Header list of 2cq1.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 19-MAY-05 2CQ1 TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN PTB-LIKE PROTEIN L COMPND MOL_ID: 1; COMPND 2 MOLECULE: PTB-LIKE PROTEIN L; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF; COMPND 5 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: PTBLP; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040921-04; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RRM DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.TSUDA,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 2CQ1 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CQ1 1 VERSN REVDAT 1 19-NOV-05 2CQ1 0 JRNL AUTH K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN PTB-LIKE PROTEIN JRNL TITL 2 L 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 2CQ1 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_1000024492. 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 : 1.34MM 13C/15N-PROTEIN, 20MM D REMARK 210 -TRIS-HCL (PH 7.0), 100MM NACL, REMARK 210 1MM D-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 0.9297, 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 SER A 48 129.99 -170.63 REMARK 500 1 ALA A 56 73.71 -119.20 REMARK 500 1 PRO A 57 155.95 -45.80 REMARK 500 1 THR A 138 -40.72 -134.36 REMARK 500 1 SER A 143 -42.90 -134.98 REMARK 500 2 GLU A 72 -39.57 -35.69 REMARK 500 2 THR A 138 44.34 70.49 REMARK 500 3 SER A 45 43.33 38.61 REMARK 500 3 ASP A 51 104.50 -51.96 REMARK 500 3 LYS A 52 179.49 -50.87 REMARK 500 3 ASP A 54 81.65 -56.50 REMARK 500 3 PRO A 67 161.58 -47.44 REMARK 500 3 GLU A 69 46.55 73.80 REMARK 500 3 ASN A 95 42.36 -87.87 REMARK 500 3 SER A 115 -32.21 -39.27 REMARK 500 3 LYS A 134 41.38 30.39 REMARK 500 3 GLU A 135 132.26 -171.52 REMARK 500 3 LYS A 137 173.35 -51.73 REMARK 500 3 PRO A 141 167.74 -45.83 REMARK 500 4 PRO A 67 160.24 -46.87 REMARK 500 4 ASN A 95 49.10 -106.67 REMARK 500 4 SER A 115 -31.74 -38.73 REMARK 500 4 ASN A 123 35.17 73.08 REMARK 500 4 LYS A 134 36.53 34.40 REMARK 500 4 LEU A 136 93.49 -69.33 REMARK 500 4 PRO A 141 161.12 -45.63 REMARK 500 5 ASP A 51 176.96 -58.99 REMARK 500 5 PRO A 57 153.04 -46.06 REMARK 500 5 PRO A 125 165.93 -47.80 REMARK 500 6 ALA A 56 76.11 -114.14 REMARK 500 6 PRO A 57 101.93 -45.23 REMARK 500 6 ARG A 59 32.18 -87.18 REMARK 500 6 TYR A 113 -35.13 -36.76 REMARK 500 6 SER A 115 -38.95 -38.30 REMARK 500 6 HIS A 120 119.97 -160.89 REMARK 500 6 PRO A 141 47.17 -74.54 REMARK 500 7 SER A 49 90.12 -67.53 REMARK 500 7 PRO A 57 -176.75 -48.68 REMARK 500 7 PRO A 67 158.82 -47.07 REMARK 500 7 THR A 73 -33.50 -35.66 REMARK 500 7 HIS A 120 118.14 -161.10 REMARK 500 7 ASN A 123 31.32 70.78 REMARK 500 7 ASN A 132 -64.69 -95.97 REMARK 500 7 HIS A 133 -72.74 -121.79 REMARK 500 7 LYS A 134 47.00 38.95 REMARK 500 7 GLU A 135 87.18 -61.96 REMARK 500 7 LYS A 137 92.15 -67.16 REMARK 500 7 PRO A 141 40.99 -77.04 REMARK 500 8 ASP A 51 42.73 -106.00 REMARK 500 8 ALA A 56 105.01 -172.88 REMARK 500 REMARK 500 THIS ENTRY HAS 128 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002009793.1 RELATED DB: TARGETDB DBREF 2CQ1 A 51 138 UNP Q969N9 Q969N9_HUMAN 51 138 SEQADV 2CQ1 GLY A 44 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 SER A 45 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 SER A 46 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 GLY A 47 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 SER A 48 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 SER A 49 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 GLY A 50 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 SER A 139 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 GLY A 140 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 PRO A 141 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 SER A 142 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 SER A 143 UNP Q969N9 CLONING ARTIFACT SEQADV 2CQ1 GLY A 144 UNP Q969N9 CLONING ARTIFACT SEQRES 1 A 101 GLY SER SER GLY SER SER GLY ASP LYS MET ASP GLY ALA SEQRES 2 A 101 PRO SER ARG VAL LEU HIS ILE ARG LYS LEU PRO GLY GLU SEQRES 3 A 101 VAL THR GLU THR GLU VAL ILE ALA LEU GLY LEU PRO PHE SEQRES 4 A 101 GLY LYS VAL THR ASN ILE LEU MET LEU LYS GLY LYS ASN SEQRES 5 A 101 GLN ALA PHE LEU GLU LEU ALA THR GLU GLU ALA ALA ILE SEQRES 6 A 101 THR MET VAL ASN TYR TYR SER ALA VAL THR PRO HIS LEU SEQRES 7 A 101 ARG ASN GLN PRO ILE TYR ILE GLN TYR SER ASN HIS LYS SEQRES 8 A 101 GLU LEU LYS THR SER GLY PRO SER SER GLY HELIX 1 1 THR A 71 LEU A 78 1 8 HELIX 2 2 THR A 103 VAL A 117 1 15 SHEET 1 A 4 VAL A 85 LEU A 91 0 SHEET 2 A 4 GLN A 96 LEU A 101 -1 O PHE A 98 N LEU A 89 SHEET 3 A 4 VAL A 60 ARG A 64 -1 N LEU A 61 O LEU A 99 SHEET 4 A 4 TYR A 127 TYR A 130 -1 O TYR A 127 N ARG A 64 SHEET 1 B 2 HIS A 120 LEU A 121 0 SHEET 2 B 2 GLN A 124 PRO A 125 -1 O GLN A 124 N LEU A 121 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