Header list of 2i9y.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 06-SEP-06 2I9Y TITLE SOLUTION STRUCTURE OF ARABIDOPSIS THALIANA PROTEIN AT1G70830, A MEMBER TITLE 2 OF THE MAJOR LATEX PROTEIN FAMILY COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAJOR LATEX PROTEIN-LIKE PROTEIN 28 OR MLP-LIKE PROTEIN 28; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 17-157; COMPND 5 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: AT1G70830, MLP28; SOURCE 6 EXPRESSION_SYSTEM: CELL-FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEU-HIS; SOURCE 9 OTHER_DETAILS: WHEAT GERM CELL-FREE, IN VITRO EXPRESSION KEYWDS AT1G70830, BET V1-LIKE, STRUCTURAL GENOMICS, PROTEIN STRUCTURE KEYWDS 2 INITIATIVE, PSI, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, CESG, KEYWDS 3 UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.F.VOLKMAN,N.B.DE LA CRUZ,B.L.LYTLE,F.C.PETERSON,CENTER FOR AUTHOR 2 EUKARYOTIC STRUCTURAL GENOMICS (CESG) REVDAT 4 09-MAR-22 2I9Y 1 REMARK SEQADV REVDAT 3 29-SEP-09 2I9Y 1 JRNL REVDAT 2 22-APR-08 2I9Y 1 VERSN REVDAT 1 19-SEP-06 2I9Y 0 JRNL AUTH B.L.LYTLE,J.SONG,N.B.DE LA CRUZ,F.C.PETERSON,K.A.JOHNSON, JRNL AUTH 2 C.A.BINGMAN,G.N.PHILLIPS,B.F.VOLKMAN JRNL TITL STRUCTURES OF TWO ARABIDOPSIS THALIANA MAJOR LATEX PROTEINS JRNL TITL 2 REPRESENT NOVEL HELIX-GRIP FOLDS. JRNL REF PROTEINS V. 76 237 2009 JRNL REFN ISSN 0887-3585 JRNL PMID 19326460 JRNL DOI 10.1002/PROT.22396 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, XPLOR-NIH 2.9.3 REMARK 3 AUTHORS : BRUKER (XWINNMR), SCHWIETERS, C.D., KUSZEWSKI, REMARK 3 J.J., TJANDRA, N., CLORE, G.M. (XPLOR-NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 STRUCTURES ARE BASED ON A TOTAL OF 1766 NOE CONSTRAINTS ( 597 REMARK 3 INTRA, 423 SEQUENTIAL, 224 MEDIUM AND 522 LONG RANGE CONSTRAINTS) REMARK 3 AND 197 PHI AND PSI DIHEDRAL ANGLE CONSTRAINTS. REMARK 4 REMARK 4 2I9Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-06. REMARK 100 THE DEPOSITION ID IS D_1000039322. 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 : 0.002 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.7 MM AT1G70830 U-15N/13C REMARK 210 PROTEIN, 10 MM DEUTERATED BIS- REMARK 210 TRIS, 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 : NMRPIPE 2004, XEASY 1.3, SPSCAN REMARK 210 1.1.0, GARANT 2.1, CYANA 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 REMARK 210 SPECTRA WERE ACQUIRED 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 8 REMARK 465 HIS A 9 REMARK 465 HIS A 10 REMARK 465 HIS A 11 REMARK 465 HIS A 12 REMARK 465 HIS A 13 REMARK 465 HIS A 14 REMARK 465 LEU A 15 REMARK 465 GLU A 16 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 HE2 HIS A 81 OE2 GLU A 160 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 GLU A 18 -178.21 63.07 REMARK 500 1 LEU A 22 -22.67 62.04 REMARK 500 1 LYS A 46 90.04 -170.96 REMARK 500 1 HIS A 48 96.50 73.05 REMARK 500 1 HIS A 49 113.21 -177.37 REMARK 500 1 GLN A 59 17.28 -164.34 REMARK 500 1 GLU A 65 139.90 -38.32 REMARK 500 1 THR A 70 -78.93 69.74 REMARK 500 1 ASN A 100 73.00 53.22 REMARK 500 1 LYS A 127 -59.13 -135.56 REMARK 500 2 GLU A 18 -77.49 64.34 REMARK 500 2 LEU A 22 -15.65 55.46 REMARK 500 2 PRO A 47 106.92 -56.44 REMARK 500 2 VAL A 50 100.86 -169.33 REMARK 500 2 ASN A 57 86.22 62.07 REMARK 500 2 HIS A 64 -148.71 -148.08 REMARK 500 2 ASP A 67 -56.74 -169.62 REMARK 500 2 GLU A 108 -80.62 -75.06 REMARK 500 3 GLU A 18 21.76 -142.75 REMARK 500 3 LEU A 22 -40.20 65.61 REMARK 500 3 LYS A 46 111.54 64.75 REMARK 500 3 SER A 54 93.88 67.61 REMARK 500 3 ASN A 57 96.05 62.45 REMARK 500 3 GLN A 59 -168.49 62.49 REMARK 500 3 CYS A 61 -42.66 69.72 REMARK 500 3 ILE A 107 -40.21 -137.37 REMARK 500 3 LYS A 127 -53.97 -129.03 REMARK 500 4 HIS A 64 89.86 66.93 REMARK 500 4 ASP A 67 149.49 70.77 REMARK 500 4 THR A 70 -68.77 72.52 REMARK 500 4 SER A 117 139.26 -172.87 REMARK 500 4 HIS A 150 78.95 -156.91 REMARK 500 5 LEU A 22 -20.93 63.58 REMARK 500 5 LYS A 52 -168.17 67.18 REMARK 500 5 ALA A 53 -46.08 76.56 REMARK 500 5 ILE A 58 99.81 76.47 REMARK 500 5 LEU A 63 -168.85 -105.61 REMARK 500 5 ASP A 67 2.26 -68.48 REMARK 500 5 THR A 70 -64.80 74.79 REMARK 500 5 ALA A 171 72.60 46.33 REMARK 500 5 GLU A 172 -158.46 -134.52 REMARK 500 6 ALA A 19 -14.98 70.39 REMARK 500 6 SER A 51 -43.71 -164.12 REMARK 500 6 LYS A 52 145.69 70.34 REMARK 500 6 ALA A 53 73.33 58.99 REMARK 500 6 SER A 117 141.44 -170.60 REMARK 500 6 ALA A 171 86.93 38.24 REMARK 500 7 LEU A 22 15.38 56.69 REMARK 500 7 HIS A 49 -80.18 63.23 REMARK 500 7 GLN A 59 -62.03 71.77 REMARK 500 REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GO.74365 RELATED DB: TARGETDB DBREF 2I9Y A 17 173 UNP Q9SSK9 MLP28_ARATH 17 173 SEQADV 2I9Y GLY A 8 UNP Q9SSK9 EXPRESSION TAG SEQADV 2I9Y HIS A 9 UNP Q9SSK9 EXPRESSION TAG SEQADV 2I9Y HIS A 10 UNP Q9SSK9 EXPRESSION TAG SEQADV 2I9Y HIS A 11 UNP Q9SSK9 EXPRESSION TAG SEQADV 2I9Y HIS A 12 UNP Q9SSK9 EXPRESSION TAG SEQADV 2I9Y HIS A 13 UNP Q9SSK9 EXPRESSION TAG SEQADV 2I9Y HIS A 14 UNP Q9SSK9 EXPRESSION TAG SEQADV 2I9Y LEU A 15 UNP Q9SSK9 EXPRESSION TAG SEQADV 2I9Y GLU A 16 UNP Q9SSK9 EXPRESSION TAG SEQRES 1 A 166 GLY HIS HIS HIS HIS HIS HIS LEU GLU THR GLU ALA SER SEQRES 2 A 166 SER LEU VAL GLY LYS LEU GLU THR ASP VAL GLU ILE LYS SEQRES 3 A 166 ALA SER ALA ASP LYS PHE HIS HIS MET PHE ALA GLY LYS SEQRES 4 A 166 PRO HIS HIS VAL SER LYS ALA SER PRO GLY ASN ILE GLN SEQRES 5 A 166 GLY CYS ASP LEU HIS GLU GLY ASP TRP GLY THR VAL GLY SEQRES 6 A 166 SER ILE VAL PHE TRP ASN TYR VAL HIS ASP GLY GLU ALA SEQRES 7 A 166 LYS VAL ALA LYS GLU ARG ILE GLU ALA VAL GLU PRO ASP SEQRES 8 A 166 LYS ASN LEU ILE THR PHE ARG VAL ILE GLU GLY ASP LEU SEQRES 9 A 166 MET LYS GLU TYR LYS SER PHE LEU LEU THR ILE GLN VAL SEQRES 10 A 166 THR PRO LYS PRO GLY GLY PRO GLY SER ILE VAL HIS TRP SEQRES 11 A 166 HIS LEU GLU TYR GLU LYS ILE SER GLU GLU VAL ALA HIS SEQRES 12 A 166 PRO GLU THR LEU LEU GLN PHE CYS VAL GLU VAL SER LYS SEQRES 13 A 166 GLU ILE ASP GLU HIS LEU LEU ALA GLU GLU HELIX 1 1 SER A 35 HIS A 41 1 7 HELIX 2 2 MET A 42 ALA A 44 5 3 HELIX 3 3 ASP A 110 LYS A 113 5 4 HELIX 4 4 PRO A 151 ALA A 171 1 21 SHEET 1 A 6 VAL A 23 ILE A 32 0 SHEET 2 A 6 GLY A 132 LYS A 143 -1 O TYR A 141 N GLY A 24 SHEET 3 A 6 TYR A 115 GLY A 129 -1 N THR A 121 O HIS A 138 SHEET 4 A 6 LEU A 101 VAL A 106 -1 N PHE A 104 O LEU A 120 SHEET 5 A 6 GLU A 84 GLU A 96 -1 N ALA A 94 O THR A 103 SHEET 6 A 6 PHE A 76 HIS A 81 -1 N TYR A 79 O LYS A 86 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