Header list of 1gjz.pdb file
Complete list - r 25 2 Bytes
HEADER UBIQUITIN 06-AUG-01 1GJZ
TITLE SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF
TITLE 2 HUMAN UBIQUITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-51;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: FRAGMENT CONTAINS FIRST 51 RESIDUES OF
COMPND 7 HUMAN UBIQUITIN PRECEDED AT THE N-TERMINUS BY GLYCINE AND
COMPND 8 SERINE
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-4T3
KEYWDS UBIQUITIN, DIMER, PROTEIN DISSECTION
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR D.BOLTON,P.A.EVANS,K.STOTT,R.W.BROADHURST
REVDAT 2 24-FEB-09 1GJZ 1 VERSN
REVDAT 1 13-DEC-01 1GJZ 0
JRNL AUTH D.BOLTON,P.A.EVANS,K.STOTT,R.W.BROADHURST
JRNL TITL STRUCTURE AND PROPERTIES OF A DIMERIC N-TERMINAL
JRNL TITL 2 FRAGMENT OF HUMAN UBIQUITIN.
JRNL REF J.MOL.BIOL. V. 314 773 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11733996
JRNL DOI 10.1006/JMBI.2001.5181
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1GJZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-AUG-01.
REMARK 100 THE PDBE ID CODE IS EBI-8428.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 800MM SODIUM SULPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB, CBCA(CO)NH,
REMARK 210 15N-TOCSY-HSQC, 15N-NOESY-HSQC,
REMARK 210 HCCH-TOCSY, 13C-NOESY-HSQC,
REMARK 210 12C-FILTERED-NOESY-13C-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500
REMARK 210 SPECTROMETER MODEL : DRX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA, ANSIG3.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 65
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW ENERGY, LEAST
REMARK 210 RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED FRAGMENTS CONTAINING THE
REMARK 210 FIRST 51 RESIDUES OF HUMAN UBIQUITIN
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HG1 THR A 7 - H GLY A 10 1.48
REMARK 500 HG22 THR A 7 - HZ3 LYS A 11 1.57
REMARK 500 HD13 LEU A 15 - HG3 LYS A 33 1.49
REMARK 500 HD11 ILE A 30 - HG2 GLN A 41 1.60
REMARK 500 H ARG A 42 - H ALA B 46 1.38
REMARK 500 HE ARG A 42 - HG3 LYS B 48 1.46
REMARK 500 HD13 LEU A 43 - HD13 LEU B 43 1.39
REMARK 500 H ALA A 46 - H ARG B 42 1.41
REMARK 500 HG3 LYS A 48 - HE ARG B 42 1.51
REMARK 500 HG1 THR B 7 - H GLY B 10 1.52
REMARK 500 HG23 ILE B 36 - HE21 GLN B 40 1.51
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 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 MET A 1 52.89 -167.02
REMARK 500 1 LEU A 50 80.41 -45.09
REMARK 500 1 MET B 1 51.76 -168.29
REMARK 500 1 LEU B 50 79.92 -54.33
REMARK 500 2 SER A 0 -125.50 -67.97
REMARK 500 2 THR A 7 -156.63 -63.81
REMARK 500 2 LEU A 15 114.34 -161.55
REMARK 500 2 PRO A 37 143.14 -39.80
REMARK 500 2 LYS A 48 74.72 -68.52
REMARK 500 2 GLN A 49 96.29 -65.41
REMARK 500 2 LEU A 50 80.21 -44.27
REMARK 500 2 SER B 0 -125.20 -68.07
REMARK 500 2 THR B 7 -156.75 -68.86
REMARK 500 2 LEU B 15 113.22 -160.66
REMARK 500 2 LEU B 50 79.05 -54.54
REMARK 500 3 SER A 0 -47.35 -168.71
REMARK 500 3 MET A 1 121.56 -172.67
REMARK 500 3 THR A 7 -157.35 -70.41
REMARK 500 3 PRO A 37 155.72 -49.88
REMARK 500 3 LYS A 48 75.91 -67.31
REMARK 500 3 LEU A 50 84.00 -44.71
REMARK 500 3 SER B 0 -48.52 -171.41
REMARK 500 3 MET B 1 120.04 -174.28
REMARK 500 3 THR B 7 -157.00 -74.53
REMARK 500 3 LEU B 15 118.62 -162.80
REMARK 500 3 LYS B 48 75.94 -67.27
REMARK 500 3 LEU B 50 79.73 -52.22
REMARK 500 4 SER A 0 -128.36 56.03
REMARK 500 4 MET A 1 117.13 -165.54
REMARK 500 4 THR A 7 -157.20 -73.13
REMARK 500 4 LYS A 48 74.93 -67.19
REMARK 500 4 GLN A 49 97.93 -66.73
REMARK 500 4 LEU A 50 80.74 -44.88
REMARK 500 4 SER B 0 -127.82 56.88
REMARK 500 4 MET B 1 115.74 -166.64
REMARK 500 4 THR B 7 -157.39 -73.29
REMARK 500 4 LEU B 50 79.52 -56.90
REMARK 500 5 SER A 0 -120.09 -65.85
REMARK 500 5 THR A 7 -156.75 -69.16
REMARK 500 5 PRO A 37 150.09 -45.84
REMARK 500 5 LYS A 48 82.29 -159.74
REMARK 500 5 GLN A 49 98.07 -65.82
REMARK 500 5 LEU A 50 81.08 -44.14
REMARK 500 5 SER B 0 -121.15 -65.69
REMARK 500 5 THR B 7 -156.75 -72.72
REMARK 500 5 LYS B 48 111.40 -160.24
REMARK 500 5 LEU B 50 79.40 -59.62
REMARK 500 6 SER A 0 -125.90 -67.46
REMARK 500 6 THR A 7 -159.55 -67.70
REMARK 500 6 LEU A 15 115.10 -162.32
REMARK 500 6 LYS A 48 73.80 -161.49
REMARK 500 6 LEU A 50 80.12 -45.38
REMARK 500 6 SER B 0 -125.26 -67.75
REMARK 500 6 MET B 1 115.30 -163.54
REMARK 500 6 THR B 7 -160.09 -69.96
REMARK 500 6 LEU B 15 112.97 -162.94
REMARK 500 6 LYS B 48 73.97 -160.27
REMARK 500 6 LEU B 50 80.43 -50.47
REMARK 500 7 MET A 1 57.05 -163.83
REMARK 500 7 THR A 7 -156.54 -68.49
REMARK 500 7 LEU A 15 114.05 -163.94
REMARK 500 7 LYS A 48 75.28 -69.50
REMARK 500 7 LEU A 50 80.40 -44.99
REMARK 500 7 MET B 1 57.60 -156.37
REMARK 500 7 THR B 7 -156.94 -69.53
REMARK 500 7 LEU B 15 113.75 -161.35
REMARK 500 7 LYS B 48 75.89 -69.60
REMARK 500 7 LEU B 50 80.36 -49.62
REMARK 500 8 SER A 0 -135.68 -68.77
REMARK 500 8 THR A 7 -158.20 -67.21
REMARK 500 8 GLN A 49 90.57 -67.48
REMARK 500 8 LEU A 50 79.93 -45.93
REMARK 500 8 SER B 0 -133.66 -68.47
REMARK 500 8 THR B 7 -157.77 -68.44
REMARK 500 8 LEU B 50 79.98 -59.61
REMARK 500 9 MET A 1 49.02 -163.42
REMARK 500 9 THR A 7 -157.56 -70.48
REMARK 500 9 LEU A 50 80.03 -47.33
REMARK 500 9 MET B 1 51.13 -155.87
REMARK 500 9 THR B 7 -157.64 -71.05
REMARK 500 9 LEU B 50 80.01 -52.74
REMARK 500 10 MET A 1 106.95 178.54
REMARK 500 10 THR A 7 -157.62 -72.48
REMARK 500 10 LYS A 48 74.59 -69.20
REMARK 500 10 LEU A 50 80.45 -45.05
REMARK 500 10 MET B 1 106.61 179.67
REMARK 500 10 THR B 7 -157.30 -77.54
REMARK 500 10 LEU B 15 115.04 -162.53
REMARK 500 10 PRO B 37 146.30 -38.89
REMARK 500 10 LYS B 48 74.89 -69.19
REMARK 500 10 LEU B 50 80.21 -52.85
REMARK 500 11 MET A 1 115.73 -175.54
REMARK 500 11 THR A 7 -157.00 -71.43
REMARK 500 11 LEU A 15 114.05 -160.58
REMARK 500 11 LEU A 50 80.28 -44.90
REMARK 500 11 MET B 1 108.45 179.56
REMARK 500 11 THR B 7 -157.02 -68.61
REMARK 500 11 LEU B 15 112.84 -162.72
REMARK 500 11 LEU B 50 80.30 -51.45
REMARK 500 12 GLN A 49 99.80 -66.34
REMARK 500 12 LEU A 50 80.55 -44.91
REMARK 500 12 LEU B 50 80.26 -53.12
REMARK 500 13 SER A 0 -126.96 -164.25
REMARK 500 13 MET A 1 117.38 -160.19
REMARK 500 13 THR A 7 -159.95 -66.53
REMARK 500 13 GLN A 49 99.46 -65.40
REMARK 500 13 LEU A 50 80.48 -44.79
REMARK 500 13 SER B 0 -124.42 -164.40
REMARK 500 13 MET B 1 117.16 -163.32
REMARK 500 13 THR B 7 -157.39 -70.57
REMARK 500 13 LEU B 15 114.62 -164.20
REMARK 500 13 LEU B 50 80.07 -52.76
REMARK 500 14 SER A 0 -50.01 -171.46
REMARK 500 14 THR A 7 -157.12 -77.37
REMARK 500 14 LEU A 50 80.45 -44.96
REMARK 500 14 SER B 0 -46.65 -173.00
REMARK 500 14 THR B 7 -157.17 -76.54
REMARK 500 14 LEU B 15 115.64 -163.36
REMARK 500 14 LEU B 50 79.80 -56.32
REMARK 500 15 MET A 1 112.58 177.61
REMARK 500 15 THR A 7 -157.31 -68.38
REMARK 500 15 PRO A 37 158.76 -46.63
REMARK 500 15 LEU A 50 80.28 -44.83
REMARK 500 15 MET B 1 110.42 177.69
REMARK 500 15 THR B 7 -157.49 -70.62
REMARK 500 15 PRO B 37 157.98 -47.17
REMARK 500 15 LEU B 50 80.46 -52.50
REMARK 500 16 SER A 0 -140.19 56.05
REMARK 500 16 MET A 1 48.81 -82.23
REMARK 500 16 THR A 7 -156.88 -68.29
REMARK 500 16 LYS A 48 74.67 -159.91
REMARK 500 16 LEU A 50 80.49 -48.81
REMARK 500 16 SER B 0 -140.61 56.05
REMARK 500 16 MET B 1 48.84 -82.14
REMARK 500 16 THR B 7 -156.81 -67.80
REMARK 500 16 LYS B 48 74.82 -159.81
REMARK 500 16 LEU B 50 79.72 -55.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AAR RELATED DB: PDB
REMARK 900 DI-UBIQUITIN
REMARK 900 RELATED ID: 1CMX RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR THE SPECIFICITY OF
REMARK 900 UBIQUITIN C- TERMINAL HYDROLASES
REMARK 900 RELATED ID: 1G6J RELATED DB: PDB
REMARK 900 STRUCTURE OF RECOMBINANT HUMAN UBIQUITIN IN
REMARK 900 AOT REVERSEMICELLES
REMARK 900 RELATED ID: 1TBE RELATED DB: PDB
REMARK 900 TETRAUBIQUITIN
REMARK 900 RELATED ID: 1UBI RELATED DB: PDB
REMARK 900 UBIQUITIN
REMARK 900 RELATED ID: 1UBQ RELATED DB: PDB
REMARK 900 UBIQUITIN
DBREF 1GJZ A -1 0 PDB 1GJZ 1GJZ -1 0
DBREF 1GJZ A 1 51 UNP P02248 UBIQ_HUMAN 1 51
DBREF 1GJZ B -1 0 PDB 1GJZ 1GJZ -1 0
DBREF 1GJZ B 1 51 UNP P02248 UBIQ_HUMAN 1 51
SEQRES 1 A 53 GLY SER MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS
SEQRES 2 A 53 THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU
SEQRES 3 A 53 ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO
SEQRES 4 A 53 PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU
SEQRES 5 A 53 GLU
SEQRES 1 B 53 GLY SER MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS
SEQRES 2 B 53 THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU
SEQRES 3 B 53 ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO
SEQRES 4 B 53 PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU
SEQRES 5 B 53 GLU
HELIX 1 1 THR A 22 GLU A 34 1 13
HELIX 2 2 THR B 22 GLU B 34 1 13
SHEET 1 AA 3 THR A 12 GLU A 16 0
SHEET 2 AA 3 GLN A 2 LYS A 6 -1 O ILE A 3 N LEU A 15
SHEET 3 AA 3 ILE B 44 ALA B 46 1 O PHE B 45 N LYS A 6
SHEET 1 AB 3 ILE A 44 ALA A 46 0
SHEET 2 AB 3 GLN B 2 LYS B 6 1 O PHE B 4 N PHE A 45
SHEET 3 AB 3 THR B 12 GLU B 16 -1 O ILE B 13 N VAL B 5
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