Header list of 1n0z.pdb file
Complete list - v 10 2 Bytes
HEADER TRANSCRIPTION 15-OCT-02 1N0Z
TITLE SOLUTION STRUCTURE OF THE FIRST ZINC-FINGER DOMAIN FROM ZNF265
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZNF265;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZNF265-F1;
COMPND 5 SYNONYM: ZINC FINGER PROTEIN 265;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ZNF265;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T
KEYWDS ZINC FINGER, RNA SPLICING, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.A.PLAMBECK,K.FAIRLEY,A.H.Y.KWAN,B.J.WESTMAN,D.ADAMS,B.MORRIS,
AUTHOR 2 J.P.MACKAY
REVDAT 3 10-NOV-21 1N0Z 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1N0Z 1 VERSN
REVDAT 1 22-JUL-03 1N0Z 0
JRNL AUTH C.A.PLAMBECK,A.H.Y.KWAN,D.J.ADAMS,B.J.WESTMAN,
JRNL AUTH 2 L.VAN DER WEYDEN,R.L.MEDCALF,B.J.MORRIS,J.P.MACKAY
JRNL TITL THE STRUCTURE OF THE ZINC FINGER DOMAIN FROM HUMAN SPLICING
JRNL TITL 2 FACTOR ZNF265 FOLD
JRNL REF J.BIOL.CHEM. V. 278 22805 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12657633
JRNL DOI 10.1074/JBC.M301896200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, DYANA 1.5
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT ET AL (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE CALCULATIONS WERE PERFORMED
REMARK 3 USING THE PACKAGE ARIA1.2 (AMBIGUOUS RESTRAINTS IN ITERATIVE
REMARK 3 ASSIGNMENT). FINAL STRUCTURES ARE BASED ON 709 UNAMBIGUOUS NOE-
REMARK 3 DERIVED DISTANCE CONSTRAINTS, 14 SETS OF AMBIGUOUS NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS AND 22 ADDITIONAL DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1N0Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017383.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM ZNF265-F1, 2MM TCEP, 1.7MM
REMARK 210 ZNZO4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 SHORT MIXING TIME NOESY; SHORT
REMARK 210 MIXING TIME TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, ARIA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 2D NMR
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
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 MET A 3 83.71 62.64
REMARK 500 1 ARG A 9 49.43 -91.59
REMARK 500 1 CYS A 22 -79.67 -90.42
REMARK 500 1 PHE A 27 -82.24 -45.41
REMARK 500 1 ALA A 28 -66.65 178.39
REMARK 500 1 LYS A 40 107.22 -59.19
REMARK 500 2 THR A 5 -89.32 62.66
REMARK 500 2 ILE A 16 -75.48 -135.40
REMARK 500 2 CYS A 22 -86.76 -119.41
REMARK 500 2 CYS A 36 -61.24 -93.26
REMARK 500 2 ARG A 38 -132.10 -175.73
REMARK 500 2 THR A 41 88.44 -69.86
REMARK 500 3 THR A 5 -133.02 -90.70
REMARK 500 3 VAL A 10 95.12 -66.95
REMARK 500 3 ILE A 16 -108.89 -111.88
REMARK 500 3 LYS A 20 150.66 72.46
REMARK 500 3 LYS A 21 39.01 -75.62
REMARK 500 3 CYS A 22 -78.60 -77.20
REMARK 500 3 PHE A 27 -80.84 -48.41
REMARK 500 3 ALA A 28 -59.32 179.81
REMARK 500 3 THR A 41 106.49 -46.71
REMARK 500 4 THR A 5 -106.91 -77.91
REMARK 500 4 LYS A 6 48.65 -100.80
REMARK 500 4 VAL A 10 133.54 78.25
REMARK 500 4 ILE A 16 138.98 71.11
REMARK 500 4 CYS A 22 -73.11 -97.06
REMARK 500 4 PHE A 27 -74.91 -65.27
REMARK 500 4 ALA A 28 -76.80 -179.09
REMARK 500 4 ARG A 29 42.79 -77.45
REMARK 500 4 LYS A 40 107.21 -58.60
REMARK 500 4 THR A 42 -42.76 -143.96
REMARK 500 5 MET A 3 -80.23 -104.08
REMARK 500 5 SER A 4 -100.67 54.86
REMARK 500 5 LYS A 6 69.41 -100.86
REMARK 500 5 PHE A 8 77.45 59.55
REMARK 500 5 LYS A 20 31.78 -77.62
REMARK 500 5 CYS A 22 -91.25 -98.65
REMARK 500 6 THR A 5 104.37 68.68
REMARK 500 6 PHE A 8 92.53 -65.73
REMARK 500 6 ILE A 16 -117.21 -98.80
REMARK 500 6 CYS A 22 -79.74 -88.02
REMARK 500 6 PHE A 27 -131.85 -73.75
REMARK 500 6 ALA A 28 -62.99 -140.09
REMARK 500 6 ARG A 29 41.61 -78.95
REMARK 500 6 ARG A 35 -68.26 -104.44
REMARK 500 6 PRO A 44 99.90 -65.83
REMARK 500 7 MET A 3 -52.69 73.10
REMARK 500 7 ASN A 7 -153.33 -100.40
REMARK 500 7 VAL A 10 25.68 -151.58
REMARK 500 7 SER A 11 -139.06 -102.05
REMARK 500
REMARK 500 THIS ENTRY HAS 140 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 46 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 17 SG
REMARK 620 2 CYS A 22 SG 107.9
REMARK 620 3 CYS A 33 SG 108.5 113.0
REMARK 620 4 CYS A 36 SG 110.1 107.8 109.5
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 46
DBREF 1N0Z A 3 42 UNP O95218 ZN265_HUMAN 1 40
SEQADV 1N0Z GLY A 1 UNP O95218 CLONING ARTIFACT
SEQADV 1N0Z SER A 2 UNP O95218 CLONING ARTIFACT
SEQADV 1N0Z ASP A 34 UNP O95218 ASN 32 ENGINEERED MUTATION
SEQADV 1N0Z GLY A 43 UNP O95218 CLONING ARTIFACT
SEQADV 1N0Z PRO A 44 UNP O95218 CLONING ARTIFACT
SEQADV 1N0Z ILE A 45 UNP O95218 CLONING ARTIFACT
SEQRES 1 A 45 GLY SER MET SER THR LYS ASN PHE ARG VAL SER ASP GLY
SEQRES 2 A 45 ASP TRP ILE CYS PRO ASP LYS LYS CYS GLY ASN VAL ASN
SEQRES 3 A 45 PHE ALA ARG ARG THR SER CYS ASP ARG CYS GLY ARG GLU
SEQRES 4 A 45 LYS THR THR GLY PRO ILE
HET ZN A 46 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
LINK SG CYS A 17 ZN ZN A 46 1555 1555 2.24
LINK SG CYS A 22 ZN ZN A 46 1555 1555 2.28
LINK SG CYS A 33 ZN ZN A 46 1555 1555 2.29
LINK SG CYS A 36 ZN ZN A 46 1555 1555 2.29
SITE 1 AC1 4 CYS A 17 CYS A 22 CYS A 33 CYS A 36
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 - v 10 2 Bytes