Header list of 1r4g.pdb file
Complete list - r 2 2 Bytes
HEADER VIRAL PROTEIN, TRANSFERASE 06-OCT-03 1R4G
TITLE SOLUTION STRUCTURE OF THE SENDAI VIRUS PROTEIN X C-SUBDOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA POLYMERASE ALPHA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-SUBDOMAIN (RESIDUES 516-568);
COMPND 5 SYNONYM: NUCLEOCAPSID PHOSPHOPROTEIN, PROTEIN X;
COMPND 6 EC: 2.7.7.48;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SENDAI VIRUS (STRAIN HARRIS);
SOURCE 3 ORGANISM_TAXID: 11196;
SOURCE 4 STRAIN: HARRIS;
SOURCE 5 GENE: P;
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: PET
KEYWDS THREE HELIX-BUNDLE, VIRAL PROTEIN, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.BLANCHARD,N.TARBOURIECH,M.BLACKLEDGE,P.TIMMINS,W.P.BURMEISTER,
AUTHOR 2 R.W.RUIGROK,D.MARION
REVDAT 3 02-MAR-22 1R4G 1 REMARK
REVDAT 2 24-FEB-09 1R4G 1 VERSN
REVDAT 1 09-MAR-04 1R4G 0
JRNL AUTH L.BLANCHARD,N.TARBOURIECH,M.BLACKLEDGE,P.TIMMINS,
JRNL AUTH 2 W.P.BURMEISTER,R.W.RUIGROK,D.MARION
JRNL TITL STRUCTURE AND DYNAMICS OF THE NUCLEOCAPSID-BINDING DOMAIN OF
JRNL TITL 2 THE SENDAI VIRUS PHOSPHOPROTEIN IN SOLUTION
JRNL REF VIROLOGY V. 319 201 2004
JRNL REFN ISSN 0042-6822
JRNL PMID 14980481
JRNL DOI 10.1016/J.VIROL.2003.10.029
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.MARION,N.TARBOURIECH,R.W.RUIGROK,W.P.BURMEISTER,
REMARK 1 AUTH 2 L.BLANCHARD
REMARK 1 TITL ASSIGNMENT OF THE 1H, 15N AND 13C RESONANCES OF THE
REMARK 1 TITL 2 NUCLEOCAPSID-BINDING DOMAIN OF THE SENDAI VIRUS
REMARK 1 TITL 3 PHOSPHOPROTEIN
REMARK 1 REF J.BIOMOL.NMR V. 21 75 2001
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1011990021282
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER 2.98, SCULPTOR
REMARK 3 AUTHORS : ACCELRYS, INC. (DISCOVER), HUS & BLACKLEDGE
REMARK 3 (SCULPTOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R4G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020424.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 0.5M NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.2-1.5MM 15N/13C PROTEIN X,
REMARK 210 50MM POTASSIUM PHOSPHATE BUFFER,
REMARK 210 0.5M NACL, 10MM DTT,
REMARK 210 ANTIPROTEASE COCKTAIL; 1MM 15N/
REMARK 210 13C PROTEIN X, 5% C12/E6/HEXANOL,
REMARK 210 50MM POTASSIUM PHOSPHATE BUFFER,
REMARK 210 0.5M NACL, 10MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D HNCO TYPE
REMARK 210 EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: SAMPLE 2 WAS USED TO MEASURE THE THREE DIFFERENT TYPES OF
REMARK 210 RESIDUAL DIPOLAR COUPLINGS USED FOR STRUCTURE REFINEMENT.
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 8 VAL A 552 CA - CB - CG1 ANGL. DEV. = 9.2 DEGREES
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 528 -48.58 -162.28
REMARK 500 1 SER A 532 -152.80 -101.42
REMARK 500 1 LYS A 545 12.96 -66.34
REMARK 500 1 CYS A 546 177.46 -59.46
REMARK 500 1 LYS A 547 -56.63 -172.16
REMARK 500 1 THR A 548 -112.56 -99.47
REMARK 500 1 ASP A 549 -55.02 -156.93
REMARK 500 2 SER A 532 -154.84 -95.32
REMARK 500 2 LYS A 545 7.70 -64.15
REMARK 500 2 CYS A 546 176.27 -57.86
REMARK 500 2 LYS A 547 -63.91 -169.63
REMARK 500 2 THR A 548 -134.81 -93.03
REMARK 500 2 ASP A 549 -51.17 -137.61
REMARK 500 2 SER A 565 51.57 76.85
REMARK 500 2 THR A 567 76.35 56.72
REMARK 500 3 LEU A 531 -174.28 -65.86
REMARK 500 3 SER A 532 -150.60 -97.77
REMARK 500 3 LYS A 545 6.02 -65.98
REMARK 500 3 CYS A 546 175.37 -58.37
REMARK 500 3 LYS A 547 -64.15 -172.72
REMARK 500 3 THR A 548 -119.22 -94.79
REMARK 500 3 ASP A 549 -48.39 -151.67
REMARK 500 3 THR A 567 -65.60 73.89
REMARK 500 4 THR A 518 170.08 146.99
REMARK 500 4 SER A 528 -41.76 -140.88
REMARK 500 4 SER A 532 -160.21 -60.60
REMARK 500 4 LYS A 545 14.06 -67.85
REMARK 500 4 CYS A 546 178.38 -58.80
REMARK 500 4 LYS A 547 -62.39 -167.46
REMARK 500 4 THR A 548 -142.69 -107.79
REMARK 500 5 SER A 528 -49.67 -163.88
REMARK 500 5 PRO A 530 -108.58 -70.33
REMARK 500 5 LEU A 531 179.50 89.99
REMARK 500 5 SER A 532 -150.41 -99.76
REMARK 500 5 LYS A 545 10.76 -68.20
REMARK 500 5 CYS A 546 177.42 -56.90
REMARK 500 5 LYS A 547 -63.20 -169.08
REMARK 500 5 THR A 548 -108.53 -102.96
REMARK 500 5 ASP A 549 -41.52 -163.08
REMARK 500 5 SER A 565 48.01 71.57
REMARK 500 6 THR A 518 -163.94 178.37
REMARK 500 6 LEU A 531 -169.95 -76.39
REMARK 500 6 SER A 532 -156.10 -96.55
REMARK 500 6 THR A 548 -136.15 -82.67
REMARK 500 6 ASP A 549 -59.94 -139.45
REMARK 500 6 THR A 567 62.96 -112.30
REMARK 500 7 SER A 528 -103.32 -66.95
REMARK 500 7 SER A 532 -142.56 -103.08
REMARK 500 7 LYS A 545 9.65 -65.29
REMARK 500 7 THR A 548 -149.36 -99.66
REMARK 500
REMARK 500 THIS ENTRY HAS 134 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 TYR A 539 0.08 SIDE CHAIN
REMARK 500 2 TYR A 539 0.09 SIDE CHAIN
REMARK 500 4 TYR A 539 0.08 SIDE CHAIN
REMARK 500 5 TYR A 539 0.10 SIDE CHAIN
REMARK 500 6 TYR A 539 0.07 SIDE CHAIN
REMARK 500 8 TYR A 539 0.10 SIDE CHAIN
REMARK 500 9 TYR A 539 0.09 SIDE CHAIN
REMARK 500 10 TYR A 539 0.08 SIDE CHAIN
REMARK 500 11 TYR A 539 0.11 SIDE CHAIN
REMARK 500 12 TYR A 539 0.14 SIDE CHAIN
REMARK 500 13 TYR A 539 0.07 SIDE CHAIN
REMARK 500 14 TYR A 539 0.14 SIDE CHAIN
REMARK 500 15 TYR A 539 0.11 SIDE CHAIN
REMARK 500 18 TYR A 539 0.10 SIDE CHAIN
REMARK 500 19 TYR A 539 0.12 SIDE CHAIN
REMARK 500 20 TYR A 539 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4999 RELATED DB: BMRB
REMARK 900 1H, 15N AND 13C RESONANCES OF PROTEIN X
DBREF 1R4G A 516 568 UNP P04859 PHOSP_SENDH 516 568
SEQRES 1 A 53 LYS PRO THR MET HIS SER LEU ARG LEU VAL ILE GLU SER
SEQRES 2 A 53 SER PRO LEU SER ARG ALA GLU LYS ALA ALA TYR VAL LYS
SEQRES 3 A 53 SER LEU SER LYS CYS LYS THR ASP GLN GLU VAL LYS ALA
SEQRES 4 A 53 VAL MET GLU LEU VAL GLU GLU ASP ILE GLU SER LEU THR
SEQRES 5 A 53 ASN
HELIX 1 1 THR A 518 GLU A 527 1 10
HELIX 2 2 ARG A 533 LYS A 545 1 13
HELIX 3 3 ASP A 549 THR A 567 1 19
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 - r 2 2 Bytes