Header list of 1xne.pdb file
Complete list - r 25 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 04-OCT-04 1XNE
TITLE SOLUTION STRUCTURE OF PYROCOCCUS FURIOSUS PROTEIN PF0470: THE
TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET PFR14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN PF0469;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 186497;
SOURCE 4 STRAIN: DSM 3638;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GFT NMR, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, PSI,
KEYWDS 2 NESG, PFR14, ALPHA AND BETA PROTEIN, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.LIU,R.XIAO,D.PARISH,L.MA,D.SUKUMARAN,T.ACTON,G.T.MONTELIONE,
AUTHOR 2 T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 13-JUL-11 1XNE 1 VERSN
REVDAT 3 24-FEB-09 1XNE 1 VERSN
REVDAT 2 25-JAN-05 1XNE 1 AUTHOR KEYWDS
REVDAT 1 14-DEC-04 1XNE 0
JRNL AUTH G.LIU,Y.SHEN,H.S.ATREYA,D.PARISH,Y.SHAO,D.K.SUKUMARAN,
JRNL AUTH 2 R.XIAO,A.YEE,A.LEMAK,A.BHATTACHARYA,T.A.ACTON,
JRNL AUTH 3 C.H.ARROWSMITH,G.T.MONTELIONE,T.SZYPERSKI
JRNL TITL NMR DATA COLLECTION AND ANALYSIS PROTOCOL FOR
JRNL TITL 2 HIGH-THROUGHPUT PROTEIN STRUCTURE DETERMINATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 10487 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 16027363
JRNL DOI 10.1073/PNAS.0504338102
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUENTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XNE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-04.
REMARK 100 THE RCSB ID CODE IS RCSB030544.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.02 MM, NMR BUFFER 6.5, 5% D2O,
REMARK 210 0.02% NAN3, 10MM DTT, 5MM CACL2,
REMARK 210 100MM NACL, 20MM MES, PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : GFT (4,3)D HNNCABCA; GFT (4,3)D
REMARK 210 CABCA(CO)NHN; GFT (4,3)D
REMARK 210 HABCAB(CO)NHN; GFT (4,3) HCCH;
REMARK 210 SIMULTANEOUS HETERONUCLEAR
REMARK 210 RESOLVED -NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3, XEASY 1.3.1.3,
REMARK 210 DYANA 1.5, AUTOASSIGN 1.13.2,
REMARK 210 CYANA 1.0.5, AUTOSTRUCTURE 2.0.0
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: HIGH THROUGHPUT STRUCTURE DETERMINATION BY GFT NMR
REMARK 210 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: 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 9 H LEU A 13 1.50
REMARK 500 H ILE A 41 O ALA A 49 1.55
REMARK 500 O SER A 78 H ALA A 82 1.56
REMARK 500 O GLU A 50 H ARG A 106 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 ARG A 26 147.96 -173.93
REMARK 500 1 ALA A 28 -84.29 -42.39
REMARK 500 1 TYR A 29 160.21 56.49
REMARK 500 1 GLN A 31 -9.72 83.77
REMARK 500 1 LEU A 32 -59.13 -138.70
REMARK 500 1 ILE A 35 154.81 -40.34
REMARK 500 1 LEU A 46 -43.38 -165.96
REMARK 500 1 THR A 59 124.15 69.14
REMARK 500 1 TYR A 90 87.96 54.96
REMARK 500 1 GLU A 95 165.72 178.08
REMARK 500 1 ARG A 110 162.16 -44.40
REMARK 500 2 LYS A 21 99.75 -55.80
REMARK 500 2 ARG A 26 59.28 -145.57
REMARK 500 2 VAL A 27 141.33 62.18
REMARK 500 2 ALA A 28 -84.57 -63.36
REMARK 500 2 TYR A 29 153.34 59.16
REMARK 500 2 GLN A 31 -5.43 80.98
REMARK 500 2 LEU A 32 -59.74 -140.45
REMARK 500 2 ILE A 35 156.18 -41.19
REMARK 500 2 LEU A 46 -45.71 -162.32
REMARK 500 2 GLU A 58 -60.85 -97.91
REMARK 500 2 MET A 89 -46.79 -174.66
REMARK 500 2 LYS A 92 157.79 -47.41
REMARK 500 2 TRP A 93 110.22 66.48
REMARK 500 2 LYS A 94 -74.82 -54.82
REMARK 500 2 TYR A 98 -49.09 -159.42
REMARK 500 2 VAL A 100 73.27 -153.94
REMARK 500 2 ARG A 110 153.31 -39.08
REMARK 500 2 LYS A 112 -178.51 -60.64
REMARK 500 3 ARG A 26 -70.67 -164.56
REMARK 500 3 TYR A 29 160.59 -47.80
REMARK 500 3 GLN A 31 -55.75 -165.15
REMARK 500 3 ILE A 35 161.35 -43.70
REMARK 500 3 LEU A 46 -44.82 -161.01
REMARK 500 3 LYS A 76 64.40 62.90
REMARK 500 3 PHE A 86 48.98 -83.69
REMARK 500 3 HIS A 87 -54.39 -167.59
REMARK 500 3 LYS A 94 -55.01 -148.57
REMARK 500 3 GLU A 95 82.36 63.02
REMARK 500 3 ARG A 110 164.52 -42.88
REMARK 500 4 ARG A 22 -45.88 -143.48
REMARK 500 4 ALA A 28 -107.45 54.45
REMARK 500 4 TYR A 29 172.20 52.44
REMARK 500 4 GLN A 31 -64.30 -156.29
REMARK 500 4 ILE A 35 152.27 -41.59
REMARK 500 4 LEU A 46 -46.31 -156.56
REMARK 500 4 GLU A 53 145.64 -172.53
REMARK 500 4 HIS A 87 -56.09 176.84
REMARK 500 4 ASN A 88 88.77 -65.21
REMARK 500 4 MET A 89 121.25 179.94
REMARK 500
REMARK 500 THIS ENTRY HAS 303 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PFR14 RELATED DB: TARGETDB
DBREF 1XNE A 1 113 UNP Q8U3J6 Q8U3J6_PYRFU 1 113
SEQRES 1 A 113 MET LYS VAL TYR ARG LEU TYR LEU LYS ASP GLU TYR LEU
SEQRES 2 A 113 GLU MET VAL LYS SER GLY LYS LYS ARG ILE GLU VAL ARG
SEQRES 3 A 113 VAL ALA TYR PRO GLN LEU LYS ASP ILE LYS ARG GLY ASP
SEQRES 4 A 113 LYS ILE ILE PHE ASN ASP LEU ILE PRO ALA GLU VAL VAL
SEQRES 5 A 113 GLU VAL LYS LYS TYR GLU THR PHE ARG GLN VAL LEU ARG
SEQRES 6 A 113 GLU GLU PRO ILE ASP LYS ILE PHE PRO ASP LYS PRO SER
SEQRES 7 A 113 PHE GLU LYS ALA LEU LYS ARG PHE HIS ASN MET TYR PRO
SEQRES 8 A 113 LYS TRP LYS GLU TYR ARG TYR GLY VAL LEU ALA ILE LYS
SEQRES 9 A 113 PHE ARG VAL LEU GLY ARG ASP LYS GLU
HELIX 1 1 LYS A 9 GLY A 19 1 11
HELIX 2 2 THR A 59 GLU A 67 1 9
HELIX 3 3 PRO A 68 PHE A 73 1 6
HELIX 4 4 SER A 78 HIS A 87 1 10
SHEET 1 A 5 VAL A 3 LEU A 6 0
SHEET 2 A 5 LYS A 40 PHE A 43 1 O ILE A 42 N LEU A 6
SHEET 3 A 5 ILE A 47 LYS A 56 -1 O ALA A 49 N ILE A 41
SHEET 4 A 5 LEU A 101 VAL A 107 -1 O ARG A 106 N GLU A 50
SHEET 5 A 5 ILE A 23 VAL A 25 -1 N GLU A 24 O ILE A 103
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 25 2 Bytes