Header list of 1jyt.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 13-SEP-01 1JYT TITLE SOLUTION STRUCTURE OF OLFACTORY MARKER PROTEIN FROM RAT COMPND MOL_ID: 1; COMPND 2 MOLECULE: OLFACTORY MARKER PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: OMP; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS BETA-CLAMBSHELL, OMEGA-LOOP, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR D.M.BALDISSERI,J.W.MARGOLIS,D.J.WEBER,J.H.KOO,F.M.MARGOLIS REVDAT 6 23-FEB-22 1JYT 1 REMARK REVDAT 5 24-FEB-09 1JYT 1 VERSN REVDAT 4 01-APR-03 1JYT 1 JRNL REVDAT 3 28-AUG-02 1JYT 1 JRNL REVDAT 2 07-AUG-02 1JYT 1 JRNL AUTHOR REMARK REVDAT 1 03-OCT-01 1JYT 0 JRNL AUTH D.M.BALDISSERI,J.W.MARGOLIS,D.J.WEBER,J.H.KOO,F.L.MARGOLIS JRNL TITL OLFACTORY MARKER PROTEIN (OMP) EXHIBITS A BETA-CLAM FOLD IN JRNL TITL 2 SOLUTION: IMPLICATIONS FOR TARGET PEPTIDE INTERACTION AND JRNL TITL 3 OLFACTORY SIGNAL TRANSDUCTION. JRNL REF J.MOL.BIOL. V. 319 823 2002 JRNL REFN ISSN 0022-2836 JRNL PMID 12054873 JRNL DOI 10.1016/S0022-2836(02)00282-6 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.0, X-PLOR 3.851 REMARK 3 AUTHORS : BRUKER ANALYTIK GMBH (XWINNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1JYT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-01. REMARK 100 THE DEPOSITION ID IS D_1000014345. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.6 REMARK 210 IONIC STRENGTH : 10MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : SAMPLE 1: 2MM OMP UNLABELED; REMARK 210 10MM PHOSPHATE BUFFER 0.1MM EDTA REMARK 210 0.3MM NAN3; PH 6.6.; SAMPLE 2: REMARK 210 1.5MM OMP U-15N; 10MM PHOSPHATE REMARK 210 BUFFER 0.1MM EDTA 0.3MM NAN3; PH REMARK 210 6.6; SAMPLE 3: 1.8MM OMP U-15N, REMARK 210 13C; 10MM PHOSPHATE BUFFER 0.1MM REMARK 210 EDTA 0.3MM NAN3; PH 6.6; SAMPLE REMARK 210 4: 1.8MM OMP U-15N,13C, 70%-2H; REMARK 210 10MM PHOSPHATE BUFFER 0.1MM EDTA REMARK 210 0.3MM NAN3; PH 6.6 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; HNHA; 4D_13C/15N REMARK 210 -SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.8, X-PLOR 3.851 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 17 REMARK 210 REMARK 210 REMARK: THESE STRUCTURES WERE CALCULATED USING DISTANCE, DIHEDRAL REMARK 210 ANGLE AND HYDROGEN BOND RESTRAINTS FROM HOMONUCLEAR AND DOUBLE- REMARK 210 AND TRIPLE-RESONANCE NMR EXPERIMENTS. 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 O SER A 112 H ALA A 114 1.27 REMARK 500 O GLU A 119 H LEU A 123 1.44 REMARK 500 O ARG A 35 H GLU A 37 1.47 REMARK 500 HD1 HIS A 67 O VAL A 159 1.50 REMARK 500 O GLY A 5 H GLN A 7 1.54 REMARK 500 O LEU A 21 H GLN A 24 1.54 REMARK 500 O MET A 25 H ARG A 28 1.55 REMARK 500 OD1 ASP A 18 H ASP A 20 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 PRO A 6 47.67 -63.83 REMARK 500 1 LYS A 8 -124.64 -95.70 REMARK 500 1 GLN A 34 -72.99 -112.94 REMARK 500 1 GLU A 37 -80.00 -90.46 REMARK 500 1 PRO A 48 -81.85 -52.60 REMARK 500 1 ALA A 49 67.67 178.86 REMARK 500 1 GLN A 59 25.27 -67.66 REMARK 500 1 GLN A 61 -8.35 70.47 REMARK 500 1 GLN A 64 52.75 -100.89 REMARK 500 1 PHE A 65 96.79 -45.57 REMARK 500 1 ASP A 73 6.89 -66.25 REMARK 500 1 ASN A 93 -156.85 -151.89 REMARK 500 1 LEU A 94 100.90 -51.98 REMARK 500 1 THR A 96 -159.77 -52.20 REMARK 500 1 ASP A 113 51.67 -60.11 REMARK 500 1 ARG A 136 -8.85 -45.63 REMARK 500 1 GLU A 147 118.12 -38.45 REMARK 500 1 PRO A 151 8.49 -55.00 REMARK 500 1 ALA A 152 13.18 -59.85 REMARK 500 2 PRO A 6 5.23 -67.56 REMARK 500 2 LYS A 8 -126.95 -117.99 REMARK 500 2 ASP A 20 -18.07 -39.90 REMARK 500 2 LEU A 21 -66.42 -97.09 REMARK 500 2 PRO A 48 -6.16 -49.50 REMARK 500 2 ALA A 49 69.74 84.40 REMARK 500 2 GLN A 61 -4.52 64.79 REMARK 500 2 GLN A 64 57.49 -94.93 REMARK 500 2 PHE A 65 101.08 -45.73 REMARK 500 2 ASP A 73 5.72 -59.39 REMARK 500 2 PRO A 75 101.00 -55.97 REMARK 500 2 THR A 96 -129.55 -92.73 REMARK 500 2 LEU A 99 -170.78 -59.63 REMARK 500 2 LEU A 100 178.72 -47.36 REMARK 500 2 PRO A 102 168.45 -47.50 REMARK 500 2 ASP A 113 48.45 -61.58 REMARK 500 2 ARG A 136 -7.57 -44.36 REMARK 500 2 PRO A 151 102.91 -40.09 REMARK 500 2 ALA A 152 46.73 -93.47 REMARK 500 3 ASP A 4 74.49 -168.77 REMARK 500 3 PRO A 6 -7.71 -52.58 REMARK 500 3 GLN A 7 -87.35 -116.69 REMARK 500 3 LYS A 8 -113.25 -112.22 REMARK 500 3 LEU A 17 -177.66 -59.03 REMARK 500 3 GLN A 19 -39.26 -10.29 REMARK 500 3 GLN A 34 -74.88 -110.72 REMARK 500 3 GLU A 37 -51.48 -135.17 REMARK 500 3 LYS A 44 33.86 -84.63 REMARK 500 3 ARG A 47 105.45 -49.38 REMARK 500 3 ALA A 49 27.37 84.15 REMARK 500 3 GLN A 60 -114.52 -120.58 REMARK 500 REMARK 500 THIS ENTRY HAS 412 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 1 ARG A 26 0.30 SIDE CHAIN REMARK 500 1 ARG A 35 0.20 SIDE CHAIN REMARK 500 1 ARG A 47 0.29 SIDE CHAIN REMARK 500 1 ARG A 54 0.30 SIDE CHAIN REMARK 500 1 ARG A 97 0.14 SIDE CHAIN REMARK 500 1 ARG A 108 0.26 SIDE CHAIN REMARK 500 1 ARG A 128 0.28 SIDE CHAIN REMARK 500 1 ARG A 136 0.31 SIDE CHAIN REMARK 500 2 ARG A 26 0.21 SIDE CHAIN REMARK 500 2 ARG A 28 0.16 SIDE CHAIN REMARK 500 2 ARG A 35 0.32 SIDE CHAIN REMARK 500 2 ARG A 47 0.33 SIDE CHAIN REMARK 500 2 ARG A 54 0.32 SIDE CHAIN REMARK 500 2 ARG A 97 0.28 SIDE CHAIN REMARK 500 2 ARG A 108 0.20 SIDE CHAIN REMARK 500 2 ARG A 128 0.19 SIDE CHAIN REMARK 500 2 ARG A 136 0.15 SIDE CHAIN REMARK 500 3 ARG A 26 0.28 SIDE CHAIN REMARK 500 3 ARG A 28 0.15 SIDE CHAIN REMARK 500 3 ARG A 35 0.23 SIDE CHAIN REMARK 500 3 ARG A 47 0.32 SIDE CHAIN REMARK 500 3 ARG A 54 0.26 SIDE CHAIN REMARK 500 3 ARG A 97 0.18 SIDE CHAIN REMARK 500 3 ARG A 108 0.24 SIDE CHAIN REMARK 500 3 ARG A 128 0.16 SIDE CHAIN REMARK 500 3 ARG A 136 0.31 SIDE CHAIN REMARK 500 4 ARG A 26 0.18 SIDE CHAIN REMARK 500 4 ARG A 28 0.30 SIDE CHAIN REMARK 500 4 ARG A 35 0.31 SIDE CHAIN REMARK 500 4 ARG A 47 0.26 SIDE CHAIN REMARK 500 4 ARG A 54 0.23 SIDE CHAIN REMARK 500 4 ARG A 97 0.31 SIDE CHAIN REMARK 500 4 ARG A 108 0.27 SIDE CHAIN REMARK 500 4 ARG A 128 0.14 SIDE CHAIN REMARK 500 4 ARG A 136 0.08 SIDE CHAIN REMARK 500 5 ARG A 26 0.30 SIDE CHAIN REMARK 500 5 ARG A 35 0.12 SIDE CHAIN REMARK 500 5 ARG A 47 0.32 SIDE CHAIN REMARK 500 5 ARG A 54 0.17 SIDE CHAIN REMARK 500 5 ARG A 97 0.29 SIDE CHAIN REMARK 500 5 ARG A 108 0.26 SIDE CHAIN REMARK 500 5 ARG A 128 0.32 SIDE CHAIN REMARK 500 5 ARG A 136 0.22 SIDE CHAIN REMARK 500 6 ARG A 26 0.20 SIDE CHAIN REMARK 500 6 ARG A 35 0.28 SIDE CHAIN REMARK 500 6 ARG A 47 0.20 SIDE CHAIN REMARK 500 6 ARG A 54 0.26 SIDE CHAIN REMARK 500 6 ARG A 108 0.32 SIDE CHAIN REMARK 500 6 ARG A 136 0.30 SIDE CHAIN REMARK 500 7 ARG A 26 0.30 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 158 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4735 RELATED DB: BMRB DBREF 1JYT A 1 163 UNP P08523 OMP_RAT 0 162 SEQRES 1 A 163 MET ALA GLU ASP GLY PRO GLN LYS GLN GLN LEU ASP MET SEQRES 2 A 163 PRO LEU VAL LEU ASP GLN ASP LEU THR LYS GLN MET ARG SEQRES 3 A 163 LEU ARG VAL GLU SER LEU LYS GLN ARG GLY GLU LYS LYS SEQRES 4 A 163 GLN ASP GLY GLU LYS LEU LEU ARG PRO ALA GLU SER VAL SEQRES 5 A 163 TYR ARG LEU ASP PHE ILE GLN GLN GLN LYS LEU GLN PHE SEQRES 6 A 163 ASP HIS TRP ASN VAL VAL LEU ASP LYS PRO GLY LYS VAL SEQRES 7 A 163 THR ILE THR GLY THR SER GLN ASN TRP THR PRO ASP LEU SEQRES 8 A 163 THR ASN LEU MET THR ARG GLN LEU LEU ASP PRO ALA ALA SEQRES 9 A 163 ILE PHE TRP ARG LYS GLU ASP SER ASP ALA MET ASP TRP SEQRES 10 A 163 ASN GLU ALA ASP ALA LEU GLU PHE GLY GLU ARG LEU SER SEQRES 11 A 163 ASP LEU ALA LYS ILE ARG LYS VAL MET TYR PHE LEU ILE SEQRES 12 A 163 THR PHE GLY GLU GLY VAL GLU PRO ALA ASN LEU LYS ALA SEQRES 13 A 163 SER VAL VAL PHE ASN GLN LEU HELIX 1 1 ASP A 18 GLN A 34 1 17 HELIX 2 2 GLU A 119 ILE A 135 1 17 SHEET 1 A 4 VAL A 138 THR A 144 0 SHEET 2 A 4 GLY A 76 THR A 83 -1 N THR A 79 O THR A 144 SHEET 3 A 4 LEU A 100 LYS A 109 -1 N ALA A 104 O ILE A 80 SHEET 4 A 4 ALA A 114 ASN A 118 -1 N ASP A 116 O TRP A 107 SHEET 1 B 4 GLU A 50 ASP A 56 0 SHEET 2 B 4 GLN A 10 ASP A 18 -1 N ARG A 54 O VAL A 16 SHEET 3 B 4 ASN A 153 GLN A 162 -1 N ALA A 156 O LEU A 15 SHEET 4 B 4 ASN A 69 ASP A 73 -1 N ASN A 69 O SER A 157 CRYST1 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 - b 23 2 Bytes