Header list of 1q0v.pdb file
Complete list - c 21 2 Bytes
HEADER TRANSPORT BINDING 17-JUL-03 1Q0V
TITLE SOLUTION STRUCTURE OF TANDEM UIMS OF VPS27
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROPHILIC PROTEIN; HAS CYSTEINE RICH PUTATIVE ZINC FINGER
COMPND 3 ESSENTIAL FOR FUNCTION; VPS27P;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: TANDEM UIM;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: VPS27;
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: PET30 DERIVATIVE
KEYWDS STABLE, NON-INTERACTING ALPHA-HELICES, TRANSPORT BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.A.SWANSON,R.S.KANG,S.D.STAMENOVA,L.HICKE,I.RADHAKRISHNAN
REVDAT 4 21-DEC-22 1Q0V 1 SEQADV
REVDAT 3 02-MAR-22 1Q0V 1 REMARK
REVDAT 2 24-FEB-09 1Q0V 1 VERSN
REVDAT 1 23-DEC-03 1Q0V 0
JRNL AUTH K.A.SWANSON,R.S.KANG,S.D.STAMENOVA,L.HICKE,I.RADHAKRISHNAN
JRNL TITL SOLUTION STRUCTURE OF VPS27 UIM-UBIQUITIN COMPLEX IMPORTANT
JRNL TITL 2 FOR ENDOSOMAL SORTING AND RECEPTOR DOWNREGULATION.
JRNL REF EMBO J. V. 22 4597 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 12970172
JRNL DOI 10.1093/EMBOJ/CDG471
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, CNS 1.1, ARIA 1.2
REMARK 3 AUTHORS : VARIAN INSTRUMENTS (VNMR), BRUNGER ET AL. (CNS),
REMARK 3 LINGE AND NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 858 DISTANCE RESTRAINTS,
REMARK 3 INCLUDING 808 NOE-DERIVED
REMARK 3 DISTANCE RESTRAINTS [412 UNAMBIGUOUS AND 396 AMBIGUOUS RESTRAINTS],
REMARK 3 50 HYDROGEN BONDING
REMARK 3 DISTANCE RESTRAINTS, AND 66 TORSION ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1Q0V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019775.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 20 MM SODIUM PHOSPHATE, PH 6.0,
REMARK 210 0.2% NAN3
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM VPS27 UIM U-15N; 1 MM VPS27
REMARK 210 UIM U-15N,U-13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 20 STRUCTURES WITH THE
REMARK 210 LOWEST RESTRAINT ENERGIES,
REMARK 210 RESTRAINT VIOLATIONS, AND RMS
REMARK 210 DEVIATIONS FROM IDEAL COVALENT
REMARK 210 GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 252 -52.67 -172.16
REMARK 500 1 TYR A 253 43.18 -108.28
REMARK 500 1 SER A 254 131.13 63.32
REMARK 500 1 PRO A 256 -133.18 -67.06
REMARK 500 1 ASP A 258 -134.83 -165.75
REMARK 500 1 SER A 274 -135.17 -163.25
REMARK 500 1 ARG A 275 -137.63 -72.41
REMARK 500 1 ASN A 276 49.32 178.67
REMARK 500 1 SER A 279 141.91 66.52
REMARK 500 1 GLU A 281 57.95 -167.68
REMARK 500 1 ILE A 283 140.04 63.77
REMARK 500 1 VAL A 287 43.42 -94.10
REMARK 500 1 GLU A 288 46.70 -78.20
REMARK 500 1 GLN A 296 -112.25 -155.97
REMARK 500 1 ILE A 298 45.55 -78.38
REMARK 500 1 GLU A 299 133.13 64.67
REMARK 500 1 GLU A 301 134.22 64.22
REMARK 500 1 GLU A 325 -39.68 75.04
REMARK 500 2 ASP A 258 -133.00 -175.90
REMARK 500 2 SER A 274 139.34 178.39
REMARK 500 2 ASN A 276 47.78 -145.44
REMARK 500 2 ALA A 278 130.91 64.81
REMARK 500 2 SER A 279 144.20 -174.46
REMARK 500 2 SER A 280 -172.56 -61.73
REMARK 500 2 VAL A 286 131.06 65.09
REMARK 500 2 GLU A 288 46.62 -78.79
REMARK 500 2 ASN A 291 35.28 -155.07
REMARK 500 2 ARG A 295 -132.18 -91.06
REMARK 500 2 GLN A 296 134.93 64.88
REMARK 500 2 GLU A 325 144.04 -171.04
REMARK 500 2 GLN A 327 136.77 -170.78
REMARK 500 3 ASP A 252 44.64 -171.43
REMARK 500 3 TYR A 253 -46.17 75.47
REMARK 500 3 SER A 254 42.74 -82.46
REMARK 500 3 PRO A 256 -150.23 -71.19
REMARK 500 3 GLU A 257 -127.24 -94.22
REMARK 500 3 ASP A 258 -52.50 -132.51
REMARK 500 3 SER A 274 58.70 -159.78
REMARK 500 3 ARG A 275 -49.27 -150.27
REMARK 500 3 SER A 277 -46.68 -163.78
REMARK 500 3 ALA A 278 134.93 64.79
REMARK 500 3 SER A 279 46.96 -169.19
REMARK 500 3 GLU A 281 57.37 -147.05
REMARK 500 3 PRO A 282 43.23 -78.18
REMARK 500 3 PRO A 285 45.32 -78.39
REMARK 500 3 VAL A 287 47.86 -164.11
REMARK 500 3 GLU A 288 34.72 -171.54
REMARK 500 3 LYS A 290 -60.81 -171.05
REMARK 500 3 ASN A 291 39.57 36.16
REMARK 500 3 GLU A 299 -52.67 -143.62
REMARK 500
REMARK 500 THIS ENTRY HAS 404 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O06 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE C-TERMINAL UIM OF VPS27
DBREF 1Q0V A 249 329 UNP P40343 VPS27_YEAST 249 329
SEQADV 1Q0V MET A 249 UNP P40343 249 INITIATING METHIONINE
SEQRES 1 A 81 MET ASP ARG ASP TYR SER THR PRO GLU ASP GLU GLU GLU
SEQRES 2 A 81 LEU ILE ARG LYS ALA ILE GLU LEU SER LEU LYS GLU SER
SEQRES 3 A 81 ARG ASN SER ALA SER SER GLU PRO ILE VAL PRO VAL VAL
SEQRES 4 A 81 GLU SER LYS ASN GLU VAL LYS ARG GLN GLU ILE GLU GLU
SEQRES 5 A 81 GLU GLU ASP PRO ASP LEU LYS ALA ALA ILE GLN GLU SER
SEQRES 6 A 81 LEU ARG GLU ALA GLU GLU ALA LYS LEU ARG SER GLU ARG
SEQRES 7 A 81 GLN LYS ALA
HELIX 1 1 ASP A 258 GLU A 273 1 16
HELIX 2 2 ASP A 303 GLU A 325 1 23
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 - c 21 2 Bytes