Header list of 2g0q.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 13-FEB-06 2G0Q TITLE SOLUTION STRUCTURE OF AT5G39720.1 FROM ARABIDOPSIS THALIANA COMPND MOL_ID: 1; COMPND 2 MOLECULE: AT5G39720.1 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 GENE: AT5G39720.1; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PEU-HIS; SOURCE 8 OTHER_DETAILS: WHEAT GERM CELL-FREE, IN VITRO EXPRESSION KEYWDS AT5G39720.1, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, PSI, KEYWDS 2 CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, CESG, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.F.VOLKMAN,F.C.PETERSON,B.L.LYTLE,CENTER FOR EUKARYOTIC STRUCTURAL AUTHOR 2 GENOMICS (CESG) REVDAT 4 09-MAR-22 2G0Q 1 REMARK SEQADV REVDAT 3 24-FEB-09 2G0Q 1 VERSN REVDAT 2 02-JAN-07 2G0Q 1 JRNL REVDAT 1 28-FEB-06 2G0Q 0 JRNL AUTH B.L.LYTLE,F.C.PETERSON,E.M.TYLER,C.L.NEWMAN,D.A.VINAROV, JRNL AUTH 2 J.L.MARKLEY,B.F.VOLKMAN JRNL TITL SOLUTION STRUCTURE OF ARABIDOPSIS THALIANA PROTEIN JRNL TITL 2 AT5G39720.1, A MEMBER OF THE AIG2-LIKE PROTEIN FAMILY. JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 62 490 2006 JRNL REFN ESSN 1744-3091 JRNL PMID 16754964 JRNL DOI 10.1107/S1744309106015946 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH 2.9.3 REMARK 3 AUTHORS : SCHWIETERS, C.D.,KUSZEWSKI, J.J.,TJANDRA, N., REMARK 3 CLORE, G.M. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 STRUCTURES ARE BASED ON A TOTAL OF 1989 NOE CONSTRAINTS ( 522 REMARK 3 INTRA, 564 SEQEUNTIAL, 267 MEDIUM AND 636 LONG RANGE CONSTRAINTS) REMARK 3 AND 189 PHI AND PSI DIHEDRAL ANGLE CONSTRAINTS. REMARK 4 REMARK 4 2G0Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-06. REMARK 100 THE DEPOSITION ID IS D_1000036542. 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 : 101 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.9 MM AT5G39720.1 U-15N/13C, 10 REMARK 210 MM DEUTERATED BIS-TRIS, 100 MM REMARK 210 NACL, 5 MM DITHIOTHREITOL, 95% REMARK 210 H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY (AROMATIC) REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRPIPE 2004, REMARK 210 SPSCAN 1.1.0, XEASY 1.3, GARANT REMARK 210 2.1 REMARK 210 METHOD USED : AUTOMATED METHODS WERE USED FOR REMARK 210 BACKBONE CHEMICAL SHIFT REMARK 210 ASSIGNMENT AND ITERATIVE NOE REMARK 210 REFINEMENT. FINAL STRUCTURES REMARK 210 WERE OBTAINED BY MOLECULAR REMARK 210 DYNAMICS IN EXPLICIT SOLVENT REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: ALL TRIPLE-RESONANCE AND NOESY SPECTRA WERE ACQUIRED REMARK 210 USING A CRYOGENIC PROBE. 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 GLY A 1 REMARK 465 HIS A 2 REMARK 465 HIS A 3 REMARK 465 HIS A 4 REMARK 465 HIS A 5 REMARK 465 HIS A 6 REMARK 465 HIS A 7 REMARK 465 LEU A 8 REMARK 465 GLU A 9 REMARK 465 GLY A 159 REMARK 465 GLN A 160 REMARK 465 GLY A 161 REMARK 465 ASN A 162 REMARK 465 ASP A 163 REMARK 465 ASP A 164 REMARK 465 ILE A 165 REMARK 465 SER A 166 REMARK 465 HIS A 167 REMARK 465 VAL A 168 REMARK 465 LEU A 169 REMARK 465 ARG A 170 REMARK 465 GLU A 171 REMARK 465 ASP A 172 REMARK 465 GLN A 173 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 HG1 THR A 80 OE1 GLU A 83 1.56 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 11 18.38 -146.35 REMARK 500 1 ASP A 13 89.06 65.07 REMARK 500 1 SER A 14 74.52 -106.58 REMARK 500 1 TYR A 23 -60.20 -144.08 REMARK 500 1 LEU A 36 -72.82 -115.38 REMARK 500 1 ASP A 37 -49.48 179.26 REMARK 500 1 LEU A 55 162.15 176.09 REMARK 500 1 ASN A 107 -108.55 -99.53 REMARK 500 1 SER A 108 19.31 -159.67 REMARK 500 1 PHE A 127 105.40 -58.79 REMARK 500 1 LYS A 155 -42.01 -177.72 REMARK 500 2 ASP A 13 107.54 60.22 REMARK 500 2 ASP A 37 -50.01 172.11 REMARK 500 2 LEU A 55 125.47 -171.53 REMARK 500 2 PRO A 61 94.14 -63.71 REMARK 500 2 ASN A 107 -95.99 -137.41 REMARK 500 2 SER A 108 27.80 -175.83 REMARK 500 2 LYS A 121 -37.04 58.16 REMARK 500 2 PHE A 127 128.49 -171.69 REMARK 500 3 ASP A 13 88.02 58.04 REMARK 500 3 ASP A 37 -49.07 174.98 REMARK 500 3 LEU A 55 -71.71 -141.85 REMARK 500 3 LYS A 56 -70.83 161.62 REMARK 500 3 PRO A 61 90.98 -65.98 REMARK 500 3 ASN A 107 22.18 -146.60 REMARK 500 3 ASN A 131 87.13 -64.75 REMARK 500 4 SER A 11 18.52 -141.96 REMARK 500 4 GLN A 16 -167.02 66.68 REMARK 500 4 LEU A 36 -71.86 -109.80 REMARK 500 4 ASP A 37 -45.03 176.11 REMARK 500 4 LYS A 121 1.57 56.12 REMARK 500 4 PRO A 157 98.24 -60.80 REMARK 500 5 SER A 11 83.97 -157.14 REMARK 500 5 ASP A 13 -87.44 59.88 REMARK 500 5 LEU A 36 -77.31 -103.65 REMARK 500 5 ASP A 37 -30.15 162.57 REMARK 500 5 PRO A 61 96.98 -69.63 REMARK 500 5 ASN A 107 -83.49 -138.32 REMARK 500 5 SER A 108 -13.61 177.49 REMARK 500 5 PHE A 127 92.88 -69.13 REMARK 500 5 ASN A 131 0.19 -61.96 REMARK 500 5 LYS A 155 77.32 67.23 REMARK 500 6 TYR A 23 -51.66 -121.40 REMARK 500 6 LEU A 36 -76.42 -125.18 REMARK 500 6 ASP A 37 -55.90 -169.77 REMARK 500 6 LYS A 121 65.01 37.77 REMARK 500 6 ALA A 122 -26.62 -164.29 REMARK 500 7 ASP A 13 -52.09 65.98 REMARK 500 7 LEU A 36 -71.69 -119.13 REMARK 500 7 ASP A 37 -46.73 167.96 REMARK 500 REMARK 500 THIS ENTRY HAS 168 RAMACHANDRAN OUTLIERS. 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 3 ARG A 97 0.10 SIDE CHAIN REMARK 500 3 ARG A 104 0.08 SIDE CHAIN REMARK 500 6 ARG A 54 0.15 SIDE CHAIN REMARK 500 9 ARG A 52 0.07 SIDE CHAIN REMARK 500 11 ARG A 104 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GO.22446 RELATED DB: TARGETDB DBREF 2G0Q A 10 173 GB 15242449 NP_198788 2 165 SEQADV 2G0Q GLY A 1 GB 15242449 CLONING ARTIFACT SEQADV 2G0Q HIS A 2 GB 15242449 EXPRESSION TAG SEQADV 2G0Q HIS A 3 GB 15242449 EXPRESSION TAG SEQADV 2G0Q HIS A 4 GB 15242449 EXPRESSION TAG SEQADV 2G0Q HIS A 5 GB 15242449 EXPRESSION TAG SEQADV 2G0Q HIS A 6 GB 15242449 EXPRESSION TAG SEQADV 2G0Q HIS A 7 GB 15242449 EXPRESSION TAG SEQADV 2G0Q LEU A 8 GB 15242449 CLONING ARTIFACT SEQADV 2G0Q GLU A 9 GB 15242449 CLONING ARTIFACT SEQRES 1 A 173 GLY HIS HIS HIS HIS HIS HIS LEU GLU CYS SER SER ASP SEQRES 2 A 173 SER LEU GLN LEU HIS ASN VAL PHE VAL TYR GLY SER PHE SEQRES 3 A 173 GLN ASP PRO ASP VAL ILE ASN VAL MET LEU ASP ARG THR SEQRES 4 A 173 PRO GLU ILE VAL SER ALA THR LEU PRO GLY PHE GLN ARG SEQRES 5 A 173 PHE ARG LEU LYS GLY ARG LEU TYR PRO CYS ILE VAL PRO SEQRES 6 A 173 SER GLU LYS GLY GLU VAL HIS GLY LYS VAL LEU MET GLY SEQRES 7 A 173 VAL THR SER ASP GLU LEU GLU ASN LEU ASP ALA VAL GLU SEQRES 8 A 173 GLY ASN GLU TYR GLU ARG VAL THR VAL GLY ILE VAL ARG SEQRES 9 A 173 GLU ASP ASN SER GLU LYS MET ALA VAL LYS THR TYR MET SEQRES 10 A 173 TRP ILE ASN LYS ALA ASP PRO ASP MET PHE GLY GLU TRP SEQRES 11 A 173 ASN PHE GLU GLU TRP LYS ARG LEU HIS LYS LYS LYS PHE SEQRES 12 A 173 ILE GLU THR PHE LYS LYS ILE MET GLU CYS LYS LYS LYS SEQRES 13 A 173 PRO GLN GLY GLN GLY ASN ASP ASP ILE SER HIS VAL LEU SEQRES 14 A 173 ARG GLU ASP GLN HELIX 1 1 GLY A 24 GLN A 27 5 4 HELIX 2 2 ASP A 28 LEU A 36 1 9 HELIX 3 3 THR A 80 GLY A 92 1 13 HELIX 4 4 TRP A 130 LYS A 155 1 26 SHEET 1 A 6 HIS A 18 VAL A 22 0 SHEET 2 A 6 GLU A 70 VAL A 79 -1 O LEU A 76 N VAL A 20 SHEET 3 A 6 GLU A 41 PRO A 48 -1 N LEU A 47 O VAL A 71 SHEET 4 A 6 TYR A 95 ARG A 104 -1 O VAL A 103 N THR A 46 SHEET 5 A 6 LYS A 110 TRP A 118 -1 O MET A 111 N ILE A 102 SHEET 6 A 6 HIS A 18 VAL A 22 1 N PHE A 21 O LYS A 114 SHEET 1 B 2 GLN A 51 ARG A 52 0 SHEET 2 B 2 ILE A 63 VAL A 64 -1 O VAL A 64 N GLN A 51 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