Header list of 1svj.pdb file
Complete list - 2 20 Bytes
HEADER HYDROLASE 29-MAR-04 1SVJ
TITLE THE SOLUTION STRUCTURE OF THE NUCLEOTIDE BINDING DOMAIN OF KDPB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM-TRANSPORTING ATPASE B CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: POTASSIUM-TRANSLOCATING ATPASE B CHAIN, ATP PHOSPHOHYDROLASE
COMPND 6 [POTASSIUM-TRANSPORTING] B CHAIN, POTASSIUM BINDING AND TRANSLOCATING
COMPND 7 SUBUNIT B, KDPB N-DOMAIN, KDPBN, KDP B CHAIN N-DOMAIN;
COMPND 8 EC: 3.6.3.12;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: KDPB, B0697;
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: PET16B
KEYWDS ALPHA-BETA SANDWICH, HYDROLASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR M.HAUPT,M.BRAMKAMP,M.COLES,K.ALTENDORF,H.KESSLER
REVDAT 3 02-MAR-22 1SVJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1SVJ 1 VERSN
REVDAT 1 21-SEP-04 1SVJ 0
JRNL AUTH M.HAUPT,M.BRAMKAMP,M.COLES,K.ALTENDORF,H.KESSLER
JRNL TITL INTER-DOMAIN MOTIONS OF THE N-DOMAIN OF THE KDPFABC COMPLEX,
JRNL TITL 2 A P-TYPE ATPASE, ARE NOT DRIVEN BY ATP-INDUCED
JRNL TITL 3 CONFORMATIONAL CHANGES.
JRNL REF J.MOL.BIOL. V. 342 1547 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15364580
JRNL DOI 10.1016/J.JMB.2004.07.060
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH-2.9.3 NIH-2.9.3
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BASED ON A TOTAL OF 2232 NOE-BASED
REMARK 3 DISTANCE RESTRAINTS, 256 DIHEDRAL ANGLE RESTRAINTS, 67 J-
REMARK 3 RESTRAINTS AND 66 HYDROGEN BOND RESTRAINTS
REMARK 4
REMARK 4 1SVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022029.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.4MM KDPBN U-15N,13C, 50MM
REMARK 210 PHOSPHATE BUFFER, 100MM NACL,
REMARK 210 0.05% SODIUM AZIDE; 1.2MM KDPBN
REMARK 210 U-15N, 50MM PHOSPHATE BUFFER,
REMARK 210 100MM NACL, 0.05% SODIUM AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; CNH-
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, X-PLOR NIH-2.9.3
REMARK 210 NIH-2.9.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 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 RES C SSSEQI
REMARK 465 MET A 296
REMARK 465 GLY A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 SER A 308
REMARK 465 SER A 309
REMARK 465 GLY A 310
REMARK 465 HIS A 311
REMARK 465 GLY A 312
REMARK 465 GLY A 313
REMARK 465 ARG A 314
REMARK 465 HIS A 315
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 HIS A 404 HD21 ASN A 408 1.47
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 GLU A 321 147.08 -170.83
REMARK 500 PHE A 360 -35.31 -134.83
REMARK 500 ASN A 361 97.31 -160.62
REMARK 500 LEU A 362 89.71 -57.78
REMARK 500 GLU A 364 -151.41 -126.88
REMARK 500 ASP A 389 -62.98 -22.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U7Q RELATED DB: PDB
REMARK 900 ENSEMBLE OF 20 STRUCTURES
REMARK 900 RELATED ID: 1X6K RELATED DB: PDB
REMARK 900 ATPPNP-BOUND FORM
REMARK 900 RELATED ID: 6029 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS FREE PROTEIN
REMARK 900 RELATED ID: 6030 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS ATPPNP-BOUND
DBREF 1SVJ A 316 451 UNP P03960 ATKB_ECOLI 316 451
SEQADV 1SVJ MET A 296 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ GLY A 297 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 298 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 299 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 300 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 301 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 302 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 303 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 304 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 305 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 306 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 307 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ SER A 308 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ SER A 309 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ GLY A 310 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 311 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ GLY A 312 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ GLY A 313 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ ARG A 314 UNP P03960 EXPRESSION TAG
SEQADV 1SVJ HIS A 315 UNP P03960 EXPRESSION TAG
SEQRES 1 A 156 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 156 SER GLY HIS GLY GLY ARG HIS ASN ARG GLN ALA SER GLU
SEQRES 3 A 156 PHE ILE PRO ALA GLN GLY VAL ASP GLU LYS THR LEU ALA
SEQRES 4 A 156 ASP ALA ALA GLN LEU ALA SER LEU ALA ASP GLU THR PRO
SEQRES 5 A 156 GLU GLY ARG SER ILE VAL ILE LEU ALA LYS GLN ARG PHE
SEQRES 6 A 156 ASN LEU ARG GLU ARG ASP VAL GLN SER LEU HIS ALA THR
SEQRES 7 A 156 PHE VAL PRO PHE THR ALA GLN SER ARG MET SER GLY ILE
SEQRES 8 A 156 ASN ILE ASP ASN ARG MET ILE ARG LYS GLY SER VAL ASP
SEQRES 9 A 156 ALA ILE ARG ARG HIS VAL GLU ALA ASN GLY GLY HIS PHE
SEQRES 10 A 156 PRO THR ASP VAL ASP GLN LYS VAL ASP GLN VAL ALA ARG
SEQRES 11 A 156 GLN GLY ALA THR PRO LEU VAL VAL VAL GLU GLY SER ARG
SEQRES 12 A 156 VAL LEU GLY VAL ILE ALA LEU LYS ASP ILE VAL LYS GLY
HELIX 1 1 ASP A 329 ALA A 343 1 15
HELIX 2 2 THR A 346 PHE A 360 1 15
HELIX 3 3 VAL A 398 GLY A 409 1 12
HELIX 4 4 PRO A 413 GLN A 426 1 14
SHEET 1 A 6 GLN A 318 PRO A 324 0
SHEET 2 A 6 VAL A 439 LYS A 446 -1 O VAL A 442 N ILE A 323
SHEET 3 A 6 ALA A 428 GLU A 435 -1 N LEU A 431 O ILE A 443
SHEET 4 A 6 ARG A 391 SER A 397 -1 N ARG A 394 O VAL A 434
SHEET 5 A 6 MET A 383 ILE A 388 -1 N SER A 384 O LYS A 395
SHEET 6 A 6 ALA A 372 THR A 378 -1 N THR A 373 O ASN A 387
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
Complete list - 2 20 Bytes