Header list of 1ud7.pdb file
Complete list - v 3 2 Bytes
HEADER UBIQUITIN 07-APR-99 1UD7
TITLE SOLUTION STRUCTURE OF THE DESIGNED HYDROPHOBIC CORE MUTANT OF
TITLE 2 UBIQUITIN, 1D7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (UBIQUITIN CORE MUTANT 1D7);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 3 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 5 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 6 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM
KEYWDS UBIQUITIN, DESIGNED CORE MUTANT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.C.JOHNSON,G.A.LAZAR,J.R.DESJARLAIS,T.M.HANDEL
REVDAT 4 03-NOV-21 1UD7 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1UD7 1 VERSN
REVDAT 2 20-AUG-99 1UD7 1 JRNL
REVDAT 1 06-MAY-99 1UD7 0
JRNL AUTH E.C.JOHNSON,G.A.LAZAR,J.R.DESJARLAIS,T.M.HANDEL
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF A DESIGNED HYDROPHOBIC
JRNL TITL 2 CORE VARIANT OF UBIQUITIN.
JRNL REF STRUCTURE FOLD.DES. V. 7 967 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10467150
JRNL DOI 10.1016/S0969-2126(99)80123-3
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JOURNAL CITATION ABOVE
REMARK 4
REMARK 4 1UD7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000811.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.0
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N EDITED 3D NOESY; 13C EDITED
REMARK 210 3D NOESY; 13C/13C EDITED 4D
REMARK 210 NOESY; 3D 3JHNHA; 3D HACAHB; 2D
REMARK 210 3JNCG; 2D 3JCOCG; LONG RANGE
REMARK 210 3JCC; 3D 15N ROESY; 3D 15N TOCSY;
REMARK 210 1DNH RESIDUAL DIPOLAR COUPLINGS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : RESTRAINED MOLECULAR
REMARK 210 DYNAMICS/SIULATED ANNEALING
REMARK 210 USING THE ARIA PROCEDURE OF
REMARK 210 NILGES (NILGES ET AL. (1997) J
REMARK 210 MOL BIOL 269, 408-422) AND
REMARK 210 EXPLICIT SWAPPING OF NON-
REMARK 210 STEREOSPECIFICALLY ASSIGNED
REMARK 210 METHYLS AND METHYLENES (FOLMER
REMARK 210 ET AL. & NILGES (1997) J BIOMOL
REMARK 210 NMR 9, 245-258).
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING TRIPLE- RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N LABELED UBIQUITIN 1D7.
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 ILE A 30 H GLU A 34 1.54
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 72 91.16 76.08
REMARK 500 1 LEU A 73 45.37 -143.60
REMARK 500 2 THR A 9 -96.97 -128.59
REMARK 500 2 LEU A 73 132.83 68.98
REMARK 500 2 ARG A 74 159.30 -44.80
REMARK 500 3 THR A 7 -166.83 -101.37
REMARK 500 3 PRO A 19 91.51 -50.55
REMARK 500 3 SER A 20 -3.03 150.09
REMARK 500 3 ASP A 52 56.14 -65.90
REMARK 500 3 ARG A 72 119.23 65.05
REMARK 500 3 LEU A 73 135.87 61.43
REMARK 500 4 ARG A 72 64.05 173.38
REMARK 500 4 LEU A 73 162.61 68.20
REMARK 500 4 ARG A 74 -90.82 -76.60
REMARK 500 5 THR A 7 -167.78 -103.64
REMARK 500 5 LYS A 11 152.93 -28.69
REMARK 500 5 ARG A 72 -0.23 86.57
REMARK 500 5 LEU A 73 165.02 68.69
REMARK 500 5 ARG A 74 93.40 41.94
REMARK 500 6 ASP A 52 58.04 -65.29
REMARK 500 6 ARG A 72 158.76 82.92
REMARK 500 6 LEU A 73 -165.44 61.62
REMARK 500 6 ARG A 74 75.69 -168.17
REMARK 500 7 LYS A 11 156.37 -31.07
REMARK 500 7 ARG A 72 150.01 67.57
REMARK 500 8 LYS A 11 158.25 -31.61
REMARK 500 8 ARG A 74 58.25 85.15
REMARK 500 9 PRO A 19 87.56 -49.94
REMARK 500 9 SER A 20 -6.95 153.42
REMARK 500 10 PRO A 19 86.65 -58.09
REMARK 500 10 SER A 20 -8.17 154.91
REMARK 500 10 GLN A 49 93.57 -69.92
REMARK 500 10 ASP A 52 57.78 -65.77
REMARK 500 10 ARG A 72 68.75 -114.05
REMARK 500 10 ARG A 74 102.21 63.07
REMARK 500 11 LYS A 11 129.49 -12.24
REMARK 500 11 PRO A 19 86.33 -48.88
REMARK 500 11 SER A 20 -5.26 152.28
REMARK 500 11 ASP A 52 57.18 -65.60
REMARK 500 11 ARG A 72 94.47 97.73
REMARK 500 11 ARG A 74 -170.93 52.23
REMARK 500 12 ASP A 52 59.01 -64.91
REMARK 500 12 ARG A 72 109.93 83.84
REMARK 500 12 LEU A 73 53.73 -148.05
REMARK 500 13 ARG A 72 87.23 59.69
REMARK 500 13 ARG A 74 -48.74 -130.60
REMARK 500 14 GLN A 49 96.88 -65.83
REMARK 500 14 ARG A 72 154.30 55.83
REMARK 500 14 LEU A 73 115.04 54.71
REMARK 500 14 ARG A 74 -38.82 -158.86
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1UD7 A 1 76 UNP P02248 UBIQ_HUMANX 41 116
SEQADV 1UD7 VAL A 3 UNP P02248 ILE 43 ENGINEERED MUTATION
SEQADV 1UD7 LEU A 5 UNP P02248 VAL 45 ENGINEERED MUTATION
SEQADV 1UD7 VAL A 13 UNP P02248 ILE 53 ENGINEERED MUTATION
SEQADV 1UD7 ILE A 15 UNP P02248 LEU 55 ENGINEERED MUTATION
SEQADV 1UD7 VAL A 23 UNP P02248 ILE 63 ENGINEERED MUTATION
SEQADV 1UD7 PHE A 26 UNP P02248 VAL 66 ENGINEERED MUTATION
SEQADV 1UD7 ILE A 67 UNP P02248 LEU 107 ENGINEERED MUTATION
SEQRES 1 A 76 MET GLN VAL PHE LEU LYS THR LEU THR GLY LYS THR VAL
SEQRES 2 A 76 THR ILE GLU VAL GLU PRO SER ASP THR VAL GLU ASN PHE
SEQRES 3 A 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 A 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 A 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 A 76 THR ILE HIS LEU VAL LEU ARG LEU ARG GLY GLY
HELIX 1 H1 VAL A 23 GLU A 34 1 12
HELIX 2 H2 LEU A 56 TYR A 59 5 4
SHEET 1 S1 1 THR A 12 GLU A 16 0
SHEET 1 S2 1 GLN A 2 LYS A 6 0
SHEET 1 S3 1 THR A 66 LEU A 71 0
SHEET 1 S4 1 GLN A 41 PHE A 45 0
SHEET 1 S5 1 LYS A 48 GLN A 49 0
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 - v 3 2 Bytes