Header list of 1rfl.pdb file
Complete list - r 2 2 Bytes
HEADER UNKNOWN FUNCTION 10-NOV-03 1RFL
TITLE NMR DATA DRIVEN STRUCTURAL MODEL OF G-DOMAIN OF MNME PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE TRNA MODIFICATION GTPASE TRME;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GDOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: TRME, THDF, MNME, B3706;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GTPASE DOMAIN, ALPHA/BETA, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.MONLEON,V.ESTEVE,M.MARTINEZ-VICENTE,L.YIM,M.E.ARMENGOD,B.CELDA
REVDAT 4 02-MAR-22 1RFL 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1RFL 1 VERSN
REVDAT 2 24-APR-07 1RFL 1 JRNL
REVDAT 1 02-DEC-03 1RFL 0
JRNL AUTH D.MONLEON,M.MARTINEZ-VICENTE,V.ESTEVE,L.YIM,S.PRADO,
JRNL AUTH 2 M.E.ARMENGOD,B.CELDA
JRNL TITL STRUCTURAL INSIGHTS INTO THE GTPASE DOMAIN OF ESCHERICHIA
JRNL TITL 2 COLI MNME PROTEIN.
JRNL REF PROTEINS V. 66 726 2007
JRNL REFN ISSN 0887-3585
JRNL PMID 17143896
JRNL DOI 10.1002/PROT.21186
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2002, DYANA 2000
REMARK 3 AUTHORS : DELAGLIO ET AL. (NMRPIPE), GUNTERT ET AL. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RFL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020704.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 50 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.3 GDOMAIN MNME, PHOSPHATE
REMARK 210 BUFFER, NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE EXPERIMENTS FOR
REMARK 210 BB ASSIGNMENT; 3D_15N-SEPARATED_
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DPX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 2002, DYANA 2000
REMARK 210 METHOD USED : NMR RESTRAINTS WERE OBTAINED
REMARK 210 FROM THE BACKBONE ASSIGNMENT
REMARK 210 (TALOS ANALYSIS FOR DIHEDRAL
REMARK 210 ANGLE CONSTRAINTS) AND FROM THE
REMARK 210 15N-EDITED 3D NOESY. ADDITIONAL
REMARK 210 STRUCTURAL INFORMATION WAS
REMARK 210 OBTAINED FROM THE HOMOLOGOUS
REMARK 210 GTPASE PROTEIN STRUCTURES.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: BACKBONE ASSIGNMENT WOULD NOT BE POSSIBLE WITHOUT
REMARK 210 CRYOPROBE SPECTROMETERS BECAUSE OF THE LOW SOLUBILITY AND
REMARK 210 STABILITY OF THE PROTEIN.
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
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 LEU A 4 86.65 -160.74
REMARK 500 1 MET A 8 -176.35 -171.68
REMARK 500 1 ARG A 15 150.56 63.87
REMARK 500 1 ASN A 17 85.44 78.56
REMARK 500 1 ALA A 18 35.86 -168.78
REMARK 500 1 LYS A 20 -63.02 -103.63
REMARK 500 1 GLU A 31 -63.46 -92.65
REMARK 500 1 ALA A 32 98.04 -43.40
REMARK 500 1 ALA A 39 30.54 39.26
REMARK 500 1 HIS A 49 -175.84 51.38
REMARK 500 1 ALA A 63 -96.26 -88.28
REMARK 500 1 ARG A 74 -43.25 -165.43
REMARK 500 1 ILE A 77 84.96 40.36
REMARK 500 1 TRP A 81 -162.30 -106.91
REMARK 500 1 GLU A 83 88.77 170.52
REMARK 500 1 ILE A 84 128.50 -173.88
REMARK 500 1 ASP A 88 -55.34 -133.74
REMARK 500 1 ALA A 105 62.85 -69.97
REMARK 500 1 GLU A 106 -32.13 169.80
REMARK 500 1 GLU A 110 -51.54 -150.16
REMARK 500 1 ARG A 114 54.93 -115.18
REMARK 500 1 ALA A 117 -70.06 -101.11
REMARK 500 1 LYS A 118 88.84 82.88
REMARK 500 1 PRO A 120 -168.61 -75.04
REMARK 500 1 VAL A 123 42.31 -142.14
REMARK 500 1 ARG A 125 177.67 -52.95
REMARK 500 1 ASN A 126 107.42 59.36
REMARK 500 1 ALA A 128 76.02 -67.80
REMARK 500 1 ASP A 129 -36.57 176.20
REMARK 500 1 GLU A 133 48.19 -102.32
REMARK 500 1 SER A 138 -69.14 70.76
REMARK 500 1 GLU A 139 -176.01 174.42
REMARK 500 1 VAL A 140 152.56 73.14
REMARK 500 1 ALA A 150 -75.44 -78.96
REMARK 500 1 ARG A 151 -85.12 -43.50
REMARK 500 1 GLU A 154 -70.30 -50.21
REMARK 500 1 SER A 166 -72.36 -58.41
REMARK 500 1 ILE A 169 169.09 55.16
REMARK 500 1 HIS A 170 113.99 87.12
REMARK 500 2 MET A 8 -166.48 -165.97
REMARK 500 2 ASN A 17 83.89 67.48
REMARK 500 2 ALA A 18 -57.50 -158.19
REMARK 500 2 LYS A 20 -87.01 -110.20
REMARK 500 2 ASN A 25 -70.54 -44.07
REMARK 500 2 LEU A 27 -70.67 -48.94
REMARK 500 2 GLU A 31 169.64 54.48
REMARK 500 2 ALA A 32 81.19 42.96
REMARK 500 2 ASP A 37 78.00 -111.93
REMARK 500 2 THR A 41 -160.56 40.64
REMARK 500 2 HIS A 49 -175.55 50.36
REMARK 500
REMARK 500 THIS ENTRY HAS 851 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5861 RELATED DB: BMRB
REMARK 900 BACKBONE RESONANCE ASSIGNMENT OF GDOMAIN MNME PROTEIN
DBREF 1RFL A 1 168 UNP P25522 TRME_ECOLI 210 377
SEQADV 1RFL ILE A 169 UNP P25522 CLONING ARTIFACT
SEQADV 1RFL HIS A 170 UNP P25522 CLONING ARTIFACT
SEQADV 1RFL ARG A 171 UNP P25522 CLONING ARTIFACT
SEQADV 1RFL ASP A 172 UNP P25522 CLONING ARTIFACT
SEQRES 1 A 172 GLY SER LEU LEU ARG GLU GLY MET LYS VAL VAL ILE ALA
SEQRES 2 A 172 GLY ARG PRO ASN ALA GLY LYS SER SER LEU LEU ASN ALA
SEQRES 3 A 172 LEU ALA GLY ARG GLU ALA ALA ILE VAL THR ASP ILE ALA
SEQRES 4 A 172 GLY THR THR ARG ASP VAL LEU ARG GLU HIS ILE HIS ILE
SEQRES 5 A 172 ASP GLY MET PRO LEU HIS ILE ILE ASP THR ALA GLY LEU
SEQRES 6 A 172 ARG GLU ALA SER ASP GLU VAL GLU ARG ILE GLY ILE GLU
SEQRES 7 A 172 ARG ALA TRP GLN GLU ILE GLU GLN ALA ASP ARG VAL LEU
SEQRES 8 A 172 PHE MET VAL ASP GLY THR THR THR ASP ALA VAL ASP PRO
SEQRES 9 A 172 ALA GLU ILE TRP PRO GLU PHE ILE ALA ARG LEU PRO ALA
SEQRES 10 A 172 LYS LEU PRO ILE THR VAL VAL ARG ASN LYS ALA ASP ILE
SEQRES 11 A 172 THR GLY GLU THR LEU GLY MET SER GLU VAL ASN GLY HIS
SEQRES 12 A 172 ALA LEU ILE ARG LEU SER ALA ARG THR GLY GLU GLY VAL
SEQRES 13 A 172 ASP VAL LEU ARG ASN HIS LEU LYS GLN SER MET GLY ILE
SEQRES 14 A 172 HIS ARG ASP
HELIX 1 1 LYS A 20 ALA A 28 1 9
HELIX 2 2 LEU A 65 GLY A 76 1 12
HELIX 3 3 ASP A 103 ILE A 112 1 10
HELIX 4 4 ILE A 130 THR A 134 5 5
HELIX 5 5 VAL A 156 GLN A 165 1 10
SHEET 1 A 2 LYS A 9 ILE A 12 0
SHEET 2 A 2 ALA A 87 LEU A 91 1 O ASP A 88 N LYS A 9
SHEET 1 B 2 PRO A 120 ILE A 121 0
SHEET 2 B 2 ILE A 146 ARG A 147 1 O ILE A 146 N ILE A 121
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 2 2 Bytes