Header list of 2cqh.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 20-MAY-05 2CQH TITLE SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN OF IGF-II MRNA-BINDING TITLE 2 PROTEIN 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGF-II MRNA-BINDING PROTEIN 2 ISOFORM A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF; COMPND 5 SYNONYM: INSULIN-LIKE GROWTH FACTOR 2 MRNA-BINDING PROTEIN 2; 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: IMP2; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041108-02; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RNA RECOGNITION MOTIF, RRM, RNA BINDING DOMAIN, RBD, RNP, STRUCTURAL KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 4 INITIATIVE, RSGI, RNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.SUZUKI,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 2CQH 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CQH 1 VERSN REVDAT 1 20-NOV-05 2CQH 0 JRNL AUTH S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN OF IGF-II JRNL TITL 2 MRNA-BINDING PROTEIN 2 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 2CQH 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_1000024508. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.2MM 13C/15N-PROTEIN; 20MM D REMARK 210 -TRIS-HCL(PH7.0); 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 : 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 0.9295, OLIVIA 1.10.5, REMARK 210 CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 0 150.45 -38.59 REMARK 500 1 ASN A 9 41.16 70.83 REMARK 500 1 PRO A 12 0.00 -69.78 REMARK 500 1 ALA A 31 30.70 -89.68 REMARK 500 1 SER A 38 92.02 -67.60 REMARK 500 1 LEU A 58 -71.71 -100.35 REMARK 500 1 SER A 74 86.22 -68.62 REMARK 500 1 SER A 76 -60.05 -122.08 REMARK 500 1 LYS A 77 43.40 39.76 REMARK 500 1 PRO A 84 -172.08 -69.77 REMARK 500 2 SER A 11 143.61 -39.91 REMARK 500 2 PRO A 12 2.89 -69.70 REMARK 500 2 SER A 38 92.27 -67.91 REMARK 500 2 LEU A 58 -73.29 -97.18 REMARK 500 3 MET A 2 150.71 -43.64 REMARK 500 3 ASN A 9 41.22 71.49 REMARK 500 3 ALA A 31 34.44 -85.41 REMARK 500 3 SER A 38 92.66 -67.95 REMARK 500 3 LEU A 58 -67.66 -99.69 REMARK 500 3 TYR A 73 153.75 -38.69 REMARK 500 3 LYS A 77 107.55 -168.79 REMARK 500 4 ASN A 9 42.96 70.38 REMARK 500 4 SER A 11 151.19 -41.85 REMARK 500 4 PRO A 12 0.14 -69.71 REMARK 500 4 ALA A 31 37.31 -84.49 REMARK 500 4 SER A 38 92.38 -67.78 REMARK 500 4 LEU A 58 -74.23 -102.27 REMARK 500 4 TYR A 73 152.42 -40.71 REMARK 500 5 SER A -4 -61.90 -125.71 REMARK 500 5 SER A -3 96.49 -57.25 REMARK 500 5 PRO A 12 0.29 -69.83 REMARK 500 5 LEU A 30 100.40 -58.23 REMARK 500 5 ALA A 31 36.08 -83.46 REMARK 500 5 SER A 38 91.36 -68.36 REMARK 500 5 LEU A 58 -67.86 -101.61 REMARK 500 5 TYR A 73 148.28 -37.68 REMARK 500 6 ASN A 3 107.92 -52.19 REMARK 500 6 ASN A 9 35.67 73.90 REMARK 500 6 ALA A 31 34.49 -94.74 REMARK 500 6 SER A 38 91.08 -68.28 REMARK 500 6 LEU A 58 -67.08 -95.19 REMARK 500 6 SER A 74 44.03 -101.95 REMARK 500 7 SER A -4 109.66 -170.04 REMARK 500 7 SER A 11 150.95 -46.27 REMARK 500 7 LEU A 28 77.82 -113.21 REMARK 500 7 ALA A 31 31.36 -84.42 REMARK 500 7 SER A 38 96.14 -67.24 REMARK 500 7 LEU A 58 -72.70 -104.27 REMARK 500 7 TYR A 73 144.63 -34.49 REMARK 500 7 LYS A 77 176.52 -51.29 REMARK 500 REMARK 500 THIS ENTRY HAS 150 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002013968.1 RELATED DB: TARGETDB DBREF 2CQH A 2 81 UNP Q9Y6M1 Q9Y6M1_HUMAN 2 81 SEQADV 2CQH GLY A -5 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH SER A -4 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH SER A -3 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH GLY A -2 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH SER A -1 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH SER A 0 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH GLY A 1 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH SER A 82 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH GLY A 83 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH PRO A 84 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH SER A 85 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH SER A 86 UNP Q9Y6M1 CLONING ARTIFACT SEQADV 2CQH GLY A 87 UNP Q9Y6M1 CLONING ARTIFACT SEQRES 1 A 93 GLY SER SER GLY SER SER GLY MET ASN LYS LEU TYR ILE SEQRES 2 A 93 GLY ASN LEU SER PRO ALA VAL THR ALA ASP ASP LEU ARG SEQRES 3 A 93 GLN LEU PHE GLY ASP ARG LYS LEU PRO LEU ALA GLY GLN SEQRES 4 A 93 VAL LEU LEU LYS SER GLY TYR ALA PHE VAL ASP TYR PRO SEQRES 5 A 93 ASP GLN ASN TRP ALA ILE ARG ALA ILE GLU THR LEU SER SEQRES 6 A 93 GLY LYS VAL GLU LEU HIS GLY LYS ILE MET GLU VAL ASP SEQRES 7 A 93 TYR SER VAL SER LYS LYS LEU ARG SER SER GLY PRO SER SEQRES 8 A 93 SER GLY HELIX 1 1 ALA A 16 ARG A 26 1 11 HELIX 2 2 GLN A 48 THR A 57 1 10 SHEET 1 A 4 LYS A 4 GLY A 8 0 SHEET 2 A 4 GLN A 33 LYS A 37 -1 SHEET 3 A 4 TYR A 40 ASP A 44 -1 SHEET 4 A 4 GLU A 63 LEU A 64 -1 SHEET 1 B 2 LYS A 67 ILE A 68 0 SHEET 2 B 2 GLU A 70 TYR A 73 -1 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