Header list of 1bxd.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSFERASE 02-OCT-98 1BXD TITLE NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR TITLE 2 ENVZ COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (OSMOLARITY SENSOR PROTEIN (ENVZ)); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 290-450; COMPND 5 SYNONYM: ENVZ(290-450); COMPND 6 EC: 2.7.3.-; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI BL21(DE3); SOURCE 3 ORGANISM_TAXID: 469008; SOURCE 4 STRAIN: BL21-DE3; SOURCE 5 CELLULAR_LOCATION: CYTOPLASM; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A KEYWDS HISTIDINE KINASE, OSMOSENSOR, HIS-ASP PHOSPHORELAY SYSTEM, SIGNAL KEYWDS 2 TRANSDUCTION, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.TANAKA,S.K.SAHA,C.TOMOMORI,R.ISHIMA,D.LIU,K.I.TONG,H.PARK,R.DUTTA, AUTHOR 2 L.QIN,M.B.SWINDELLS,T.YAMAZAKI,A.M.ONO,M.KAINOSHO,M.INOUYE,M.IKURA REVDAT 3 16-FEB-22 1BXD 1 REMARK REVDAT 2 24-FEB-09 1BXD 1 VERSN REVDAT 1 02-OCT-99 1BXD 0 JRNL AUTH T.TANAKA,S.K.SAHA,C.TOMOMORI,R.ISHIMA,D.LIU,K.I.TONG,H.PARK, JRNL AUTH 2 R.DUTTA,L.QIN,M.B.SWINDELLS,T.YAMAZAKI,A.M.ONO,M.KAINOSHO, JRNL AUTH 3 M.INOUYE,M.IKURA JRNL TITL NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI JRNL TITL 2 OSMOSENSOR ENVZ. JRNL REF NATURE V. 396 88 1998 JRNL REFN ISSN 0028-0836 JRNL PMID 9817206 JRNL DOI 10.1038/23968 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8.5.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1BXD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-99. REMARK 100 THE DEPOSITION ID IS D_1000007021. 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 : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-1H HSQC; 1H-13C CT-HSQC; 1H REMARK 210 -15N HMQC-J; 1H NOESY; 1H TOCSY; REMARK 210 (HB)CBCA(CO)NNH; HNCACB; (HB) REMARK 210 CBCACO(CA)HA; HNCO; HCCH-TOCSY; REMARK 210 15N-EDITED TOCSY-HMQC; 15N- REMARK 210 EDITED NOESY-HSQC; 13C-EDITED REMARK 210 NOESY-HMQC; SIMULTANEOUS 13C/ REMARK 210 15N-EDITED NOESY-HMQC; 13C- REMARK 210 FILTERED TOCSY; [13C/ F1]-EDITED REMARK 210 [13C/F2]-FILTERED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : UNITY-PLUS 500; UNITY-600; REMARK 210 DMX750 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NULL 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: 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 292 166.63 54.86 REMARK 500 1 GLU A 293 40.88 -165.19 REMARK 500 1 MET A 296 89.39 23.68 REMARK 500 1 GLU A 297 -159.51 -144.42 REMARK 500 1 SER A 313 66.36 -115.67 REMARK 500 1 TYR A 315 74.43 -155.26 REMARK 500 1 GLU A 316 12.80 91.50 REMARK 500 1 GLU A 318 73.14 -65.74 REMARK 500 1 ALA A 322 77.73 -150.73 REMARK 500 1 SER A 327 107.97 171.35 REMARK 500 1 GLU A 329 103.95 -173.98 REMARK 500 1 LEU A 335 -73.92 -76.30 REMARK 500 1 ASN A 343 -19.28 -47.52 REMARK 500 1 ARG A 350 -72.56 -63.95 REMARK 500 1 ASN A 353 29.81 -171.68 REMARK 500 1 TRP A 355 129.39 178.46 REMARK 500 1 ASN A 365 34.02 80.49 REMARK 500 1 ARG A 366 105.50 172.50 REMARK 500 1 HIS A 385 68.95 -117.47 REMARK 500 1 LEU A 386 71.74 -109.50 REMARK 500 1 PHE A 390 128.95 61.04 REMARK 500 1 SER A 400 -175.76 -171.23 REMARK 500 1 ALA A 407 44.29 -90.73 REMARK 500 1 ILE A 408 164.40 -43.50 REMARK 500 1 VAL A 409 -59.30 80.52 REMARK 500 1 ILE A 412 -70.73 -67.29 REMARK 500 1 ASN A 417 42.91 81.43 REMARK 500 1 VAL A 440 143.30 -39.26 REMARK 500 2 GLN A 292 105.97 -161.91 REMARK 500 2 GLU A 293 38.72 -174.25 REMARK 500 2 GLU A 297 -156.33 -134.53 REMARK 500 2 ARG A 317 -82.79 -71.66 REMARK 500 2 GLU A 318 55.90 -147.14 REMARK 500 2 SER A 327 100.12 55.29 REMARK 500 2 GLU A 329 110.96 -171.45 REMARK 500 2 LYS A 331 98.25 -68.69 REMARK 500 2 ALA A 349 -81.68 -56.65 REMARK 500 2 ASN A 353 28.64 -159.21 REMARK 500 2 TRP A 355 132.12 -176.15 REMARK 500 2 ARG A 366 116.73 171.64 REMARK 500 2 TRP A 368 143.93 -170.55 REMARK 500 2 LYS A 384 -18.57 -44.03 REMARK 500 2 LEU A 386 104.08 -169.08 REMARK 500 2 PHE A 387 78.30 62.61 REMARK 500 2 GLN A 388 69.46 -172.80 REMARK 500 2 PHE A 390 62.65 -178.66 REMARK 500 2 VAL A 391 64.29 -151.37 REMARK 500 2 ALA A 396 112.93 60.57 REMARK 500 2 THR A 398 -170.09 43.93 REMARK 500 2 THR A 402 -51.90 -133.33 REMARK 500 REMARK 500 THIS ENTRY HAS 556 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 317 0.17 SIDE CHAIN REMARK 500 1 ARG A 339 0.25 SIDE CHAIN REMARK 500 1 ARG A 350 0.29 SIDE CHAIN REMARK 500 1 ARG A 366 0.32 SIDE CHAIN REMARK 500 1 ARG A 383 0.25 SIDE CHAIN REMARK 500 1 ARG A 392 0.21 SIDE CHAIN REMARK 500 1 ARG A 397 0.25 SIDE CHAIN REMARK 500 1 ARG A 411 0.32 SIDE CHAIN REMARK 500 1 ARG A 427 0.31 SIDE CHAIN REMARK 500 1 ARG A 433 0.29 SIDE CHAIN REMARK 500 1 ARG A 442 0.31 SIDE CHAIN REMARK 500 2 ARG A 317 0.32 SIDE CHAIN REMARK 500 2 ARG A 339 0.29 SIDE CHAIN REMARK 500 2 ARG A 350 0.13 SIDE CHAIN REMARK 500 2 ARG A 366 0.09 SIDE CHAIN REMARK 500 2 ARG A 383 0.27 SIDE CHAIN REMARK 500 2 ARG A 392 0.31 SIDE CHAIN REMARK 500 2 ARG A 397 0.12 SIDE CHAIN REMARK 500 2 ARG A 411 0.18 SIDE CHAIN REMARK 500 2 ARG A 427 0.20 SIDE CHAIN REMARK 500 2 ARG A 433 0.16 SIDE CHAIN REMARK 500 2 ARG A 442 0.27 SIDE CHAIN REMARK 500 3 ARG A 317 0.20 SIDE CHAIN REMARK 500 3 ARG A 339 0.30 SIDE CHAIN REMARK 500 3 ARG A 350 0.32 SIDE CHAIN REMARK 500 3 ARG A 366 0.26 SIDE CHAIN REMARK 500 3 ARG A 383 0.25 SIDE CHAIN REMARK 500 3 ARG A 392 0.30 SIDE CHAIN REMARK 500 3 ARG A 397 0.21 SIDE CHAIN REMARK 500 3 ARG A 411 0.14 SIDE CHAIN REMARK 500 3 ARG A 427 0.31 SIDE CHAIN REMARK 500 3 ARG A 433 0.25 SIDE CHAIN REMARK 500 3 ARG A 442 0.30 SIDE CHAIN REMARK 500 4 ARG A 317 0.31 SIDE CHAIN REMARK 500 4 ARG A 339 0.29 SIDE CHAIN REMARK 500 4 ARG A 350 0.25 SIDE CHAIN REMARK 500 4 ARG A 366 0.29 SIDE CHAIN REMARK 500 4 ARG A 383 0.29 SIDE CHAIN REMARK 500 4 ARG A 392 0.32 SIDE CHAIN REMARK 500 4 ARG A 397 0.31 SIDE CHAIN REMARK 500 4 ARG A 411 0.28 SIDE CHAIN REMARK 500 4 ARG A 427 0.23 SIDE CHAIN REMARK 500 4 ARG A 433 0.31 SIDE CHAIN REMARK 500 4 ARG A 442 0.16 SIDE CHAIN REMARK 500 5 ARG A 317 0.29 SIDE CHAIN REMARK 500 5 ARG A 339 0.22 SIDE CHAIN REMARK 500 5 ARG A 350 0.24 SIDE CHAIN REMARK 500 5 ARG A 366 0.26 SIDE CHAIN REMARK 500 5 ARG A 383 0.31 SIDE CHAIN REMARK 500 5 ARG A 392 0.32 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 211 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 451 DBREF 1BXD A 290 450 UNP P02933 ENVZ_ECOLI 290 450 SEQRES 1 A 161 THR GLY GLN GLU MET PRO MET GLU MET ALA ASP LEU ASN SEQRES 2 A 161 ALA VAL LEU GLY GLU VAL ILE ALA ALA GLU SER GLY TYR SEQRES 3 A 161 GLU ARG GLU ILE GLU THR ALA LEU TYR PRO GLY SER ILE SEQRES 4 A 161 GLU VAL LYS MET HIS PRO LEU SER ILE LYS ARG ALA VAL SEQRES 5 A 161 ALA ASN MET VAL VAL ASN ALA ALA ARG TYR GLY ASN GLY SEQRES 6 A 161 TRP ILE LYS VAL SER SER GLY THR GLU PRO ASN ARG ALA SEQRES 7 A 161 TRP PHE GLN VAL GLU ASP ASP GLY PRO GLY ILE ALA PRO SEQRES 8 A 161 GLU GLN ARG LYS HIS LEU PHE GLN PRO PHE VAL ARG GLY SEQRES 9 A 161 ASP SER ALA ARG THR ILE SER GLY THR GLY LEU GLY LEU SEQRES 10 A 161 ALA ILE VAL GLN ARG ILE VAL ASP ASN HIS ASN GLY MET SEQRES 11 A 161 LEU GLU LEU GLY THR SER GLU ARG GLY GLY LEU SER ILE SEQRES 12 A 161 ARG ALA TRP LEU PRO VAL PRO VAL THR ARG ALA GLN GLY SEQRES 13 A 161 THR THR LYS GLU GLY HET ANP A 451 45 HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER FORMUL 2 ANP C10 H17 N6 O12 P3 HELIX 1 1 LEU A 301 ALA A 311 1 11 HELIX 2 2 PRO A 334 ASN A 343 1 10 HELIX 3 3 PRO A 380 LYS A 384 1 5 HELIX 4 4 GLN A 410 ASP A 414 1 5 SHEET 1 1 1 GLU A 297 ALA A 299 0 SHEET 1 2 1 VAL A 330 MET A 332 0 SHEET 1 3 1 ILE A 319 LEU A 323 0 SHEET 1 4 1 ILE A 356 THR A 362 0 SHEET 1 5 1 ALA A 367 ASP A 373 0 SHEET 1 6 1 SER A 431 LEU A 436 0 SHEET 1 7 1 LEU A 420 GLY A 423 0 SITE 1 AC1 8 ASP A 373 ILE A 378 GLN A 382 LEU A 386 SITE 2 AC1 8 PHE A 387 LEU A 422 LEU A 430 ILE A 432 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 16 2 Bytes