Header list of 2db9.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 15-DEC-05 2DB9 TITLE SOLUTION STRUCTURE OF THE PLUS-3 DOMAIN OF HUMAN KIAA0252 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PAF1/RNA POLYMERASE II COMPLEX COMPONENT; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PLUS-3 DOMAIN, RESIDUES 8-143; COMPND 5 SYNONYM: KIAA0252 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: RTF1; SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050302-16; SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PLUS-3 DOMAIN; STRUCTURAL GENOMICS, KIAA0252, NPPSFA, NATIONAL KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL KEYWDS 4 GENOMICS, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.YONEYAMA,T.KIGAWA,N.TOCHIO,N.NAMEKI,S.KOSHIBA,M.INOUE,S.YOKOYAMA, AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2DB9 1 REMARK SEQADV REVDAT 2 24-FEB-09 2DB9 1 VERSN REVDAT 1 15-JUN-06 2DB9 0 JRNL AUTH M.YONEYAMA,T.KIGAWA,N.TOCHIO,N.NAMEKI,S.KOSHIBA,M.INOUE, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE PLUS-3 DOMAIN OF HUMAN KIAA0252 JRNL TITL 2 PROTEIN 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 1.0.8 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2DB9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000025210. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 296 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.73MM PLUS-3 DOMAIN U-15N,13C; REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90% REMARK 210 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 : 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 0.9318, CYANA 1.0.8 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, 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: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O GLU A 132 H LYS A 136 1.50 REMARK 500 O LYS A 29 H TRP A 33 1.51 REMARK 500 O GLU A 112 H TRP A 116 1.51 REMARK 500 O SER A 111 H LYS A 115 1.53 REMARK 500 O ARG A 27 H GLU A 31 1.58 REMARK 500 OD1 ASN A 21 H PHE A 108 1.60 REMARK 500 REMARK 500 REMARK: NULL 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 5 137.60 175.66 REMARK 500 1 LYS A 10 92.44 63.58 REMARK 500 1 VAL A 14 89.67 21.16 REMARK 500 1 LEU A 25 161.82 -41.29 REMARK 500 1 PHE A 38 47.11 -81.95 REMARK 500 1 PHE A 39 -72.84 -81.48 REMARK 500 1 THR A 42 -72.02 -69.58 REMARK 500 1 VAL A 43 -34.70 -35.32 REMARK 500 1 ASN A 54 -56.21 -160.36 REMARK 500 1 HIS A 55 -173.81 59.89 REMARK 500 1 SER A 57 -70.28 162.56 REMARK 500 1 LEU A 78 73.99 -151.33 REMARK 500 1 ASN A 84 44.48 -141.26 REMARK 500 1 VAL A 103 96.63 -59.71 REMARK 500 1 SER A 104 -174.03 -63.59 REMARK 500 1 PHE A 108 105.01 -50.87 REMARK 500 1 SER A 144 108.18 -172.53 REMARK 500 2 SER A 2 138.24 -173.07 REMARK 500 2 SER A 3 159.71 66.57 REMARK 500 2 SER A 5 149.23 62.98 REMARK 500 2 VAL A 14 91.02 18.42 REMARK 500 2 LEU A 25 152.03 -44.47 REMARK 500 2 PHE A 38 45.40 -83.79 REMARK 500 2 VAL A 43 -36.06 -35.94 REMARK 500 2 HIS A 55 71.85 173.27 REMARK 500 2 ASN A 56 67.19 -178.75 REMARK 500 2 SER A 57 -66.82 71.82 REMARK 500 2 LEU A 78 86.15 -153.46 REMARK 500 2 ASN A 84 16.26 -140.53 REMARK 500 2 SER A 111 -73.50 -41.85 REMARK 500 2 LEU A 130 -36.02 -38.34 REMARK 500 2 SER A 144 -57.98 -156.44 REMARK 500 3 SER A 2 120.14 -175.23 REMARK 500 3 SER A 11 -163.02 -164.16 REMARK 500 3 VAL A 14 88.69 24.62 REMARK 500 3 PHE A 38 21.34 43.93 REMARK 500 3 THR A 42 -70.44 -83.10 REMARK 500 3 VAL A 43 -33.04 -36.75 REMARK 500 3 SER A 57 179.36 -53.01 REMARK 500 3 ASN A 84 45.00 -140.94 REMARK 500 3 PHE A 98 -168.93 -115.25 REMARK 500 3 ASN A 105 -85.52 -39.18 REMARK 500 3 GLN A 106 -172.89 52.69 REMARK 500 3 SER A 148 -57.88 -147.78 REMARK 500 4 SER A 5 126.30 62.10 REMARK 500 4 LYS A 10 94.17 -172.53 REMARK 500 4 SER A 11 -164.84 -165.86 REMARK 500 4 VAL A 14 89.04 22.69 REMARK 500 4 LEU A 25 154.39 -48.54 REMARK 500 4 PHE A 38 49.56 -79.12 REMARK 500 REMARK 500 THIS ENTRY HAS 328 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002010055.1 RELATED DB: TARGETDB DBREF 2DB9 A 8 143 UNP Q92541 RTF1_HUMAN 307 442 SEQADV 2DB9 GLY A 1 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 SER A 2 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 SER A 3 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 GLY A 4 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 SER A 5 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 SER A 6 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 GLY A 7 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 SER A 144 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 GLY A 145 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 PRO A 146 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 SER A 147 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 SER A 148 UNP Q92541 CLONING ARTIFACT SEQADV 2DB9 GLY A 149 UNP Q92541 CLONING ARTIFACT SEQRES 1 A 149 GLY SER SER GLY SER SER GLY PRO PRO LYS SER GLN PRO SEQRES 2 A 149 VAL SER LEU PRO GLU GLU LEU ASN ARG VAL ARG LEU SER SEQRES 3 A 149 ARG HIS LYS LEU GLU ARG TRP CYS HIS MET PRO PHE PHE SEQRES 4 A 149 ALA LYS THR VAL THR GLY CYS PHE VAL ARG ILE GLY ILE SEQRES 5 A 149 GLY ASN HIS ASN SER LYS PRO VAL TYR ARG VAL ALA GLU SEQRES 6 A 149 ILE THR GLY VAL VAL GLU THR ALA LYS VAL TYR GLN LEU SEQRES 7 A 149 GLY GLY THR ARG THR ASN LYS GLY LEU GLN LEU ARG HIS SEQRES 8 A 149 GLY ASN ASP GLN ARG VAL PHE ARG LEU GLU PHE VAL SER SEQRES 9 A 149 ASN GLN GLU PHE THR GLU SER GLU PHE MET LYS TRP LYS SEQRES 10 A 149 GLU ALA MET PHE SER ALA GLY MET GLN LEU PRO THR LEU SEQRES 11 A 149 ASP GLU ILE ASN LYS LYS GLU LEU SER ILE LYS GLU ALA SEQRES 12 A 149 SER GLY PRO SER SER GLY HELIX 1 1 LEU A 16 VAL A 23 1 8 HELIX 2 2 SER A 26 CYS A 34 1 9 HELIX 3 3 PHE A 38 THR A 44 1 7 HELIX 4 4 THR A 109 GLY A 124 1 16 HELIX 5 5 THR A 129 SER A 144 1 16 SHEET 1 A 2 PHE A 47 GLY A 53 0 SHEET 2 A 2 VAL A 60 GLU A 65 -1 O ARG A 62 N ILE A 50 SHEET 1 B 2 GLY A 68 LEU A 78 0 SHEET 2 B 2 THR A 81 GLN A 88 -1 O GLY A 86 N VAL A 70 SHEET 1 C 2 ARG A 90 HIS A 91 0 SHEET 2 C 2 ASP A 94 GLN A 95 -1 O ASP A 94 N HIS A 91 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