Header list of 1xx3.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSPORT PROTEIN 03-NOV-04 1XX3
TITLE SOLUTION STRUCTURE OF ESCHERICHIA COLI TONB-CTD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TONB PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: TONB, EXBA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDEST14
KEYWDS TONB-CTD, C-TERMINAL DOMAIN, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.S.PEACOCK,A.M.WELJIE,S.P.HOWARD,F.D.PRICE,H.J.VOGEL
REVDAT 3 02-MAR-22 1XX3 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1XX3 1 VERSN
REVDAT 1 15-FEB-05 1XX3 0
JRNL AUTH R.S.PEACOCK,A.M.WELJIE,S.P.HOWARD,F.D.PRICE,H.J.VOGEL
JRNL TITL THE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF TONB AND
JRNL TITL 2 INTERACTION STUDIES WITH TONB BOX PEPTIDES
JRNL REF J.MOL.BIOL. V. 345 1185 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15644214
JRNL DOI 10.1016/J.JMB.2004.11.026
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), AXEL BRUNGER ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2711 RESTRAINTS, 2544 OF WHICH ARE NOE-DERIVED, 21 OF WHICH ARE
REMARK 3 HYDROGEN BOND RESTRAINTS, AND 146 OF WHICH ARE DIHEDRAL ANGLE
REMARK 3 RESTRAINTS
REMARK 4
REMARK 4 1XX3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030867.
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 : 100 MM SODIUM CHLORIDE, 50 MM
REMARK 210 SODIUM PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0 MM TONB-CTD U-15N,13C; 50 MM
REMARK 210 SODIUM PHOSPHATE BUFFER; 100 MM
REMARK 210 NACL; 600 UM SODIUM AZIDE, 90%
REMARK 210 H2O 10% D2O; 1.0 MM TONB-CTD U-
REMARK 210 15N; 50 MM SODIUM PHOSPHATE
REMARK 210 BUFFER; 100 MM NACL ; 600 UM
REMARK 210 SODIUM AZIDE; PH 7.0, 90% H2O 10%
REMARK 210 D2O; 1.0 MM TONB-CTD U-15N; 50
REMARK 210 MM SODIUM PHOSPHATE BUFFER; 100
REMARK 210 MM NACL; 600 UM SODIUM AZIDE; PH
REMARK 210 7.0, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3 REV 2004.194.17.02,
REMARK 210 NMRVIEW 5.0.4, ARIA 2.0
REMARK 210 METHOD USED : THIS STRUCTURE WAS REFINED USING
REMARK 210 STANDARD ARIA2.0 PROTOCOLS
REMARK 210 (DISTANCE GEOMETRY,SIMULATED
REMARK 210 ANNEALING, TORSION ANGLE
REMARK 210 DYNAMICS, WATER REFINEMENT)
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: THIS STRUCTURE WAS DETERMINED USING STANDARD TRIPLE
REMARK 210 -RESONANCE NMR SPECTROSCOPY TECHNIQUES
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A 96
REMARK 465 HIS A 97
REMARK 465 HIS A 98
REMARK 465 HIS A 99
REMARK 465 HIS A 100
REMARK 465 HIS A 101
REMARK 465 HIS A 102
REMARK 465 VAL A 103
REMARK 465 LYS A 104
REMARK 465 LYS A 105
REMARK 465 VAL A 106
REMARK 465 GLN A 107
REMARK 465 GLU A 108
REMARK 465 GLN A 109
REMARK 465 PRO A 110
REMARK 465 LYS A 111
REMARK 465 ARG A 112
REMARK 465 ASP A 113
REMARK 465 VAL A 114
REMARK 465 LYS A 115
REMARK 465 PRO A 116
REMARK 465 VAL A 117
REMARK 465 GLU A 118
REMARK 465 SER A 119
REMARK 465 ARG A 120
REMARK 465 PRO A 121
REMARK 465 ALA A 122
REMARK 465 SER A 123
REMARK 465 PRO A 124
REMARK 465 PHE A 125
REMARK 465 GLU A 126
REMARK 465 ASN A 127
REMARK 465 THR A 128
REMARK 465 ALA A 129
REMARK 465 PRO A 130
REMARK 465 ALA A 131
REMARK 465 ARG A 132
REMARK 465 LEU A 133
REMARK 465 THR A 134
REMARK 465 SER A 135
REMARK 465 SER A 136
REMARK 465 THR A 137
REMARK 465 ALA A 138
REMARK 465 THR A 139
REMARK 465 ALA A 140
REMARK 465 ALA A 141
REMARK 465 THR A 142
REMARK 465 SER A 143
REMARK 465 LYS A 144
REMARK 465 PRO A 145
REMARK 465 VAL A 146
REMARK 465 THR A 147
REMARK 465 SER A 148
REMARK 465 VAL A 149
REMARK 465 ALA A 150
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 LYS A 197 -74.23 -61.45
REMARK 500 1 ALA A 199 -83.34 -44.01
REMARK 500 2 PRO A 198 -151.37 -92.08
REMARK 500 2 ALA A 199 -94.81 -120.04
REMARK 500 3 SER A 157 -81.16 -116.58
REMARK 500 3 PRO A 184 2.25 -65.07
REMARK 500 3 ALA A 199 -92.93 -97.04
REMARK 500 4 ARG A 158 52.29 -103.27
REMARK 500 4 ALA A 199 -97.16 -81.55
REMARK 500 5 SER A 157 95.28 -160.04
REMARK 500 5 PRO A 184 2.03 -65.49
REMARK 500 5 ALA A 199 -89.49 -72.21
REMARK 500 6 SER A 157 92.70 -161.71
REMARK 500 6 PRO A 184 3.43 -68.78
REMARK 500 6 PRO A 198 -155.05 -82.98
REMARK 500 6 ALA A 199 -89.75 -121.06
REMARK 500 7 PRO A 184 4.84 -65.65
REMARK 500 7 PRO A 198 -153.88 -91.05
REMARK 500 7 ALA A 199 -88.80 -107.27
REMARK 500 8 ARG A 158 57.24 -114.17
REMARK 500 8 PRO A 198 -143.76 -92.89
REMARK 500 8 ALA A 199 -96.29 -122.67
REMARK 500 9 PRO A 153 100.83 -55.80
REMARK 500 9 PRO A 184 3.07 -65.61
REMARK 500 9 ALA A 199 -87.59 -93.71
REMARK 500 10 PRO A 153 101.18 -52.93
REMARK 500 10 SER A 157 103.46 -163.89
REMARK 500 10 ALA A 199 -83.77 -95.12
REMARK 500 11 ARG A 158 59.82 -93.96
REMARK 500 11 PRO A 184 2.04 -65.28
REMARK 500 11 PRO A 198 -154.50 -84.44
REMARK 500 11 ALA A 199 -82.46 -132.34
REMARK 500 12 PRO A 198 -147.66 -85.11
REMARK 500 12 ALA A 199 -96.14 -122.47
REMARK 500 13 PRO A 184 3.24 -65.53
REMARK 500 13 ALA A 199 -93.09 -91.30
REMARK 500 14 ARG A 158 52.94 -111.42
REMARK 500 14 PRO A 198 -155.64 -80.31
REMARK 500 14 ALA A 199 -84.05 -119.98
REMARK 500 15 ARG A 158 58.58 -118.16
REMARK 500 15 PRO A 198 -159.14 -89.51
REMARK 500 15 ALA A 199 -104.48 -105.56
REMARK 500 16 SER A 195 146.78 -170.48
REMARK 500 16 ALA A 199 -110.61 -99.03
REMARK 500 17 ARG A 158 71.48 -109.02
REMARK 500 17 PRO A 198 -155.00 -89.94
REMARK 500 17 ALA A 199 -92.11 -102.83
REMARK 500 18 PRO A 184 8.36 -67.32
REMARK 500 18 LYS A 197 -174.11 -58.07
REMARK 500 18 PRO A 198 -75.73 -24.00
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6375 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS OF TONB-CTD
DBREF 1XX3 A 103 239 UNP P02929 TONB_ECOLI 103 239
SEQADV 1XX3 MET A 96 UNP P02929 CLONING ARTIFACT
SEQADV 1XX3 HIS A 97 UNP P02929 CLONING ARTIFACT
SEQADV 1XX3 HIS A 98 UNP P02929 CLONING ARTIFACT
SEQADV 1XX3 HIS A 99 UNP P02929 CLONING ARTIFACT
SEQADV 1XX3 HIS A 100 UNP P02929 CLONING ARTIFACT
SEQADV 1XX3 HIS A 101 UNP P02929 CLONING ARTIFACT
SEQADV 1XX3 HIS A 102 UNP P02929 CLONING ARTIFACT
SEQRES 1 A 144 MET HIS HIS HIS HIS HIS HIS VAL LYS LYS VAL GLN GLU
SEQRES 2 A 144 GLN PRO LYS ARG ASP VAL LYS PRO VAL GLU SER ARG PRO
SEQRES 3 A 144 ALA SER PRO PHE GLU ASN THR ALA PRO ALA ARG LEU THR
SEQRES 4 A 144 SER SER THR ALA THR ALA ALA THR SER LYS PRO VAL THR
SEQRES 5 A 144 SER VAL ALA SER GLY PRO ARG ALA LEU SER ARG ASN GLN
SEQRES 6 A 144 PRO GLN TYR PRO ALA ARG ALA GLN ALA LEU ARG ILE GLU
SEQRES 7 A 144 GLY GLN VAL LYS VAL LYS PHE ASP VAL THR PRO ASP GLY
SEQRES 8 A 144 ARG VAL ASP ASN VAL GLN ILE LEU SER ALA LYS PRO ALA
SEQRES 9 A 144 ASN MET PHE GLU ARG GLU VAL LYS ASN ALA MET ARG ARG
SEQRES 10 A 144 TRP ARG TYR GLU PRO GLY LYS PRO GLY SER GLY ILE VAL
SEQRES 11 A 144 VAL ASN ILE LEU PHE LYS ILE ASN GLY THR THR GLU ILE
SEQRES 12 A 144 GLN
HELIX 1 1 PRO A 164 ALA A 169 1 6
HELIX 2 2 PRO A 198 ARG A 211 1 14
SHEET 1 A 2 ALA A 155 SER A 157 0
SHEET 2 A 2 ARG A 214 TYR A 215 -1 O ARG A 214 N LEU A 156
SHEET 1 B 4 VAL A 188 SER A 195 0
SHEET 2 B 4 GLY A 174 VAL A 182 -1 N LYS A 177 O SER A 195
SHEET 3 B 4 GLY A 221 LYS A 231 -1 O PHE A 230 N GLY A 174
SHEET 4 B 4 THR A 235 GLN A 239 -1 O GLN A 239 N ASN A 227
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