Header list of 1x6e.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 17-MAY-05 1X6E
TITLE SOLUTION STRUCTURES OF THE C2H2 TYPE ZINC FINGER DOMAIN OF HUMAN ZINC
TITLE 2 FINGER PROTEIN 24
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER PROTEIN 24;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C2H2 TYPE ZINC FINGER DOMAIN;
COMPND 5 SYNONYM: ZINC FINGER PROTEIN 191, ZINC FINGER PROTEIN KOX17, RETINOIC
COMPND 6 ACID SUPPRESSION PROTEIN A, RSG-A, ZINC FINGER AND SCAN DOMAIN
COMPND 7 CONTAINING PROTEIN 3;
COMPND 8 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: ZNF24;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040712-01;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ZNF24, KOX17, ZNF191, ZSCAN3, ZINC FINGER, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, DNA
KEYWDS 4 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SATO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X6E 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1X6E 1 VERSN
REVDAT 1 17-NOV-05 1X6E 0
JRNL AUTH M.SATO,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURES OF THE C2H2 TYPE ZINC FINGER DOMAIN OF
JRNL TITL 2 HUMAN ZINC FINGER PROTEIN 24
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 1X6E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024436.
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 : 1MM C2H2 TYPE ZINC FINGER DOMAIN
REMARK 210 U-15N, 13C; 20MM D-TRIS HCL;
REMARK 210 100MM NACL; 5MM D-DTT; 0.02%
REMARK 210 NAN3; 0.01MM 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 : 900 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 0.9295, 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 CYS A 20 -45.94 -133.06
REMARK 500 1 GLU A 40 50.01 -97.80
REMARK 500 1 LYS A 41 67.42 -110.11
REMARK 500 1 LYS A 50 137.35 -171.22
REMARK 500 2 ILE A 8 38.15 34.37
REMARK 500 2 CYS A 20 -45.13 -132.54
REMARK 500 2 LYS A 41 69.82 -107.87
REMARK 500 2 SER A 67 145.18 -35.40
REMARK 500 3 CYS A 20 -47.84 -133.10
REMARK 500 3 CYS A 48 -43.76 -133.08
REMARK 500 3 LYS A 50 142.13 -172.10
REMARK 500 3 SER A 53 -31.76 -38.90
REMARK 500 3 THR A 66 49.49 -89.35
REMARK 500 3 PRO A 69 5.38 -69.78
REMARK 500 3 SER A 70 116.15 -29.65
REMARK 500 4 LYS A 41 54.97 30.96
REMARK 500 4 THR A 66 179.84 -51.74
REMARK 500 4 SER A 70 134.33 -37.96
REMARK 500 5 ILE A 8 146.62 -174.41
REMARK 500 5 CYS A 20 -40.96 -130.39
REMARK 500 5 LYS A 22 125.12 -33.31
REMARK 500 5 GLU A 40 39.15 -93.92
REMARK 500 5 PRO A 69 92.55 -69.79
REMARK 500 6 SER A 2 42.83 70.62
REMARK 500 6 HIS A 9 -64.66 -93.56
REMARK 500 6 SER A 10 41.88 36.19
REMARK 500 6 LYS A 13 99.79 -37.90
REMARK 500 6 LYS A 41 69.59 -108.20
REMARK 500 6 SER A 67 108.33 -168.79
REMARK 500 6 PRO A 69 91.53 -69.73
REMARK 500 7 GLU A 40 30.19 -84.69
REMARK 500 7 LYS A 41 69.39 -114.79
REMARK 500 8 SER A 5 116.49 -167.04
REMARK 500 8 LYS A 13 100.14 -38.56
REMARK 500 8 THR A 38 114.35 -33.80
REMARK 500 8 PRO A 69 -174.61 -69.77
REMARK 500 9 LYS A 50 137.97 -173.09
REMARK 500 10 ILE A 8 47.49 -80.40
REMARK 500 10 HIS A 9 74.83 -102.36
REMARK 500 10 GLU A 12 -54.31 -121.93
REMARK 500 10 LYS A 13 106.25 -44.90
REMARK 500 10 CYS A 20 -38.58 -134.39
REMARK 500 10 LYS A 22 128.02 -32.22
REMARK 500 10 LYS A 41 68.56 -113.15
REMARK 500 10 CYS A 48 -41.47 -131.42
REMARK 500 10 SER A 71 92.04 -64.22
REMARK 500 11 LYS A 13 98.95 -36.63
REMARK 500 11 PRO A 14 1.33 -69.79
REMARK 500 11 THR A 38 125.37 -38.69
REMARK 500 11 LYS A 41 69.90 -115.88
REMARK 500
REMARK 500 THIS ENTRY HAS 96 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 17 SG
REMARK 620 2 CYS A 20 SG 115.5
REMARK 620 3 HIS A 33 NE2 115.5 85.2
REMARK 620 4 HIS A 37 NE2 115.4 109.8 111.7
REMARK 620 N 1 2 3
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 45 SG
REMARK 620 2 CYS A 48 SG 115.5
REMARK 620 3 HIS A 61 NE2 116.4 86.0
REMARK 620 4 HIS A 65 NE2 116.8 117.7 98.9
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 800
REMARK 800 SITE_IDENTIFIER: AC2
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: HSS001000602.1 RELATED DB: TARGETDB
DBREF 1X6E A 8 66 UNP P17028 ZNF24_HUMAN 272 330
SEQADV 1X6E GLY A 1 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E SER A 2 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E SER A 3 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E GLY A 4 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E SER A 5 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E SER A 6 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E GLY A 7 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E SER A 67 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E GLY A 68 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E PRO A 69 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E SER A 70 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E SER A 71 UNP P17028 CLONING ARTIFACT
SEQADV 1X6E GLY A 72 UNP P17028 CLONING ARTIFACT
SEQRES 1 A 72 GLY SER SER GLY SER SER GLY ILE HIS SER GLY GLU LYS
SEQRES 2 A 72 PRO TYR GLY CYS VAL GLU CYS GLY LYS ALA PHE SER ARG
SEQRES 3 A 72 SER SER ILE LEU VAL GLN HIS GLN ARG VAL HIS THR GLY
SEQRES 4 A 72 GLU LYS PRO TYR LYS CYS LEU GLU CYS GLY LYS ALA PHE
SEQRES 5 A 72 SER GLN ASN SER GLY LEU ILE ASN HIS GLN ARG ILE HIS
SEQRES 6 A 72 THR SER GLY PRO SER SER GLY
HET ZN A 201 1
HET ZN A 401 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 ARG A 26 VAL A 36 1 11
HELIX 2 2 HIS A 37 GLY A 39 5 3
HELIX 3 3 GLN A 54 SER A 67 1 14
SHEET 1 A 2 TYR A 15 GLY A 16 0
SHEET 2 A 2 ALA A 23 PHE A 24 -1 O PHE A 24 N TYR A 15
SHEET 1 B 2 TYR A 43 LYS A 44 0
SHEET 2 B 2 ALA A 51 PHE A 52 -1 O PHE A 52 N TYR A 43
LINK SG CYS A 17 ZN ZN A 201 1555 1555 2.37
LINK SG CYS A 20 ZN ZN A 201 1555 1555 2.36
LINK NE2 HIS A 33 ZN ZN A 201 1555 1555 2.36
LINK NE2 HIS A 37 ZN ZN A 201 1555 1555 2.36
LINK SG CYS A 45 ZN ZN A 401 1555 1555 2.35
LINK SG CYS A 48 ZN ZN A 401 1555 1555 2.33
LINK NE2 HIS A 61 ZN ZN A 401 1555 1555 2.36
LINK NE2 HIS A 65 ZN ZN A 401 1555 1555 2.34
SITE 1 AC1 4 CYS A 17 CYS A 20 HIS A 33 HIS A 37
SITE 1 AC2 4 CYS A 45 CYS A 48 HIS A 61 HIS A 65
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