Header list of 1lr1.pdb file
Complete list - t 27 2 Bytes
HEADER DNA BINDING PROTEIN 14-MAY-02 1LR1
TITLE SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF THE BACTERIAL
TITLE 2 CHROMATIN-STRUCTURING PROTEIN H-NS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN H-NS;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 1-57);
COMPND 5 SYNONYM: HISTONE-LIKE PROTEIN HLP-II, PROTEIN H1, PROTEIN B1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: HNS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(LAMBDA DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS CHROMATIN, COILED-COIL, DNA PACKAGING, NUCLEOID ASSEMBLY, DNA BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.ESPOSITO,A.PETROVIC,R.HARRIS,S.ONO,J.ECCLESTON,A.MBABAALI,I.HAQ,
AUTHOR 2 C.F.HIGGINS,J.C.D.HINTON,P.C.DRISCOLL,J.E.LADBURY
REVDAT 3 27-OCT-21 1LR1 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1LR1 1 VERSN
REVDAT 1 14-JAN-03 1LR1 0
JRNL AUTH D.ESPOSITO,A.PETROVIC,R.HARRIS,S.ONO,J.ECCLESTON,A.MBABAALI,
JRNL AUTH 2 I.HAQ,C.F.HIGGINS,J.C.HINTON,P.C.DRISCOLL,J.E.LADBURY
JRNL TITL H-NS OLIGOMERIZATION DOMAIN STRUCTURE REVEALS THE MECHANISM
JRNL TITL 2 FOR HIGH ORDER SELF-ASSOCIATION OF THE INTACT PROTEIN
JRNL REF J.MOL.BIOL. V. 324 841 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12460581
JRNL DOI 10.1016/S0022-2836(02)01141-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AZARA 2.6, CNS 1.1
REMARK 3 AUTHORS : BOUCHER, W. (AZARA), BRUNGER, A.T. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE CALCULATIONS WERE CARRIED OUT USING
REMARK 3 THE PARALLHDGV5.1 PARAMETER, WITH THE NON-BONDED ENERGY FUNCTION
REMARK 3 OF PROLSQ, MODIFIED TO ALLOW FLOATING STEREOCHEMISTRY OF
REMARK 3 PROCHIRAL CENTERS
REMARK 4
REMARK 4 1LR1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-02.
REMARK 100 THE DEPOSITION ID IS D_1000016203.
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 : 300 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 15N LABELLED; 15N,13C LABELLED;
REMARK 210 14N,12C/15N,13C 1:1 MIXED
REMARK 210 LABELLED CHAINS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D 13CF1-
REMARK 210 FILTERED, F3-EDITED NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3, CNS 1.1
REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: ASSIGNMENT WAS ACCOMPLISHED BY USING STANDARD TRIPLE
REMARK 210 RESONANCE 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
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 HG3 ARG A 39 HG3 GLU B 43 1.17
REMARK 500 HG3 GLU A 43 HG3 ARG B 39 1.17
REMARK 500 O VAL A 36 H ARG A 40 1.51
REMARK 500 O VAL B 36 H ARG B 40 1.51
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 9 128.85 67.50
REMARK 500 1 GLU A 19 35.58 -94.80
REMARK 500 1 SER A 20 -162.83 -168.49
REMARK 500 1 GLU A 23 -25.33 -39.17
REMARK 500 1 GLU A 51 -112.40 60.22
REMARK 500 1 GLU A 52 -47.33 -167.86
REMARK 500 1 ARG A 55 -42.58 -174.99
REMARK 500 1 ASN B 9 128.82 67.69
REMARK 500 1 GLU B 19 35.49 -94.75
REMARK 500 1 SER B 20 -162.80 -168.44
REMARK 500 1 GLU B 23 -25.32 -39.01
REMARK 500 1 GLU B 51 -112.44 60.21
REMARK 500 1 GLU B 52 -47.30 -167.89
REMARK 500 1 ARG B 55 -42.72 -174.96
REMARK 500 2 ASN A 9 129.09 59.01
REMARK 500 2 SER A 20 -166.60 -163.50
REMARK 500 2 VAL A 50 -56.13 71.45
REMARK 500 2 GLU A 51 -144.99 59.59
REMARK 500 2 GLU A 52 131.01 62.74
REMARK 500 2 ARG A 53 -40.06 72.89
REMARK 500 2 ARG A 55 -139.59 -67.76
REMARK 500 2 ASN B 9 130.01 62.82
REMARK 500 2 ARG B 18 -31.05 -39.87
REMARK 500 2 VAL B 50 137.35 64.98
REMARK 500 2 GLU B 52 -42.42 -171.00
REMARK 500 2 ARG B 53 40.32 -172.61
REMARK 500 2 THR B 54 36.53 -80.98
REMARK 500 2 ARG B 55 -143.50 52.76
REMARK 500 3 ASN A 9 124.56 67.98
REMARK 500 3 GLU A 19 31.91 -91.63
REMARK 500 3 SER A 20 -162.85 -164.69
REMARK 500 3 GLU A 23 -25.78 -39.91
REMARK 500 3 GLU A 52 -41.32 -136.43
REMARK 500 3 LYS A 56 54.80 -170.80
REMARK 500 3 ASN B 9 126.80 62.20
REMARK 500 3 SER B 20 -155.35 -161.81
REMARK 500 3 GLU B 51 132.23 67.61
REMARK 500 3 GLU B 52 50.02 -179.71
REMARK 500 3 ARG B 53 -38.51 -158.29
REMARK 500 3 ARG B 55 40.85 -75.29
REMARK 500 4 ASN A 9 129.56 63.51
REMARK 500 4 GLU A 19 35.14 -94.05
REMARK 500 4 SER A 20 -163.55 -169.70
REMARK 500 4 GLU A 52 -63.08 -151.65
REMARK 500 4 ARG A 53 -46.35 -158.50
REMARK 500 4 ASN B 9 127.24 61.65
REMARK 500 4 SER B 20 -156.02 -165.12
REMARK 500 4 ARG B 53 44.82 -75.92
REMARK 500 4 THR B 54 -39.40 -149.13
REMARK 500 4 ARG B 55 129.15 64.95
REMARK 500
REMARK 500 THIS ENTRY HAS 256 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HNS RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE C-TERMINAL DNA BINDING DOMAIN OF H-NS
DBREF 1LR1 A 1 57 UNP P0ACF8 HNS_ECOLI 1 57
DBREF 1LR1 B 1 57 UNP P0ACF8 HNS_ECOLI 1 57
SEQADV 1LR1 GLY A -3 UNP P0ACF8 CLONING ARTIFACT
SEQADV 1LR1 SER A -2 UNP P0ACF8 CLONING ARTIFACT
SEQADV 1LR1 HIS A -1 UNP P0ACF8 CLONING ARTIFACT
SEQADV 1LR1 MET A 0 UNP P0ACF8 CLONING ARTIFACT
SEQADV 1LR1 SER A 20 UNP P0ACF8 CYS 20 ENGINEERED MUTATION
SEQADV 1LR1 GLY B -3 UNP P0ACF8 CLONING ARTIFACT
SEQADV 1LR1 SER B -2 UNP P0ACF8 CLONING ARTIFACT
SEQADV 1LR1 HIS B -1 UNP P0ACF8 CLONING ARTIFACT
SEQADV 1LR1 MET B 0 UNP P0ACF8 CLONING ARTIFACT
SEQADV 1LR1 SER B 20 UNP P0ACF8 CYS 20 ENGINEERED MUTATION
SEQRES 1 A 61 GLY SER HIS MET SER GLU ALA LEU LYS ILE LEU ASN ASN
SEQRES 2 A 61 ILE ARG THR LEU ARG ALA GLN ALA ARG GLU SER THR LEU
SEQRES 3 A 61 GLU THR LEU GLU GLU MET LEU GLU LYS LEU GLU VAL VAL
SEQRES 4 A 61 VAL ASN GLU ARG ARG GLU GLU GLU SER ALA ALA ALA ALA
SEQRES 5 A 61 GLU VAL GLU GLU ARG THR ARG LYS LEU
SEQRES 1 B 61 GLY SER HIS MET SER GLU ALA LEU LYS ILE LEU ASN ASN
SEQRES 2 B 61 ILE ARG THR LEU ARG ALA GLN ALA ARG GLU SER THR LEU
SEQRES 3 B 61 GLU THR LEU GLU GLU MET LEU GLU LYS LEU GLU VAL VAL
SEQRES 4 B 61 VAL ASN GLU ARG ARG GLU GLU GLU SER ALA ALA ALA ALA
SEQRES 5 B 61 GLU VAL GLU GLU ARG THR ARG LYS LEU
HELIX 1 1 SER A 1 LEU A 7 1 7
HELIX 2 2 ASN A 8 ALA A 17 1 10
HELIX 3 3 LEU A 22 GLU A 51 1 30
HELIX 4 4 SER B 1 LEU B 7 1 7
HELIX 5 5 ASN B 8 ALA B 17 1 10
HELIX 6 6 LEU B 22 GLU B 51 1 30
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 - t 27 2 Bytes