Header list of 1s79.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN, TRANSLATION 29-JAN-04 1S79 TITLE SOLUTION STRUCTURE OF THE CENTRAL RRM OF HUMAN LA PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: LUPUS LA PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CENTRAL RRM; COMPND 5 SYNONYM: SJOGREN SYNDROME TYPE B ANTIGEN, SS-B, LA RIBONUCLEOPROTEIN, COMPND 6 LA AUTOANTIGEN; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: SSB; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28 KEYWDS RRM, ALPHA/BETA, RNA BINDING PROTEIN, TRANSLATION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.ALFANO,D.SANFELICE,J.BABON,G.KELLY,A.JACKS,S.CURRY,M.R.CONTE REVDAT 3 02-MAR-22 1S79 1 REMARK SEQADV REVDAT 2 24-FEB-09 1S79 1 VERSN REVDAT 1 06-APR-04 1S79 0 JRNL AUTH C.ALFANO,D.SANFELICE,J.BABON,G.KELLY,A.JACKS,S.CURRY, JRNL AUTH 2 M.R.CONTE JRNL TITL STRUCTURAL ANALYSIS OF COOPERATIVE RNA BINDING BY THE LA JRNL TITL 2 MOTIF AND CENTRAL RRM DOMAIN OF HUMAN LA PROTEIN. JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 323 2004 JRNL REFN ISSN 1545-9993 JRNL PMID 15004549 JRNL DOI 10.1038/NSMB747 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.ALFANO,J.BABON,G.KELLY,S.CURRY,M.R.CONTE REMARK 1 TITL RESONANCE ASSIGNMENT AND SECONDARY STRUCTURE OF AN REMARK 1 TITL 2 N-TERMINAL FRAGMENT OF THE HUMAN LA PROTEIN REMARK 1 REF J.BIOMOL.NMR V. 27 93 2003 REMARK 1 REFN ISSN 0925-2738 REMARK 1 DOI 10.1023/A:1024741228802 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1S79 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-04. REMARK 100 THE DEPOSITION ID IS D_1000021455. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6 REMARK 210 IONIC STRENGTH : 100 MM KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.4 MM RRM U-15N,13C; 20MM REMARK 210 PHOSPHATE BUFFER, 100MM KCL, 90% REMARK 210 H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; HNCA; HNCOCA; REMARK 210 CBCACONH; HNCACB REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1, VNMR 1C, XEASY 6600, REMARK 210 MOLMOL 2.6, TALOS 1999.019.15.47 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 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: NULL 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 OD1 ASN A 193 H GLU A 194 1.54 REMARK 500 HH21 ARG A 111 O ASP A 159 1.57 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 TRP A 102 99.41 53.49 REMARK 500 1 LYS A 105 -147.91 44.09 REMARK 500 1 ALA A 122 72.06 -58.89 REMARK 500 1 LYS A 134 101.14 177.22 REMARK 500 1 LYS A 151 -101.04 -122.67 REMARK 500 1 PRO A 171 161.74 -48.12 REMARK 500 1 LYS A 176 -164.02 -52.90 REMARK 500 1 GLU A 177 -96.28 40.49 REMARK 500 1 GLU A 194 83.09 66.84 REMARK 500 1 GLU A 195 117.65 -163.22 REMARK 500 1 LYS A 197 -54.61 -123.72 REMARK 500 1 ASN A 199 176.92 -55.68 REMARK 500 1 LYS A 200 -151.35 -179.94 REMARK 500 2 ARG A 101 108.34 57.32 REMARK 500 2 LYS A 105 -77.18 -145.71 REMARK 500 2 ALA A 122 68.91 -60.78 REMARK 500 2 LYS A 134 101.71 179.59 REMARK 500 2 LEU A 146 150.30 -43.65 REMARK 500 2 LYS A 151 -139.32 -97.18 REMARK 500 2 PRO A 171 176.31 -45.14 REMARK 500 2 LYS A 176 -161.25 -53.44 REMARK 500 2 GLU A 177 -97.66 41.54 REMARK 500 2 GLU A 194 108.03 55.89 REMARK 500 2 ASN A 199 -89.49 -128.80 REMARK 500 2 LYS A 200 -153.06 49.53 REMARK 500 3 LEU A 104 -68.71 -173.30 REMARK 500 3 PHE A 118 169.41 49.66 REMARK 500 3 LYS A 134 25.08 -177.17 REMARK 500 3 LEU A 146 150.29 -43.90 REMARK 500 3 LYS A 151 -122.85 -85.45 REMARK 500 3 PRO A 171 159.57 -48.73 REMARK 500 3 LYS A 176 -160.36 -52.76 REMARK 500 3 GLU A 177 -94.44 44.59 REMARK 500 3 ASP A 179 106.83 -57.07 REMARK 500 3 ASN A 199 70.82 177.40 REMARK 500 3 LYS A 200 -68.89 -173.73 REMARK 500 4 LEU A 104 -67.29 -142.24 REMARK 500 4 PRO A 119 176.18 -58.46 REMARK 500 4 ASP A 121 30.14 -141.72 REMARK 500 4 ALA A 122 68.47 -61.52 REMARK 500 4 LYS A 134 104.76 174.25 REMARK 500 4 LEU A 146 150.27 -43.65 REMARK 500 4 LYS A 151 -139.20 -101.86 REMARK 500 4 PRO A 171 159.63 -47.16 REMARK 500 4 LYS A 176 -165.01 -52.22 REMARK 500 4 GLU A 177 -97.05 42.14 REMARK 500 4 GLU A 194 -96.26 41.99 REMARK 500 4 ARG A 196 -70.52 -131.41 REMARK 500 4 LYS A 200 -162.81 -69.41 REMARK 500 5 ARG A 101 55.23 -140.27 REMARK 500 REMARK 500 THIS ENTRY HAS 289 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5719 RELATED DB: BMRB REMARK 900 NMR ASSIGNMENT OF THE SAME DOMAIN REMARK 900 RELATED ID: 1OWX RELATED DB: PDB REMARK 900 C-TERMINAL DOMAIN OF HUMAN LA REMARK 900 RELATED ID: 1S7A RELATED DB: PDB REMARK 900 NMR STRUCTURE OF THE LA MOTIF OF HUMAN LA PROTEIN DBREF 1S79 A 105 202 UNP P05455 LA_HUMAN 105 202 SEQADV 1S79 GLY A 100 UNP P05455 CLONING ARTIFACT SEQADV 1S79 ARG A 101 UNP P05455 CLONING ARTIFACT SEQADV 1S79 TRP A 102 UNP P05455 CLONING ARTIFACT SEQADV 1S79 ILE A 103 UNP P05455 CLONING ARTIFACT SEQADV 1S79 LEU A 104 UNP P05455 CLONING ARTIFACT SEQRES 1 A 103 GLY ARG TRP ILE LEU LYS ASN ASP VAL LYS ASN ARG SER SEQRES 2 A 103 VAL TYR ILE LYS GLY PHE PRO THR ASP ALA THR LEU ASP SEQRES 3 A 103 ASP ILE LYS GLU TRP LEU GLU ASP LYS GLY GLN VAL LEU SEQRES 4 A 103 ASN ILE GLN MET ARG ARG THR LEU HIS LYS ALA PHE LYS SEQRES 5 A 103 GLY SER ILE PHE VAL VAL PHE ASP SER ILE GLU SER ALA SEQRES 6 A 103 LYS LYS PHE VAL GLU THR PRO GLY GLN LYS TYR LYS GLU SEQRES 7 A 103 THR ASP LEU LEU ILE LEU PHE LYS ASP ASP TYR PHE ALA SEQRES 8 A 103 LYS LYS ASN GLU GLU ARG LYS GLN ASN LYS VAL GLU HELIX 1 1 VAL A 108 ARG A 111 5 4 HELIX 2 2 THR A 123 ASP A 133 1 11 HELIX 3 3 SER A 160 GLU A 169 1 10 HELIX 4 4 LYS A 185 GLU A 194 1 10 SHEET 1 A 4 VAL A 137 ARG A 143 0 SHEET 2 A 4 SER A 153 PHE A 158 -1 O VAL A 157 N ASN A 139 SHEET 3 A 4 VAL A 113 LYS A 116 -1 N VAL A 113 O VAL A 156 SHEET 4 A 4 LEU A 181 PHE A 184 -1 O LEU A 183 N TYR A 114 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