Header list of 1ner.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 24-AUG-95 1NER
TITLE SOLUTION STRUCTURE OF THE MU NER PROTEIN BY MULTIDIMENSIONAL NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN NER;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE MU;
SOURCE 3 ORGANISM_TAXID: 10677
KEYWDS DNA-BINDING PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.M.CLORE,T.E.STRZELECKA,A.M.GRONENBORN
REVDAT 3 23-FEB-22 1NER 1 KEYWDS REMARK
REVDAT 2 24-FEB-09 1NER 1 VERSN
REVDAT 1 07-DEC-95 1NER 0
JRNL AUTH T.E.STRZELECKA,G.M.CLORE,A.M.GRONENBORN
JRNL TITL THE SOLUTION STRUCTURE OF THE MU NER PROTEIN REVEALS A
JRNL TITL 2 HELIX-TURN-HELIX DNA RECOGNITION MOTIF.
JRNL REF STRUCTURE V. 3 1087 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 8590003
JRNL DOI 10.1016/S0969-2126(01)00244-1
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.M.GRONENBORN,P.T.WINGFIELD,G.M.CLORE
REMARK 1 TITL DETERMINATION OF THE SECONDARY STRUCTURE OF THE DNA BINDING
REMARK 1 TITL 2 PROTEIN NER FROM PHAGE MU USING 1H HOMONUCLEAR AND 15N-1H
REMARK 1 TITL 3 HETERONUCLEAR NMR SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 28 5081 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE 3D STRUCTURE OF THE MU NER PROTEIN BY MULTI-DIMENSIONAL
REMARK 3 HETERONUCLEAR NMR IS BASED ON 1546 EXPERIMENTAL RESTRAINTS
REMARK 3 COMPRISING THE FOLLOWING: 944 INTERPROTON DISTANCE
REMARK 3 RESTRAINTS [251 SEQUENTIAL; 202 SHORT RANGE (1<|I-J|<=5;
REMARK 3 157 LONG RANGE (|I-J|>5); AND 334 INTRARESIDUE]; 40
REMARK 3 DISTANCE RESTRAINTS FOR 20 BACKBONE HYDROGEN BONDS; 89
REMARK 3 TORSION ANGLE RESTRAINTS 56 PHI, 27 CH1 AND 6 CHI2); 46 3
REMARK 3 BOND HN-HA COUPLING CONSTANTS; 140 SECONDARY 13C SHIFTS (72
REMARK 3 CA AND 68 CB); 287 1H CHEMICAL SHIFTS (74 HA, 39 METHYL AND
REMARK 3 174 OTHER, WITH NO EXCHANGEABLE PROTON SHIFTS).
REMARK 3
REMARK 3 THE STRUCTURE WAS DETERMINED BY SIMULATED ANNEALING
REMARK 3 [NILGES, CLORE AND GRONENBORN (1988) FEBS LETT. 229, 317 -
REMARK 3 324] USING THE PROGRAM X-PLOR (BRUNGER) MODIFIED TO
REMARK 3 INCORPORATE COUPLING CONSTANT [GARRETT ET AL. AND CLORE
REMARK 3 (1994) J. MAGN. RESON. B104, 99 - 103], CARBON CHEMICAL
REMARK 3 SHIFT [KUSZEWSKI, QIN, GRONENBORN AND CLORE (1995) J. MAGN.
REMARK 3 RESON. B106, 92 - 96] AND PROTON CHEMICAL SHIFT
REMARK 3 [KUSZEWSKI, GRONENBORN AND CLORE (1995) J. MAGN. RESON.
REMARK 3 B107, 293 - 297] RESTRAINTS.
REMARK 3
REMARK 3 ENTRY 1NEQ IS THE RESTRAINED REGULARIZED MEAN STRUCTURE
REMARK 3 OBTAINED BY AVERAGING THE COORDINATES OF THE 30 SIMULATED
REMARK 3 ANNEALING STRUCTURES BEST FITTED TO EACH OTHER
REMARK 3 (RESIDUES 8 - 66). THE N- AND C-TERMINI ARE DISORDERED,
REMARK 3 AND THE NUMBER IN THE LAST COLUMN (THE B- FACTOR COLUMN)
REMARK 3 GIVES THE AVERAGE RMS TO THE MEAN COORDINATE POSITIONS.
REMARK 4
REMARK 4 1NER COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175261.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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
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 SER A 2 -92.44 52.19
REMARK 500 1 ASN A 3 -114.82 57.79
REMARK 500 1 GLU A 4 -6.40 -166.38
REMARK 500 1 LYS A 5 29.67 -77.01
REMARK 500 1 ALA A 6 -105.03 -57.66
REMARK 500 1 HIS A 10 162.63 -41.13
REMARK 500 1 ARG A 21 -94.51 -95.36
REMARK 500 1 LYS A 22 50.92 -154.79
REMARK 500 1 ALA A 40 -74.09 -55.77
REMARK 500 1 ASN A 41 -1.04 -56.35
REMARK 500 1 HIS A 46 99.11 -56.22
REMARK 500 1 TRP A 47 70.50 -160.73
REMARK 500 1 THR A 60 -169.83 -110.37
REMARK 500 1 SER A 68 5.82 -58.11
REMARK 500 1 ALA A 72 3.10 55.62
REMARK 500 2 ASN A 3 -163.92 51.81
REMARK 500 2 LYS A 5 84.03 -169.57
REMARK 500 2 ALA A 6 -176.74 49.29
REMARK 500 2 ASP A 8 -143.78 -75.33
REMARK 500 2 HIS A 10 167.59 -47.15
REMARK 500 2 LYS A 19 -9.07 -56.24
REMARK 500 2 ARG A 21 -97.13 -94.03
REMARK 500 2 LYS A 22 59.08 -155.08
REMARK 500 2 LEU A 25 -16.70 -47.15
REMARK 500 2 ALA A 35 164.44 -48.88
REMARK 500 2 HIS A 46 86.99 -64.59
REMARK 500 2 TRP A 47 73.65 -160.94
REMARK 500 2 THR A 60 -169.39 -111.02
REMARK 500 2 TYR A 70 -107.13 -118.34
REMARK 500 2 GLN A 71 -102.66 -158.76
REMARK 500 2 ALA A 72 -36.23 -148.10
REMARK 500 3 SER A 2 -108.62 -159.63
REMARK 500 3 ASN A 3 45.49 -162.30
REMARK 500 3 GLU A 4 108.58 56.24
REMARK 500 3 LYS A 5 -173.50 48.61
REMARK 500 3 ALA A 6 -89.04 -178.10
REMARK 500 3 ARG A 7 -101.16 -94.12
REMARK 500 3 ASP A 8 -148.15 -74.97
REMARK 500 3 HIS A 10 174.04 -47.82
REMARK 500 3 ARG A 21 -95.02 -98.04
REMARK 500 3 LYS A 22 49.27 -155.01
REMARK 500 3 ALA A 35 161.26 -45.67
REMARK 500 3 ALA A 40 -71.44 -56.09
REMARK 500 3 ASN A 41 -7.91 -58.49
REMARK 500 3 HIS A 46 79.72 -65.47
REMARK 500 3 TRP A 47 71.60 -165.44
REMARK 500 3 THR A 60 -164.97 -111.45
REMARK 500 3 GLU A 63 -4.69 -57.60
REMARK 500 3 GLN A 71 77.46 -160.33
REMARK 500 3 ALA A 72 -65.44 -169.51
REMARK 500
REMARK 500 THIS ENTRY HAS 438 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NEQ RELATED DB: PDB
DBREF 1NER A 1 74 UNP P06020 NER_BPMU 1 74
SEQRES 1 A 74 CYS SER ASN GLU LYS ALA ARG ASP TRP HIS ARG ALA ASP
SEQRES 2 A 74 VAL ILE ALA GLY LEU LYS LYS ARG LYS LEU SER LEU SER
SEQRES 3 A 74 ALA LEU SER ARG GLN PHE GLY TYR ALA PRO THR THR LEU
SEQRES 4 A 74 ALA ASN ALA LEU GLU ARG HIS TRP PRO LYS GLY GLU GLN
SEQRES 5 A 74 ILE ILE ALA ASN ALA LEU GLU THR LYS PRO GLU VAL ILE
SEQRES 6 A 74 TRP PRO SER ARG TYR GLN ALA GLY GLU
HELIX 1 1 ARG A 11 LEU A 18 1 8
HELIX 2 2 LEU A 25 PHE A 32 1 8
HELIX 3 3 PRO A 36 LEU A 43 1 8
HELIX 4 4 PRO A 48 LEU A 58 1 11
HELIX 5 5 PRO A 62 ILE A 65 1 4
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