Header list of 1cz5.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE 01-SEP-99 1CZ5
TITLE NMR STRUCTURE OF VAT-N: THE N-TERMINAL DOMAIN OF VAT (VCP-LIKE ATPASE
TITLE 2 OF THERMOPLASMA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VCP-LIKE ATPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN: M1 TO E183 FOLLOWED BY A DIGLYCINE
COMPND 5 SPACER;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM;
SOURCE 3 ORGANISM_TAXID: 2303;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS DOUBLE-PSI BETA-BARREL, BETA-CLAM, SUBSTRATE RECOGNITION DOMAIN,
KEYWDS 2 FUSION PROTEIN, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR M.COLES,T.DIERCKS,J.LIERMANN,A.GROEGER,B.ROCKEL,W.BAUMEISTER,
AUTHOR 2 K.KORETKE,A.LUPAS,J.PETERS,H.KESSLER
REVDAT 5 16-FEB-22 1CZ5 1 REMARK
REVDAT 4 24-FEB-09 1CZ5 1 VERSN
REVDAT 3 01-APR-03 1CZ5 1 JRNL
REVDAT 2 05-JUL-00 1CZ5 1 SOURCE REMARK DBREF SEQADV
REVDAT 2 2 1 CRYST1
REVDAT 1 12-OCT-99 1CZ5 0
JRNL AUTH M.COLES,T.DIERCKS,J.LIERMANN,A.GROGER,B.ROCKEL,W.BAUMEISTER,
JRNL AUTH 2 K.K.KORETKE,A.LUPAS,J.PETERS,H.KESSLER
JRNL TITL THE SOLUTION STRUCTURE OF VAT-N REVEALS A 'MISSING LINK' IN
JRNL TITL 2 THE EVOLUTION OF COMPLEX ENZYMES FROM A SIMPLE
JRNL TITL 3 BETAALPHABETABETA ELEMENT.
JRNL REF CURR.BIOL. V. 9 1158 1999
JRNL REFN ISSN 0960-9822
JRNL PMID 10531028
JRNL DOI 10.1016/S0960-9822(00)80017-2
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER ET AL. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURES BASED ON 1923 DISTANCE RESTRAINTS; 1817 NOE BASED
REMARK 3 RESTRAINTS, 196
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 56 J-COUPLING RESTRAINTS, 106 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FOR H-BONDS, 158 CA AND 148 CB CHEMICAL SHIFT RESTRAINTS. REFINED
REMARK 3 WITH A
REMARK 3 CONFORMATIONAL DATABASE POTENTIAL
REMARK 4
REMARK 4 1CZ5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-99.
REMARK 100 THE DEPOSITION ID IS D_1000009635.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 320; 320
REMARK 210 PH : 5.9; 5.9
REMARK 210 IONIC STRENGTH : 80 MM; 80 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.4 MM VAT-N U-15N,13C; 40 MM
REMARK 210 PHOSPHATE BUFFER NA; 90% H2O, 10%
REMARK 210 D2O; 1.2 MM VAT-N U-15N; 40 MM
REMARK 210 PHOSPHATE BUFFER NA; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_CNH
REMARK 210 -NOESY; 3D_NCH-NOESY; 3D_CCH-
REMARK 210 NOESY; 3D_15N-SEPARATED_NOESY;
REMARK 210 3D_NNH-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.5, AURELIA 2.5.11, X
REMARK 210 -PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY. 3JHNHA
REMARK 210 COUPLING-CONSTANTS FROM AN HNHA SPECTRUM
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 OD1 ASP A 27 H SER A 30 1.51
REMARK 500 H GLU A 37 OD2 ASP A 40 1.53
REMARK 500 O LYS A 96 H LYS A 169 1.56
REMARK 500 O VAL A 11 H GLY A 82 1.57
REMARK 500 HE22 GLN A 121 O GLY A 165 1.57
REMARK 500 H SER A 80 OD2 ASP A 83 1.57
REMARK 500 HG SER A 30 O ASN A 63 1.58
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 GLU A 13 142.18 -175.74
REMARK 500 1 SER A 16 -158.45 -175.40
REMARK 500 1 PRO A 19 -175.01 -63.38
REMARK 500 1 LEU A 34 -74.51 -101.65
REMARK 500 1 ASP A 35 -23.81 -170.24
REMARK 500 1 ALA A 36 121.27 -34.71
REMARK 500 1 LYS A 46 -66.95 -99.06
REMARK 500 1 GLU A 60 37.18 -73.59
REMARK 500 1 ASP A 61 -29.20 -147.71
REMARK 500 1 ASN A 63 41.51 -81.13
REMARK 500 1 ASP A 83 -160.16 -58.23
REMARK 500 1 GLN A 108 -80.07 -90.54
REMARK 500 1 LEU A 110 43.12 -97.99
REMARK 500 1 GLU A 114 94.80 44.40
REMARK 500 1 ILE A 125 166.23 -41.96
REMARK 500 1 ARG A 126 54.34 34.20
REMARK 500 1 GLN A 132 -1.33 79.73
REMARK 500 1 ASP A 133 -171.05 -69.02
REMARK 500 1 PRO A 138 76.76 -51.78
REMARK 500 1 THR A 141 -167.14 -180.00
REMARK 500 1 LEU A 142 -131.45 -141.86
REMARK 500 1 ALA A 143 -151.41 -55.52
REMARK 500 1 PRO A 157 -165.47 -55.54
REMARK 500 1 SER A 158 40.94 -88.64
REMARK 500 1 LYS A 159 18.76 59.99
REMARK 500 1 PRO A 176 -149.86 -64.64
REMARK 500 1 LEU A 181 29.01 -147.44
REMARK 500 2 GLU A 13 86.39 -177.96
REMARK 500 2 PRO A 19 -170.65 -60.30
REMARK 500 2 LEU A 34 -75.01 -105.27
REMARK 500 2 ASP A 35 -24.44 -170.12
REMARK 500 2 ALA A 36 118.97 -26.77
REMARK 500 2 GLU A 45 89.44 -150.21
REMARK 500 2 LYS A 46 -66.39 -98.37
REMARK 500 2 GLU A 60 33.81 -74.04
REMARK 500 2 ASP A 61 -29.08 -147.53
REMARK 500 2 ASN A 63 42.08 -81.25
REMARK 500 2 ASP A 83 -160.81 -58.55
REMARK 500 2 LEU A 110 57.37 -99.78
REMARK 500 2 PHE A 112 -86.44 -143.75
REMARK 500 2 GLU A 114 82.06 -43.87
REMARK 500 2 ILE A 125 163.08 -43.43
REMARK 500 2 ARG A 126 49.97 33.84
REMARK 500 2 GLN A 132 -2.74 82.43
REMARK 500 2 VAL A 137 -62.91 -106.61
REMARK 500 2 LEU A 142 -125.06 -130.54
REMARK 500 2 ALA A 143 -157.22 -54.01
REMARK 500 2 PRO A 157 -176.30 -61.75
REMARK 500 2 SER A 158 -156.49 -90.25
REMARK 500 2 PRO A 176 -154.21 -72.30
REMARK 500
REMARK 500 THIS ENTRY HAS 625 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CZ4 RELATED DB: PDB
REMARK 900 BEST CONFORMER FROM THIS ENSEMBLE
REMARK 900 RELATED ID: 4376 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS, 3JHNHA COUPLING-CONSTANTS AND HET. NOE VALUES
DBREF 1CZ5 A 1 183 UNP O05209 VAT_THEAC 1 183
SEQADV 1CZ5 GLY A 184 UNP O05209 VAL 184 SEE REMARK 999
SEQADV 1CZ5 GLY A 185 UNP O05209 SER 185 SEE REMARK 999
SEQRES 1 A 185 MET GLU SER ASN ASN GLY ILE ILE LEU ARG VAL ALA GLU
SEQRES 2 A 185 ALA ASN SER THR ASP PRO GLY MET SER ARG VAL ARG LEU
SEQRES 3 A 185 ASP GLU SER SER ARG ARG LEU LEU ASP ALA GLU ILE GLY
SEQRES 4 A 185 ASP VAL VAL GLU ILE GLU LYS VAL ARG LYS THR VAL GLY
SEQRES 5 A 185 ARG VAL TYR ARG ALA ARG PRO GLU ASP GLU ASN LYS GLY
SEQRES 6 A 185 ILE VAL ARG ILE ASP SER VAL MET ARG ASN ASN CYS GLY
SEQRES 7 A 185 ALA SER ILE GLY ASP LYS VAL LYS VAL ARG LYS VAL ARG
SEQRES 8 A 185 THR GLU ILE ALA LYS LYS VAL THR LEU ALA PRO ILE ILE
SEQRES 9 A 185 ARG LYS ASP GLN ARG LEU LYS PHE GLY GLU GLY ILE GLU
SEQRES 10 A 185 GLU TYR VAL GLN ARG ALA LEU ILE ARG ARG PRO MET LEU
SEQRES 11 A 185 GLU GLN ASP ASN ILE SER VAL PRO GLY LEU THR LEU ALA
SEQRES 12 A 185 GLY GLN THR GLY LEU LEU PHE LYS VAL VAL LYS THR LEU
SEQRES 13 A 185 PRO SER LYS VAL PRO VAL GLU ILE GLY GLU GLU THR LYS
SEQRES 14 A 185 ILE GLU ILE ARG GLU GLU PRO ALA SER GLU VAL LEU GLU
SEQRES 15 A 185 GLU GLY GLY
HELIX 1 1 ASP A 27 LEU A 33 1 7
HELIX 2 2 ASP A 70 GLY A 78 1 9
HELIX 3 3 GLY A 115 ILE A 125 1 11
SHEET 1 A 7 GLY A 6 ALA A 12 0
SHEET 2 A 7 ILE A 66 ARG A 68 1 O VAL A 67 N ALA A 12
SHEET 3 A 7 GLY A 6 ALA A 12 1 O ARG A 10 N VAL A 67
SHEET 4 A 7 VAL A 85 VAL A 90 -1 N VAL A 85 O LEU A 9
SHEET 5 A 7 VAL A 41 GLU A 45 -1 O VAL A 41 N VAL A 90
SHEET 6 A 7 LYS A 49 ARG A 56 -1 N THR A 50 O ILE A 44
SHEET 7 A 7 ARG A 23 LEU A 26 1 O VAL A 24 N TYR A 55
SHEET 1 B 4 ASN A 134 ILE A 135 0
SHEET 2 B 4 PHE A 150 THR A 155 -1 O PHE A 150 N ILE A 135
SHEET 3 B 4 LYS A 97 PRO A 102 -1 N THR A 99 O LYS A 154
SHEET 4 B 4 LYS A 169 ILE A 172 1 O LYS A 169 N VAL A 98
SHEET 1 C 2 PRO A 128 MET A 129 0
SHEET 2 C 2 VAL A 162 GLU A 163 -1 O VAL A 162 N MET A 129
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