Header list of 2d8r.pdb file
Complete list - r 9 2 Bytes
HEADER METAL BINDING PROTEIN 08-DEC-05 2D8R TITLE SOLUTION STRUCTURE OF THE THAP DOMAIN OF THE HUMAN THAP DOMAIN- TITLE 2 CONTAINING PROTEIN 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: THAP DOMAIN-CONTAINING PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: THAP; 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: THAP2; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050302-85; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS THAP DOMAIN-CONTAINING PROTEIN 2, THAP2, THAP, STRUCTURAL GENOMICS, KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 4 METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.MIYAMOTO,T.KIGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2D8R 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 2D8R 1 VERSN REVDAT 1 08-JUN-06 2D8R 0 JRNL AUTH K.MIYAMOTO,T.KIGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE THAP DOMAIN OF THE HUMAN THAP JRNL TITL 2 DOMAIN-CONTAINING 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 2D8R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000025128. 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 : 120 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.84MM THAP DOMAIN U-13C,15N; REMARK 210 20MM D-TRIS-HCL(PH7.0); 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; REMARK 210 0.05MM ZNCL2; 1.0MM IDA; 90% H2O, REMARK 210 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 0.9321, 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 SER A 2 -62.12 -109.56 REMARK 500 1 SER A 5 139.01 65.56 REMARK 500 1 SER A 6 43.01 73.36 REMARK 500 1 PRO A 9 77.71 -69.83 REMARK 500 1 ALA A 14 157.14 -40.98 REMARK 500 1 THR A 20 -56.55 -168.22 REMARK 500 1 TYR A 21 87.95 176.90 REMARK 500 1 ASN A 22 -87.49 -88.72 REMARK 500 1 LYS A 23 -62.16 -171.50 REMARK 500 1 ARG A 31 -174.55 -54.26 REMARK 500 1 ARG A 47 74.12 52.06 REMARK 500 1 ARG A 48 73.23 -151.00 REMARK 500 1 LYS A 49 -170.49 48.76 REMARK 500 1 LYS A 55 144.77 -172.97 REMARK 500 1 ALA A 66 -48.61 75.69 REMARK 500 1 ASP A 70 59.03 -103.24 REMARK 500 1 THR A 72 -27.15 -38.21 REMARK 500 1 GLN A 74 168.42 81.47 REMARK 500 1 THR A 75 -154.11 46.46 REMARK 500 1 ARG A 76 83.79 -168.79 REMARK 500 1 PRO A 84 92.20 -69.79 REMARK 500 1 PHE A 87 -24.84 167.36 REMARK 500 1 CYS A 90 81.15 34.78 REMARK 500 1 THR A 91 -72.40 -35.46 REMARK 500 1 HIS A 92 -68.48 -131.00 REMARK 500 1 ILE A 93 -43.12 -138.38 REMARK 500 1 SER A 94 -33.14 -172.50 REMARK 500 1 PRO A 96 -164.41 -69.79 REMARK 500 1 SER A 98 -94.24 45.02 REMARK 500 2 CYS A 17 -68.59 -155.10 REMARK 500 2 THR A 20 -75.10 -139.50 REMARK 500 2 ASN A 22 25.22 -145.59 REMARK 500 2 LYS A 23 -82.12 61.57 REMARK 500 2 ILE A 25 134.52 -36.80 REMARK 500 2 ARG A 31 176.71 -53.88 REMARK 500 2 TRP A 42 -26.17 -38.80 REMARK 500 2 ARG A 47 78.43 42.52 REMARK 500 2 LYS A 49 128.36 61.13 REMARK 500 2 ASN A 50 56.21 36.93 REMARK 500 2 LYS A 55 -88.13 -169.24 REMARK 500 2 THR A 57 122.59 -37.59 REMARK 500 2 ALA A 66 -9.46 77.48 REMARK 500 2 LEU A 71 -94.05 -124.35 REMARK 500 2 THR A 72 32.37 39.68 REMARK 500 2 THR A 75 -165.56 -65.52 REMARK 500 2 PRO A 84 77.01 -69.81 REMARK 500 2 THR A 85 42.70 -88.13 REMARK 500 2 ILE A 86 -73.27 -139.69 REMARK 500 2 PHE A 87 70.46 45.93 REMARK 500 2 ASP A 88 124.28 64.18 REMARK 500 REMARK 500 THIS ENTRY HAS 488 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 401 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 12 SG REMARK 620 2 CYS A 17 SG 112.2 REMARK 620 3 CYS A 60 SG 102.5 107.8 REMARK 620 4 HIS A 63 NE2 114.1 105.8 114.4 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002006992.1 RELATED DB: TARGETDB DBREF 2D8R A 8 93 UNP Q9H0W7 THAP2_HUMAN 1 86 SEQADV 2D8R GLY A 1 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R SER A 2 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R SER A 3 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R GLY A 4 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R SER A 5 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R SER A 6 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R GLY A 7 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R SER A 94 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R GLY A 95 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R PRO A 96 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R SER A 97 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R SER A 98 UNP Q9H0W7 CLONING ARTIFACT SEQADV 2D8R GLY A 99 UNP Q9H0W7 CLONING ARTIFACT SEQRES 1 A 99 GLY SER SER GLY SER SER GLY MET PRO THR ASN CYS ALA SEQRES 2 A 99 ALA ALA GLY CYS ALA THR THR TYR ASN LYS HIS ILE ASN SEQRES 3 A 99 ILE SER PHE HIS ARG PHE PRO LEU ASP PRO LYS ARG ARG SEQRES 4 A 99 LYS GLU TRP VAL ARG LEU VAL ARG ARG LYS ASN PHE VAL SEQRES 5 A 99 PRO GLY LYS HIS THR PHE LEU CYS SER LYS HIS PHE GLU SEQRES 6 A 99 ALA SER CYS PHE ASP LEU THR GLY GLN THR ARG ARG LEU SEQRES 7 A 99 LYS MET ASP ALA VAL PRO THR ILE PHE ASP PHE CYS THR SEQRES 8 A 99 HIS ILE SER GLY PRO SER SER GLY HET ZN A 401 1 HETNAM ZN ZINC ION FORMUL 2 ZN ZN 2+ HELIX 1 1 ASP A 35 VAL A 46 1 12 SHEET 1 A 2 HIS A 30 ARG A 31 0 SHEET 2 A 2 PHE A 58 LEU A 59 -1 O LEU A 59 N HIS A 30 LINK SG CYS A 12 ZN ZN A 401 1555 1555 2.34 LINK SG CYS A 17 ZN ZN A 401 1555 1555 2.34 LINK SG CYS A 60 ZN ZN A 401 1555 1555 2.34 LINK NE2 HIS A 63 ZN ZN A 401 1555 1555 2.33 SITE 1 AC1 4 CYS A 12 CYS A 17 CYS A 60 HIS A 63 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