Header list of 1j2o.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN 08-JAN-03 1J2O
TITLE STRUCTURE OF FLIN2, A COMPLEX CONTAINING THE N-TERMINAL LIM DOMAIN OF
TITLE 2 LMO2 AND LDB1-LID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUSION OF RHOMBOTIN-2 AND LIM DOMAIN-BINDING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FLIN2;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: PROTEIN IS A FUSION OF THE N-TERMINAL LIM DOMAIN OF
COMPND 7 LMO2 (RESIDUES 26-87) FOLLOWED BY AN ELEVEN RESIDUE LINKER
COMPND 8 (GGSGGHMGSGG) THAN THE LID DOMAIN FROM LDB1 (RESIDUES 300-339).
COMPND 9 ORIGINALLY EXPRESSED AS A FUSION WITH GST. GST PORTION REMOVED BY
COMPND 10 TREATMENT WITH THROMBIN.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: LMO2, LDB1;
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-2T
KEYWDS LIM DOMAIN, LIM-INTERACTION-DOMAIN (LID), METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.E.DEANE,J.P.MACKAY,A.H.KWAN,E.Y.SUM,J.E.VISVADER,J.M.MATTHEWS
REVDAT 5 23-FEB-22 1J2O 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1J2O 1 VERSN
REVDAT 3 30-DEC-03 1J2O 1 AUTHOR
REVDAT 2 23-DEC-03 1J2O 1 SEQADV
REVDAT 1 13-MAY-03 1J2O 0
JRNL AUTH J.E.DEANE,J.P.MACKAY,A.H.KWAN,E.Y.SUM,J.E.VISVADER,
JRNL AUTH 2 J.M.MATTHEWS
JRNL TITL STRUCTURAL BASIS FOR THE RECOGNITION OF LDB1 BY THE
JRNL TITL 2 N-TERMINAL LIM DOMAINS OF LMO2 AND LMO4
JRNL REF EMBO J. V. 22 2224 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 12727888
JRNL DOI 10.1093/EMBOJ/CDG196
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.E.DEANE,J.E.VISVADER,J.P.MACKAY,J.M.MATTHEWS
REMARK 1 TITL DESIGN, PRODUCTION AND CHARACTERIZATION OF FLIN2 AND FLIN4:
REMARK 1 TITL 2 THE ENGINEERING OF INTRAMOLECULAR LDB1:LMO COMPLEXES.
REMARK 1 REF PROTEIN ENG. V. 14 493 2001
REMARK 1 REFN ISSN 0269-2139
REMARK 1 DOI 10.1093/PROTEIN/14.7.493
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, CNS 1.1
REMARK 3 AUTHORS : GUNTERT ET AL. (DYANA),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1690 NOE
REMARK 3 CONTRAINTS (INCLUDING 50 AMBIGUOUS CONSTRAINTS) AND 134 TORSION
REMARK 3 ANGLE RESTAINTS
REMARK 4
REMARK 4 1J2O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000005554.
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 : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : FLIN2 0.5MM, NACL 50MM, DTRIS
REMARK 210 -HCL 20MM, PH 7.0,
REMARK 210 DITHIOTHREITOL 1MM, TSP;
REMARK 210 UNIFORMLY 15-N LABELLED FLIN2
REMARK 210 0.5MM, NACL 50MM, DTRIS-HCL 20MM,
REMARK 210 PH 7.0, DITHIOTHREITOL 1MM, DSS;
REMARK 210 UNIFORMLY 13-C/15-N LABELLED
REMARK 210 0.5MM, NACL 50MM, NAH2P04/
REMARK 210 NA2HPO4 20MM, PH 7.0,
REMARK 210 DITHIOTHREITOL 1MM, DSS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
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 : XWINNMR 2.5, XEASY 1.3.13,
REMARK 210 TALOS, ARIA 1.1.2, CNS 1.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 AUTOMATED NOE ASSIGNMENT OF
REMARK 210 AMBIGUOUS NOES
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: BACKBONE AND SIDE-CHAIN ASSIGNMENT MADE USING STANDARD 2D
REMARK 210 AND 3D EXPERIMENTS.
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 H GLY A 74 HA LEU A 84 1.19
REMARK 500 HB2 LEU A 40 H GLY A 41 1.35
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 ASN A 12 145.36 77.22
REMARK 500 1 ALA A 21 -43.36 179.21
REMARK 500 1 ASP A 23 -12.19 176.50
REMARK 500 1 CYS A 38 -118.22 -110.68
REMARK 500 1 ARG A 39 43.66 -170.83
REMARK 500 1 LEU A 40 -112.70 43.01
REMARK 500 1 ARG A 45 -93.08 -158.97
REMARK 500 1 ARG A 46 -169.85 -104.12
REMARK 500 1 LEU A 51 -50.00 -29.59
REMARK 500 1 THR A 83 -96.50 53.11
REMARK 500 1 LEU A 84 95.93 -51.08
REMARK 500 1 MET A 85 -47.25 -140.47
REMARK 500 1 PHE A 89 -153.49 -59.54
REMARK 500 1 ASP A 91 -109.00 -122.65
REMARK 500 1 GLU A 92 -44.92 76.85
REMARK 500 1 GLU A 94 -163.49 -78.03
REMARK 500 1 ARG A 95 73.78 -67.75
REMARK 500 1 ASP A 106 -68.39 -4.16
REMARK 500 1 ALA A 107 64.02 72.32
REMARK 500 1 ILE A 111 43.18 -94.64
REMARK 500 2 ASN A 12 128.66 71.65
REMARK 500 2 ALA A 21 -47.87 170.48
REMARK 500 2 ASP A 23 -22.30 178.97
REMARK 500 2 CYS A 38 -90.38 -78.02
REMARK 500 2 GLU A 42 -107.56 49.63
REMARK 500 2 ARG A 62 -86.44 -164.08
REMARK 500 2 HIS A 69 -91.65 -124.80
REMARK 500 2 ASP A 91 -84.31 -86.91
REMARK 500 2 GLU A 92 -45.41 67.57
REMARK 500 2 THR A 103 -104.91 -115.21
REMARK 500 2 GLN A 104 93.51 -168.19
REMARK 500 2 PHE A 105 -57.71 -129.65
REMARK 500 2 ILE A 111 -101.88 -98.19
REMARK 500 3 LEU A 3 -66.56 -102.43
REMARK 500 3 ASN A 12 134.49 71.88
REMARK 500 3 ALA A 21 -53.24 178.22
REMARK 500 3 ASP A 23 -12.58 178.82
REMARK 500 3 CYS A 38 -98.52 -112.51
REMARK 500 3 GLU A 42 -91.58 58.58
REMARK 500 3 SER A 66 43.46 28.95
REMARK 500 3 PRO A 82 -144.81 -88.79
REMARK 500 3 ASP A 91 -112.62 -93.42
REMARK 500 3 GLU A 92 -67.31 -168.10
REMARK 500 3 ASP A 93 -34.83 -140.73
REMARK 500 3 GLU A 94 106.37 73.90
REMARK 500 3 ARG A 95 -145.42 -92.18
REMARK 500 3 LEU A 96 -139.31 -155.62
REMARK 500 3 THR A 103 -96.54 -83.78
REMARK 500 3 GLN A 104 86.63 -168.33
REMARK 500 3 ASP A 106 -56.50 -124.99
REMARK 500
REMARK 500 THIS ENTRY HAS 402 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 16 ARG A 45 -11.42
REMARK 500 17 TYR A 48 10.03
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 115 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 6 SG
REMARK 620 2 CYS A 9 SG 107.9
REMARK 620 3 HIS A 27 ND1 110.1 108.8
REMARK 620 4 CYS A 30 SG 110.1 109.9 110.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 116 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 33 SG
REMARK 620 2 CYS A 36 SG 114.9
REMARK 620 3 CYS A 56 SG 116.8 119.6
REMARK 620 4 ASP A 59 OD1 108.6 59.7 125.0
REMARK 620 5 ASP A 59 OD2 99.8 100.1 99.9 41.2
REMARK 620 N 1 2 3 4
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 115
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 116
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M3V RELATED DB: PDB
REMARK 900 1M3V CONTAINS SIMILAR PROTEIN
DBREF 1J2O A 2 63 UNP P25801 RHM2_MOUSE 26 87
DBREF 1J2O A 75 114 UNP P70662 LDB1_MOUSE 300 339
SEQADV 1J2O GLY A 1 UNP P25801 CLONING ARTIFACT
SEQADV 1J2O GLY A 64 UNP P25801 LINKER
SEQADV 1J2O GLY A 65 UNP P25801 LINKER
SEQADV 1J2O SER A 66 UNP P25801 LINKER
SEQADV 1J2O GLY A 67 UNP P25801 LINKER
SEQADV 1J2O GLY A 68 UNP P25801 LINKER
SEQADV 1J2O HIS A 69 UNP P25801 LINKER
SEQADV 1J2O MET A 70 UNP P25801 LINKER
SEQADV 1J2O GLY A 71 UNP P25801 LINKER
SEQADV 1J2O SER A 72 UNP P25801 LINKER
SEQADV 1J2O GLY A 73 UNP P25801 LINKER
SEQADV 1J2O GLY A 74 UNP P25801 LINKER
SEQRES 1 A 114 GLY SER LEU LEU THR CYS GLY GLY CYS GLN GLN ASN ILE
SEQRES 2 A 114 GLY ASP ARG TYR PHE LEU LYS ALA ILE ASP GLN TYR TRP
SEQRES 3 A 114 HIS GLU ASP CYS LEU SER CYS ASP LEU CYS GLY CYS ARG
SEQRES 4 A 114 LEU GLY GLU VAL GLY ARG ARG LEU TYR TYR LYS LEU GLY
SEQRES 5 A 114 ARG LYS LEU CYS ARG ARG ASP TYR LEU ARG LEU GLY GLY
SEQRES 6 A 114 SER GLY GLY HIS MET GLY SER GLY GLY ASP VAL MET VAL
SEQRES 7 A 114 VAL GLY GLU PRO THR LEU MET GLY GLY GLU PHE GLY ASP
SEQRES 8 A 114 GLU ASP GLU ARG LEU ILE THR ARG LEU GLU ASN THR GLN
SEQRES 9 A 114 PHE ASP ALA ALA ASN GLY ILE ASP ASP GLU
HET ZN A 115 1
HET ZN A 116 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 CYS A 56 GLY A 64 1 9
SHEET 1 A 3 TYR A 25 TRP A 26 0
SHEET 2 A 3 TYR A 17 LYS A 20 -1 N LEU A 19 O TRP A 26
SHEET 3 A 3 THR A 98 GLU A 101 -1 O LEU A 100 N PHE A 18
LINK SG CYS A 6 ZN ZN A 115 1555 1555 2.28
LINK SG CYS A 9 ZN ZN A 115 1555 1555 2.27
LINK ND1 HIS A 27 ZN ZN A 115 1555 1555 2.00
LINK SG CYS A 30 ZN ZN A 115 1555 1555 2.31
LINK SG CYS A 33 ZN ZN A 116 1555 1555 2.25
LINK SG CYS A 36 ZN ZN A 116 1555 1555 2.24
LINK SG CYS A 56 ZN ZN A 116 1555 1555 2.28
LINK OD1 ASP A 59 ZN ZN A 116 1555 1555 3.28
LINK OD2 ASP A 59 ZN ZN A 116 1555 1555 2.02
SITE 1 AC1 4 CYS A 6 CYS A 9 HIS A 27 CYS A 30
SITE 1 AC2 4 CYS A 33 CYS A 36 CYS A 56 ASP A 59
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 - b 23 2 Bytes