Header list of 1x5t.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 16-MAY-05 1X5T TITLE SOLUTION STRUCTURE OF THE SECOND RRM DOMAIN IN SPLICING FACTOR = 3B COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPLICING FACTOR 3B SUBUNIT 4; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RRM DOMAIN; COMPND 5 SYNONYM: SPLICEOSOME ASSOCIATED PROTEIN 49, SAP 49, SF3B50, PRE-MRNA COMPND 6 SPLICING FACTOR SF3B 49 KDA SUBUNIT; 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: SF3B4, SAP49; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040517-06; SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS STRUCTURE GENOMICS, RRM DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.SATO,K.KUWASAKO,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA, AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1X5T 1 REMARK SEQADV REVDAT 2 24-FEB-09 1X5T 1 VERSN REVDAT 1 16-NOV-05 1X5T 0 JRNL AUTH A.SATO,K.KUWASAKO,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU, JRNL AUTH 2 T.TERADA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE SECOND RRM DOMAIN IN SPLICING JRNL TITL 2 FACTOR = 3B JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT,P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1X5T 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 DEPOSITION ID IS D_1000024415. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.8MM U-15, 13C; 20MM PHOSPHATE REMARK 210 BUFFER NA; 100MM NACL; 1MM D-DTT; REMARK 210 0.02% NAN3; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.925, CYANA 2.0.17 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 : TARGET FUNCTION, STRUCTURES WITH REMARK 210 THE LOWEST 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: 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 SER A 2 137.82 -172.80 REMARK 500 1 THR A 25 -36.81 -39.97 REMARK 500 1 THR A 35 132.34 -38.39 REMARK 500 1 ASP A 43 -71.99 -96.78 REMARK 500 1 SER A 47 121.14 -174.82 REMARK 500 1 ASN A 69 84.04 -64.04 REMARK 500 1 GLN A 71 119.77 -35.46 REMARK 500 1 CYS A 74 91.09 -32.19 REMARK 500 1 ASN A 75 47.57 39.39 REMARK 500 1 ARG A 76 109.83 -170.43 REMARK 500 1 TYR A 82 122.98 -38.16 REMARK 500 2 ASN A 12 49.69 74.10 REMARK 500 2 THR A 25 -38.48 -37.54 REMARK 500 2 PHE A 29 -70.60 -57.51 REMARK 500 2 THR A 35 138.97 -35.42 REMARK 500 2 PRO A 42 1.67 -69.76 REMARK 500 2 ASN A 46 104.26 -43.30 REMARK 500 2 SER A 47 122.87 -35.64 REMARK 500 2 ALA A 67 -60.12 -93.10 REMARK 500 2 ASN A 69 86.93 -69.18 REMARK 500 2 CYS A 74 90.90 -33.69 REMARK 500 2 ARG A 76 106.03 -170.32 REMARK 500 2 TYR A 82 108.14 -45.71 REMARK 500 2 LYS A 85 123.21 -171.68 REMARK 500 2 SER A 94 49.54 34.45 REMARK 500 3 PRO A 15 0.50 -69.75 REMARK 500 3 LEU A 21 -70.17 -48.28 REMARK 500 3 THR A 35 133.41 -37.05 REMARK 500 3 SER A 47 105.48 -48.03 REMARK 500 3 ASN A 69 81.47 -65.99 REMARK 500 3 CYS A 74 90.87 -33.17 REMARK 500 3 ARG A 76 105.58 -170.42 REMARK 500 3 ASP A 87 134.29 -172.41 REMARK 500 4 THR A 35 135.19 -39.72 REMARK 500 4 ASP A 43 -64.36 -100.37 REMARK 500 4 ASN A 69 73.91 -63.98 REMARK 500 4 GLN A 71 127.90 -34.06 REMARK 500 4 CYS A 74 90.96 -32.16 REMARK 500 4 ASN A 75 47.15 39.35 REMARK 500 4 ARG A 76 112.81 -170.60 REMARK 500 4 TYR A 82 127.42 -35.79 REMARK 500 4 LYS A 86 56.34 -112.82 REMARK 500 5 THR A 35 136.67 -36.52 REMARK 500 5 THR A 44 -74.49 -77.08 REMARK 500 5 SER A 47 107.32 -47.60 REMARK 500 5 ALA A 67 -60.66 -96.59 REMARK 500 5 ASN A 69 96.54 -56.69 REMARK 500 5 CYS A 74 90.39 -31.71 REMARK 500 5 ASN A 75 48.08 39.81 REMARK 500 5 ARG A 76 106.66 -170.93 REMARK 500 REMARK 500 THIS ENTRY HAS 234 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSS001003928.2 RELATED DB: TARGETDB DBREF 1X5T A 8 90 UNP Q15427 SF3B4_HUMAN 102 184 SEQADV 1X5T GLY A 1 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T SER A 2 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T SER A 3 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T GLY A 4 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T SER A 5 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T SER A 6 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T GLY A 7 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T SER A 91 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T GLY A 92 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T PRO A 93 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T SER A 94 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T SER A 95 UNP Q15427 CLONING ARTIFACT SEQADV 1X5T GLY A 96 UNP Q15427 CLONING ARTIFACT SEQRES 1 A 96 GLY SER SER GLY SER SER GLY ILE PHE ILE GLY ASN LEU SEQRES 2 A 96 ASP PRO GLU ILE ASP GLU LYS LEU LEU TYR ASP THR PHE SEQRES 3 A 96 SER ALA PHE GLY VAL ILE LEU GLN THR PRO LYS ILE MET SEQRES 4 A 96 ARG ASP PRO ASP THR GLY ASN SER LYS GLY TYR ALA PHE SEQRES 5 A 96 ILE ASN PHE ALA SER PHE ASP ALA SER ASP ALA ALA ILE SEQRES 6 A 96 GLU ALA MET ASN GLY GLN TYR LEU CYS ASN ARG PRO ILE SEQRES 7 A 96 THR VAL SER TYR ALA PHE LYS LYS ASP SER LYS GLY SER SEQRES 8 A 96 GLY PRO SER SER GLY HELIX 1 1 GLU A 19 SER A 27 1 9 HELIX 2 2 SER A 57 ALA A 67 1 11 SHEET 1 A 4 LYS A 37 ILE A 38 0 SHEET 2 A 4 TYR A 50 ASN A 54 -1 O PHE A 52 N LYS A 37 SHEET 3 A 4 GLY A 7 GLY A 11 -1 N ILE A 8 O ILE A 53 SHEET 4 A 4 THR A 79 TYR A 82 -1 O SER A 81 N PHE A 9 SHEET 1 B 2 TYR A 72 LEU A 73 0 SHEET 2 B 2 ARG A 76 PRO A 77 -1 O ARG A 76 N LEU A 73 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