Header list of 2d9m.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 12-DEC-05 2D9M TITLE SOLUTION STRUCTURE OF CCCH TYPE ZINC-FINGER DOMAIN 3 IN ZINC FINGER TITLE 2 CCCH-TYPE DOMAIN CONTAINING 7A COMPND MOL_ID: 1; COMPND 2 MOLECULE: ZINC FINGER CCCH-TYPE DOMAIN CONTAINING PROTEIN 7A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CCCH-TYPE ZINC FINGER 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: ZC3H7A; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050302-09; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS CCCH ZINC-FINGER, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.ABE,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 2D9M 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 2D9M 1 VERSN REVDAT 1 12-JUN-06 2D9M 0 JRNL AUTH C.ABE,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF CCCH TYPE ZINC-FINGER DOMAIN 3 IN ZINC JRNL TITL 2 FINGER CCCH-TYPE DOMAIN CONTAINING 7A 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 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT,P (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2D9M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000025157. 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 : 100MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 20MM D-TRIS-HCL(PH7.0), 100MM REMARK 210 NACL, 1MM D-DTT, 0.02% NAN3, REMARK 210 50UM ZNCL2+1MM IDA, 90% H2O, 10% REMARK 210 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 0.93191, CYANA 2.0 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 PRO A 900 96.47 -69.77 REMARK 500 1 THR A 901 -33.03 -34.36 REMARK 500 1 GLU A 917 -71.83 -56.11 REMARK 500 1 SER A 920 31.69 -87.04 REMARK 500 1 ALA A 947 100.05 -50.44 REMARK 500 2 SER A 890 30.40 -96.57 REMARK 500 2 GLN A 892 79.80 -105.23 REMARK 500 2 CYS A 894 40.35 -100.12 REMARK 500 2 TRP A 895 98.54 -52.28 REMARK 500 2 ARG A 898 161.17 -47.58 REMARK 500 2 PRO A 900 93.22 -69.76 REMARK 500 2 THR A 901 -36.49 -33.04 REMARK 500 2 PHE A 904 54.39 -97.95 REMARK 500 2 GLU A 917 -72.34 -63.25 REMARK 500 2 HIS A 925 73.28 -114.20 REMARK 500 2 ASN A 945 45.21 -80.77 REMARK 500 2 SER A 948 -39.18 -34.73 REMARK 500 2 SER A 951 40.77 36.19 REMARK 500 2 SER A 952 129.55 -34.82 REMARK 500 3 CYS A 894 43.08 -81.66 REMARK 500 3 TRP A 895 100.85 -48.85 REMARK 500 3 PRO A 900 99.06 -69.73 REMARK 500 3 THR A 901 -27.98 -37.30 REMARK 500 3 PHE A 904 55.02 -107.00 REMARK 500 4 SER A 889 142.29 -36.21 REMARK 500 4 TYR A 893 107.04 -168.07 REMARK 500 4 CYS A 894 77.42 -115.03 REMARK 500 4 ARG A 898 99.48 -62.73 REMARK 500 4 PHE A 899 139.95 -34.04 REMARK 500 4 PRO A 900 93.85 -69.73 REMARK 500 4 THR A 901 -37.09 -32.66 REMARK 500 4 PHE A 904 57.00 -119.31 REMARK 500 4 GLU A 917 -70.77 -54.82 REMARK 500 4 HIS A 925 73.38 -115.83 REMARK 500 4 ARG A 936 -70.25 -33.99 REMARK 500 4 MET A 942 -38.63 -35.27 REMARK 500 4 PRO A 950 5.44 -69.79 REMARK 500 5 SER A 886 91.91 -58.32 REMARK 500 5 TYR A 893 94.19 -52.56 REMARK 500 5 CYS A 894 40.57 -107.28 REMARK 500 5 TRP A 895 93.73 -53.24 REMARK 500 5 ARG A 898 96.46 -61.91 REMARK 500 5 PHE A 899 139.75 -32.13 REMARK 500 5 THR A 901 -31.10 -38.12 REMARK 500 5 GLU A 917 -74.81 -59.54 REMARK 500 5 LYS A 946 38.43 -90.46 REMARK 500 6 TRP A 895 76.20 -67.27 REMARK 500 6 PRO A 900 94.62 -69.71 REMARK 500 6 THR A 901 -33.10 -34.00 REMARK 500 6 MET A 942 -37.53 -35.74 REMARK 500 REMARK 500 THIS ENTRY HAS 152 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 A1085 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 907 SG REMARK 620 2 CYS A 915 SG 113.4 REMARK 620 3 CYS A 921 SG 118.5 114.3 REMARK 620 4 HIS A 925 NE2 114.0 92.1 100.7 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 1085 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002012167.1 RELATED DB: TARGETDB DBREF 2D9M A 892 947 UNP Q8IWR0 Z3H7A_HUMAN 892 947 SEQADV 2D9M GLY A 885 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M SER A 886 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M SER A 887 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M GLY A 888 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M SER A 889 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M SER A 890 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M GLY A 891 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M SER A 948 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M GLY A 949 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M PRO A 950 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M SER A 951 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M SER A 952 UNP Q8IWR0 CLONING ARTIFACT SEQADV 2D9M GLY A 953 UNP Q8IWR0 CLONING ARTIFACT SEQRES 1 A 69 GLY SER SER GLY SER SER GLY GLN TYR CYS TRP GLN HIS SEQRES 2 A 69 ARG PHE PRO THR GLY TYR PHE SER ILE CYS ASP ARG TYR SEQRES 3 A 69 MET ASN GLY THR CYS PRO GLU GLY ASN SER CYS LYS PHE SEQRES 4 A 69 ALA HIS GLY ASN ALA GLU LEU HIS GLU TRP GLU GLU ARG SEQRES 5 A 69 ARG ASP ALA LEU LYS MET LYS LEU ASN LYS ALA SER GLY SEQRES 6 A 69 PRO SER SER GLY HET ZN A1085 1 HETNAM ZN ZINC ION FORMUL 2 ZN ZN 2+ HELIX 1 1 CYS A 907 GLY A 913 1 7 HELIX 2 2 GLY A 926 LYS A 941 1 16 LINK SG CYS A 907 ZN ZN A1085 1555 1555 2.33 LINK SG CYS A 915 ZN ZN A1085 1555 1555 2.33 LINK SG CYS A 921 ZN ZN A1085 1555 1555 2.33 LINK NE2 HIS A 925 ZN ZN A1085 1555 1555 2.34 SITE 1 AC1 4 CYS A 907 CYS A 915 CYS A 921 HIS A 925 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