Header list of 1pqx.pdb file
Complete list - t 19 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-JUN-03 1PQX
TITLE SOLUTION NMR STRUCTURE OF STAPHYLOCOCCUS AUREUS PROTEIN SAV1430.
TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET ZR18.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HYPOTHETICAL PROTEIN MW1320;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: ZR18
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MU50;
SOURCE 3 ORGANISM_TAXID: 158878;
SOURCE 4 STRAIN: SUBSP. AUREUS MU50;
SOURCE 5 VARIANT: SUBSP. AUREUS MU50;
SOURCE 6 GENE: SAV1430;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21MGK;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: ZR18-21
KEYWDS ZR18, AUTOSTRUCTURE, SPINS, AUTOASSIGN, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, PSI,
KEYWDS 3 NESG, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.C.BARAN,J.M.ARAMINI,R.XIAO,Y.J.HUANG,T.B.ACTON,L.SHIH,
AUTHOR 2 G.T.MONTELIONE,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 7 24-AUG-22 1PQX 1 REMARK
REVDAT 6 09-SEP-20 1PQX 1 TITLE REMARK SEQADV
REVDAT 5 06-JUN-18 1PQX 1 REMARK
REVDAT 4 24-FEB-09 1PQX 1 VERSN
REVDAT 3 25-JAN-05 1PQX 1 AUTHOR KEYWDS REMARK
REVDAT 2 28-SEP-04 1PQX 1 REMARK
REVDAT 1 07-SEP-04 1PQX 0
JRNL AUTH M.C.BARAN,J.M.ARAMINI,R.XIAO,Y.J.HUANG,T.B.ACTON,L.SHIH,
JRNL AUTH 2 G.T.MONTELIONE
JRNL TITL SOLUTION STRUCUTRE OF THE HYPOTHETICAL STAPHYLOCOCCUS AUREUS
JRNL TITL 2 PROTEIN SAV1430. NORTHEST STRUCUTRAL GENOMICS CONSORTIUM
JRNL TITL 3 TARGET ZR18
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, X-PLOR
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1100 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE
REMARK 3 RESTRAINTS, 185 DIHEDRAL ANGLE RESTRAINTS, AND 28 HYDROGEN BOND
REMARK 3 RESTRAINTS.(14.8 CONSTRAINTS PER RESIDUE; 4.4 LONG-RANGE
REMARK 3 CONSTRAINTS PER RESIDUE). STRUCTURE DETERMINATION WAS PERFORMED
REMARK 3 ITERATIVLY USING AUTOSTRUCTURE (XPLOR). THE CONSTRAIN FILE FOR
REMARK 3 THIS ENTRY WAS UPDATED TO CORRESPOND TO THE XPLOR FORMAT ON
REMARK 3 SEPTEMBER 28, 2004.
REMARK 4
REMARK 4 1PQX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019518.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 274
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.15 MM ZR18, 20MM MES, 100MM
REMARK 210 NACL, 5MM CACL2, 10MM DTT, 0.02%
REMARK 210 NAN3, 5% D20 PH 6.5; 1.3 MM ZR18,
REMARK 210 20MM MES, 100MM NACL, 5MM CACL2,
REMARK 210 10MM DTT, 0.02% NAN3, 5% D20 PH
REMARK 210 6.5; 0.88 MM ZR18, 20MM MES,
REMARK 210 100MM NACL, 5MM CACL2, 10MM DTT,
REMARK 210 0.02% NAN3, 5% D20 PH 6.5; 0.88
REMARK 210 MM ZR18, 20MM MES, 100MM NACL,
REMARK 210 5MM CACL2, 10MM DTT, 0.02% NAN3,
REMARK 210 5% D20 PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-NOESY, 3D 13C-NOESY
REMARK 210 (ALIPHATIC AND AROMATIC); HNHA;
REMARK 210 HIGH RESOLUTION 13C, 1H-HSQC; H/
REMARK 210 D EXCHANGE; BACKBONE TR
REMARK 210 EXPERIMENTS AND 3D TOCSY'S; HCCH-
REMARK 210 COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, AUTOPROC 1.0,
REMARK 210 SPARKY 3.106, AUTOASSIGN 1.9,
REMARK 210 AUTOSTRUCTURE 1.1.2, X-PLOR
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 56
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : OVERALL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY. ALL AUTOMATIC ANALYSIS SOFTWARE WAS RUN OUT OF THE
REMARK 210 SPINS SOFTWARE. AUTOMATIC BACKBONE RESONANCE ASSIGNMENTS WERE
REMARK 210 MADE USING AUTOASSIGN. AUTOMATIC NOESY ASSIGNMENTS AS WELL AS
REMARK 210 DISTANCE AND HYDROGEN BOND RESTRAINTS WERE DETERMINED USING
REMARK 210 HYPER AND TALOS.
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 TRP A 71 H LEU A 75 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 LYS A 2 62.80 -166.84
REMARK 500 1 ILE A 3 101.64 55.10
REMARK 500 1 SER A 5 139.99 -172.59
REMARK 500 1 HIS A 12 20.13 -140.76
REMARK 500 1 ARG A 23 -158.56 44.10
REMARK 500 1 GLU A 24 -96.95 32.56
REMARK 500 1 MET A 26 -123.61 -90.49
REMARK 500 1 LYS A 33 34.76 -154.09
REMARK 500 1 VAL A 34 177.93 51.57
REMARK 500 1 ASP A 35 109.26 62.52
REMARK 500 1 ASP A 36 21.06 175.24
REMARK 500 1 MET A 58 -138.99 44.00
REMARK 500 1 GLU A 83 88.11 -160.26
REMARK 500 1 LEU A 84 21.63 -164.17
REMARK 500 1 GLU A 85 123.71 83.32
REMARK 500 1 HIS A 90 -36.36 -155.99
REMARK 500 2 GLU A 8 -12.39 -161.20
REMARK 500 2 ASN A 11 -152.45 -145.19
REMARK 500 2 HIS A 12 149.33 -175.97
REMARK 500 2 ASN A 13 -16.93 69.36
REMARK 500 2 GLU A 21 83.15 56.92
REMARK 500 2 GLU A 24 68.37 38.94
REMARK 500 2 THR A 27 -124.18 -76.73
REMARK 500 2 LYS A 33 106.59 89.52
REMARK 500 2 VAL A 34 108.38 15.57
REMARK 500 2 ASP A 36 -100.20 50.69
REMARK 500 2 SER A 37 61.02 -174.43
REMARK 500 2 MET A 58 -107.53 41.03
REMARK 500 2 PHE A 82 44.55 -85.70
REMARK 500 2 GLU A 83 -35.08 -160.59
REMARK 500 2 LEU A 84 56.16 39.72
REMARK 500 2 GLU A 85 -150.93 42.22
REMARK 500 2 HIS A 89 -103.50 -60.60
REMARK 500 2 HIS A 90 -36.90 -130.96
REMARK 500 3 SER A 5 147.42 -171.13
REMARK 500 3 SER A 7 -157.82 -93.63
REMARK 500 3 THR A 9 59.85 -149.95
REMARK 500 3 PRO A 10 20.43 -76.73
REMARK 500 3 ASN A 11 -16.92 -142.75
REMARK 500 3 HIS A 12 -157.18 63.27
REMARK 500 3 ASN A 13 -51.79 71.55
REMARK 500 3 GLU A 21 131.29 66.07
REMARK 500 3 ARG A 23 90.28 39.28
REMARK 500 3 GLU A 24 -91.31 51.31
REMARK 500 3 THR A 27 -151.87 38.79
REMARK 500 3 LYS A 33 31.87 -155.38
REMARK 500 3 VAL A 34 166.10 73.71
REMARK 500 3 ASP A 35 -110.32 -155.60
REMARK 500 3 ASP A 36 -39.45 -167.94
REMARK 500 3 LYS A 52 -64.19 51.83
REMARK 500
REMARK 500 THIS ENTRY HAS 203 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 23 0.10 SIDE CHAIN
REMARK 500 2 ARG A 23 0.13 SIDE CHAIN
REMARK 500 3 ARG A 23 0.30 SIDE CHAIN
REMARK 500 4 ARG A 23 0.24 SIDE CHAIN
REMARK 500 5 ARG A 23 0.27 SIDE CHAIN
REMARK 500 7 ARG A 23 0.17 SIDE CHAIN
REMARK 500 8 ARG A 23 0.29 SIDE CHAIN
REMARK 500 9 ARG A 23 0.18 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ZR18 RELATED DB: TARGETDB
DBREF 1PQX A 1 83 UNP Q99U58 Q99U58_STAAM 1 83
SEQADV 1PQX LEU A 84 UNP Q99U58 EXPRESSION TAG
SEQADV 1PQX GLU A 85 UNP Q99U58 EXPRESSION TAG
SEQADV 1PQX HIS A 86 UNP Q99U58 EXPRESSION TAG
SEQADV 1PQX HIS A 87 UNP Q99U58 EXPRESSION TAG
SEQADV 1PQX HIS A 88 UNP Q99U58 EXPRESSION TAG
SEQADV 1PQX HIS A 89 UNP Q99U58 EXPRESSION TAG
SEQADV 1PQX HIS A 90 UNP Q99U58 EXPRESSION TAG
SEQADV 1PQX HIS A 91 UNP Q99U58 EXPRESSION TAG
SEQRES 1 A 91 MET LYS ILE ILE SER ILE SER GLU THR PRO ASN HIS ASN
SEQRES 2 A 91 THR MET LYS ILE THR LEU SER GLU SER ARG GLU GLY MET
SEQRES 3 A 91 THR SER ASP THR TYR THR LYS VAL ASP ASP SER GLN PRO
SEQRES 4 A 91 ALA PHE ILE ASN ASP ILE LEU LYS VAL GLU GLY VAL LYS
SEQRES 5 A 91 SER ILE PHE HIS VAL MET ASP PHE ILE SER VAL ASP LYS
SEQRES 6 A 91 GLU ASN ASP ALA ASN TRP GLU THR VAL LEU PRO LYS VAL
SEQRES 7 A 91 GLU ALA VAL PHE GLU LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 PRO A 39 VAL A 48 1 10
HELIX 2 2 ASN A 70 PHE A 82 1 13
SHEET 1 A 4 THR A 14 THR A 18 0
SHEET 2 A 4 PHE A 60 LYS A 65 -1 O ILE A 61 N ILE A 17
SHEET 3 A 4 VAL A 51 VAL A 57 -1 N PHE A 55 O SER A 62
SHEET 4 A 4 ASP A 29 TYR A 31 -1 N ASP A 29 O HIS A 56
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 - t 19 2 Bytes