Header list of 1a5r.pdb file
Complete list - b 16 2 Bytes
HEADER TARGETING PROTEIN 18-FEB-98 1A5R
TITLE STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN-RELATED MODIFIER SUMO-
TITLE 2 1, NMR, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUMO-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PIC1, GMP1, UBL1, SENTRIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX2T
KEYWDS SUMO-1, POST-TRANSLATIONAL PROTEIN MODIFICATION, UBIQUITIN-LIKE
KEYWDS 2 PROTEINS, TARGETING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR P.BAYER,A.ARNDT,S.METZGER,R.MAHAJAN,F.MELCHIOR,R.JAENICKE,J.BECKER
REVDAT 3 16-FEB-22 1A5R 1 REMARK
REVDAT 2 24-FEB-09 1A5R 1 VERSN
REVDAT 1 14-OCT-98 1A5R 0
JRNL AUTH P.BAYER,A.ARNDT,S.METZGER,R.MAHAJAN,F.MELCHIOR,R.JAENICKE,
JRNL AUTH 2 J.BECKER
JRNL TITL STRUCTURE DETERMINATION OF THE SMALL UBIQUITIN-RELATED
JRNL TITL 2 MODIFIER SUMO-1.
JRNL REF J.MOL.BIOL. V. 280 275 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9654451
JRNL DOI 10.1006/JMBI.1998.1839
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.MAHAJAN,C.DELPHIN,T.GUAN,L.GERACE,F.MELCHIOR
REMARK 1 TITL A SMALL UBIQUITIN-RELATED POLYPEPTIDE INVOLVED IN TARGETING
REMARK 1 TITL 2 RANGAP1 TO NUCLEAR PORE COMPLEX PROTEIN RANBP2
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 88 97 1997
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.KAMITANI,H.P.NGUYEN,E.T.YEH
REMARK 1 TITL PREFERENTIAL MODIFICATION OF NUCLEAR PROTEINS BY A NOVEL
REMARK 1 TITL 2 UBIQUITIN-LIKE MOLECULE
REMARK 1 REF J.BIOL.CHEM. V. 272 14001 1997
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.J.MATUNIS,E.COUTAVAS,G.BLOBEL
REMARK 1 TITL A NOVEL UBIQUITIN-LIKE MODIFICATION MODULATES THE
REMARK 1 TITL 2 PARTITIONING OF THE RAN-GTPASE-ACTIVATING PROTEIN RANGAP1
REMARK 1 TITL 3 BETWEEN THE CYTOSOL AND THE NUCLEAR PORE COMPLEX
REMARK 1 REF J.CELL BIOL. V. 135 1457 1996
REMARK 1 REFN ISSN 0021-9525
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A5R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170426.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100 MM
REMARK 210 PRESSURE : STANDARD
REMARK 210 SAMPLE CONTENTS : H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; NOESY; CLEAN-TOCSY; GS
REMARK 210 -15N-HSQC; 15N-NOESY-HMQC; 15N-
REMARK 210 TOCSY-HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE, X-PLOR 3.851 PRE-RELEASE
REMARK 210 VERSION VERSION
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: 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 ASP A 30 21.21 -76.66
REMARK 500 1 MET A 40 60.37 -119.09
REMARK 500 1 HIS A 43 175.95 -52.24
REMARK 500 1 SER A 61 -36.19 -143.99
REMARK 500 1 PHE A 66 -85.89 -114.91
REMARK 500 1 ALA A 72 -166.02 -106.99
REMARK 500 1 LYS A 78 -94.29 -57.70
REMARK 500 2 ALA A 6 161.43 163.11
REMARK 500 2 THR A 42 -99.99 -121.00
REMARK 500 2 SER A 61 -46.55 -137.24
REMARK 500 2 PHE A 66 -81.29 -123.16
REMARK 500 2 ASP A 73 50.45 -114.92
REMARK 500 2 GLU A 84 11.68 -144.38
REMARK 500 3 GLN A 29 -18.91 -48.94
REMARK 500 3 THR A 42 -67.24 -132.02
REMARK 500 3 SER A 61 -1.99 -148.51
REMARK 500 3 PHE A 66 -80.13 -121.71
REMARK 500 3 ASP A 73 56.74 -107.71
REMARK 500 3 LYS A 78 -78.94 -54.05
REMARK 500 3 GLU A 84 16.24 -144.85
REMARK 500 4 LYS A 16 -155.54 60.09
REMARK 500 4 THR A 42 -107.90 -129.45
REMARK 500 4 ASN A 60 0.07 -157.53
REMARK 500 4 PHE A 66 -80.09 -122.99
REMARK 500 4 LYS A 78 -79.81 -56.25
REMARK 500 4 GLU A 84 -11.32 -151.37
REMARK 500 5 SER A 31 40.56 70.29
REMARK 500 5 THR A 42 -139.15 -125.10
REMARK 500 5 CYS A 52 -72.10 -75.96
REMARK 500 5 VAL A 57 96.15 -33.91
REMARK 500 5 PHE A 66 -82.16 -126.89
REMARK 500 5 THR A 76 -70.62 -126.62
REMARK 500 5 LYS A 78 -70.61 -61.64
REMARK 500 5 GLU A 84 -4.42 -154.45
REMARK 500 6 LYS A 16 -121.32 60.23
REMARK 500 6 THR A 42 -85.88 -129.39
REMARK 500 6 GLN A 55 -50.11 -124.30
REMARK 500 6 SER A 61 -10.58 -145.95
REMARK 500 6 PHE A 66 -92.46 -108.75
REMARK 500 6 THR A 76 -62.24 -126.60
REMARK 500 6 LYS A 78 -73.51 -62.92
REMARK 500 6 GLU A 84 -14.28 67.26
REMARK 500 7 THR A 42 -111.04 -131.79
REMARK 500 7 LEU A 44 2.85 -69.13
REMARK 500 7 ASN A 60 -3.69 -169.31
REMARK 500 7 SER A 61 -9.51 -141.86
REMARK 500 7 PHE A 66 -83.28 -111.57
REMARK 500 7 HIS A 75 47.43 -100.63
REMARK 500 7 LYS A 78 -87.39 -77.31
REMARK 500 8 ASP A 30 30.78 -77.66
REMARK 500
REMARK 500 THIS ENTRY HAS 73 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 54 0.30 SIDE CHAIN
REMARK 500 1 ARG A 63 0.19 SIDE CHAIN
REMARK 500 1 ARG A 70 0.26 SIDE CHAIN
REMARK 500 2 ARG A 63 0.30 SIDE CHAIN
REMARK 500 2 ARG A 70 0.28 SIDE CHAIN
REMARK 500 3 ARG A 54 0.26 SIDE CHAIN
REMARK 500 3 ARG A 63 0.08 SIDE CHAIN
REMARK 500 3 ARG A 70 0.25 SIDE CHAIN
REMARK 500 4 ARG A 63 0.08 SIDE CHAIN
REMARK 500 4 ARG A 70 0.32 SIDE CHAIN
REMARK 500 5 ARG A 54 0.20 SIDE CHAIN
REMARK 500 5 ARG A 63 0.18 SIDE CHAIN
REMARK 500 5 ARG A 70 0.10 SIDE CHAIN
REMARK 500 6 ARG A 54 0.22 SIDE CHAIN
REMARK 500 6 ARG A 63 0.29 SIDE CHAIN
REMARK 500 6 ARG A 70 0.30 SIDE CHAIN
REMARK 500 7 ARG A 54 0.32 SIDE CHAIN
REMARK 500 7 ARG A 70 0.21 SIDE CHAIN
REMARK 500 8 ARG A 63 0.30 SIDE CHAIN
REMARK 500 8 ARG A 70 0.31 SIDE CHAIN
REMARK 500 9 ARG A 54 0.28 SIDE CHAIN
REMARK 500 9 ARG A 63 0.22 SIDE CHAIN
REMARK 500 9 ARG A 70 0.10 SIDE CHAIN
REMARK 500 10 ARG A 54 0.32 SIDE CHAIN
REMARK 500 10 ARG A 70 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1A5R A 1 101 UNP P63165 SMT3C_HUMAN 1 101
SEQRES 1 A 103 GLY SER MET SER ASP GLN GLU ALA LYS PRO SER THR GLU
SEQRES 2 A 103 ASP LEU GLY ASP LYS LYS GLU GLY GLU TYR ILE LYS LEU
SEQRES 3 A 103 LYS VAL ILE GLY GLN ASP SER SER GLU ILE HIS PHE LYS
SEQRES 4 A 103 VAL LYS MET THR THR HIS LEU LYS LYS LEU LYS GLU SER
SEQRES 5 A 103 TYR CYS GLN ARG GLN GLY VAL PRO MET ASN SER LEU ARG
SEQRES 6 A 103 PHE LEU PHE GLU GLY GLN ARG ILE ALA ASP ASN HIS THR
SEQRES 7 A 103 PRO LYS GLU LEU GLY MET GLU GLU GLU ASP VAL ILE GLU
SEQRES 8 A 103 VAL TYR GLN GLU GLN THR GLY GLY HIS SER THR VAL
HELIX 1 H1 LEU A 44 GLN A 55 1 12
HELIX 2 H2 THR A 76 LEU A 80 1 5
SHEET 1 A 4 SER A 32 LYS A 39 0
SHEET 2 A 4 TYR A 21 GLY A 28 -1 N GLY A 28 O SER A 32
SHEET 3 A 4 ASP A 86 GLN A 92 1 N ASP A 86 O LYS A 25
SHEET 4 A 4 LEU A 62 LEU A 65 -1 N LEU A 65 O GLU A 89
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 - b 16 2 Bytes