Header list of 2cqd.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSLATION 19-MAY-05 2CQD TITLE SOLUTION STRUCTURE OF THE RNA RECOGNITION MOTIF IN RNA-BINDING REGION TITLE 2 CONTAINING PROTEIN 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RNA-BINDING REGION CONTAINING PROTEIN 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF; COMPND 5 SYNONYM: HSRNASEB, SSDNA BINDING PROTEIN SEB4, CLL-ASSOCIATED ANTIGEN COMPND 6 KW-5; 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: RNPC1; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050125-15; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RNA RECOGNITION MOTIF, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT KEYWDS 2 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSLATION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.SOMEYA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2CQD 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CQD 1 VERSN REVDAT 1 19-NOV-05 2CQD 0 JRNL AUTH T.SOMEYA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE RNA RECOGNITION MOTIF IN JRNL TITL 2 RNA-BINDING REGION CONTAINING PROTEIN 1 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2CQD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024504. 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 : 1.30MM PROTEIN U-15N, 13C; 20MM REMARK 210 D-TRIS-HCL; 100MM NACL; 1MM D- REMARK 210 DTT; 0.02% NAN3; 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.9295, CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 RESTRAINTED MOLECULAR 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, STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 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 PRO A 19 -165.68 -69.82 REMARK 500 1 HIS A 21 39.62 -85.52 REMARK 500 1 ALA A 25 -70.62 -63.53 REMARK 500 1 LYS A 29 -35.10 -38.75 REMARK 500 1 GLU A 32 -30.14 -37.46 REMARK 500 1 ALA A 63 -70.55 -63.68 REMARK 500 1 LYS A 70 -25.62 -39.22 REMARK 500 1 LEU A 85 178.92 -50.29 REMARK 500 2 MET A 1 97.66 -51.65 REMARK 500 2 THR A 9 -61.90 -121.94 REMARK 500 2 PRO A 19 -164.57 -69.77 REMARK 500 2 HIS A 21 42.22 -90.66 REMARK 500 2 SER A 26 -70.97 -54.32 REMARK 500 2 ARG A 46 -53.41 -120.90 REMARK 500 2 LYS A 50 79.75 -117.20 REMARK 500 2 SER A 51 151.49 -36.86 REMARK 500 2 LYS A 70 -28.90 -36.93 REMARK 500 2 ILE A 75 96.06 -38.96 REMARK 500 2 ASP A 77 26.05 48.22 REMARK 500 2 ASN A 84 149.70 -174.31 REMARK 500 2 LEU A 85 170.32 -50.03 REMARK 500 2 VAL A 103 37.27 35.72 REMARK 500 2 PRO A 106 -174.46 -69.72 REMARK 500 3 LYS A 6 75.02 -116.69 REMARK 500 3 PRO A 19 -175.95 -69.73 REMARK 500 3 HIS A 21 38.07 -91.66 REMARK 500 3 ARG A 46 -51.89 -121.83 REMARK 500 3 LYS A 50 88.95 -54.46 REMARK 500 3 LYS A 70 -34.30 -34.31 REMARK 500 3 LEU A 85 174.31 -47.50 REMARK 500 3 PRO A 92 93.14 -69.75 REMARK 500 4 PRO A 19 -168.49 -69.77 REMARK 500 4 HIS A 21 46.88 -91.47 REMARK 500 4 ASP A 24 -32.95 -37.38 REMARK 500 4 ILE A 43 86.12 -51.08 REMARK 500 4 ASP A 45 -179.97 -57.50 REMARK 500 4 ARG A 62 -36.33 -38.06 REMARK 500 4 LYS A 70 -31.88 -37.17 REMARK 500 4 LEU A 85 -177.54 -56.35 REMARK 500 4 PRO A 92 -177.38 -69.72 REMARK 500 5 SER A -4 49.73 -93.07 REMARK 500 5 GLN A 5 167.28 -45.70 REMARK 500 5 THR A 9 -61.13 -122.73 REMARK 500 5 PRO A 19 -164.49 -69.82 REMARK 500 5 HIS A 21 40.27 -84.14 REMARK 500 5 ILE A 43 89.98 -46.34 REMARK 500 5 LEU A 85 175.62 -47.80 REMARK 500 5 TYR A 87 -34.55 -132.02 REMARK 500 5 ARG A 93 122.45 -38.99 REMARK 500 5 LEU A 95 100.85 -35.88 REMARK 500 REMARK 500 THIS ENTRY HAS 201 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002013305.1 RELATED DB: TARGETDB DBREF 2CQD A 1 103 UNP Q9H0Z9 RNPC1_HUMAN 1 103 SEQADV 2CQD GLY A -6 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD SER A -5 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD SER A -4 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD GLY A -3 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD SER A -2 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD SER A -1 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD GLY A 0 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD SER A 104 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD GLY A 105 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD PRO A 106 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD SER A 107 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD SER A 108 UNP Q9H0Z9 CLONING ARTIFACT SEQADV 2CQD GLY A 109 UNP Q9H0Z9 CLONING ARTIFACT SEQRES 1 A 116 GLY SER SER GLY SER SER GLY MET HIS GLY SER GLN LYS SEQRES 2 A 116 ASP THR THR PHE THR LYS ILE PHE VAL GLY GLY LEU PRO SEQRES 3 A 116 TYR HIS THR THR ASP ALA SER LEU ARG LYS TYR PHE GLU SEQRES 4 A 116 GLY PHE GLY ASP ILE GLU GLU ALA VAL VAL ILE THR ASP SEQRES 5 A 116 ARG GLN THR GLY LYS SER ARG GLY TYR GLY PHE VAL THR SEQRES 6 A 116 MET ALA ASP ARG ALA ALA ALA GLU ARG ALA CYS LYS ASP SEQRES 7 A 116 PRO ASN PRO ILE ILE ASP GLY ARG LYS ALA ASN VAL ASN SEQRES 8 A 116 LEU ALA TYR LEU GLY ALA LYS PRO ARG SER LEU GLN THR SEQRES 9 A 116 GLY PHE ALA ILE GLY VAL SER GLY PRO SER SER GLY HELIX 1 1 ASP A 24 GLU A 32 1 9 HELIX 2 2 ALA A 64 LYS A 70 1 7 SHEET 1 A 4 ALA A 40 VAL A 42 0 SHEET 2 A 4 TYR A 54 THR A 58 -1 O THR A 58 N GLU A 38 SHEET 3 A 4 LYS A 12 GLY A 16 -1 N ILE A 13 O VAL A 57 SHEET 4 A 4 ASN A 82 ASN A 84 -1 O ASN A 82 N GLY A 16 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 9 2 Bytes