Header list of 1wjv.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 29-MAY-04 1WJV
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER DOMAIN OF MOUSE CELL
TITLE 2 GROWTH REGULATING NUCLEOLAR PROTEIN LYAR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL GROWTH REGULATING NUCLEOLAR PROTEIN LYAR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC FINGER DNA BINDING 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 1700026C17;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030421-25;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CELL GROWTH REGULATING NUCLEOLAR PROTEIN LYAR, DNA-BINDING PROTEIN,
KEYWDS 2 C2H2 TYPE ZINC-FINGER, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,Y.MUTO,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 02-MAR-22 1WJV 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1WJV 1 VERSN
REVDAT 2 17-JAN-06 1WJV 1 TITLE JRNL
REVDAT 1 29-NOV-04 1WJV 0
JRNL AUTH M.YONEYAMA,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,Y.MUTO,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER DOMAIN OF
JRNL TITL 2 MOUSE CELL GROWTH REGULATING NUCLEOLAR PROTEIN LYAR
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 1WJV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023655.
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 : 220MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM ZINC FINGER DNA BINDING
REMARK 210 DOMAIN U-15N, 13C; 20MM D-TRIS-
REMARK 210 HCL; 200MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 100UM ZNCL2; 10% 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 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.896, 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, 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 SER A 2 81.52 -67.42
REMARK 500 1 ASP A 50 46.42 -92.70
REMARK 500 1 SER A 60 44.73 73.24
REMARK 500 1 LYS A 68 157.15 -44.31
REMARK 500 1 LYS A 73 -59.97 -120.35
REMARK 500 1 SER A 78 95.36 -63.73
REMARK 500 2 CYS A 40 156.30 -47.17
REMARK 500 2 ASP A 50 46.09 -96.60
REMARK 500 2 CYS A 58 43.22 -99.45
REMARK 500 2 LYS A 73 102.16 -51.69
REMARK 500 2 PRO A 76 -175.71 -69.76
REMARK 500 3 CYS A 43 -45.58 -133.03
REMARK 500 3 LYS A 45 111.48 -160.83
REMARK 500 3 PRO A 76 -174.42 -69.82
REMARK 500 4 ASP A 50 44.94 -79.95
REMARK 500 4 GLU A 71 144.36 -35.15
REMARK 500 5 SER A 2 103.92 -46.27
REMARK 500 5 CYS A 58 92.80 -61.38
REMARK 500 5 GLU A 61 -62.95 -106.64
REMARK 500 5 GLN A 63 -53.33 -130.34
REMARK 500 5 TYR A 70 42.54 -86.74
REMARK 500 5 SER A 74 142.46 -170.05
REMARK 500 6 CYS A 32 86.89 -69.42
REMARK 500 6 ASP A 50 43.21 -87.10
REMARK 500 6 VAL A 56 -67.38 -94.92
REMARK 500 7 CYS A 13 157.20 -46.38
REMARK 500 7 ASN A 34 31.43 -86.33
REMARK 500 7 ASP A 50 39.68 -84.60
REMARK 500 7 HIS A 55 100.06 -57.80
REMARK 500 7 CYS A 58 93.71 -59.23
REMARK 500 7 GLU A 71 82.12 -67.80
REMARK 500 8 SER A 3 97.73 -64.53
REMARK 500 8 ASP A 50 41.20 -82.96
REMARK 500 8 VAL A 56 -39.08 -131.66
REMARK 500 8 LYS A 64 171.50 -47.26
REMARK 500 8 PRO A 76 0.50 -69.70
REMARK 500 9 GLU A 36 -39.49 -133.14
REMARK 500 9 CYS A 43 -42.57 -133.96
REMARK 500 9 ASP A 50 43.94 -80.86
REMARK 500 9 LYS A 68 157.05 -44.38
REMARK 500 10 SER A 3 132.99 -39.75
REMARK 500 10 GLN A 24 42.80 -100.59
REMARK 500 10 SER A 54 35.61 -84.62
REMARK 500 10 LYS A 64 85.37 -65.96
REMARK 500 10 LYS A 68 155.07 -48.50
REMARK 500 10 SER A 74 -177.27 -58.44
REMARK 500 11 SER A 3 110.66 -165.79
REMARK 500 11 VAL A 9 132.08 -36.54
REMARK 500 11 GLN A 24 42.49 -104.36
REMARK 500 11 ASP A 50 44.23 -80.87
REMARK 500
REMARK 500 THIS ENTRY HAS 106 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 13 SG
REMARK 620 2 CYS A 16 SG 115.9
REMARK 620 3 HIS A 28 NE2 87.6 115.8
REMARK 620 4 CYS A 32 SG 114.2 117.1 101.6
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 40 SG
REMARK 620 2 CYS A 43 SG 109.2
REMARK 620 3 HIS A 55 NE2 104.4 111.5
REMARK 620 4 CYS A 58 SG 114.0 117.4 99.2
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: MMT007015432.1 RELATED DB: TARGETDB
DBREF 1WJV A 8 73 UNP Q08288 LYAR_MOUSE 1 66
SEQADV 1WJV GLY A 1 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV SER A 2 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV SER A 3 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV GLY A 4 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV SER A 5 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV SER A 6 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV GLY A 7 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV SER A 74 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV GLY A 75 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV PRO A 76 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV SER A 77 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV SER A 78 UNP Q08288 CLONING ARTIFACT
SEQADV 1WJV GLY A 79 UNP Q08288 CLONING ARTIFACT
SEQRES 1 A 79 GLY SER SER GLY SER SER GLY MET VAL PHE PHE THR CYS
SEQRES 2 A 79 ASN ALA CYS GLY GLU SER VAL LYS LYS ILE GLN VAL GLU
SEQRES 3 A 79 LYS HIS VAL SER ASN CYS ARG ASN CYS GLU CYS LEU SER
SEQRES 4 A 79 CYS ILE ASP CYS GLY LYS ASP PHE TRP GLY ASP ASP TYR
SEQRES 5 A 79 LYS SER HIS VAL LYS CYS ILE SER GLU GLY GLN LYS TYR
SEQRES 6 A 79 GLY GLY LYS GLY TYR GLU ALA LYS SER GLY PRO SER SER
SEQRES 7 A 79 GLY
HET ZN A 201 1
HET ZN A 401 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 ILE A 23 CYS A 32 1 10
HELIX 2 2 ASP A 50 TYR A 52 5 3
SHEET 1 A 4 SER A 19 LYS A 21 0
SHEET 2 A 4 PHE A 10 CYS A 13 -1 N PHE A 11 O VAL A 20
SHEET 3 A 4 CYS A 37 CYS A 40 -1 O SER A 39 N THR A 12
SHEET 4 A 4 LYS A 45 TRP A 48 -1 O PHE A 47 N LEU A 38
LINK SG CYS A 13 ZN ZN A 201 1555 1555 2.34
LINK SG CYS A 16 ZN ZN A 201 1555 1555 2.33
LINK NE2 HIS A 28 ZN ZN A 201 1555 1555 2.35
LINK SG CYS A 32 ZN ZN A 201 1555 1555 2.34
LINK SG CYS A 40 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 43 ZN ZN A 401 1555 1555 2.33
LINK NE2 HIS A 55 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 58 ZN ZN A 401 1555 1555 2.33
SITE 1 AC1 4 CYS A 13 CYS A 16 HIS A 28 CYS A 32
SITE 1 AC2 4 CYS A 40 CYS A 43 HIS A 55 CYS A 58
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