Header list of 2cof.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 17-MAY-05 2COF TITLE SOLUTION STRUCTURE OF THE C-TERMINAL PH DOMAIN OF HYPOTHETICAL PROTEIN TITLE 2 KIAA1914 FROM HUMAN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN KIAA1914; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PH DOMAIN; 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: KIAA1914; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040921-07; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS HYPOTHETICAL PROTEIN KIAA1914, PH DOMAIN, STRUCTURAL GENOMICS, RIKEN KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, NPPSFA, NATIONAL KEYWDS 3 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, UNKNOWN KEYWDS 4 FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.LI,K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2COF 1 REMARK SEQADV REVDAT 2 24-FEB-09 2COF 1 VERSN REVDAT 1 17-NOV-05 2COF 0 JRNL AUTH H.LI,K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL PH DOMAIN OF JRNL TITL 2 HYPOTHETICAL PROTEIN KIAA1914 FROM HUMAN 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), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2COF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024447. 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 : 1.59MM PH DOMAIN U-13C, 15N; REMARK 210 20MM D-TRIS-HCL(PH7.0); 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 20031121, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.913, 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 LEAST RESTRAINT 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 THR A 10 39.34 34.64 REMARK 500 1 ARG A 42 44.68 35.20 REMARK 500 1 GLN A 48 139.53 -33.61 REMARK 500 1 VAL A 53 98.58 -43.86 REMARK 500 1 CYS A 55 179.32 -52.91 REMARK 500 1 PRO A 59 91.09 -69.80 REMARK 500 1 ASP A 60 76.57 -106.70 REMARK 500 1 PRO A 63 3.88 -69.71 REMARK 500 1 HIS A 65 107.26 -163.71 REMARK 500 1 PRO A 104 2.78 -69.73 REMARK 500 2 SER A 6 155.47 -42.17 REMARK 500 2 GLN A 38 44.32 -107.61 REMARK 500 2 ASP A 39 25.11 39.93 REMARK 500 2 ARG A 40 58.72 -104.07 REMARK 500 2 ARG A 42 40.14 37.51 REMARK 500 2 LYS A 44 76.78 -108.76 REMARK 500 2 VAL A 53 102.88 -47.04 REMARK 500 2 CYS A 55 -179.61 -67.95 REMARK 500 2 PRO A 59 90.16 -69.83 REMARK 500 2 ASP A 60 75.68 -106.77 REMARK 500 2 PRO A 63 4.60 -69.86 REMARK 500 2 HIS A 65 105.02 -167.41 REMARK 500 2 TYR A 67 51.49 -119.87 REMARK 500 2 HIS A 73 -74.24 -92.91 REMARK 500 3 GLU A 9 -60.97 -94.47 REMARK 500 3 TYR A 13 102.79 -42.73 REMARK 500 3 LYS A 44 72.31 -110.04 REMARK 500 3 VAL A 53 103.50 -49.64 REMARK 500 3 PRO A 59 91.26 -69.82 REMARK 500 3 ASP A 60 76.24 -106.85 REMARK 500 3 PRO A 63 4.36 -69.70 REMARK 500 3 HIS A 65 105.40 -166.23 REMARK 500 3 HIS A 73 -71.28 -99.78 REMARK 500 3 SER A 100 93.00 -62.22 REMARK 500 4 SER A 5 42.05 -108.83 REMARK 500 4 SER A 11 118.16 -37.58 REMARK 500 4 ASN A 41 44.97 -79.51 REMARK 500 4 ARG A 42 40.99 34.76 REMARK 500 4 SER A 51 79.97 -109.53 REMARK 500 4 VAL A 53 101.26 -45.45 REMARK 500 4 CYS A 55 -179.31 -67.88 REMARK 500 4 PRO A 59 92.70 -69.70 REMARK 500 4 ASP A 60 76.29 -106.59 REMARK 500 4 PRO A 63 3.48 -69.73 REMARK 500 4 LYS A 74 33.65 75.06 REMARK 500 5 ARG A 30 -73.80 -130.96 REMARK 500 5 ASN A 32 39.03 32.41 REMARK 500 5 ASN A 41 41.62 -102.28 REMARK 500 5 ARG A 42 38.45 35.77 REMARK 500 5 GLN A 48 142.06 -35.92 REMARK 500 REMARK 500 THIS ENTRY HAS 258 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002010814.1 RELATED DB: TARGETDB DBREF 2COF A 8 101 UNP Q8N4X5 K1914_HUMAN 354 447 SEQADV 2COF GLY A 1 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF SER A 2 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF SER A 3 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF GLY A 4 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF SER A 5 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF SER A 6 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF GLY A 7 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF SER A 102 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF GLY A 103 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF PRO A 104 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF SER A 105 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF SER A 106 UNP Q8N4X5 CLONING ARTIFACT SEQADV 2COF GLY A 107 UNP Q8N4X5 CLONING ARTIFACT SEQRES 1 A 107 GLY SER SER GLY SER SER GLY LEU GLU THR SER SER TYR SEQRES 2 A 107 LEU ASN VAL LEU VAL ASN SER GLN TRP LYS SER ARG TRP SEQRES 3 A 107 CYS SER VAL ARG ASP ASN HIS LEU HIS PHE TYR GLN ASP SEQRES 4 A 107 ARG ASN ARG SER LYS VAL ALA GLN GLN PRO LEU SER LEU SEQRES 5 A 107 VAL GLY CYS GLU VAL VAL PRO ASP PRO SER PRO ASP HIS SEQRES 6 A 107 LEU TYR SER PHE ARG ILE LEU HIS LYS GLY GLU GLU LEU SEQRES 7 A 107 ALA LYS LEU GLU ALA LYS SER SER GLU GLU MET GLY HIS SEQRES 8 A 107 TRP LEU GLY LEU LEU LEU SER GLU SER GLY SER GLY PRO SEQRES 9 A 107 SER SER GLY HELIX 1 1 SER A 86 SER A 100 1 15 SHEET 1 A 7 GLN A 47 LEU A 50 0 SHEET 2 A 7 HIS A 33 TYR A 37 -1 SHEET 3 A 7 TRP A 22 ARG A 30 -1 SHEET 4 A 7 SER A 11 LEU A 17 -1 SHEET 5 A 7 LEU A 78 GLU A 82 -1 SHEET 6 A 7 SER A 68 LEU A 72 -1 SHEET 7 A 7 GLU A 56 VAL A 58 -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