Header list of 1wir.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 28-MAY-04 1WIR TITLE SOLUTION STRUCTURE OF THE C2H2 ZINC FINGER DOMAIN OF THE PROTEIN TITLE 2 ARGININE N-METHYLTRANSFERASE 3 FROM MUS MUSCULUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN ARGININE N-METHYLTRANSFERASE 3; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C2H2 ZINC FINGER DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: RIKEN CDNA 2410018A17; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040126-40; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS C2H2 ZINC FINGER DOMAIN, PROTEIN ARGININE N-METHYLTRANSFERASE 3, KEYWDS 2 PRMT3, STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 3 INITIATIVE, RSGI, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.MIYAMOTO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WIR 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1WIR 1 VERSN REVDAT 1 28-NOV-04 1WIR 0 JRNL AUTH K.MIYAMOTO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE C2H2 ZINC FINGER DOMAIN OF THE JRNL TITL 2 PROTEIN ARGININE N-METHYLTRANSFERASE 3 FROM MUS MUSCULUS 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 1WIR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023623. 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 : 1.14MM C2H2 ZINC FINGER DOMAIN U REMARK 210 -13C,15N; 20MM D-TRIS-HCL(PH7.0); REMARK 210 100MM NACL; 1MM D-DTT;0.02% REMARK 210 NAN3;0.1MM ZNCL2; 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N 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 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.8996, 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 : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY, TARGET REMARK 210 FUNCTION 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 ASP A 22 45.84 -106.76 REMARK 500 1 GLN A 40 41.21 36.61 REMARK 500 1 ASN A 68 47.76 70.03 REMARK 500 1 PRO A 69 -165.00 -69.77 REMARK 500 1 PRO A 82 0.48 -69.73 REMARK 500 1 GLU A 84 40.32 -82.87 REMARK 500 1 LEU A 89 -38.27 -39.40 REMARK 500 1 PRO A 113 8.29 -69.77 REMARK 500 1 PHE A 114 118.50 -33.49 REMARK 500 1 SER A 115 47.52 36.42 REMARK 500 2 SER A 5 151.23 -35.30 REMARK 500 2 SER A 6 -61.00 -124.92 REMARK 500 2 ASP A 22 42.66 -106.99 REMARK 500 2 GLU A 38 -64.95 -90.64 REMARK 500 2 GLN A 40 27.82 42.39 REMARK 500 2 PRO A 69 -170.10 -69.76 REMARK 500 2 SER A 76 79.52 -104.12 REMARK 500 2 PRO A 82 1.04 -69.72 REMARK 500 2 ASP A 95 54.70 33.66 REMARK 500 2 ASP A 96 95.76 -69.62 REMARK 500 2 PRO A 109 -170.15 -69.83 REMARK 500 2 VAL A 110 79.18 -119.71 REMARK 500 2 SER A 111 107.21 -172.05 REMARK 500 2 THR A 112 133.07 -170.85 REMARK 500 2 PRO A 113 2.02 -69.73 REMARK 500 2 PHE A 114 145.93 -32.31 REMARK 500 3 PRO A 9 4.11 -69.75 REMARK 500 3 GLN A 14 106.27 -168.12 REMARK 500 3 ASP A 22 48.94 -106.22 REMARK 500 3 GLU A 38 -65.76 -90.36 REMARK 500 3 GLN A 40 38.13 34.06 REMARK 500 3 GLU A 53 -174.83 -61.94 REMARK 500 3 PRO A 69 -166.29 -69.81 REMARK 500 3 SER A 76 79.70 -100.68 REMARK 500 3 GLU A 84 33.95 -88.29 REMARK 500 3 PRO A 91 99.76 -69.75 REMARK 500 3 PRO A 109 81.74 -69.76 REMARK 500 3 PRO A 113 0.43 -69.76 REMARK 500 3 PHE A 114 84.34 -65.24 REMARK 500 3 PRO A 118 95.24 -69.73 REMARK 500 4 SER A 6 -54.52 -121.91 REMARK 500 4 ARG A 13 42.28 -81.80 REMARK 500 4 ASP A 22 41.39 -107.81 REMARK 500 4 GLU A 38 -63.33 -95.78 REMARK 500 4 GLN A 40 29.97 38.68 REMARK 500 4 PRO A 69 -171.20 -69.78 REMARK 500 4 MET A 74 -18.98 -49.03 REMARK 500 4 SER A 76 79.67 -103.45 REMARK 500 4 GLU A 84 47.89 -76.12 REMARK 500 4 LEU A 89 -33.48 -36.59 REMARK 500 REMARK 500 THIS ENTRY HAS 239 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 201 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 18 SG REMARK 620 2 CYS A 21 SG 98.3 REMARK 620 3 HIS A 34 NE2 118.3 103.5 REMARK 620 4 HIS A 39 NE2 112.1 115.4 108.8 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 201 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007007317.1 RELATED DB: TARGETDB DBREF 1WIR A 8 115 UNP Q922H1 ANM3_MOUSE 38 145 SEQADV 1WIR GLY A 1 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR SER A 2 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR SER A 3 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR GLY A 4 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR SER A 5 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR SER A 6 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR GLY A 7 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR SER A 116 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR GLY A 117 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR PRO A 118 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR SER A 119 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR SER A 120 UNP Q922H1 CLONING ARTIFACT SEQADV 1WIR GLY A 121 UNP Q922H1 CLONING ARTIFACT SEQRES 1 A 121 GLY SER SER GLY SER SER GLY GLU PRO ALA HIS GLY ARG SEQRES 2 A 121 GLN HIS THR PRO CYS LEU PHE CYS ASP ARG LEU PHE ALA SEQRES 3 A 121 SER ALA GLU GLU THR PHE SER HIS CYS LYS LEU GLU HIS SEQRES 4 A 121 GLN PHE ASN ILE ASP SER MET VAL HIS LYS HIS GLY LEU SEQRES 5 A 121 GLU PHE TYR GLY TYR ILE LYS LEU ILE ASN PHE ILE ARG SEQRES 6 A 121 LEU LYS ASN PRO THR VAL GLU TYR MET ASN SER ILE TYR SEQRES 7 A 121 ASN PRO VAL PRO TRP GLU LYS ASP GLU TYR LEU LYS PRO SEQRES 8 A 121 VAL LEU GLU ASP ASP LEU LEU LEU GLN PHE ASP VAL GLU SEQRES 9 A 121 ASP LEU TYR GLU PRO VAL SER THR PRO PHE SER SER GLY SEQRES 10 A 121 PRO SER SER GLY HET ZN A 201 1 HETNAM ZN ZINC ION FORMUL 2 ZN ZN 2+ HELIX 1 1 ALA A 28 LEU A 37 1 10 HELIX 2 2 ILE A 43 LYS A 49 1 7 HELIX 3 3 PHE A 54 LEU A 66 1 13 HELIX 4 4 VAL A 71 ASN A 75 1 5 HELIX 5 5 ASP A 86 LEU A 89 1 4 HELIX 6 6 LEU A 97 GLN A 100 1 4 HELIX 7 7 GLU A 104 LEU A 106 5 3 SHEET 1 A 2 THR A 16 PRO A 17 0 SHEET 2 A 2 LEU A 24 PHE A 25 -1 O PHE A 25 N THR A 16 LINK SG CYS A 18 ZN ZN A 201 1555 1555 2.33 LINK SG CYS A 21 ZN ZN A 201 1555 1555 2.33 LINK NE2 HIS A 34 ZN ZN A 201 1555 1555 2.33 LINK NE2 HIS A 39 ZN ZN A 201 1555 1555 2.33 CISPEP 1 ASN A 79 PRO A 80 1 -0.04 CISPEP 2 ASN A 79 PRO A 80 2 -0.06 CISPEP 3 ASN A 79 PRO A 80 3 -0.06 CISPEP 4 ASN A 79 PRO A 80 4 -0.07 CISPEP 5 ASN A 79 PRO A 80 5 0.00 CISPEP 6 ASN A 79 PRO A 80 6 0.01 CISPEP 7 ASN A 79 PRO A 80 7 -0.03 CISPEP 8 ASN A 79 PRO A 80 8 -0.08 CISPEP 9 ASN A 79 PRO A 80 9 -0.02 CISPEP 10 ASN A 79 PRO A 80 10 -0.12 CISPEP 11 ASN A 79 PRO A 80 11 -0.10 CISPEP 12 ASN A 79 PRO A 80 12 0.01 CISPEP 13 ASN A 79 PRO A 80 13 -0.13 CISPEP 14 ASN A 79 PRO A 80 14 0.01 CISPEP 15 ASN A 79 PRO A 80 15 -0.12 CISPEP 16 ASN A 79 PRO A 80 16 -0.07 CISPEP 17 ASN A 79 PRO A 80 17 -0.11 CISPEP 18 ASN A 79 PRO A 80 18 -0.04 CISPEP 19 ASN A 79 PRO A 80 19 0.03 CISPEP 20 ASN A 79 PRO A 80 20 -0.04 SITE 1 AC1 4 CYS A 18 CYS A 21 HIS A 34 HIS A 39 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 2 2 Bytes