Header list of 1wg2.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 27-MAY-04 1WG2
TITLE SOLUTION STRUCTURE OF ZF-AN1 DOMAIN FROM ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER (AN1-LIKE) FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZF-AN1 DOMAIN;
COMPND 5 SYNONYM: HYPOTHETICAL ZINC-FINGER PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: RIKEN CDNA RAFL09-11-C11;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030421-16;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS ZINC FINGER, AN1, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 2 RSGI, STRUCTURAL GENOMICS, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.SUETAKE,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WG2 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1WG2 1 VERSN
REVDAT 1 27-NOV-04 1WG2 0
JRNL AUTH T.SUETAKE,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF ZF-AN1 DOMAIN FROM ARABIDOPSIS
JRNL TITL 2 THALIANA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.31
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WG2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023541.
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 NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.21MM 13C, 15N-LABELED PROTEIN;
REMARK 210 0.1MM ZNCL2; 20MM D-TRIS-HCL;
REMARK 210 100MM NACL; 1MM D10-DTT;0.02%
REMARK 210 NAN3
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 : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2002045, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.860, CYANA 2.0.31
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 VIOLATION, 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 PRO A 11 -175.83 -69.75
REMARK 500 1 VAL A 12 44.47 -81.21
REMARK 500 1 PRO A 14 -176.10 -69.76
REMARK 500 1 SER A 20 -41.98 -134.29
REMARK 500 1 CYS A 39 30.24 -91.79
REMARK 500 1 HIS A 48 124.93 -172.25
REMARK 500 1 GLU A 49 91.49 -42.53
REMARK 500 1 PHE A 52 138.39 -36.92
REMARK 500 1 LYS A 55 141.19 -34.70
REMARK 500 1 GLU A 56 170.62 -52.28
REMARK 500 1 SER A 59 170.74 -55.36
REMARK 500 2 ARG A 10 151.68 -48.03
REMARK 500 2 PRO A 11 -166.84 -69.78
REMARK 500 2 VAL A 12 33.67 -84.23
REMARK 500 2 SER A 20 -40.09 -134.14
REMARK 500 2 CYS A 39 34.92 -96.72
REMARK 500 2 HIS A 48 134.76 -172.83
REMARK 500 2 GLU A 49 88.65 -47.99
REMARK 500 2 SER A 51 35.90 -92.17
REMARK 500 2 ASP A 53 89.70 -58.62
REMARK 500 2 VAL A 57 99.76 -41.35
REMARK 500 2 SER A 59 105.38 -42.15
REMARK 500 3 SER A 2 89.18 -67.54
REMARK 500 3 SER A 5 46.77 -82.14
REMARK 500 3 PRO A 11 -163.42 -69.80
REMARK 500 3 VAL A 12 46.51 -76.83
REMARK 500 3 ASN A 16 86.22 -53.82
REMARK 500 3 SER A 20 -43.12 -134.77
REMARK 500 3 CYS A 39 34.55 -93.09
REMARK 500 3 HIS A 48 126.44 -171.60
REMARK 500 3 GLU A 49 89.64 -45.41
REMARK 500 3 SER A 51 33.46 -86.59
REMARK 500 3 LYS A 55 108.00 -54.00
REMARK 500 4 ARG A 10 150.50 -40.90
REMARK 500 4 PRO A 11 -163.93 -69.80
REMARK 500 4 VAL A 12 39.12 -82.18
REMARK 500 4 SER A 20 -39.55 -133.62
REMARK 500 4 LYS A 24 109.52 -42.24
REMARK 500 4 CYS A 39 37.24 -98.68
REMARK 500 4 HIS A 48 134.09 -172.28
REMARK 500 4 GLU A 49 87.65 -49.06
REMARK 500 4 SER A 51 33.58 -93.20
REMARK 500 4 ASP A 53 68.94 -104.22
REMARK 500 5 PRO A 8 92.75 -69.76
REMARK 500 5 PRO A 11 -166.23 -69.81
REMARK 500 5 VAL A 12 34.96 -84.17
REMARK 500 5 ASN A 16 84.64 -54.37
REMARK 500 5 ARG A 17 145.28 -171.66
REMARK 500 5 SER A 20 -41.91 -134.14
REMARK 500 5 LYS A 24 119.19 -36.66
REMARK 500
REMARK 500 THIS ENTRY HAS 204 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 200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 18 SG
REMARK 620 2 CYS A 21 SG 93.4
REMARK 620 3 CYS A 39 SG 119.0 117.7
REMARK 620 4 HIS A 42 ND1 86.1 102.6 129.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 32 SG
REMARK 620 2 CYS A 34 SG 90.6
REMARK 620 3 HIS A 48 NE2 122.2 111.0
REMARK 620 4 CYS A 50 SG 101.6 117.3 112.7
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 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ATR001009308.1 RELATED DB: TARGETDB
DBREF 1WG2 A 8 58 UNP Q9SZ69 ZF2N3_ARATH 106 156
SEQADV 1WG2 GLY A 1 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 SER A 2 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 SER A 3 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 GLY A 4 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 SER A 5 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 SER A 6 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 GLY A 7 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 SER A 59 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 GLY A 60 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 PRO A 61 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 SER A 62 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 SER A 63 UNP Q9SZ69 CLONING ARTIFACT
SEQADV 1WG2 GLY A 64 UNP Q9SZ69 CLONING ARTIFACT
SEQRES 1 A 64 GLY SER SER GLY SER SER GLY PRO SER ARG PRO VAL ARG
SEQRES 2 A 64 PRO ASN ASN ARG CYS PHE SER CYS ASN LYS LYS VAL GLY
SEQRES 3 A 64 VAL MET GLY PHE LYS CYS LYS CYS GLY SER THR PHE CYS
SEQRES 4 A 64 GLY SER HIS ARG TYR PRO GLU LYS HIS GLU CYS SER PHE
SEQRES 5 A 64 ASP PHE LYS GLU VAL GLY SER GLY PRO SER SER GLY
HET ZN A 200 1
HET ZN A 400 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
SHEET 1 A 2 PHE A 30 LYS A 31 0
SHEET 2 A 2 THR A 37 PHE A 38 -1 O PHE A 38 N PHE A 30
LINK SG CYS A 18 ZN ZN A 200 1555 1555 2.26
LINK SG CYS A 21 ZN ZN A 200 1555 1555 2.34
LINK SG CYS A 32 ZN ZN A 400 1555 1555 2.35
LINK SG CYS A 34 ZN ZN A 400 1555 1555 2.35
LINK SG CYS A 39 ZN ZN A 200 1555 1555 2.25
LINK ND1 HIS A 42 ZN ZN A 200 1555 1555 2.01
LINK NE2 HIS A 48 ZN ZN A 400 1555 1555 2.05
LINK SG CYS A 50 ZN ZN A 400 1555 1555 2.33
SITE 1 AC1 4 CYS A 18 CYS A 21 CYS A 39 HIS A 42
SITE 1 AC2 4 CYS A 32 CYS A 34 HIS A 48 CYS A 50
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