Header list of 1kvn.pdb file
Complete list - t 27 2 Bytes
HEADER RNA BINDING PROTEIN 27-JAN-02 1KVN
TITLE SOLUTION STRUCTURE OF PROTEIN SRP19 OF THE ARHAEOGLOBUS FULGIDUS
TITLE 2 SIGNAL RECOGNITION PARTICLE, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SRP19;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SIGNAL RECOGNITION PARTICLE 19 KDA PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 2234;
SOURCE 4 GENE: AF1258;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PET-23C(+)
KEYWDS RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR O.N.PAKHOMOVA,S.DEEP,Q.HUANG,C.ZWIEB,A.P.HINCK
REVDAT 3 27-OCT-21 1KVN 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1KVN 1 VERSN
REVDAT 1 20-MAR-02 1KVN 0
JRNL AUTH O.N.PAKHOMOVA,S.DEEP,Q.HUANG,C.ZWIEB,A.P.HINCK
JRNL TITL SOLUTION STRUCTURE OF PROTEIN SRP19 OF ARCHAEOGLOBUS
JRNL TITL 2 FULGIDUS SIGNAL RECOGNITION PARTICLE.
JRNL REF J.MOL.BIOL. V. 317 145 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11916385
JRNL DOI 10.1006/JMBI.2002.5411
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER ANALYTIK GMBH (XWINNMR), BRUNGER, A.T.;
REMARK 3 CLORE, G.M., GRONENBORN, A.M., TJUNDRA, N. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 886 RESTRAINTS, 690 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 130
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 66 1H-15N RESIDUAL DIPOLAR COUPLING
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1KVN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015388.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 310
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 75 MM; 75 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 25 MM KH2PO4, 50MM NACL, 95%
REMARK 210 H2O, 5% D2O; 25 MM KH2PO4, 50 MM
REMARK 210 NACL, 99.99% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; 3D 15N-
REMARK 210 SEPARATED NOESY WITH 13C
REMARK 210 CHEMICAL SHIFT EVOLUTION IN F2
REMARK 210 DIMENTION; IPAP-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX2
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.8, PIPP 4.3.1, X-PLOR
REMARK 210 3.851, TALOS 98.040.28.02, PALES
REMARK 210 2.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED
REMARK 210 ANNEALING PROTOCOL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 26
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: IPAP-HSQC EXPERIMENT WAS PERFORMED IN A SAMPLE OF THE
REMARK 210 PROTEIN IN EITHER AN UNSTRESSED OR MECHANICALLY STRESSED 8%
REMARK 210 POLYACRYLAMIDE GEL.
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 LYS A 47 H GLU A 69 1.59
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 11 35.64 -96.23
REMARK 500 1 ARG A 22 29.12 -155.28
REMARK 500 1 ASN A 31 69.14 61.58
REMARK 500 1 LEU A 46 113.27 -177.13
REMARK 500 1 LYS A 47 -39.74 172.49
REMARK 500 1 LYS A 57 -167.31 38.53
REMARK 500 1 SER A 58 -163.93 42.52
REMARK 500 1 LYS A 70 -69.09 157.36
REMARK 500 1 ARG A 71 128.45 59.04
REMARK 500 1 LYS A 74 -113.06 -125.67
REMARK 500 1 LYS A 101 -76.07 -117.13
REMARK 500 2 LYS A 2 -154.29 -124.39
REMARK 500 2 ARG A 21 97.68 45.38
REMARK 500 2 ASN A 31 128.94 61.76
REMARK 500 2 LEU A 46 126.96 -175.85
REMARK 500 2 LYS A 47 -43.59 -178.00
REMARK 500 2 LYS A 53 96.61 49.57
REMARK 500 2 LYS A 54 -130.83 -90.81
REMARK 500 2 LYS A 70 56.56 176.02
REMARK 500 2 LYS A 74 -134.15 -112.21
REMARK 500 2 GLN A 95 80.31 20.23
REMARK 500 2 LYS A 96 -74.91 -89.91
REMARK 500 2 LYS A 99 92.19 48.14
REMARK 500 2 LYS A 101 -44.59 -154.27
REMARK 500 3 LYS A 2 -96.04 -155.61
REMARK 500 3 ARG A 22 36.94 -159.82
REMARK 500 3 LEU A 46 128.15 -176.36
REMARK 500 3 LYS A 47 -50.99 -173.96
REMARK 500 3 LYS A 54 168.94 53.71
REMARK 500 3 LYS A 70 60.00 170.03
REMARK 500 3 LYS A 74 -101.16 -123.61
REMARK 500 3 GLN A 95 74.00 44.04
REMARK 500 3 LYS A 97 -87.29 53.77
REMARK 500 3 LYS A 100 -62.90 -148.84
REMARK 500 3 LYS A 101 -63.61 64.45
REMARK 500 4 LYS A 2 -114.00 -145.95
REMARK 500 4 LEU A 11 39.09 -93.36
REMARK 500 4 ARG A 22 34.12 -160.65
REMARK 500 4 ASN A 31 117.70 67.85
REMARK 500 4 LEU A 46 124.93 -175.91
REMARK 500 4 LYS A 47 -44.74 -176.00
REMARK 500 4 LYS A 54 93.11 44.77
REMARK 500 4 TYR A 55 135.23 62.26
REMARK 500 4 TRP A 60 77.82 -167.80
REMARK 500 4 LYS A 70 -44.73 -163.27
REMARK 500 4 ARG A 71 -160.09 47.25
REMARK 500 4 LYS A 74 -72.79 -98.30
REMARK 500 4 GLN A 95 175.27 58.83
REMARK 500 4 LYS A 96 -77.85 -171.19
REMARK 500 5 LYS A 2 -92.86 -160.68
REMARK 500
REMARK 500 THIS ENTRY HAS 119 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 17 0.31 SIDE CHAIN
REMARK 500 1 ARG A 21 0.30 SIDE CHAIN
REMARK 500 1 ARG A 22 0.26 SIDE CHAIN
REMARK 500 1 ARG A 25 0.24 SIDE CHAIN
REMARK 500 1 ARG A 26 0.28 SIDE CHAIN
REMARK 500 1 ARG A 49 0.22 SIDE CHAIN
REMARK 500 1 ARG A 65 0.30 SIDE CHAIN
REMARK 500 1 ARG A 71 0.31 SIDE CHAIN
REMARK 500 1 ARG A 83 0.26 SIDE CHAIN
REMARK 500 1 ARG A 89 0.32 SIDE CHAIN
REMARK 500 1 ARG A 93 0.30 SIDE CHAIN
REMARK 500 2 ARG A 17 0.25 SIDE CHAIN
REMARK 500 2 ARG A 21 0.29 SIDE CHAIN
REMARK 500 2 ARG A 22 0.25 SIDE CHAIN
REMARK 500 2 ARG A 25 0.21 SIDE CHAIN
REMARK 500 2 ARG A 26 0.20 SIDE CHAIN
REMARK 500 2 ARG A 49 0.32 SIDE CHAIN
REMARK 500 2 ARG A 65 0.27 SIDE CHAIN
REMARK 500 2 ARG A 71 0.30 SIDE CHAIN
REMARK 500 2 ARG A 83 0.31 SIDE CHAIN
REMARK 500 2 ARG A 89 0.27 SIDE CHAIN
REMARK 500 2 ARG A 93 0.32 SIDE CHAIN
REMARK 500 3 ARG A 17 0.30 SIDE CHAIN
REMARK 500 3 ARG A 21 0.31 SIDE CHAIN
REMARK 500 3 ARG A 22 0.31 SIDE CHAIN
REMARK 500 3 ARG A 25 0.24 SIDE CHAIN
REMARK 500 3 ARG A 26 0.23 SIDE CHAIN
REMARK 500 3 ARG A 49 0.26 SIDE CHAIN
REMARK 500 3 ARG A 65 0.31 SIDE CHAIN
REMARK 500 3 ARG A 71 0.23 SIDE CHAIN
REMARK 500 3 ARG A 83 0.23 SIDE CHAIN
REMARK 500 3 ARG A 89 0.21 SIDE CHAIN
REMARK 500 3 ARG A 93 0.20 SIDE CHAIN
REMARK 500 4 ARG A 17 0.17 SIDE CHAIN
REMARK 500 4 ARG A 21 0.17 SIDE CHAIN
REMARK 500 4 ARG A 22 0.28 SIDE CHAIN
REMARK 500 4 ARG A 25 0.24 SIDE CHAIN
REMARK 500 4 ARG A 26 0.26 SIDE CHAIN
REMARK 500 4 ARG A 49 0.27 SIDE CHAIN
REMARK 500 4 ARG A 65 0.20 SIDE CHAIN
REMARK 500 4 ARG A 71 0.22 SIDE CHAIN
REMARK 500 4 ARG A 83 0.30 SIDE CHAIN
REMARK 500 4 ARG A 89 0.31 SIDE CHAIN
REMARK 500 4 ARG A 93 0.31 SIDE CHAIN
REMARK 500 5 ARG A 17 0.16 SIDE CHAIN
REMARK 500 5 ARG A 21 0.30 SIDE CHAIN
REMARK 500 5 ARG A 22 0.29 SIDE CHAIN
REMARK 500 5 ARG A 25 0.28 SIDE CHAIN
REMARK 500 5 ARG A 26 0.31 SIDE CHAIN
REMARK 500 5 ARG A 49 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 108 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4935 RELATED DB: BMRB
REMARK 900 DEPOSITION 4935 CONTAINS ASSIGNMENTS FOR PROTEIN SRP19 OF
REMARK 900 ARCHAEOGLOBUS FULGIDUS.
REMARK 900 RELATED ID: 1KVV RELATED DB: PDB
REMARK 900 1KVV CONTAINS THE COORDINATES FOR THE MINIMIZED AVERAGE STRUCTURE
REMARK 900 FOR THE SAME PROTEIN.
DBREF 1KVN A 1 104 UNP O29010 SRP19_ARCFU 1 104
SEQADV 1KVN SER A 4 UNP O29010 CYS 4 ENGINEERED MUTATION
SEQADV 1KVN SER A 41 UNP O29010 CYS 41 ENGINEERED MUTATION
SEQRES 1 A 104 MET LYS GLU SER VAL VAL TRP THR VAL ASN LEU ASP SER
SEQRES 2 A 104 LYS LYS SER ARG ALA GLU GLY ARG ARG ILE PRO ARG ARG
SEQRES 3 A 104 PHE ALA VAL PRO ASN VAL LYS LEU HIS GLU LEU VAL GLU
SEQRES 4 A 104 ALA SER LYS GLU LEU GLY LEU LYS PHE ARG ALA GLU GLU
SEQRES 5 A 104 LYS LYS TYR PRO LYS SER TRP TRP GLU GLU GLY GLY ARG
SEQRES 6 A 104 VAL VAL VAL GLU LYS ARG GLY THR LYS THR LYS LEU MET
SEQRES 7 A 104 ILE GLU LEU ALA ARG LYS ILE ALA GLU ILE ARG GLU GLN
SEQRES 8 A 104 LYS ARG GLU GLN LYS LYS ASP LYS LYS LYS LYS LYS LYS
HELIX 1 1 PRO A 24 ALA A 28 5 5
HELIX 2 2 LYS A 33 GLY A 45 1 13
HELIX 3 3 LYS A 74 GLN A 95 1 22
HELIX 4 4 LYS A 96 LYS A 101 1 6
SHEET 1 A 3 SER A 4 TRP A 7 0
SHEET 2 A 3 ARG A 65 VAL A 68 -1 O VAL A 66 N VAL A 6
SHEET 3 A 3 PHE A 48 ALA A 50 -1 N ARG A 49 O VAL A 67
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