Header list of 1m8m.pdb file
Complete list - 21 20 Bytes
HEADER STRUCTURAL PROTEIN 25-JUL-02 1M8M
TITLE SOLID-STATE MAS NMR STRUCTURE OF THE A-SPECTRIN SH3 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPECTRIN ALPHA CHAIN, BRAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SRC HOMOLOGY 3 DOMAIN (RESIDUES 965-1025);
COMPND 5 SYNONYM: SPECTRIN, NON-ERYTHROID ALPHA CHAIN, FODRIN ALPHA CHAIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 ORGAN: BRAIN;
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: PET3D
KEYWDS SOLID-STATE MAS NMR STRUCTURE, STRUCTURAL PROTEIN
EXPDTA SOLID-STATE NMR
NUMMDL 12
AUTHOR F.CASTELLANI,B.VAN ROSSUM,A.DIEHL,M.SCHUBERT,K.REHBEIN,H.OSCHKINAT
REVDAT 4 21-DEC-22 1M8M 1 SEQADV
REVDAT 3 23-FEB-22 1M8M 1 REMARK
REVDAT 2 24-FEB-09 1M8M 1 VERSN
REVDAT 1 20-NOV-02 1M8M 0
JRNL AUTH F.CASTELLANI,B.VAN ROSSUM,A.DIEHL,M.SCHUBERT,K.REHBEIN,
JRNL AUTH 2 H.OSCHKINAT
JRNL TITL STRUCTURE OF A PROTEIN DETERMINED BY SOLID-STATE
JRNL TITL 2 MAGIC-ANGLE-SPINNING NMR SPECTROSCOPY
JRNL REF NATURE V. 420 98 2002
JRNL REFN ISSN 0028-0836
JRNL PMID 12422222
JRNL DOI 10.1038/NATURE01070
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUENGER ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 286 13C-13C RESTRAINTS AND 6 15N-15N RESTRAINTS. ALL RESTRAINTS
REMARK 3 ARE EXTRACTED FROM PDSD SPECTRA.
REMARK 4
REMARK 4 1M8M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016732.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 280
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : SOLID SAMPLE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : A 200 MM (NH4)2SO4 SOLUTION WAS
REMARK 210 ADDED TO A 1.15 MM SH3 SOLUTION
REMARK 210 (PH=3.5) AT A VOLUME RATIO 1:1.
REMARK 210 THE SOLID SAMPLE WAS OBTAINED BY
REMARK 210 PRECIPITATION, CHANGING THE PH
REMARK 210 TO 7.5 IN NH3 ATMOSPHERE.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 13C-13C PROTON-DRIVEN SPIN-
REMARK 210 DIFFUSION (PDSD); 15N-15N PROTON-
REMARK 210 DRIVEN SPIN-DIFFUSION (PDSD)
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, SPARKY 3.1, CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
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: THIS SOLID-STATE NMR STRUCTURE WAS DETERMINED BY COMBINING
REMARK 210 BROAD-BAND RECOUPLING METHODS WITH DILUTION OF THE 13C SPINS
REMARK 217
REMARK 217 SOLID STATE NMR STUDY
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 217 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 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 1-12
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 GLY A 5
REMARK 465 LYS A 6
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 8 -71.71 -178.50
REMARK 500 1 VAL A 9 64.67 -163.51
REMARK 500 1 TYR A 13 -77.72 177.19
REMARK 500 1 ASP A 14 -34.17 169.29
REMARK 500 1 TYR A 15 -62.58 68.25
REMARK 500 1 GLN A 16 88.65 44.94
REMARK 500 1 LYS A 18 106.85 -176.69
REMARK 500 1 SER A 19 161.54 59.61
REMARK 500 1 PRO A 20 63.16 -69.55
REMARK 500 1 ARG A 21 -61.60 -134.68
REMARK 500 1 VAL A 23 101.40 -59.21
REMARK 500 1 LYS A 27 -79.79 62.85
REMARK 500 1 ILE A 30 172.21 57.66
REMARK 500 1 ASN A 35 -164.01 62.20
REMARK 500 1 TRP A 41 57.36 -177.10
REMARK 500 1 TRP A 42 29.67 -152.66
REMARK 500 1 ASN A 47 49.31 -159.28
REMARK 500 1 ASP A 48 82.39 61.70
REMARK 500 1 GLN A 50 86.12 -69.93
REMARK 500 1 VAL A 58 -80.96 -74.27
REMARK 500 1 LYS A 59 24.78 -147.88
REMARK 500 2 TYR A 13 63.02 61.87
REMARK 500 2 ASP A 14 -80.83 -60.73
REMARK 500 2 TYR A 15 -165.27 61.84
REMARK 500 2 GLN A 16 -170.26 -69.91
REMARK 500 2 SER A 19 -61.61 -178.90
REMARK 500 2 ARG A 21 128.62 63.43
REMARK 500 2 MET A 25 174.37 75.73
REMARK 500 2 LYS A 26 -164.83 -176.80
REMARK 500 2 LYS A 27 165.92 62.97
REMARK 500 2 ASP A 29 144.99 62.95
REMARK 500 2 LEU A 31 -106.07 -130.31
REMARK 500 2 ASN A 35 -80.12 62.58
REMARK 500 2 SER A 36 150.27 62.72
REMARK 500 2 THR A 37 -47.93 -145.82
REMARK 500 2 ASN A 38 -161.60 -100.47
REMARK 500 2 LYS A 39 97.77 -47.72
REMARK 500 2 TRP A 41 -35.03 -177.12
REMARK 500 2 TRP A 42 -96.84 -46.82
REMARK 500 2 ARG A 49 -170.02 177.46
REMARK 500 2 PHE A 52 31.28 -164.23
REMARK 500 2 ALA A 55 -70.97 67.49
REMARK 500 2 ALA A 56 -80.29 63.06
REMARK 500 2 VAL A 58 -70.99 -152.36
REMARK 500 2 LYS A 59 -68.02 -144.59
REMARK 500 2 LEU A 61 130.46 -176.38
REMARK 500 3 LEU A 10 -177.23 -62.10
REMARK 500 3 LEU A 12 -62.97 75.10
REMARK 500 3 ASP A 14 -174.43 46.88
REMARK 500 3 GLN A 16 120.02 64.85
REMARK 500
REMARK 500 THIS ENTRY HAS 342 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1M8M A 2 62 UNP P07751 SPTA2_CHICK 965 1025
SEQADV 1M8M MET A 1 UNP P07751 INITIATING METHIONINE
SEQRES 1 A 62 MET ASP GLU THR GLY LYS GLU LEU VAL LEU ALA LEU TYR
SEQRES 2 A 62 ASP TYR GLN GLU LYS SER PRO ARG GLU VAL THR MET LYS
SEQRES 3 A 62 LYS GLY ASP ILE LEU THR LEU LEU ASN SER THR ASN LYS
SEQRES 4 A 62 ASP TRP TRP LYS VAL GLU VAL ASN ASP ARG GLN GLY PHE
SEQRES 5 A 62 VAL PRO ALA ALA TYR VAL LYS LYS LEU ASP
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 - 21 20 Bytes