Header list of 1xhj.pdb file
Complete list - r 25 2 Bytes
HEADER METAL BINDING PROTEIN 20-SEP-04 1XHJ
TITLE SOLUTION STRUCTURE OF THE STAPHYLOCOCCUS EPIDERMIDIS PROTEIN SE0630.
TITLE 2 NORTHEST STRUCTURAL GENOMICS CONSORTIUM TARGET SER8.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITROGEN FIXATION PROTEIN NIFU;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS EPIDERMIDIS;
SOURCE 3 ORGANISM_TAXID: 176280;
SOURCE 4 STRAIN: ATCC 12228;
SOURCE 5 GENE: SE0936;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21MGK;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET21;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: SER8-21
KEYWDS ALPHA-BETA, NIFU-LIKE, STRUCTURAL GENOMICS, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NESG, PSI, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 3 METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.C.BARAN,Y.P.HUANG,T.ACTON,R.XIAO,G.T.MONTELIONE,NORTHEAST
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 5 13-JUL-11 1XHJ 1 VERSN
REVDAT 4 24-FEB-09 1XHJ 1 VERSN
REVDAT 3 10-MAY-05 1XHJ 1 TITLE
REVDAT 2 25-JAN-05 1XHJ 1 AUTHOR KEYWDS REMARK
REVDAT 1 07-DEC-04 1XHJ 0
JRNL AUTH M.C.BARAN,Y.P.HUANG,T.ACTON,R.XIAO,G.T.MONTELIONE
JRNL TITL SOLUTION STRUCTURE OF THE STAPHYLOCOCCUS EPIDERMIDIS PROTEIN
JRNL TITL 2 SE0630. NORTHEST STRUCUTRAL GENOMICS CONSORTIUM TARGET SER8.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 2.9.7
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON A TOTAL OF
REMARK 3 1311 CONFORMATIONALLY RESTRICTING NON-DERIVED DISTANCE
REMARK 3 RESTRAINTS. THE STRUCTURE CONTAINS 14.9 RESTRAINTS PER RESIDUE,
REMARK 3 WITH 3.5 LONG RANGE RESTRAINTS PER RESIDUE. STRUCTURE
REMARK 3 DETERMINATION WAS PERFORMED ITERATIVELY USING AUTOSTRUCTURE.
REMARK 4
REMARK 4 1XHJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-04.
REMARK 100 THE RCSB ID CODE IS RCSB030368.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.02% NAN3, 10MM DTT, 5MM CACL2,
REMARK 210 100MM NACL, 20MM MES, PH 6.5, 5%
REMARK 210 C13, 100% N15, 5% D2O, 95% H20;
REMARK 210 0.02% NAN3, 10MM DTT, 5MM CACL2,
REMARK 210 100MM NACL, 20MM MES, PH 6.5,
REMARK 210 100% C13, 100% N15, 5% D2O, 95%
REMARK 210 H20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : C13-HSQC; NH-HSQC; HNCO; HNCAB;
REMARK 210 N15-NOESY; C13-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 2.9.7, NMRPIPE 2.1,
REMARK 210 AUTOASSIGN 1.14, AUTOSTRUCTURE
REMARK 210 2.0, SPINS 5.0, HYPER 3.2, SPARKY
REMARK 210 3.106, VNMR 6.1, XWIN-NMR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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. AUTOMATIC BACKBONE ASSIGNMENTS WERE MADE USING
REMARK 210 AUTOASSIGN. AUTOMATIC NOESY ASSIGNMENTS WERE MADE USING
REMARK 210 AUTOSTRUCTURE. DIHEDRAL ANGLE RESTRAINTS WERE MADE USING HYPER
REMARK 210 AND TALOS. THE SPINS DATABASE SOFTWARE WAS USED AS AN INTEGRATING
REMARK 210 AGENT.
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 HG1 THR A 50 H CYS A 51 1.56
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 PRO A 2 -81.06 -75.05
REMARK 500 1 GLU A 4 37.64 -81.36
REMARK 500 1 ASN A 5 175.41 -53.68
REMARK 500 1 PRO A 6 91.03 -39.83
REMARK 500 1 THR A 7 -175.27 -66.76
REMARK 500 1 ALA A 47 -103.27 -173.75
REMARK 500 1 CYS A 48 98.82 -175.84
REMARK 500 1 THR A 50 -44.40 -140.25
REMARK 500 1 VAL A 70 70.11 -152.47
REMARK 500 1 LEU A 81 44.66 -95.95
REMARK 500 1 GLU A 82 154.83 64.05
REMARK 500 1 HIS A 83 76.96 -178.85
REMARK 500 1 HIS A 84 179.21 -59.51
REMARK 500 2 THR A 3 170.06 -58.02
REMARK 500 2 PRO A 6 40.87 -76.84
REMARK 500 2 THR A 7 -161.11 -71.72
REMARK 500 2 ASP A 37 -9.17 -55.45
REMARK 500 2 HIS A 45 112.70 -162.21
REMARK 500 2 ALA A 47 -90.21 -77.57
REMARK 500 2 CYS A 51 76.82 32.64
REMARK 500 2 GLU A 69 -120.39 -85.87
REMARK 500 2 VAL A 70 53.24 36.53
REMARK 500 2 PRO A 71 99.81 -42.46
REMARK 500 2 ILE A 74 -50.50 -127.72
REMARK 500 2 GLU A 75 109.28 -164.86
REMARK 500 2 HIS A 84 -104.65 -59.18
REMARK 500 2 HIS A 85 164.89 58.13
REMARK 500 3 GLU A 4 32.35 -93.17
REMARK 500 3 ASP A 37 -85.55 52.69
REMARK 500 3 ALA A 47 -46.35 70.25
REMARK 500 3 CYS A 48 31.50 -166.18
REMARK 500 3 CYS A 51 -63.92 -178.28
REMARK 500 3 GLU A 69 -118.93 -84.02
REMARK 500 3 VAL A 70 53.89 35.91
REMARK 500 3 PRO A 71 109.38 -42.15
REMARK 500 3 ILE A 74 -32.62 -140.01
REMARK 500 3 GLU A 75 107.33 -167.01
REMARK 500 3 HIS A 84 139.55 61.99
REMARK 500 3 HIS A 87 -163.60 -66.72
REMARK 500 4 PRO A 2 -83.63 -74.53
REMARK 500 4 THR A 3 147.35 62.83
REMARK 500 4 ASN A 5 -165.87 43.70
REMARK 500 4 PRO A 6 84.69 -68.97
REMARK 500 4 GLU A 36 85.34 -154.20
REMARK 500 4 ASP A 37 -86.12 56.52
REMARK 500 4 HIS A 45 78.55 -155.87
REMARK 500 4 ALA A 47 98.94 67.84
REMARK 500 4 THR A 50 -36.77 -152.76
REMARK 500 4 CYS A 51 48.88 -151.95
REMARK 500 4 VAL A 70 71.26 -153.76
REMARK 500
REMARK 500 THIS ENTRY HAS 124 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 18 0.28 SIDE CHAIN
REMARK 500 1 ARG A 20 0.09 SIDE CHAIN
REMARK 500 1 ARG A 25 0.25 SIDE CHAIN
REMARK 500 1 ARG A 64 0.31 SIDE CHAIN
REMARK 500 2 ARG A 18 0.31 SIDE CHAIN
REMARK 500 2 ARG A 20 0.31 SIDE CHAIN
REMARK 500 2 ARG A 25 0.17 SIDE CHAIN
REMARK 500 2 ARG A 64 0.30 SIDE CHAIN
REMARK 500 3 ARG A 20 0.26 SIDE CHAIN
REMARK 500 3 ARG A 25 0.28 SIDE CHAIN
REMARK 500 3 ARG A 64 0.29 SIDE CHAIN
REMARK 500 4 ARG A 18 0.30 SIDE CHAIN
REMARK 500 4 ARG A 20 0.15 SIDE CHAIN
REMARK 500 4 ARG A 25 0.26 SIDE CHAIN
REMARK 500 4 ARG A 64 0.31 SIDE CHAIN
REMARK 500 5 ARG A 18 0.17 SIDE CHAIN
REMARK 500 5 ARG A 20 0.28 SIDE CHAIN
REMARK 500 5 ARG A 64 0.31 SIDE CHAIN
REMARK 500 6 ARG A 18 0.08 SIDE CHAIN
REMARK 500 6 ARG A 20 0.31 SIDE CHAIN
REMARK 500 6 ARG A 25 0.20 SIDE CHAIN
REMARK 500 7 ARG A 18 0.21 SIDE CHAIN
REMARK 500 7 ARG A 20 0.28 SIDE CHAIN
REMARK 500 7 ARG A 64 0.29 SIDE CHAIN
REMARK 500 8 ARG A 20 0.17 SIDE CHAIN
REMARK 500 8 ARG A 25 0.12 SIDE CHAIN
REMARK 500 8 ARG A 64 0.18 SIDE CHAIN
REMARK 500 9 ARG A 18 0.31 SIDE CHAIN
REMARK 500 9 ARG A 20 0.19 SIDE CHAIN
REMARK 500 9 ARG A 25 0.31 SIDE CHAIN
REMARK 500 9 ARG A 64 0.20 SIDE CHAIN
REMARK 500 10 ARG A 18 0.30 SIDE CHAIN
REMARK 500 10 ARG A 20 0.27 SIDE CHAIN
REMARK 500 10 ARG A 25 0.27 SIDE CHAIN
REMARK 500 10 ARG A 64 0.18 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SER8 RELATED DB: TARGETDB
DBREF 1XHJ A 1 80 UNP Q8CPV7 Q8CPV7_STAES 1 80
SEQADV 1XHJ LEU A 81 UNP Q8CPV7 EXPRESSION TAG
SEQADV 1XHJ GLU A 82 UNP Q8CPV7 EXPRESSION TAG
SEQADV 1XHJ HIS A 83 UNP Q8CPV7 EXPRESSION TAG
SEQADV 1XHJ HIS A 84 UNP Q8CPV7 EXPRESSION TAG
SEQADV 1XHJ HIS A 85 UNP Q8CPV7 EXPRESSION TAG
SEQADV 1XHJ HIS A 86 UNP Q8CPV7 EXPRESSION TAG
SEQADV 1XHJ HIS A 87 UNP Q8CPV7 EXPRESSION TAG
SEQADV 1XHJ HIS A 88 UNP Q8CPV7 EXPRESSION TAG
SEQRES 1 A 88 MET PRO THR GLU ASN PRO THR MET PHE ASP GLN VAL ALA
SEQRES 2 A 88 GLU VAL ILE GLU ARG LEU ARG PRO PHE LEU LEU ARG ASP
SEQRES 3 A 88 GLY GLY ASP CYS THR LEU VAL ASP VAL GLU ASP GLY ILE
SEQRES 4 A 88 VAL LYS LEU GLN LEU HIS GLY ALA CYS GLY THR CYS PRO
SEQRES 5 A 88 SER SER THR ILE THR LEU LYS ALA GLY ILE GLU ARG ALA
SEQRES 6 A 88 LEU HIS GLU GLU VAL PRO GLY VAL ILE GLU VAL GLU GLN
SEQRES 7 A 88 VAL PHE LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 THR A 7 GLY A 27 1 21
HELIX 2 2 PRO A 52 VAL A 70 1 19
SHEET 1 A 3 ASP A 29 ASP A 34 0
SHEET 2 A 3 ILE A 39 HIS A 45 -1 O LYS A 41 N VAL A 33
SHEET 3 A 3 GLU A 75 PHE A 80 1 O GLU A 77 N VAL A 40
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