Header list of 1nj3.pdb file
Complete list - 22 20 Bytes
HEADER PROTEIN BINDING 30-DEC-02 1NJ3
TITLE STRUCTURE AND UBIQUITIN INTERACTIONS OF THE CONSERVED NZF DOMAIN OF
TITLE 2 NPL4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NPL4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NZF DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: NPL4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T
KEYWDS NZF DOMAIN, NPL4, RUBREDOXIN KNUCKLE, BETA-RIBBON, ZINC-FINGER,
KEYWDS 2 UBIQUITIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.WANG,S.L.ALAM,H.H.MEYER,M.PAYNE,T.L.STEMMLER,D.R.DAVIS,
AUTHOR 2 W.I.SUNDQUIST
REVDAT 4 22-NOV-17 1NJ3 1 REMARK
REVDAT 3 24-FEB-09 1NJ3 1 VERSN
REVDAT 2 01-MAR-05 1NJ3 1 JRNL
REVDAT 1 22-APR-03 1NJ3 0
JRNL AUTH B.WANG,S.L.ALAM,H.H.MEYER,M.PAYNE,T.L.STEMMLER,D.R.DAVIS,
JRNL AUTH 2 W.I.SUNDQUIST
JRNL TITL STRUCTURE AND UBIQUITIN INTERACTIONS OF THE CONSERVED ZINC
JRNL TITL 2 FINGER DOMAIN OF NPL4.
JRNL REF J.BIOL.CHEM. V. 278 20225 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12644454
JRNL DOI 10.1074/JBC.M300459200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.H.MEYER,J.G.SHORTER,D.PAPPIN,G.WARREN
REMARK 1 TITL A COMPLEX OF MAMMALIAN UFD1 AND NLP4 LINKS THE AAA-ATPASE,
REMARK 1 TITL 2 P97, TO UBIQUITIN AND NUCLEAR TRANSPORT
REMARK 1 REF EMBO J. V. 15 2181 2000
REMARK 1 REFN ISSN 0261-4189
REMARK 1 DOI 10.1093/EMBOJ/19.10.2181
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.H.MEYER,Y.WANG,G.WARREN
REMARK 1 TITL DIRECT BINDING OF UBIQUITIN CONJUGATES BY THE MAMMALIAN P97
REMARK 1 TITL 2 ADAPTER COMPLEXES, P47 AND UFD1-NPL4
REMARK 1 REF EMBO J. V. 21 5645 2002
REMARK 1 REFN ISSN 0261-4189
REMARK 1 DOI 10.1093/EMBOJ/CDF579
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, DYANA 1.5
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE
REMARK 3 -KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU, READ,
REMARK 3 RICE, SIMONSON, WARREN (CNS), GUNTERT, P.,
REMARK 3 MUMENTHALER, C., WUTHRICH, K. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 INITAL STRUCTURES FROM TORSION ANGLE DYNAMICS (DYANA)
REMARK 3 WERE REGULARIZED WITH A GENTLE ANNELAING
REMARK 3 PROTOCOL IN CNS
REMARK 4
REMARK 4 1NJ3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000017911.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 291
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 70 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM NPL4 NZF DOMAIN, U-15N,13C;
REMARK 210 20 MM SODIUM PHOSPHATE, PH 5.5,
REMARK 210 50MM NACL, 5 MM BME,90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB; HN(CA)CO; H(CCO)NH
REMARK 210 -TOCSY; (H)C(CO)NH-TOCSY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 97, SPARKY 3.106
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
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 84.61 60.43
REMARK 500 1 THR A 3 -168.37 -129.26
REMARK 500 1 SER A 4 -80.62 -67.39
REMARK 500 1 HIS A 11 -59.68 -137.66
REMARK 500 1 THR A 13 41.87 73.48
REMARK 500 1 THR A 20 58.86 -93.82
REMARK 500 1 HIS A 22 -110.88 -72.65
REMARK 500 1 CYS A 23 152.11 174.45
REMARK 500 1 MET A 25 -62.34 -134.23
REMARK 500 1 SER A 27 35.49 96.17
REMARK 500 2 SER A 4 -77.64 -65.68
REMARK 500 2 HIS A 11 -57.32 -137.97
REMARK 500 2 THR A 13 37.29 81.99
REMARK 500 2 THR A 20 58.30 -93.78
REMARK 500 2 HIS A 22 -110.96 -72.82
REMARK 500 2 CYS A 23 156.36 175.36
REMARK 500 2 MET A 25 -59.83 -133.03
REMARK 500 2 SER A 27 35.42 96.58
REMARK 500 3 SER A 2 -70.65 68.03
REMARK 500 3 SER A 4 -68.89 -91.42
REMARK 500 3 HIS A 11 -60.26 -138.03
REMARK 500 3 THR A 13 42.10 73.44
REMARK 500 3 HIS A 22 -110.34 -71.45
REMARK 500 3 CYS A 23 147.72 173.71
REMARK 500 3 MET A 25 -63.27 -134.44
REMARK 500 3 SER A 27 35.50 96.93
REMARK 500 4 SER A 4 -76.30 -83.21
REMARK 500 4 HIS A 11 -58.93 -137.83
REMARK 500 4 THR A 13 37.64 81.52
REMARK 500 4 HIS A 22 -110.97 -72.29
REMARK 500 4 CYS A 23 154.99 174.93
REMARK 500 4 MET A 25 -60.20 -132.79
REMARK 500 4 SER A 27 35.53 96.86
REMARK 500 5 SER A 4 -74.44 -82.36
REMARK 500 5 HIS A 11 -59.26 -137.72
REMARK 500 5 THR A 13 37.39 82.00
REMARK 500 5 THR A 20 58.41 -93.68
REMARK 500 5 HIS A 22 -110.88 -72.54
REMARK 500 5 CYS A 23 155.08 175.27
REMARK 500 5 MET A 25 -61.16 -132.93
REMARK 500 5 SER A 27 35.49 97.28
REMARK 500 6 SER A 2 103.66 60.61
REMARK 500 6 SER A 4 -78.21 -69.02
REMARK 500 6 HIS A 11 -59.12 -137.42
REMARK 500 6 THR A 13 37.66 81.68
REMARK 500 6 THR A 20 59.08 -93.62
REMARK 500 6 HIS A 22 -110.70 -71.98
REMARK 500 6 CYS A 23 153.14 174.78
REMARK 500 6 MET A 25 -60.83 -132.65
REMARK 500 6 SER A 27 35.91 95.56
REMARK 500
REMARK 500 THIS ENTRY HAS 161 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 32 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 23 SG
REMARK 620 2 CYS A 26 SG 105.7
REMARK 620 3 CYS A 12 SG 105.8 130.3
REMARK 620 4 CYS A 9 SG 101.2 106.0 104.4
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 32
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FHH RELATED DB: PDB
REMARK 900 STRUCTURALLY RELATED TO REBREDOXIN
REMARK 900 RELATED ID: 1DVB RELATED DB: PDB
REMARK 900 STRUCTURALLY REALTED TO RUBRERYTHRIN
DBREF 1NJ3 A 3 31 UNP Q9ES54 NPL4_RAT 580 608
SEQADV 1NJ3 GLY A 1 UNP Q9ES54 CLONING ARTIFACT
SEQADV 1NJ3 SER A 2 UNP Q9ES54 CLONING ARTIFACT
SEQRES 1 A 31 GLY SER THR SER ALA MET TRP ALA CYS GLN HIS CYS THR
SEQRES 2 A 31 PHE MET ASN GLN PRO GLY THR GLY HIS CYS GLU MET CYS
SEQRES 3 A 31 SER LEU PRO ARG THR
HET ZN A 32 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
SHEET 1 A 2 TRP A 7 ALA A 8 0
SHEET 2 A 2 MET A 15 ASN A 16 -1 O ASN A 16 N TRP A 7
LINK ZN ZN A 32 SG CYS A 23 1555 1555 2.41
LINK ZN ZN A 32 SG CYS A 26 1555 1555 2.30
LINK ZN ZN A 32 SG CYS A 12 1555 1555 2.31
LINK ZN ZN A 32 SG CYS A 9 1555 1555 2.42
SITE 1 AC1 4 CYS A 9 CYS A 12 CYS A 23 CYS A 26
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 - 22 20 Bytes