HEADER DNA BINDING PROTEIN 19-SEP-12 2LYS
TITLE NOE-BASED 3D STRUCTURE OF THE MONOMERIC PARTIALLY-FOLDED INTERMEDIATE
TITLE 2 OF CYLR2 AT 257K (-16 CELSIUS DEGREES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYLR2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PUTATIVE TRANSCRIPTION REGULATOR;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS;
SOURCE 3 ORGANISM_TAXID: 1351;
SOURCE 4 GENE: CYLR2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS CYLR2, DNA BINDING PROTEIN, NOE-BASED STRUCTURE, PROTEIN FOLDING,
KEYWDS 2 COLD DENATURATION, CYTOLYSIN REPRESSOR 2, HELIX-TURN-HELIX,
KEYWDS 3 PARTIALLY FOLDED
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.JAREMKO,L.JAREMKO,H.KIM,M.CHO,C.D.SCHWIETERS,K.GILLER,S.BECKER,
AUTHOR 2 M.ZWECKSTETTER
REVDAT 4 14-JUN-23 2LYS 1 REMARK
REVDAT 3 03-APR-13 2LYS 1 JRNL
REVDAT 2 27-FEB-13 2LYS 1 JRNL
REVDAT 1 20-FEB-13 2LYS 0
JRNL AUTH M.JAREMKO,L.JAREMKO,H.Y.KIM,M.K.CHO,C.D.SCHWIETERS,K.GILLER,
JRNL AUTH 2 S.BECKER,M.ZWECKSTETTER
JRNL TITL COLD DENATURATION OF A PROTEIN DIMER MONITORED AT ATOMIC
JRNL TITL 2 RESOLUTION.
JRNL REF NAT.CHEM.BIOL. V. 9 264 2013
JRNL REFN ISSN 1552-4450
JRNL PMID 23396077
JRNL DOI 10.1038/NCHEMBIO.1181
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 3.0, X-PLOR NIH 2.26
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA),
REMARK 3 SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE (X-PLOR
REMARK 3 NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000102998.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 257
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0.6
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.52 MM [U-100% 13C; U-100% 15N]
REMARK 210 CYLR2, 600 MM SODIUM CHLORIDE,
REMARK 210 50 MM HEPES, 93 % H2O, 7 % D2O,
REMARK 210 93% H2O/7% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC
REMARK 210 ALIPHATIC; 3D 1H-13C NOESY
REMARK 210 ALIPHATIC; 3D HCCH-TOCSY; 2D 1H-
REMARK 210 13C HSQC AROMATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE III
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY, NMRPIPE
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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: 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: 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 LEU A 43 H LEU A 47 1.44
REMARK 500 OE1 GLU A 25 HH TYR A 52 1.44
REMARK 500 O LEU A 57 H PHE A 61 1.44
REMARK 500 HH11 ARG A 10 O ILE A 15 1.45
REMARK 500 O ILE A 31 H ILE A 34 1.47
REMARK 500 HG SER A 16 OE2 GLU A 19 1.47
REMARK 500 O GLN A 17 H ALA A 21 1.49
REMARK 500 O GLY A 33 H ASN A 37 1.50
REMARK 500 O SER A 16 H LEU A 20 1.53
REMARK 500 O ILE A 9 H LYS A 13 1.53
REMARK 500 O SER A 42 H ALA A 46 1.53
REMARK 500 O ALA A 46 H ALA A 50 1.53
REMARK 500 O ILE A 60 HE21 GLN A 62 1.54
REMARK 500 OD1 ASN A 5 H LYS A 7 1.54
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 LEU A 24 20.61 -57.49
REMARK 500 1 GLU A 25 0.70 -55.85
REMARK 500 1 LYS A 38 -7.90 -57.84
REMARK 500 1 THR A 55 114.34 -160.19
REMARK 500 2 ILE A 2 -76.31 58.19
REMARK 500 2 ASN A 4 -37.84 169.39
REMARK 500 2 LYS A 14 79.38 47.78
REMARK 500 2 PRO A 41 105.28 -54.45
REMARK 500 2 ASN A 54 81.21 -54.03
REMARK 500 3 ILE A 3 86.15 -65.02
REMARK 500 3 LYS A 14 79.60 45.60
REMARK 500 3 GLU A 25 -5.32 -56.30
REMARK 500 3 THR A 55 118.81 -166.46
REMARK 500 3 PHE A 61 39.49 26.61
REMARK 500 4 ASN A 4 65.93 -69.77
REMARK 500 4 ASN A 5 -18.68 -48.14
REMARK 500 4 LYS A 14 75.64 50.91
REMARK 500 4 ASN A 54 83.13 -45.61
REMARK 500 4 THR A 55 110.57 -165.07
REMARK 500 4 PHE A 61 107.76 -29.27
REMARK 500 4 GLN A 64 -61.73 -132.88
REMARK 500 4 PRO A 65 40.79 -73.49
REMARK 500 5 ILE A 2 151.99 69.89
REMARK 500 5 ASN A 4 91.42 -48.29
REMARK 500 5 LYS A 38 -8.04 -50.42
REMARK 500 5 TYR A 39 -178.30 -60.80
REMARK 500 5 ASN A 54 73.59 -46.40
REMARK 500 5 PHE A 61 153.00 89.82
REMARK 500 5 GLN A 62 -149.99 -105.67
REMARK 500 5 TRP A 63 -63.21 62.96
REMARK 500 5 GLN A 64 152.50 144.77
REMARK 500 6 LYS A 38 27.57 -58.10
REMARK 500 6 PRO A 41 109.90 -51.00
REMARK 500 6 GLN A 62 -99.91 42.37
REMARK 500 6 TRP A 63 43.08 -150.89
REMARK 500 7 LEU A 24 17.28 -57.25
REMARK 500 7 GLU A 25 1.11 -63.02
REMARK 500 7 TYR A 39 -177.17 -60.71
REMARK 500 7 ASN A 54 72.44 -59.90
REMARK 500 8 ILE A 2 53.89 -68.56
REMARK 500 8 ILE A 3 -61.77 60.99
REMARK 500 8 ASN A 4 -76.59 177.52
REMARK 500 8 ASN A 32 -29.61 -38.63
REMARK 500 8 GLN A 64 71.33 175.89
REMARK 500 9 ILE A 2 67.43 -62.78
REMARK 500 9 ASN A 4 9.81 47.06
REMARK 500 9 GLU A 25 -8.51 -59.54
REMARK 500 9 LYS A 38 28.29 -52.26
REMARK 500 9 ASN A 54 85.36 -64.04
REMARK 500 9 THR A 55 119.82 -164.44
REMARK 500
REMARK 500 THIS ENTRY HAS 105 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GZU RELATED DB: PDB
REMARK 900 STRUCTURE OF THE SAME PROTEIN USING INTERMONOMER DISTANCES FROM
REMARK 900 PARAMAGNETIC RELAXATION ENHANCEMENT AND NMR DIPOLAR COUPLINGS
REMARK 900 RELATED ID: 1UTX RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE SAME PROTEIN AT 1.9 A RESOLUTION
REMARK 900 RELATED ID: 2XI8 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE SAME PROTEIN AT 1.21 A RESOLUTION
REMARK 900 RELATED ID: 2XIU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF MTSL-TAGGED CYLR2
REMARK 900 RELATED ID: 2XJ3 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF T55C MUTANT OF CYLR2
REMARK 900 RELATED ID: 2LYJ RELATED DB: PDB
REMARK 900 RELATED ID: 2LYK RELATED DB: PDB
REMARK 900 RELATED ID: 2LYL RELATED DB: PDB
REMARK 900 RELATED ID: 2LYP RELATED DB: PDB
REMARK 900 RELATED ID: 2LYQ RELATED DB: PDB
REMARK 900 RELATED ID: 2LYR RELATED DB: PDB
REMARK 900 RELATED ID: 17898 RELATED DB: BMRB
DBREF 2LYS A 1 66 UNP Q8VL32 Q8VL32_ENTFL 1 66
SEQRES 1 A 66 MET ILE ILE ASN ASN LEU LYS LEU ILE ARG GLU LYS LYS
SEQRES 2 A 66 LYS ILE SER GLN SER GLU LEU ALA ALA LEU LEU GLU VAL
SEQRES 3 A 66 SER ARG GLN THR ILE ASN GLY ILE GLU LYS ASN LYS TYR
SEQRES 4 A 66 ASN PRO SER LEU GLN LEU ALA LEU LYS ILE ALA TYR TYR
SEQRES 5 A 66 LEU ASN THR PRO LEU GLU ASP ILE PHE GLN TRP GLN PRO
SEQRES 6 A 66 GLU
HELIX 1 1 ASN A 5 LYS A 14 1 10
HELIX 2 2 SER A 16 LEU A 24 1 9
HELIX 3 3 SER A 27 ASN A 32 5 6
HELIX 4 4 GLY A 33 LYS A 38 1 6
HELIX 5 5 SER A 42 LEU A 53 1 12
HELIX 6 6 PRO A 56 PHE A 61 1 6
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
(ATOM LINES ARE NOT SHOWN.)
END