Header list of 1z2q.pdb file
Complete list - g 9 2 Bytes
HEADER MEMBRANE PROTEIN 08-MAR-05 1Z2Q
TITLE HIGH-RESOLUTION SOLUTION STRUCTURE OF THE LM5-1 FYVE DOMAIN FROM
TITLE 2 LEISHMANIA MAJOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LM5-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FYVE DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MAJOR;
SOURCE 3 ORGANISM_TAXID: 5664;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-3
KEYWDS MEMBRANE PROTEIN, FYVE DOMAIN, ZINC-FINGER
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR H.D.T.MERTENS,J.M.CALLAGHAN,M.J.MCCONVILLE,P.R.GOOLEY
REVDAT 5 14-JUN-23 1Z2Q 1 REMARK
REVDAT 4 26-FEB-20 1Z2Q 1 REMARK
REVDAT 3 07-APR-09 1Z2Q 1 JRNL REMARK
REVDAT 2 24-FEB-09 1Z2Q 1 VERSN
REVDAT 1 19-APR-05 1Z2Q 0
JRNL AUTH H.D.T.MERTENS,J.M.CALLAGHAN,J.D.SWARBRICK,M.J.MCCONVILLE,
JRNL AUTH 2 P.R.GOOLEY
JRNL TITL A HIGH-RESOLUTION SOLUTION STRUCTURE OF A TRYPANOSOMATID
JRNL TITL 2 FYVE DOMAIN.
JRNL REF PROTEIN SCI. V. 16 2552 2007
JRNL REFN ISSN 0961-8368
JRNL PMID 17905827
JRNL DOI 10.1110/PS.073009807
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, XPLOR-NIH 2.9.1
REMARK 3 AUTHORS : VARIAN INC. (VNMR),
REMARK 3 C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES BASED ON 545 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 101 DIHEDRAL ANGLE RESTRAINTS, AND 259
REMARK 3 RESIDUAL DIPOLAR COUPLINGS.
REMARK 4
REMARK 4 1Z2Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032223.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8MM LM5-1 U-15N, 13C; 50MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 50MM
REMARK 210 KCL, 1MM DTT, 1MM AEBSF, 0.05%
REMARK 210 SODIUM AZIDE; 90% H2O, 10% D2O;
REMARK 210 0.8MM LM5-1 U-15N,13C; 50MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 50MM
REMARK 210 KCL, 1MM DTT, 1MM AEBSF,0.05%
REMARK 210 SODIUM AZIDE; 100% D2O; 0.8MM
REMARK 210 LM5-1 ~10% 13C; 50MM SODIUM
REMARK 210 PHOSPHATE BUFFER, 50MM KCL, 1MM
REMARK 210 DTT, 1MM AEBSF, 0.05% SODIUM
REMARK 210 AZIDE; 100% D2O; 0.8MM LM5-1 U-
REMARK 210 15N,13C; 50MM SODIUM PHOSPHATE
REMARK 210 BUFFER, 50MM KCL, 1MM DTT, 1MM
REMARK 210 AEBSF, 0.05% SODIUM AZIDE; 10MG/
REMARK 210 ML PF1; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 2D_13C-
REMARK 210 CT-HSQC; 2D_15N-HSQC-TROSY, 2D_
REMARK 210 HN(A/B-NC-J)-TROSY, 2D_HN(CO-A/B-
REMARK 210 C'CA-J)-TROSY, 3D_1H-DEC_HN(CO)CA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.2, XEASY 1.3, CYANA
REMARK 210 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
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 : 21
REMARK 210
REMARK 210 REMARK: 2 X ZN2+ IONS NOT INCLUDED IN CALCULATIONS, LIGATING
REMARK 210 CYSTEINES TREATED AS PROTONATED SULFHYDRYL GROUPS DURING
REMARK 210 SIMULATED ANNEALING.
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 O ALA A 56 H GLU A 67 1.58
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 ALA A 21 74.37 -114.11
REMARK 500 1 ASN A 42 -70.27 -100.69
REMARK 500 2 ALA A 21 71.11 -111.37
REMARK 500 2 ASN A 42 -71.54 -101.65
REMARK 500 3 ALA A 21 68.18 -113.39
REMARK 500 3 ASN A 42 -72.06 -100.90
REMARK 500 4 ALA A 21 70.58 -111.47
REMARK 500 4 ASN A 42 -70.00 -102.88
REMARK 500 5 ALA A 21 72.12 -111.41
REMARK 500 5 ASN A 42 -70.26 -100.71
REMARK 500 5 CYS A 70 -168.41 -75.44
REMARK 500 6 ALA A 21 74.44 -110.96
REMARK 500 6 ASN A 42 -72.21 -101.70
REMARK 500 7 SER A 11 39.80 159.46
REMARK 500 7 ALA A 21 72.62 -116.49
REMARK 500 7 ASN A 42 -70.33 -101.67
REMARK 500 8 ALA A 21 74.53 -112.92
REMARK 500 8 ASN A 42 -71.71 -101.46
REMARK 500 9 ALA A 21 78.07 -112.89
REMARK 500 9 ASN A 42 -69.50 -100.70
REMARK 500 10 ALA A 21 77.54 -111.39
REMARK 500 10 ASN A 42 -71.38 -101.21
REMARK 500 11 ALA A 21 72.76 -116.49
REMARK 500 11 ASN A 42 -70.33 -101.74
REMARK 500 12 ALA A 21 75.71 -112.56
REMARK 500 12 ASN A 42 -70.04 -100.66
REMARK 500 13 ALA A 21 72.61 -112.43
REMARK 500 13 ASN A 42 -71.37 -101.54
REMARK 500 13 SER A 79 -83.66 -60.54
REMARK 500 14 ALA A 21 77.66 -114.54
REMARK 500 14 ASN A 42 -71.82 -101.28
REMARK 500 15 ALA A 21 73.57 -115.48
REMARK 500 15 ASN A 42 -72.31 -101.72
REMARK 500 16 ALA A 21 73.79 -110.68
REMARK 500 16 ASN A 42 -71.64 -100.66
REMARK 500 17 ALA A 21 74.30 -113.61
REMARK 500 17 ASN A 42 -72.53 -101.08
REMARK 500 18 ALA A 21 74.24 -111.84
REMARK 500 18 ASN A 42 -70.26 -102.90
REMARK 500 19 SER A 11 66.67 178.97
REMARK 500 19 ALA A 21 76.45 -109.91
REMARK 500 19 ASN A 42 -70.66 -101.82
REMARK 500 20 ALA A 21 75.63 -115.30
REMARK 500 20 ASN A 42 -71.49 -100.81
REMARK 500 21 LEU A 3 -53.94 -178.63
REMARK 500 21 GLU A 8 -18.91 -47.64
REMARK 500 21 SER A 11 107.62 -19.07
REMARK 500 21 LYS A 12 93.39 -38.32
REMARK 500 21 ASN A 42 -69.32 -92.97
REMARK 500 21 CYS A 70 -157.18 -100.02
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6594 RELATED DB: BMRB
DBREF 1Z2Q A 1 84 PDB 1Z2Q 1Z2Q 1 84
SEQRES 1 A 84 GLY PRO LEU GLY SER MET GLY GLU LYS GLN SER LYS GLY
SEQRES 2 A 84 TYR TRP GLN GLU ASP GLU ASP ALA PRO ALA CYS ASN GLY
SEQRES 3 A 84 CYS GLY CYS VAL PHE THR THR THR VAL ARG ARG HIS HIS
SEQRES 4 A 84 CYS ARG ASN CYS GLY TYR VAL LEU CYS GLY ASP CYS SER
SEQRES 5 A 84 ARG HIS ARG ALA ALA ILE PRO MET ARG GLY ILE THR GLU
SEQRES 6 A 84 PRO GLU ARG VAL CYS ASP ALA CYS TYR LEU ALA LEU ARG
SEQRES 7 A 84 SER SER ASN MET ALA GLY
HELIX 1 1 GLY A 49 ARG A 53 5 5
HELIX 2 2 CYS A 70 SER A 79 1 10
SHEET 1 A 2 HIS A 38 HIS A 39 0
SHEET 2 A 2 VAL A 46 LEU A 47 -1 O LEU A 47 N HIS A 38
SHEET 1 B 2 ARG A 55 ILE A 58 0
SHEET 2 B 2 ILE A 63 ARG A 68 -1 O GLU A 67 N ALA A 56
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 - g 9 2 Bytes