Header list of 1zr9.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 19-MAY-05 1ZR9 TITLE SOLUTION STRUCTURE OF A HUMAN C2H2-TYPE ZINC FINGER PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ZINC FINGER PROTEIN 593; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ZINC FINGER PROTEIN T86, ZINC FINGER PROTEIN LOC51042; 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: ZNF593; SOURCE 6 EXPRESSION_SYSTEM: CELL-FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEU(N)HIS6; SOURCE 9 OTHER_DETAILS: WHEAT GERM CELL-FREE, IN VITRO EXPRESSION KEYWDS ZINC FINGER, DNA BINDING, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE KEYWDS 2 INITIATIVE, CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, CESG, KEYWDS 3 TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.L.LYTLE,F.C.PETERSON,B.F.VOLKMAN,CENTER FOR EUKARYOTIC STRUCTURAL AUTHOR 2 GENOMICS (CESG) REVDAT 5 02-MAR-22 1ZR9 1 REMARK SEQADV REVDAT 4 30-DEC-08 1ZR9 1 JRNL VERSN REVDAT 3 29-APR-08 1ZR9 1 SOURCE REVDAT 2 12-FEB-08 1ZR9 1 REMARK REVDAT 1 07-JUN-05 1ZR9 0 JRNL AUTH P.L.HAYES,B.L.LYTLE,B.F.VOLKMAN,F.C.PETERSON JRNL TITL THE SOLUTION STRUCTURE OF ZNF593 FROM HOMO SAPIENS REVEALS A JRNL TITL 2 ZINC FINGER IN A PREDOMINANTLY UNSTRUCTURED PROTEIN. JRNL REF PROTEIN SCI. V. 17 571 2008 JRNL REFN ISSN 0961-8368 JRNL PMID 18287285 JRNL DOI 10.1110/PS.073290408 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, XPLOR-NIH 2.0.6 REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), G. MARIUS CLORE (XPLOR REMARK 3 -NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 1-27 AND 95-116 OF THE REMARK 3 CONSTRUCT WERE DISORDERED AND WERE EXCLUDED FROM THE MODEL. REMARK 3 AFTER INITIAL CALCULATIONS WITHOUT ZINC, THE ZINC ATOM WAS REMARK 3 CONSTRAINED IN A TETRAHEDRAL GEOMETRY USING DISTANCE RESTRAINTS REMARK 3 TO EACH COORDINATING CYS SG AND HIS NE2 OF 2.3 A AND 2.0 A, REMARK 3 RESPECTIVELY. REMARK 4 REMARK 4 1ZR9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000033026. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 100 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.6 MM ZNF593 U-15N,13C, 10 MM REMARK 210 BIS TRIS, 100 MM NACL, 2 MM DTT, REMARK 210 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D 13C- REMARK 210 SEPARATED NOESY (AROMATIC) REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2004, SPSCAN 1.1.0, REMARK 210 XEASY 1.3, GARANT 2.1, CYANA REMARK 210 1.0.6 REMARK 210 METHOD USED : AUTOMATED METHODS WERE USED FOR REMARK 210 BACKBONE CHEMICAL SHIFT REMARK 210 ASSIGNMENT AND ITERATIVE NOE REMARK 210 REFINEMENT. FINAL STRUCTURES REMARK 210 WERE OBTAINED BY MOLECULAR REMARK 210 DYNAMICS IN EXPLICIT SOLVENT. REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: ALL TRIPLE-RESONANCE AND NOESY SPECTRA WERE ACQUIRED USING REMARK 210 A CYROGENIC PROBE 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 GLY A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 HIS A -1 REMARK 465 LEU A 0 REMARK 465 GLU A 1 REMARK 465 LYS A 2 REMARK 465 ALA A 3 REMARK 465 LYS A 4 REMARK 465 ARG A 5 REMARK 465 ARG A 6 REMARK 465 ARG A 7 REMARK 465 PRO A 8 REMARK 465 ASP A 9 REMARK 465 LEU A 10 REMARK 465 ASP A 11 REMARK 465 GLU A 12 REMARK 465 ILE A 13 REMARK 465 HIS A 14 REMARK 465 ARG A 15 REMARK 465 GLU A 16 REMARK 465 LEU A 17 REMARK 465 ARG A 18 REMARK 465 PRO A 19 REMARK 465 GLN A 20 REMARK 465 GLY A 21 REMARK 465 SER A 22 REMARK 465 ALA A 23 REMARK 465 ARG A 24 REMARK 465 PRO A 25 REMARK 465 GLN A 26 REMARK 465 PRO A 27 REMARK 465 PRO A 95 REMARK 465 PRO A 96 REMARK 465 ARG A 97 REMARK 465 ARG A 98 REMARK 465 LEU A 99 REMARK 465 ALA A 100 REMARK 465 VAL A 101 REMARK 465 PRO A 102 REMARK 465 THR A 103 REMARK 465 GLU A 104 REMARK 465 VAL A 105 REMARK 465 SER A 106 REMARK 465 THR A 107 REMARK 465 GLU A 108 REMARK 465 VAL A 109 REMARK 465 PRO A 110 REMARK 465 GLU A 111 REMARK 465 MET A 112 REMARK 465 ASP A 113 REMARK 465 THR A 114 REMARK 465 SER A 115 REMARK 465 THR A 116 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 ASN A 30 77.86 53.29 REMARK 500 1 ALA A 31 90.07 -167.54 REMARK 500 1 TYR A 79 90.87 69.77 REMARK 500 1 SER A 80 -165.89 -103.37 REMARK 500 1 GLU A 82 -0.24 80.20 REMARK 500 1 GLU A 83 -60.12 -128.83 REMARK 500 1 GLU A 85 93.41 -172.80 REMARK 500 1 MET A 90 92.19 61.58 REMARK 500 2 PRO A 29 -177.17 -63.35 REMARK 500 2 ALA A 31 90.17 65.66 REMARK 500 2 SER A 75 86.83 71.78 REMARK 500 2 TYR A 79 169.15 67.36 REMARK 500 2 GLU A 83 -41.63 172.54 REMARK 500 2 GLU A 85 -67.62 -94.51 REMARK 500 2 ARG A 86 69.57 62.88 REMARK 500 2 ALA A 87 -85.63 -169.25 REMARK 500 2 ALA A 88 97.19 168.34 REMARK 500 2 SER A 92 129.83 68.44 REMARK 500 3 ALA A 31 79.51 75.83 REMARK 500 3 TYR A 79 115.64 64.83 REMARK 500 3 GLU A 82 -54.53 -163.20 REMARK 500 3 GLU A 85 65.61 -117.74 REMARK 500 3 ARG A 86 -24.77 70.33 REMARK 500 3 ALA A 87 87.34 71.69 REMARK 500 4 PRO A 38 106.09 -59.63 REMARK 500 4 SER A 75 -60.58 87.68 REMARK 500 4 VAL A 76 -68.11 -155.96 REMARK 500 4 GLU A 77 151.02 164.68 REMARK 500 4 PRO A 78 106.55 -46.74 REMARK 500 4 ARG A 86 98.33 70.28 REMARK 500 4 MET A 90 83.87 65.00 REMARK 500 4 TYR A 93 160.16 64.28 REMARK 500 5 ASN A 30 82.47 57.64 REMARK 500 5 ALA A 31 48.44 -146.41 REMARK 500 5 PHE A 33 167.28 177.89 REMARK 500 5 SER A 75 91.68 73.15 REMARK 500 5 VAL A 76 -67.50 -91.59 REMARK 500 5 GLU A 77 -60.99 -173.17 REMARK 500 5 GLU A 82 -38.91 78.44 REMARK 500 5 GLU A 85 -71.95 -97.80 REMARK 500 5 ALA A 88 85.13 -167.75 REMARK 500 6 ALA A 49 18.53 59.79 REMARK 500 6 SER A 80 -61.25 72.36 REMARK 500 6 GLU A 83 -50.55 -159.53 REMARK 500 6 ALA A 84 -48.93 -139.09 REMARK 500 6 GLU A 85 81.37 64.35 REMARK 500 6 ALA A 87 -57.61 -133.01 REMARK 500 6 ALA A 88 -35.73 -145.16 REMARK 500 7 PRO A 29 -163.96 -59.33 REMARK 500 7 ALA A 31 40.83 70.75 REMARK 500 REMARK 500 THIS ENTRY HAS 143 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 HIS A 67 0.11 SIDE CHAIN REMARK 500 2 HIS A 67 0.10 SIDE CHAIN REMARK 500 3 HIS A 67 0.10 SIDE CHAIN REMARK 500 5 HIS A 67 0.10 SIDE CHAIN REMARK 500 6 HIS A 67 0.11 SIDE CHAIN REMARK 500 7 HIS A 67 0.11 SIDE CHAIN REMARK 500 8 HIS A 67 0.12 SIDE CHAIN REMARK 500 9 HIS A 67 0.10 SIDE CHAIN REMARK 500 10 HIS A 67 0.10 SIDE CHAIN REMARK 500 11 HIS A 67 0.11 SIDE CHAIN REMARK 500 12 HIS A 67 0.10 SIDE CHAIN REMARK 500 13 HIS A 67 0.09 SIDE CHAIN REMARK 500 14 HIS A 67 0.11 SIDE CHAIN REMARK 500 15 HIS A 67 0.13 SIDE CHAIN REMARK 500 16 HIS A 67 0.10 SIDE CHAIN REMARK 500 17 HIS A 67 0.10 SIDE CHAIN REMARK 500 18 HIS A 67 0.10 SIDE CHAIN REMARK 500 19 HIS A 67 0.10 SIDE CHAIN REMARK 500 20 HIS A 67 0.11 SIDE CHAIN 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 117 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 45 SG REMARK 620 2 CYS A 48 SG 112.7 REMARK 620 3 HIS A 61 NE2 111.7 106.6 REMARK 620 4 HIS A 67 NE2 117.3 100.5 107.1 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 117 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GO.33810 RELATED DB: TARGETDB DBREF 1ZR9 A 2 116 UNP O00488 ZN593_HUMAN 2 116 SEQADV 1ZR9 GLY A -7 UNP O00488 CLONING ARTIFACT SEQADV 1ZR9 HIS A -6 UNP O00488 EXPRESSION TAG SEQADV 1ZR9 HIS A -5 UNP O00488 EXPRESSION TAG SEQADV 1ZR9 HIS A -4 UNP O00488 EXPRESSION TAG SEQADV 1ZR9 HIS A -3 UNP O00488 EXPRESSION TAG SEQADV 1ZR9 HIS A -2 UNP O00488 EXPRESSION TAG SEQADV 1ZR9 HIS A -1 UNP O00488 EXPRESSION TAG SEQADV 1ZR9 LEU A 0 UNP O00488 CLONING ARTIFACT SEQADV 1ZR9 GLU A 1 UNP O00488 CLONING ARTIFACT SEQRES 1 A 124 GLY HIS HIS HIS HIS HIS HIS LEU GLU LYS ALA LYS ARG SEQRES 2 A 124 ARG ARG PRO ASP LEU ASP GLU ILE HIS ARG GLU LEU ARG SEQRES 3 A 124 PRO GLN GLY SER ALA ARG PRO GLN PRO ASP PRO ASN ALA SEQRES 4 A 124 GLU PHE ASP PRO ASP LEU PRO GLY GLY GLY LEU HIS ARG SEQRES 5 A 124 CYS LEU ALA CYS ALA ARG TYR PHE ILE ASP SER THR ASN SEQRES 6 A 124 LEU LYS THR HIS PHE ARG SER LYS ASP HIS LYS LYS ARG SEQRES 7 A 124 LEU LYS GLN LEU SER VAL GLU PRO TYR SER GLN GLU GLU SEQRES 8 A 124 ALA GLU ARG ALA ALA GLY MET GLY SER TYR VAL PRO PRO SEQRES 9 A 124 ARG ARG LEU ALA VAL PRO THR GLU VAL SER THR GLU VAL SEQRES 10 A 124 PRO GLU MET ASP THR SER THR HET ZN A 117 1 HETNAM ZN ZINC ION FORMUL 2 ZN ZN 2+ HELIX 1 1 LEU A 37 LEU A 42 5 6 HELIX 2 2 ASP A 54 PHE A 62 1 9 HELIX 3 3 SER A 64 SER A 75 1 12 LINK SG CYS A 45 ZN ZN A 117 1555 1555 2.31 LINK SG CYS A 48 ZN ZN A 117 1555 1555 2.28 LINK NE2 HIS A 61 ZN ZN A 117 1555 1555 1.95 LINK NE2 HIS A 67 ZN ZN A 117 1555 1555 1.96 SITE 1 AC1 4 CYS A 45 CYS A 48 HIS A 61 HIS A 67 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