Header list of 1ny9.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 12-FEB-03 1NY9
TITLE ANTIBIOTIC BINDING DOMAIN OF A TIPA-CLASS MULTIDRUG RESISTANCE
TITLE 2 TRANSCRIPTIONAL REGULATOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL ACTIVATOR TIPA-S;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ANTIBIOTIC BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;
SOURCE 3 ORGANISM_TAXID: 1916;
SOURCE 4 GENE: TIPA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: XL-1 BLUE CELLS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PREP4 AND PDS8
KEYWDS ALL ALPHA, GLOBIN LIKE, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.D.KAHMANN,H.J.SASS,M.G.ALLAN,H.SETO,C.J.THOMPSON,S.GRZESIEK
REVDAT 3 23-FEB-22 1NY9 1 REMARK
REVDAT 2 24-FEB-09 1NY9 1 VERSN
REVDAT 1 15-APR-03 1NY9 0
JRNL AUTH J.D.KAHMANN,H.J.SASS,M.G.ALLAN,H.SETO,C.J.THOMPSON,
JRNL AUTH 2 S.GRZESIEK
JRNL TITL STRUCTURAL BASIS FOR ANTIBIOTIC RECOGNITION BY THE
JRNL TITL 2 TIPA-CLASS OF MULTIDRUG-RESISTANCE TRANSCRIPTIONAL
JRNL TITL 3 REGULATORS
JRNL REF EMBO J. V. 22 1824 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 12682015
JRNL DOI 10.1093/EMBOJ/CDG181
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851 WITH MODIFICATIONS, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE MISSING RESIDUES IN REMARK 465 ARE MISSING IN THE STRUCTURE DUE
REMARK 3 TO DISORDER, BUT HAD BEEN PRESENT DURING THE EXPERIMENT.
REMARK 4
REMARK 4 1NY9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018344.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.9
REMARK 210 IONIC STRENGTH : 6 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM TIPAS U-15N, 5MM
REMARK 210 PHOSPHATE BUFFER, 5MM DTT; 1.5
REMARK 210 MM TIPAS U-15N,13C, 5MM
REMARK 210 PHOSPHATE BUFFER, 5MM DTT; 1.5
REMARK 210 MM TIPAS U-15N,13C, 5MM
REMARK 210 PHOSPHATE BUFFER, 5MM DTT; 0.8
REMARK 210 MM TIPAS U-15N,13C, 10 MR/ML PF1
REMARK 210 PHAGES, 5MM PHOSPHATE BUFFER,
REMARK 210 5MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : STANDARD TRIPLE AND DOUBLE
REMARK 210 RESONANCE EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, XEASY 1.2, PIPP
REMARK 210 4.3.2, XWINNMR 2.6
REMARK 210 METHOD USED : SIMULATED ANNEALING WITH TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 160
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10
REMARK 210
REMARK 210 REMARK: STANDARD TRIPLE AND DOUBLE RESONANCE EXPERIMENTS AS
REMARK 210 DESCRIBED IN GRZESIEK ET AL. (1997), PROTEIN SCIENCE 6, 1248-
REMARK 210 1263.
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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 111
REMARK 465 ILE A 112
REMARK 465 ASN A 113
REMARK 465 LEU A 114
REMARK 465 THR A 115
REMARK 465 PRO A 116
REMARK 465 GLU A 117
REMARK 465 GLU A 118
REMARK 465 LYS A 119
REMARK 465 PHE A 120
REMARK 465 GLU A 121
REMARK 465 VAL A 122
REMARK 465 PHE A 123
REMARK 465 GLY A 124
REMARK 465 ASP A 125
REMARK 465 PHE A 126
REMARK 465 ASP A 127
REMARK 465 PRO A 128
REMARK 465 ASP A 129
REMARK 465 GLN A 130
REMARK 465 TYR A 131
REMARK 465 GLU A 132
REMARK 465 GLU A 133
REMARK 465 GLU A 134
REMARK 465 VAL A 135
REMARK 465 ARG A 136
REMARK 465 GLU A 137
REMARK 465 ARG A 138
REMARK 465 TRP A 139
REMARK 465 GLY A 140
REMARK 465 ASN A 141
REMARK 465 THR A 142
REMARK 465 ASP A 143
REMARK 465 ALA A 144
REMARK 465 TYR A 145
REMARK 465 ARG A 146
REMARK 465 GLN A 147
REMARK 465 SER A 148
REMARK 465 LYS A 149
REMARK 465 GLU A 150
REMARK 465 LYS A 151
REMARK 465 THR A 152
REMARK 465 ALA A 153
REMARK 465 SER A 154
REMARK 465 TYR A 155
REMARK 465 THR A 156
REMARK 465 LYS A 157
REMARK 465 GLU A 158
REMARK 465 ASP A 159
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 GLU A 217 H SER A 221 1.34
REMARK 500 O SER A 186 H MET A 190 1.37
REMARK 500 O ALA A 248 H THR A 252 1.43
REMARK 500 O ALA A 192 H HIS A 196 1.45
REMARK 500 O LEU A 245 H VAL A 249 1.45
REMARK 500 O GLU A 187 H ASP A 191 1.53
REMARK 500 O LEU A 170 H PHE A 174 1.59
REMARK 500 O THR A 171 H VAL A 175 1.60
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 GLN A 161 -2.53 60.13
REMARK 500 1 TYR A 205 -158.75 58.65
REMARK 500 1 ASP A 206 -138.79 -154.04
REMARK 500 1 TYR A 219 -7.30 -59.98
REMARK 500 1 VAL A 220 -35.73 -149.13
REMARK 500 1 ASP A 222 92.17 42.78
REMARK 500 1 GLU A 223 -14.39 -48.32
REMARK 500 1 LYS A 233 128.10 -179.49
REMARK 500 2 ILE A 163 36.29 -95.16
REMARK 500 2 HIS A 204 -129.40 -153.74
REMARK 500 2 TYR A 205 -113.22 -169.36
REMARK 500 2 ASP A 206 -144.10 49.88
REMARK 500 2 CYS A 207 -159.27 -69.91
REMARK 500 2 VAL A 220 -39.66 -148.41
REMARK 500 2 ASP A 222 92.02 44.98
REMARK 500 2 GLU A 223 -12.45 -48.74
REMARK 500 2 LYS A 233 135.73 -179.33
REMARK 500 2 HIS A 251 -60.48 -96.11
REMARK 500 2 THR A 252 150.48 50.64
REMARK 500 3 ILE A 163 34.50 -80.67
REMARK 500 3 HIS A 204 37.91 -158.12
REMARK 500 3 TYR A 205 -157.15 52.17
REMARK 500 3 ASP A 206 100.26 53.11
REMARK 500 3 TYR A 219 -4.73 -59.71
REMARK 500 3 VAL A 220 -38.20 -150.22
REMARK 500 3 GLU A 223 -15.44 -48.96
REMARK 500 3 LYS A 233 130.21 -179.74
REMARK 500 3 THR A 252 87.85 43.99
REMARK 500 4 GLN A 161 -45.26 -167.05
REMARK 500 4 ARG A 162 126.01 71.98
REMARK 500 4 ILE A 163 63.65 -66.50
REMARK 500 4 HIS A 204 -96.42 -98.28
REMARK 500 4 TYR A 205 -120.94 -152.12
REMARK 500 4 CYS A 207 -110.40 51.37
REMARK 500 4 VAL A 220 -39.24 -149.66
REMARK 500 4 GLU A 223 -16.01 -49.01
REMARK 500 4 LYS A 233 126.98 -179.79
REMARK 500 4 HIS A 251 -61.74 -96.24
REMARK 500 4 THR A 252 152.57 51.43
REMARK 500 5 HIS A 204 -127.52 -169.41
REMARK 500 5 TYR A 205 92.27 -163.91
REMARK 500 5 ASP A 206 -133.68 -156.52
REMARK 500 5 CYS A 207 -158.92 -83.81
REMARK 500 5 VAL A 220 -38.06 -150.33
REMARK 500 5 GLU A 223 -16.80 -48.98
REMARK 500 5 LYS A 233 133.60 -179.15
REMARK 500 6 ARG A 162 -127.40 -74.89
REMARK 500 6 ILE A 163 5.46 56.41
REMARK 500 6 HIS A 204 -102.75 -71.18
REMARK 500 6 TYR A 205 -34.21 -167.24
REMARK 500
REMARK 500 THIS ENTRY HAS 84 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 162 0.23 SIDE CHAIN
REMARK 500 1 ARG A 173 0.18 SIDE CHAIN
REMARK 500 1 ARG A 197 0.31 SIDE CHAIN
REMARK 500 1 ARG A 202 0.09 SIDE CHAIN
REMARK 500 1 ARG A 224 0.28 SIDE CHAIN
REMARK 500 1 ARG A 227 0.29 SIDE CHAIN
REMARK 500 1 ARG A 241 0.30 SIDE CHAIN
REMARK 500 1 ARG A 250 0.21 SIDE CHAIN
REMARK 500 2 ARG A 162 0.15 SIDE CHAIN
REMARK 500 2 ARG A 172 0.18 SIDE CHAIN
REMARK 500 2 ARG A 173 0.29 SIDE CHAIN
REMARK 500 2 ARG A 197 0.26 SIDE CHAIN
REMARK 500 2 ARG A 202 0.11 SIDE CHAIN
REMARK 500 2 ARG A 224 0.24 SIDE CHAIN
REMARK 500 2 ARG A 227 0.26 SIDE CHAIN
REMARK 500 2 ARG A 241 0.19 SIDE CHAIN
REMARK 500 2 ARG A 250 0.19 SIDE CHAIN
REMARK 500 3 ARG A 162 0.21 SIDE CHAIN
REMARK 500 3 ARG A 172 0.25 SIDE CHAIN
REMARK 500 3 ARG A 173 0.23 SIDE CHAIN
REMARK 500 3 ARG A 197 0.29 SIDE CHAIN
REMARK 500 3 ARG A 202 0.13 SIDE CHAIN
REMARK 500 3 ARG A 241 0.24 SIDE CHAIN
REMARK 500 3 ARG A 250 0.27 SIDE CHAIN
REMARK 500 4 ARG A 162 0.31 SIDE CHAIN
REMARK 500 4 ARG A 172 0.31 SIDE CHAIN
REMARK 500 4 ARG A 173 0.32 SIDE CHAIN
REMARK 500 4 ARG A 202 0.29 SIDE CHAIN
REMARK 500 4 ARG A 224 0.27 SIDE CHAIN
REMARK 500 4 ARG A 241 0.15 SIDE CHAIN
REMARK 500 4 ARG A 250 0.20 SIDE CHAIN
REMARK 500 5 ARG A 162 0.32 SIDE CHAIN
REMARK 500 5 ARG A 172 0.25 SIDE CHAIN
REMARK 500 5 ARG A 173 0.28 SIDE CHAIN
REMARK 500 5 ARG A 197 0.25 SIDE CHAIN
REMARK 500 5 ARG A 202 0.26 SIDE CHAIN
REMARK 500 5 ARG A 224 0.31 SIDE CHAIN
REMARK 500 5 ARG A 227 0.30 SIDE CHAIN
REMARK 500 5 ARG A 241 0.24 SIDE CHAIN
REMARK 500 5 ARG A 250 0.31 SIDE CHAIN
REMARK 500 6 ARG A 162 0.26 SIDE CHAIN
REMARK 500 6 ARG A 172 0.19 SIDE CHAIN
REMARK 500 6 ARG A 173 0.29 SIDE CHAIN
REMARK 500 6 ARG A 197 0.28 SIDE CHAIN
REMARK 500 6 ARG A 241 0.30 SIDE CHAIN
REMARK 500 6 ARG A 250 0.16 SIDE CHAIN
REMARK 500 7 ARG A 162 0.16 SIDE CHAIN
REMARK 500 7 ARG A 172 0.31 SIDE CHAIN
REMARK 500 7 ARG A 173 0.30 SIDE CHAIN
REMARK 500 7 ARG A 197 0.27 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 80 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EXJ RELATED DB: PDB
REMARK 900 BACILLUS SUBTILIS MULTIDRUG RESISTANCE REGULATOR BMRR
REMARK 900 RELATED ID: 1EXI RELATED DB: PDB
REMARK 900 BACILLUS SUBTILIS MULTIDRUG RESISTANCE REGULATOR BMRR
REMARK 900 RELATED ID: 1JBG RELATED DB: PDB
REMARK 900 BACILLUS SUBTILIS MULTIDRUG TRANSPORTER REGULATOR MTAN
DBREF 1NY9 A 111 253 UNP P0A4T9 TIPA_STRLI 111 253
SEQRES 1 A 143 GLY ILE ASN LEU THR PRO GLU GLU LYS PHE GLU VAL PHE
SEQRES 2 A 143 GLY ASP PHE ASP PRO ASP GLN TYR GLU GLU GLU VAL ARG
SEQRES 3 A 143 GLU ARG TRP GLY ASN THR ASP ALA TYR ARG GLN SER LYS
SEQRES 4 A 143 GLU LYS THR ALA SER TYR THR LYS GLU ASP TRP GLN ARG
SEQRES 5 A 143 ILE GLN ASP GLU ALA ASP GLU LEU THR ARG ARG PHE VAL
SEQRES 6 A 143 ALA LEU MET ASP ALA GLY GLU PRO ALA ASP SER GLU GLY
SEQRES 7 A 143 ALA MET ASP ALA ALA GLU ASP HIS ARG GLN GLY ILE ALA
SEQRES 8 A 143 ARG ASN HIS TYR ASP CYS GLY TYR GLU MET HIS THR CYS
SEQRES 9 A 143 LEU GLY GLU MET TYR VAL SER ASP GLU ARG PHE THR ARG
SEQRES 10 A 143 ASN ILE ASP ALA ALA LYS PRO GLY LEU ALA ALA TYR MET
SEQRES 11 A 143 ARG ASP ALA ILE LEU ALA ASN ALA VAL ARG HIS THR PRO
HELIX 1 1 GLN A 164 GLY A 181 1 18
HELIX 2 2 SER A 186 HIS A 204 1 19
HELIX 3 3 GLY A 208 TYR A 219 1 12
HELIX 4 4 ASP A 222 ASP A 230 1 9
HELIX 5 5 ALA A 231 LYS A 233 5 3
HELIX 6 6 GLY A 235 THR A 252 1 18
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 23 2 Bytes