Header list of 1zri.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 19-MAY-05 1ZRI TITLE NOE-BASED SOLUTION STRUCTURE WITH DIPOLAR COUPLING RESTRAINTS OF RAT TITLE 2 OMP (OLFACTORY MARKER PROTEIN) COMPND MOL_ID: 1; COMPND 2 MOLECULE: OLFACTORY MARKER PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: OLFACTORY NEURONAL SPECIFIC PROTEIN; 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 GENE: OMP; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-KN KEYWDS BETA-CLAMSHELL, OMEGA-LOOP, BEX-BINDING PROTEIN, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.T.WRIGHT,J.W.MARGOLIS,F.M.MARGOLIS,D.J.WEBER REVDAT 3 02-MAR-22 1ZRI 1 REMARK REVDAT 2 24-FEB-09 1ZRI 1 VERSN REVDAT 1 02-MAY-06 1ZRI 0 JRNL AUTH N.T.WRIGHT,J.W.MARGOLIS,F.M.MARGOLIS,D.J.WEBER JRNL TITL LREFINEMENT OF THE SOLUTION STRUCTURE OF RAT OLFACTORY JRNL TITL 2 MARKER PROTEIN (OMP) JRNL REF J.BIOMOL.NMR V. 33 63 2005 JRNL REFN ISSN 0925-2738 JRNL PMID 16222559 JRNL DOI 10.1007/S10858-005-1281-7 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH 2.9.3, XPLOR-NIH 2.9.3 REMARK 3 AUTHORS : C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE REMARK 3 (XPLOR-NIH), C.D.SCHWIETERS,J.J.KUSZEWSKI, REMARK 3 N.TJANDRA,G.M.CLORE (XPLOR-NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON A TOTAL OF REMARK 3 1764 RESTRAINTS, OF WHICH 1343 ARE NOE-DERIVED, 124 ARE H-BONDS, REMARK 3 217 ARE DIHEDRAL ANGLES, AND 80 ARE RESIDUAL DIPOLAR COUPLING REMARK 3 VALUES REMARK 4 REMARK 4 1ZRI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-05. REMARK 100 THE DEPOSITION ID IS D_1000033035. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310; 310 REMARK 210 PH : 6.6; 6.6 REMARK 210 IONIC STRENGTH : 10 MM PHOSPHATE; 10 MM PHOSPHATE REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5-1.8 MM RAT OMP, 10MM REMARK 210 PHOSPHATE BUFFER, 0.1 MM EDTA, REMARK 210 0.3 MM NAN3,95% H2O, 5% D2O; 0.5 REMARK 210 MM RAT OMP, 10 MM PHOSPHATE REMARK 210 BUFFER, 0.1 MM EDTA, 0.3 MM NAN3, REMARK 210 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY; REMARK 210 4D_13C/15N-SEPARATED_NOESY; 3D_ REMARK 210 15N-SEPARATED_NOESY; 2D IPAP-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX; DRX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.0 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 LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D AND 4D REMARK 210 HOMONUCLEAR TECHNIQUES, ALONG WITH RESIDUAL DIPOLAR COUPLING REMARK 210 EXPERIMENTS (IPAP-HSQC) 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 GLU A 119 H LEU A 123 1.54 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 37 -6.76 -142.94 REMARK 500 1 PRO A 48 -4.53 -58.21 REMARK 500 1 GLN A 61 -20.74 -153.67 REMARK 500 1 ASP A 66 -63.04 -99.09 REMARK 500 1 HIS A 67 108.81 -161.88 REMARK 500 1 PRO A 75 176.13 -55.11 REMARK 500 1 GLN A 85 7.52 -62.38 REMARK 500 1 LEU A 100 -126.78 -66.86 REMARK 500 1 PRO A 102 172.02 -50.00 REMARK 500 1 ASP A 131 -72.35 -87.53 REMARK 500 1 LEU A 132 -30.31 -39.35 REMARK 500 2 ALA A 2 -92.13 -63.22 REMARK 500 2 PRO A 6 36.17 -65.61 REMARK 500 2 LYS A 39 81.70 -69.63 REMARK 500 2 PRO A 48 -6.16 -55.22 REMARK 500 2 GLN A 60 -91.76 -63.50 REMARK 500 2 ASP A 66 -61.07 -97.29 REMARK 500 2 SER A 84 -100.18 -113.98 REMARK 500 2 ASN A 86 -165.74 -105.15 REMARK 500 2 TRP A 87 -90.02 -110.19 REMARK 500 2 LEU A 100 -128.08 -78.91 REMARK 500 2 PRO A 102 170.06 -53.14 REMARK 500 2 ASP A 131 -72.42 -85.15 REMARK 500 2 LEU A 132 -16.59 -43.63 REMARK 500 2 PRO A 151 27.77 -59.68 REMARK 500 3 PRO A 6 -81.94 -66.57 REMARK 500 3 GLN A 7 -14.55 -150.37 REMARK 500 3 ALA A 49 64.06 -103.12 REMARK 500 3 GLN A 60 -130.35 -59.23 REMARK 500 3 ASP A 66 -68.07 -95.00 REMARK 500 3 SER A 84 -166.07 -57.43 REMARK 500 3 THR A 88 41.90 -168.04 REMARK 500 3 ASN A 93 -53.24 -173.68 REMARK 500 3 LEU A 94 7.15 -60.07 REMARK 500 3 ARG A 97 8.03 -62.75 REMARK 500 3 LEU A 100 -129.55 -74.97 REMARK 500 3 ASP A 131 -73.08 -88.31 REMARK 500 3 LEU A 132 -28.23 -36.58 REMARK 500 3 PRO A 151 -70.44 -66.93 REMARK 500 3 ALA A 152 33.70 -93.68 REMARK 500 4 PRO A 6 13.29 -63.13 REMARK 500 4 GLU A 37 15.71 -140.95 REMARK 500 4 GLN A 60 -143.41 -67.44 REMARK 500 4 ASP A 66 -73.27 -89.90 REMARK 500 4 PRO A 75 -176.37 -54.82 REMARK 500 4 ASN A 86 -158.19 -81.83 REMARK 500 4 TRP A 87 -108.65 -107.39 REMARK 500 4 ASN A 93 -43.18 -174.19 REMARK 500 4 LEU A 94 0.35 -50.37 REMARK 500 4 LEU A 100 -122.23 -59.75 REMARK 500 REMARK 500 THIS ENTRY HAS 261 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 28 0.23 SIDE CHAIN REMARK 500 1 ARG A 35 0.11 SIDE CHAIN REMARK 500 1 ARG A 47 0.24 SIDE CHAIN REMARK 500 1 ARG A 54 0.27 SIDE CHAIN REMARK 500 1 ARG A 128 0.28 SIDE CHAIN REMARK 500 1 ARG A 136 0.30 SIDE CHAIN REMARK 500 2 ARG A 28 0.28 SIDE CHAIN REMARK 500 2 ARG A 35 0.27 SIDE CHAIN REMARK 500 2 ARG A 47 0.20 SIDE CHAIN REMARK 500 2 ARG A 54 0.31 SIDE CHAIN REMARK 500 2 ARG A 97 0.28 SIDE CHAIN REMARK 500 2 ARG A 108 0.27 SIDE CHAIN REMARK 500 2 ARG A 128 0.17 SIDE CHAIN REMARK 500 2 ARG A 136 0.30 SIDE CHAIN REMARK 500 3 ARG A 26 0.24 SIDE CHAIN REMARK 500 3 ARG A 28 0.23 SIDE CHAIN REMARK 500 3 ARG A 35 0.27 SIDE CHAIN REMARK 500 3 ARG A 47 0.09 SIDE CHAIN REMARK 500 3 ARG A 54 0.19 SIDE CHAIN REMARK 500 3 ARG A 97 0.31 SIDE CHAIN REMARK 500 3 ARG A 108 0.19 SIDE CHAIN REMARK 500 3 ARG A 128 0.32 SIDE CHAIN REMARK 500 3 ARG A 136 0.28 SIDE CHAIN REMARK 500 4 ARG A 26 0.30 SIDE CHAIN REMARK 500 4 ARG A 28 0.20 SIDE CHAIN REMARK 500 4 ARG A 35 0.32 SIDE CHAIN REMARK 500 4 ARG A 47 0.32 SIDE CHAIN REMARK 500 4 ARG A 54 0.30 SIDE CHAIN REMARK 500 4 ARG A 97 0.31 SIDE CHAIN REMARK 500 4 ARG A 108 0.25 SIDE CHAIN REMARK 500 4 ARG A 128 0.14 SIDE CHAIN REMARK 500 4 ARG A 136 0.29 SIDE CHAIN REMARK 500 5 ARG A 26 0.08 SIDE CHAIN REMARK 500 5 ARG A 28 0.31 SIDE CHAIN REMARK 500 5 ARG A 35 0.23 SIDE CHAIN REMARK 500 5 ARG A 47 0.28 SIDE CHAIN REMARK 500 5 ARG A 54 0.31 SIDE CHAIN REMARK 500 5 ARG A 97 0.31 SIDE CHAIN REMARK 500 5 ARG A 108 0.32 SIDE CHAIN REMARK 500 5 ARG A 136 0.28 SIDE CHAIN REMARK 500 6 ARG A 26 0.23 SIDE CHAIN REMARK 500 6 ARG A 47 0.28 SIDE CHAIN REMARK 500 6 ARG A 54 0.32 SIDE CHAIN REMARK 500 6 ARG A 97 0.28 SIDE CHAIN REMARK 500 6 ARG A 108 0.18 SIDE CHAIN REMARK 500 6 ARG A 128 0.12 SIDE CHAIN REMARK 500 6 ARG A 136 0.19 SIDE CHAIN REMARK 500 7 ARG A 26 0.32 SIDE CHAIN REMARK 500 7 ARG A 28 0.10 SIDE CHAIN REMARK 500 7 ARG A 35 0.32 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 162 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 AUTHOR DEFINED REMARK 700 REMARK 700 SHEET REMARK 700 AUTHOR DEFINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JYT RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF RAT OMP WITH NO DIPOLAR COUPLINGS REMARK 900 RELATED ID: 1F35 RELATED DB: PDB REMARK 900 X-RAY STRUCTURE OF MURINE OMP DBREF 1ZRI A 1 163 UNP P08523 OMP_RAT 1 162 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 GLY A 36 1 19 HELIX 2 2 ASN A 118 ARG A 136 1 19 HELIX 3 3 THR A 96 GLN A 98 1 3 SHEET 1 A 3 GLN A 9 ASP A 18 0 SHEET 2 A 3 LEU A 154 GLN A 162 -1 O PHE A 160 N LEU A 11 SHEET 3 A 3 PHE A 65 LEU A 72 -1 N VAL A 71 O LYS A 155 SHEET 1 B 5 GLU A 50 ASP A 56 0 SHEET 2 B 5 VAL A 138 PHE A 145 -1 O PHE A 141 N TYR A 53 SHEET 3 B 5 GLY A 76 THR A 81 -1 N THR A 81 O LEU A 142 SHEET 4 B 5 ALA A 104 ARG A 108 -1 O PHE A 106 N VAL A 78 SHEET 5 B 5 MET A 115 ASN A 118 -1 O ASN A 118 N TRP A 107 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 2 2 Bytes