Header list of 1xn9.pdb file
Complete list - r 2 2 Bytes
HEADER RIBOSOME 04-OCT-04 1XN9
TITLE SOLUTION STRUCTURE OF METHANOSARCINA MAZEI PROTEIN RPS24E: THE
TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET MAR11
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 30S RIBOSOMAL PROTEIN S24E;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOSARCINA MAZEI;
SOURCE 3 ORGANISM_TAXID: 2209;
SOURCE 4 GENE: RPS24E;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA+ALPHA, GFT NMR, STRUCTURAL GENOMICS, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, PSI, NESG, MAR11, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, RIBOSOME
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 02-MAR-22 1XN9 1 REMARK
REVDAT 3 24-FEB-09 1XN9 1 VERSN
REVDAT 2 25-JAN-05 1XN9 1 AUTHOR KEYWDS
REVDAT 1 14-DEC-04 1XN9 0
JRNL AUTH G.LIU,R.XIAO,D.PARISH,L.MA,D.SUKUMARAN,T.ACTON,
JRNL AUTH 2 G.T.MONTELIONE,T.SZYPERSKI
JRNL TITL SOLUTION STRUCTURE OF METHANOSARCINA MAZEI PROTEIN RPS24E:
JRNL TITL 2 THE NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET MAR11
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, DYANA 1.5
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), GUENTERT, P. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XN9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030543.
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 : 1.04 MM, NMR BUFFER 6.5, 10MM
REMARK 210 DTT, 5MM CACL2, 100MM NACL, 20MM
REMARK 210 NH4OAC, 0.02% NAN3, 5% D2O, PH
REMARK 210 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; SIMULTANEOUS
REMARK 210 HETERONUCLEAR RESOLVED [1H,1H]-
REMARK 210 NOESY; GFT (4,3)D HCCH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.1.3, DYANA 1.5,
REMARK 210 AUTOASSIGN 1.13.2, AUTOSTRUCTURE
REMARK 210 2.0.0, CYANA 1.0.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING GFT 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 H LYS A 56 O LYS A 65 1.54
REMARK 500 OD1 ASN A 11 H LEU A 14 1.56
REMARK 500 O ARG A 76 H VAL A 80 1.56
REMARK 500 O VAL A 51 H LYS A 69 1.58
REMARK 500 O LEU A 39 H LEU A 43 1.60
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 ASN A 15 32.15 79.75
REMARK 500 1 ARG A 54 130.60 177.48
REMARK 500 1 GLN A 62 57.49 38.11
REMARK 500 1 ASN A 89 39.96 -162.45
REMARK 500 1 PRO A 92 -162.61 -75.04
REMARK 500 1 SER A 94 -137.56 -143.44
REMARK 500 1 THR A 96 132.43 179.18
REMARK 500 1 GLU A 99 -150.73 -138.72
REMARK 500 1 GLU A 100 155.28 175.91
REMARK 500 2 GLN A 62 60.57 37.11
REMARK 500 2 VAL A 85 -140.53 -112.74
REMARK 500 2 LEU A 86 97.21 -43.10
REMARK 500 2 ASN A 89 53.90 -149.84
REMARK 500 2 SER A 94 118.42 171.58
REMARK 500 2 THR A 96 -143.86 -119.50
REMARK 500 2 GLU A 99 139.76 -174.22
REMARK 500 2 GLU A 100 153.98 179.16
REMARK 500 3 ILE A 6 -71.70 -81.54
REMARK 500 3 ASN A 15 40.96 80.84
REMARK 500 3 ARG A 54 121.41 -174.99
REMARK 500 3 MET A 61 24.78 -148.56
REMARK 500 3 GLN A 62 51.53 36.26
REMARK 500 3 VAL A 85 -138.01 -115.69
REMARK 500 3 LEU A 86 84.59 -59.69
REMARK 500 3 ASN A 89 49.39 -162.30
REMARK 500 3 PRO A 92 -166.29 -74.96
REMARK 500 3 SER A 94 121.80 168.90
REMARK 500 3 GLU A 95 143.96 -171.67
REMARK 500 3 THR A 96 -142.67 -102.23
REMARK 500 3 GLU A 99 139.76 -174.39
REMARK 500 4 ILE A 6 -73.97 -76.23
REMARK 500 4 ASN A 15 43.20 76.06
REMARK 500 4 ARG A 54 127.68 -170.73
REMARK 500 4 MET A 61 23.34 -142.29
REMARK 500 4 GLN A 62 58.49 36.40
REMARK 500 4 VAL A 85 -135.69 -120.89
REMARK 500 4 LEU A 86 76.85 -64.55
REMARK 500 4 ASN A 89 46.90 -109.90
REMARK 500 4 SER A 94 118.66 74.41
REMARK 500 4 GLU A 95 138.41 -176.34
REMARK 500 4 THR A 96 -144.60 -133.57
REMARK 500 4 GLU A 99 139.63 -173.88
REMARK 500 5 ILE A 6 -70.73 -74.31
REMARK 500 5 ASN A 15 40.61 81.84
REMARK 500 5 ARG A 54 125.53 175.80
REMARK 500 5 GLN A 62 57.07 36.56
REMARK 500 5 VAL A 85 -148.40 -84.06
REMARK 500 5 LEU A 86 115.82 -39.76
REMARK 500 5 ASN A 89 49.49 -148.52
REMARK 500 5 ALA A 90 128.38 -171.01
REMARK 500
REMARK 500 THIS ENTRY HAS 236 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MAR11 RELATED DB: TARGETDB
DBREF 1XN9 A 1 101 UNP Q8PZ95 RS24_METMA 1 101
SEQRES 1 A 101 MET ASP ILE LYS ILE ILE LYS ASP LYS LYS ASN PRO LEU
SEQRES 2 A 101 LEU ASN ARG ARG GLU LEU ASP PHE ILE VAL LYS TYR GLU
SEQRES 3 A 101 GLY SER THR PRO SER ARG ASN ASP VAL ARG ASN LYS LEU
SEQRES 4 A 101 ALA ALA MET LEU ASN ALA PRO LEU GLU LEU LEU VAL ILE
SEQRES 5 A 101 GLN ARG ILE LYS THR GLU TYR GLY MET GLN GLU SER LYS
SEQRES 6 A 101 GLY TYR ALA LYS LEU TYR GLU ASP ALA ASP ARG MET LYS
SEQRES 7 A 101 GLN VAL GLU GLN GLU TYR VAL LEU LYS ARG ASN ALA VAL
SEQRES 8 A 101 PRO GLY SER GLU THR GLU GLY GLU GLU ALA
HELIX 1 1 SER A 31 LEU A 43 1 13
HELIX 2 2 ASP A 73 GLN A 82 1 10
HELIX 3 3 GLU A 83 LEU A 86 5 4
SHEET 1 A 4 ASP A 2 ASN A 11 0
SHEET 2 A 4 ARG A 16 LYS A 24 -1 O LYS A 24 N ASP A 2
SHEET 3 A 4 GLU A 63 LEU A 70 -1 O SER A 64 N VAL A 23
SHEET 4 A 4 LEU A 50 THR A 57 -1 N LYS A 56 O LYS A 65
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