Header list of 1x65.pdb file
Complete list - r 25 2 Bytes
HEADER RNA BINDING PROTEIN 17-MAY-05 1X65 TITLE SOLUTION STRUCTURE OF THE THIRD COLD-SHOCK DOMAIN OF THE HUMAN TITLE 2 KIAA0885 PROTEIN (UNR PROTEIN) COMPND MOL_ID: 1; COMPND 2 MOLECULE: UNR PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: THIRD COLD-SHOCK DOMAIN; COMPND 5 SYNONYM: N-RAS UPSTREAM GENE PROTEIN; COMPND 6 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: UNR; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040114-41; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTESIS KEYWDS CELL-FREE PROTEIN SYNTHESIS, BETA-BARREL, TRANSLATIONAL REGULATION, KEYWDS 2 RNA CHAPERONE, RNA/DNA BINDING, QB FOLD, GREEK-KEY TOPOLOGY, UNR KEYWDS 3 PROTEIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN KEYWDS 4 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 5 GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.K.GORONCY,T.KIGAWA,S.KOSHIBA,N.KOBAYASHI,N.TOCHIO,M.INOUE, AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 01-SEP-10 1X65 1 JRNL REVDAT 2 24-FEB-09 1X65 1 VERSN REVDAT 1 17-NOV-05 1X65 0 JRNL AUTH A.K.GORONCY,S.KOSHIBA,N.TOCHIO,T.TOMIZAWA,M.INOUE, JRNL AUTH 2 S.WATANABE,T.HARADA,A.TANAKA,O.OHARA,T.KIGAWA,S.YOKOYAMA JRNL TITL THE NMR SOLUTION STRUCTURES OF THE FIVE CONSTITUENT JRNL TITL 2 COLD-SHOCK DOMAINS (CSD) OF THE HUMAN UNR (UPSTREAM OF JRNL TITL 3 N-RAS) PROTEIN. JRNL REF J.STRUCT.FUNCT.GENOM. V. 11 181 2010 JRNL REFN ISSN 1345-711X JRNL PMID 20213426 JRNL DOI 10.1007/S10969-010-9081-Z REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 2.0.26 REMARK 3 AUTHORS : PETER GUNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1X65 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-05. REMARK 100 THE RCSB ID CODE IS RCSB024427. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 120 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.67MM COLD-SHOCK DOMAIN, 20MM REMARK 210 PHOSPHATE BUFFER NA, 100MM NACL, REMARK 210 1MM D-DTT, 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRPIPE 20020425, REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.899A 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 LEAST REMARK 210 RESTRAINT VIOLATIONS 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: 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 ARG A 17 150.54 -37.53 REMARK 500 1 ASP A 18 90.17 -61.23 REMARK 500 1 PHE A 36 42.71 -80.77 REMARK 500 1 ASN A 43 118.77 172.29 REMARK 500 1 LEU A 45 168.58 -45.42 REMARK 500 1 ALA A 48 53.78 78.20 REMARK 500 1 VAL A 55 144.00 60.07 REMARK 500 1 PRO A 57 2.55 -69.78 REMARK 500 1 ASP A 58 168.63 70.49 REMARK 500 1 ALA A 62 34.84 35.34 REMARK 500 1 ARG A 64 141.85 61.12 REMARK 500 1 ARG A 69 80.85 34.58 REMARK 500 1 SER A 79 131.56 173.42 REMARK 500 1 SER A 87 94.76 -177.60 REMARK 500 1 SER A 88 139.14 -34.61 REMARK 500 2 SER A 2 -45.10 -132.80 REMARK 500 2 SER A 6 -38.90 -140.99 REMARK 500 2 MET A 16 63.39 -154.02 REMARK 500 2 ARG A 31 -171.27 -68.36 REMARK 500 2 PHE A 36 42.82 -80.66 REMARK 500 2 ASN A 43 117.78 171.17 REMARK 500 2 ILE A 47 107.58 -48.23 REMARK 500 2 ALA A 48 63.36 76.66 REMARK 500 2 VAL A 55 96.24 55.23 REMARK 500 2 SER A 61 160.56 65.97 REMARK 500 2 ALA A 62 -56.98 77.60 REMARK 500 2 ARG A 64 -159.39 -123.88 REMARK 500 2 ARG A 69 77.06 36.27 REMARK 500 2 THR A 77 -77.63 -71.45 REMARK 500 2 HIS A 81 82.78 55.73 REMARK 500 2 SER A 82 119.20 -177.70 REMARK 500 2 SER A 87 107.01 -168.16 REMARK 500 2 SER A 88 -51.14 -173.36 REMARK 500 3 SER A 6 93.73 -65.77 REMARK 500 3 ILE A 13 85.53 -61.25 REMARK 500 3 MET A 16 57.77 -150.28 REMARK 500 3 PHE A 36 42.83 -80.81 REMARK 500 3 ASN A 43 114.31 171.13 REMARK 500 3 ALA A 48 49.45 83.34 REMARK 500 3 SER A 61 40.65 -175.62 REMARK 500 3 GLN A 63 162.58 -45.56 REMARK 500 3 ARG A 64 97.49 -47.58 REMARK 500 3 ASN A 65 147.67 -34.44 REMARK 500 3 ARG A 69 81.27 37.22 REMARK 500 3 THR A 77 -65.14 -165.06 REMARK 500 3 SER A 79 -158.65 -58.73 REMARK 500 3 PHE A 80 134.11 61.61 REMARK 500 3 PRO A 86 2.69 -69.75 REMARK 500 3 SER A 87 -56.62 81.25 REMARK 500 4 SER A 5 -53.23 -128.35 REMARK 500 REMARK 500 THIS ENTRY HAS 332 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002000864.1 RELATED DB: TARGETDB DBREF 1X65 A 8 83 UNP O75534 CSDE1_HUMAN 348 423 SEQADV 1X65 GLY A 1 UNP O75534 CLONING ARTIFACT SEQADV 1X65 SER A 2 UNP O75534 CLONING ARTIFACT SEQADV 1X65 SER A 3 UNP O75534 CLONING ARTIFACT SEQADV 1X65 GLY A 4 UNP O75534 CLONING ARTIFACT SEQADV 1X65 SER A 5 UNP O75534 CLONING ARTIFACT SEQADV 1X65 SER A 6 UNP O75534 CLONING ARTIFACT SEQADV 1X65 GLY A 7 UNP O75534 CLONING ARTIFACT SEQADV 1X65 SER A 84 UNP O75534 CLONING ARTIFACT SEQADV 1X65 GLY A 85 UNP O75534 CLONING ARTIFACT SEQADV 1X65 PRO A 86 UNP O75534 CLONING ARTIFACT SEQADV 1X65 SER A 87 UNP O75534 CLONING ARTIFACT SEQADV 1X65 SER A 88 UNP O75534 CLONING ARTIFACT SEQADV 1X65 GLY A 89 UNP O75534 CLONING ARTIFACT SEQRES 1 A 89 GLY SER SER GLY SER SER GLY ARG GLU MET GLY VAL ILE SEQRES 2 A 89 ALA ALA MET ARG ASP GLY PHE GLY PHE ILE LYS CYS VAL SEQRES 3 A 89 ASP ARG ASP VAL ARG MET PHE PHE HIS PHE SER GLU ILE SEQRES 4 A 89 LEU ASP GLY ASN GLN LEU HIS ILE ALA ASP GLU VAL GLU SEQRES 5 A 89 PHE THR VAL VAL PRO ASP MET LEU SER ALA GLN ARG ASN SEQRES 6 A 89 HIS ALA ILE ARG ILE LYS LYS LEU PRO LYS GLY THR VAL SEQRES 7 A 89 SER PHE HIS SER HIS SER GLY PRO SER SER GLY HELIX 1 1 SER A 37 GLY A 42 5 6 SHEET 1 A 4 PHE A 22 CYS A 25 0 SHEET 2 A 4 GLU A 9 ALA A 15 -1 N VAL A 12 O LYS A 24 SHEET 3 A 4 VAL A 51 PHE A 53 -1 O PHE A 53 N GLU A 9 SHEET 4 A 4 LYS A 71 LYS A 72 -1 O LYS A 71 N GLU A 52 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 25 2 Bytes