 38.57 -153.88 REMARK 500 3 ASP A 54 -39.61 77.73 REMARK 500 3 LYS A 74 -40.05 -175.54 REMARK 500 3 SER A 84 -1.96 -156.61 REMARK 500 3 TYR A 87 -176.94 -69.00 REMARK 500 3 GLN A 88 -85.50 -104.72 REMARK 500 4 SER A 2 125.94 110.49 REMARK 500 4 ALA A 13 174.92 63.14 REMARK 500 REMARK 500 THIS ENTRY HAS 315 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ARG A 28 SER A 29 2 -141.18 REMARK 500 GLY A 1 SER A 2 5 147.37 REMARK 500 GLY A 1 SER A 2 9 147.57 REMARK 500 LYS A 39 VAL A 40 9 145.87 REMARK 500 SER A 30 GLY A 31 16 145.96 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 21 0.08 SIDE CHAIN REMARK 500 1 TYR A 26 0.06 SIDE CHAIN REMARK 500 1 ARG A 28 0.10 SIDE CHAIN REMARK 500 3 ARG A 28 0.17 SIDE CHAIN REMARK 500 4 TYR A 26 0.09 SIDE CHAIN REMARK 500 6 TYR A 16 0.08 SIDE CHAIN REMARK 500 7 ARG A 90 0.12 SIDE CHAIN REMARK 500 8 TYR A 26 0.07 SIDE CHAIN REMARK 500 8 ARG A 100 0.08 SIDE CHAIN REMARK 500 9 ARG A 61 0.08 SIDE CHAIN REMARK 500 10 TYR A 26 0.06 SIDE CHAIN REMARK 500 10 ARG A 61 0.07 SIDE CHAIN REMARK 500 10 ARG A 100 0.12 SIDE CHAIN REMARK 500 11 ARG A 28 0.08 SIDE CHAIN REMARK 500 12 ARG A 21 0.08 SIDE CHAIN REMARK 500 12 ARG A 86 0.10 SIDE CHAIN REMARK 500 13 ARG A 86 0.10 SIDE CHAIN REMARK 500 13 ARG A 100 0.14 SIDE CHAIN REMARK 500 14 TYR A 26 0.07 SIDE CHAIN REMARK 500 14 TYR A 87 0.09 SIDE CHAIN REMARK 500 15 TYR A 26 0.06 SIDE CHAIN REMARK 500 15 TYR A 87 0.09 SIDE CHAIN REMARK 500 16 TYR A 26 0.12 SIDE CHAIN REMARK 500 18 ARG A 90 0.10 SIDE CHAIN REMARK 500 19 ARG A 28 0.09 SIDE CHAIN REMARK 500 19 ARG A 61 0.10 SIDE CHAIN REMARK 500 20 ARG A 21 0.13 SIDE CHAIN 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: MMA001000238.1 RELATED DB: TARGETDB DBREF 1J26 A 8 106 UNP Q8R035 ICT1_MOUSE 63 161 SEQADV 1J26 GLY A 1 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 SER A 2 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 SER A 3 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 GLY A 4 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 SER A 5 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 SER A 6 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 GLY A 7 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 SER A 107 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 GLY A 108 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 PRO A 109 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 SER A 110 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 SER A 111 UNP Q8R035 EXPRESSION TAG SEQADV 1J26 GLY A 112 UNP Q8R035 EXPRESSION TAG SEQRES 1 A 112 GLY SER SER GLY SER SER GLY GLU HIS ALA LYS GLN ALA SEQRES 2 A 112 SER SER TYR ILE PRO LEU ASP ARG LEU SER ILE SER TYR SEQRES 3 A 112 CYS ARG SER SER GLY PRO GLY GLY GLN ASN VAL ASN LYS SEQRES 4 A 112 VAL ASN SER LYS ALA GLU VAL ARG PHE HIS LEU ALA SER SEQRES 5 A 112 ALA ASP TRP ILE GLU GLU PRO VAL ARG GLN LYS ILE ALA SEQRES 6 A 112 LEU THR HIS LYS ASN LYS ILE ASN LYS ALA GLY GLU LEU SEQRES 7 A 112 VAL LEU THR SER GLU SER SER ARG TYR GLN PHE ARG ASN SEQRES 8 A 112 LEU ALA GLU CYS LEU GLN LYS ILE ARG ASP MET ILE ALA SEQRES 9 A 112 GLU ALA SER GLY PRO SER SER GLY HELIX 1 1 GLU A 58 THR A 67 1 10 HELIX 2 2 PHE A 89 SER A 107 1 19 SHEET 1 A 3 SER A 23 CYS A 27 0 SHEET 2 A 3 LYS A 43 HIS A 49 -1 O ARG A 47 N SER A 23 SHEET 3 A 3 GLU A 77 SER A 82 -1 O LEU A 78 N PHE A 48 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 25 2 Bytes