Header list of 1no8.pdb file
Complete list - b 23 2 Bytes
HEADER RNA BINDING PROTEIN 15-JAN-03 1NO8 TITLE SOLUTION STRUCTURE OF THE NUCLEAR FACTOR ALY RBD DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALY; COMPND 3 CHAIN: A; COMPND 4 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: ALY; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A KEYWDS RBD, ALY, REF1-I, BEF, MRNA EXPORT FACTOR, RNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 32 AUTHOR G.C.PEREZ-ALVARADO,M.MARTINEZ-YAMOUT,M.M.ALLEN,R.GROSSCHEDL, AUTHOR 2 H.J.DYSON,P.E.WRIGHT REVDAT 3 23-FEB-22 1NO8 1 REMARK REVDAT 2 24-FEB-09 1NO8 1 VERSN REVDAT 1 12-AUG-03 1NO8 0 JRNL AUTH G.C.PEREZ-ALVARADO,M.MARTINEZ-YAMOUT,M.M.ALLEN,R.GROSSCHEDL, JRNL AUTH 2 H.J.DYSON,P.E.WRIGHT JRNL TITL STRUCTURE OF THE NUCLEAR FACTOR ALY: INSIGHTS INTO JRNL TITL 2 POST-TRANSCRIPTIONAL REGULATORY AND MRNA NUCLEAR EXPORT JRNL TITL 3 PROCESSES JRNL REF BIOCHEMISTRY V. 42 7348 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 12809490 JRNL DOI 10.1021/BI034062O REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.1, AMBER 6, 7 REMARK 3 AUTHORS : BRUKER (XWINNMR), CASE, D.A., PEARLMAN, D.A., REMARK 3 CALDWELL, J.W., CHEATHAM III, T.E., WANG, J., ROSS, REMARK 3 W.S.,SIMMERLING, C., DARDEN, T., MERZ, K.M., REMARK 3 STANTON, R.V., CHENG, A., VINCENT, J.J., CROWLEY, REMARK 3 M., TSUI, V., GOHLKE, H., RADMER, R., ET AL. AND REMARK 3 KOLLMAN, P.A. (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. REMARK 3 REMARK 3 RESIDUES 77-104 ARE HIGHLY DISORDERED AND DO NOT PRESENT A DEFINED REMARK 3 STRUCTURE IN SOLUTION. RESIDUES 77-104 ARE NOT INCLUDED IN THIS REMARK 3 ENTRY. REMARK 4 REMARK 4 1NO8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-03. REMARK 100 THE DEPOSITION ID IS D_1000018058. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 296; 289; 296 REMARK 210 PH : 6.5; 6.5; 5.9 REMARK 210 IONIC STRENGTH : 100MM NACL; 100MM NACL; 100MM REMARK 210 NACL REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5MM ALY77-182-15N; 20MM TRIS REMARK 210 -HCL-D8, 100MM NACL; 90% H2O, 10% REMARK 210 D2O; 0.5MM ALY77-182-15N, 13C; REMARK 210 20MM TRIS-HCL-D8, 100MM NACL; 90% REMARK 210 H2O, 10% D2O; 0.5MM ALY77-182- REMARK 210 15N, 13C; 20MM TRIS-HCL-D8, REMARK 210 100MM NACL; 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -HMQC-NOESY; 3D_15N/13C-NOESY- REMARK 210 HSQC; HNCA, HNCO, HN(CA)CB; REMARK 210 CBCA(CO)NH, C(CO)NH-TOCSY, HC(CO) REMARK 210 NH-TOCSY; HNHA; HCCH-COSY, CCH- REMARK 210 COSY, HCCH-TOCSY; HNHB; 2D TOCSY; REMARK 210 3D_13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.8, 2.1, NMRDRAW 1.8, REMARK 210 2.1, NMRVIEW 3, DYANA 1.5 REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION REMARK 210 ANGLE DYNAMICS MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 92 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 32 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY AND LOWEST CONSTRAINT REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING RESTRAINTS DERIVED FROM REMARK 210 A COMBINATION OF NOESY SPECTRA AND TRIPLE RESONANCE SPECTRA. 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 1-32 REMARK 465 RES C SSSEQI REMARK 465 SER A 77 REMARK 465 ARG A 78 REMARK 465 PRO A 79 REMARK 465 LYS A 80 REMARK 465 GLN A 81 REMARK 465 LEU A 82 REMARK 465 PRO A 83 REMARK 465 ASP A 84 REMARK 465 LYS A 85 REMARK 465 TRP A 86 REMARK 465 GLN A 87 REMARK 465 HIS A 88 REMARK 465 ASP A 89 REMARK 465 LEU A 90 REMARK 465 PHE A 91 REMARK 465 ASP A 92 REMARK 465 SER A 93 REMARK 465 GLY A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 GLY A 97 REMARK 465 GLY A 98 REMARK 465 ALA A 99 REMARK 465 GLY A 100 REMARK 465 VAL A 101 REMARK 465 GLU A 102 REMARK 465 THR A 103 REMARK 465 GLY A 104 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 2 ARG A 140 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 3 ARG A 154 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 5 ARG A 154 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 5 ARG A 173 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 8 ARG A 154 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 10 ARG A 154 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 10 ARG A 173 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 13 ARG A 173 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 16 ARG A 140 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 18 ARG A 143 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 25 ARG A 173 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 31 ARG A 154 NE - CZ - NH1 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 ASP A 139 -71.28 -150.76 REMARK 500 1 SER A 141 -71.13 -152.41 REMARK 500 1 LEU A 145 -73.89 -141.69 REMARK 500 3 ASP A 139 -59.15 -144.92 REMARK 500 3 ARG A 140 -45.55 -130.82 REMARK 500 4 ARG A 140 -45.75 -137.50 REMARK 500 4 LEU A 145 -76.52 -147.80 REMARK 500 5 ASP A 139 -63.68 -145.65 REMARK 500 5 ASP A 171 70.53 44.02 REMARK 500 6 LEU A 145 -66.16 -143.89 REMARK 500 7 ASP A 139 -138.09 -143.03 REMARK 500 7 LEU A 145 -68.66 -131.67 REMARK 500 8 LEU A 112 -116.01 -98.38 REMARK 500 8 VAL A 136 -126.04 -133.63 REMARK 500 8 ASP A 171 62.34 38.66 REMARK 500 9 ASP A 139 -50.47 69.03 REMARK 500 9 LEU A 145 -130.13 -122.20 REMARK 500 10 PHE A 114 104.03 -57.48 REMARK 500 10 ASP A 139 -130.58 -144.26 REMARK 500 10 LEU A 145 -68.64 -153.47 REMARK 500 11 ARG A 140 -143.83 -122.29 REMARK 500 11 ASN A 166 109.74 -59.32 REMARK 500 11 LEU A 179 -101.29 -88.60 REMARK 500 12 ASN A 111 79.12 59.28 REMARK 500 13 LEU A 112 -155.10 -88.73 REMARK 500 13 LEU A 145 -47.93 -160.83 REMARK 500 14 HIS A 137 -58.18 -25.69 REMARK 500 15 PHE A 114 88.92 -67.86 REMARK 500 16 ASP A 139 -46.40 66.95 REMARK 500 16 ASN A 166 109.32 -59.10 REMARK 500 17 HIS A 137 -71.10 -21.09 REMARK 500 17 ARG A 140 -42.77 -134.37 REMARK 500 17 LEU A 145 -56.48 -136.38 REMARK 500 17 ASN A 166 109.26 -58.33 REMARK 500 18 VAL A 136 -96.71 -128.95 REMARK 500 18 HIS A 137 -98.22 -136.44 REMARK 500 18 SER A 144 108.57 -59.90 REMARK 500 19 ASN A 111 71.66 60.74 REMARK 500 19 VAL A 136 -124.31 -125.10 REMARK 500 19 THR A 181 -69.16 -132.77 REMARK 500 20 LEU A 145 -48.72 -147.73 REMARK 500 21 ASP A 139 -55.48 66.56 REMARK 500 21 LEU A 145 -59.64 -139.30 REMARK 500 22 ASP A 139 -84.16 -156.84 REMARK 500 22 GLU A 153 -65.68 -91.54 REMARK 500 22 LEU A 179 -123.11 -80.31 REMARK 500 23 LEU A 112 -168.81 -116.16 REMARK 500 23 ASP A 139 -95.88 -145.21 REMARK 500 23 LEU A 145 -69.12 -153.85 REMARK 500 23 VAL A 180 -101.53 51.63 REMARK 500 REMARK 500 THIS ENTRY HAS 68 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 24 HIS A 137 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 AUTHOR DETERMINED THE HELIX STRUCTURE. REMARK 700 REMARK 700 SHEET REMARK 700 AUTHOR DETERMINED THE SHEET RECORDS. DBREF 1NO8 A 77 182 UNP O08583 THOC4_MOUSE 77 182 SEQRES 1 A 106 SER ARG PRO LYS GLN LEU PRO ASP LYS TRP GLN HIS ASP SEQRES 2 A 106 LEU PHE ASP SER GLY PHE GLY GLY GLY ALA GLY VAL GLU SEQRES 3 A 106 THR GLY GLY LYS LEU LEU VAL SER ASN LEU ASP PHE GLY SEQRES 4 A 106 VAL SER ASP ALA ASP ILE GLN GLU LEU PHE ALA GLU PHE SEQRES 5 A 106 GLY THR LEU LYS LYS ALA ALA VAL HIS TYR ASP ARG SER SEQRES 6 A 106 GLY ARG SER LEU GLY THR ALA ASP VAL HIS PHE GLU ARG SEQRES 7 A 106 LYS ALA ASP ALA LEU LYS ALA MET LYS GLN TYR ASN GLY SEQRES 8 A 106 VAL PRO LEU ASP GLY ARG PRO MET ASN ILE GLN LEU VAL SEQRES 9 A 106 THR SER HELIX 1 1 SER A 117 PHE A 128 1 12 HELIX 2 2 ARG A 154 TYR A 165 1 12 SHEET 1 A 4 LEU A 131 VAL A 136 0 SHEET 2 A 4 THR A 147 PHE A 152 -1 O ASP A 149 N ALA A 135 SHEET 3 A 4 GLY A 105 SER A 110 -1 N VAL A 109 O ALA A 148 SHEET 4 A 4 ASN A 176 VAL A 180 -1 O ASN A 176 N SER A 110 SHEET 1 B 2 GLY A 167 LEU A 170 0 SHEET 2 B 2 ARG A 173 MET A 175 -1 O ARG A 173 N LEU A 170 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 - b 23 2 Bytes