Header list of 1vkr.pdb file
Complete list - 25 20 Bytes
HEADER TRANSFERASE 14-JUN-04 1VKR
TITLE STRUCTURE OF IIB DOMAIN OF THE MANNITOL-SPECIFIC PERMEASE ENZYME II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANNITOL-SPECIFIC PTS SYSTEM ENZYME IIABC COMPONENTS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: IIB DOMAIN;
COMPND 5 SYNONYM: IIBMTL PHOSPHOTRANSFERASE ENZYME II, B COMPONENT, EIIB-MTL;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83334;
SOURCE 4 STRAIN: O157:H7;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOTRANSFERASE, TRANSFERASE, KINASE, SUGAR TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,P.M.LEGLER,M.CAI
REVDAT 3 13-JUL-11 1VKR 1 VERSN
REVDAT 2 24-FEB-09 1VKR 1 VERSN
REVDAT 1 21-SEP-04 1VKR 0
JRNL AUTH P.M.LEGLER,M.CAI,A.PETERKOFSKY,G.M.CLORE
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE CYTOPLASMIC B
JRNL TITL 2 DOMAIN OF THE MANNITOL TRANSPORTER II-MANNITOL OF THE
JRNL TITL 3 ESCHERICHIA COLI PHOSPHOTRANSFERASE SYSTEM.
JRNL REF J.BIOL.CHEM. V. 279 39115 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15258141
JRNL DOI 10.1074/JBC.M406764200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH (HTTP://NMR.CIT.NIH.GOV/XPLOR_NIH)
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE TARGET FUNCTION COMPRISES TERMS FOR THE NOE-DERIVED INTERPROTON
REMARK 3 DISTANCE RESTRAINTS, TORSION ANGLE RESTRAINTS, 3JHN-HALPHA COUPLING
REMARK 3 CONSTANT RESTRAINTS, 13CALPHA/BETA CHEMICAL SHIFT RESTRAINTS, AND
REMARK 3 RESIDUAL DIPOLAR COUPLING RESTRAINTS (N-H, N-C' AND HN-C'); A
REMARK 3 QUARTIC VAN DER WAALS REPULSION TERM, TORSION ANGLE AND HYDROGEN
REMARK 3 BONDING DATABASE POTENTIALS OF MEAN FORCE, AND A RADIUS OF GYRATION
REMARK 3 RESTRAINTS.
REMARK 3
REMARK 3 IN THIS ENTRY THE LAST COLUMN REPRESENTS THE AVERAGE RMS
REMARK 3 DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED BEST-FITTED
REMARK 3 TO RESIDUES 375-471. ONLY RESIDUES 375-471 ARE SHOWN
REMARK 3 SINCE RESIDUES 365-374 AND 472-489 AT THE N- AND C-TERMINI
REMARK 3 RESPECTIVELY, ARE DISORDERED IN SOLUTION.
REMARK 3
REMARK 3 EXPERIMENTAL RESTRAINTS:
REMARK 3 1444 INTERPROTON DISTANCE RESTRAINTS:
REMARK 3 (90 INTRARESIDUE; 419 SEQUENTIAL, 347
REMARK 3 MEDIUM-RANGE, AND 517 LONG-RANGE INTERRESIDUE;
REMARK 3 50 SEQUENTIAL/MEDIUM-RANGE AMBIGUOUS;
REMARK 3 21 LONG-RANGE AMBIGUOUS
REMARK 3 110 DISTANCE RESTRAINTS FOR 55 BACKBONE H-BONDS
REMARK 3 214 TORSION ANGLE RESTRAINTS (90 PHI, 94 PSI, 68 CHI)
REMARK 3 189 CALPHA/CBETA CHEMICAL SHIFT RESTRAINTS
REMARK 3 70 3JHN-HA COUPLING CONSTANT RESTRAINTS
REMARK 3 200 RESIDUAL DIPOLAR COUPLING RESTRAINTS
REMARK 3 (74 N-H, 62 N-C', 64 HN-C')
REMARK 3 DIPOLAR COUPLING R-FACTORS:
REMARK 3 N-H 2.8%
REMARK 3 N-C' 14.9%
REMARK 3 HN-C' 13.5%
REMARK 4
REMARK 4 1VKR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-04.
REMARK 100 THE RCSB ID CODE IS RCSB001960.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308.00
REMARK 210 PH : 7.1
REMARK 210 IONIC STRENGTH : 40 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1) TRIPLE RESONANCE FOR
REMARK 210 ASSIGNMENT OF PROTEIN; (2)
REMARK 210 QUANTITATIVE J CORRELATION FOR
REMARK 210 COUPLING CONSTANTS; (3) 3D, 4D
REMARK 210 HETERONUCLEAR SEPARATED NOE
REMARK 210 EXPTS; (4) IPAP AND COUPLED HSQC
REMARK 210 EXPERIMENTS FOR DIPOLAR
REMARK 210 COUPLINGS. DIPOLAR COUPLINGS WERE
REMARK 210 MEASURED IN PEG/HEXANOL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600; DRX600; DMC750;
REMARK 210 DRX800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : REGULARIZED MEAN STRUCTURE
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 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 GLY A 365
REMARK 465 SER A 366
REMARK 465 ALA A 367
REMARK 465 GLY A 368
REMARK 465 ASP A 369
REMARK 465 VAL A 370
REMARK 465 THR A 371
REMARK 465 ASN A 372
REMARK 465 ASP A 373
REMARK 465 LEU A 374
REMARK 465 THR A 472
REMARK 465 GLU A 473
REMARK 465 ASN A 474
REMARK 465 GLU A 475
REMARK 465 VAL A 476
REMARK 465 LYS A 477
REMARK 465 VAL A 478
REMARK 465 LYS A 479
REMARK 465 ASP A 480
REMARK 465 SER A 481
REMARK 465 LEU A 482
REMARK 465 LYS A 483
REMARK 465 ASP A 484
REMARK 465 SER A 485
REMARK 465 PHE A 486
REMARK 465 ASP A 487
REMARK 465 ASP A 488
REMARK 465 SER A 489
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 HD1 HIS A 430 H ASP A 432 1.16
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 ARG A 378 -3.04 -143.23
REMARK 500 MET A 388 -67.60 -149.09
REMARK 500 ASP A 454 79.20 -62.04
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1VKR A 367 489 UNP P00550 PTM3C_ECOLI 367 489
SEQADV 1VKR GLY A 365 UNP P00550 CLONING ARTIFACT
SEQADV 1VKR SER A 366 UNP P00550 CLONING ARTIFACT
SEQRES 1 A 125 GLY SER ALA GLY ASP VAL THR ASN ASP LEU SER HIS VAL
SEQRES 2 A 125 ARG LYS ILE ILE VAL ALA CYS ASP ALA GLY MET GLY SER
SEQRES 3 A 125 SER ALA MET GLY ALA GLY VAL LEU ARG LYS LYS ILE GLN
SEQRES 4 A 125 ASP ALA GLY LEU SER GLN ILE SER VAL THR ASN SER ALA
SEQRES 5 A 125 ILE ASN ASN LEU PRO PRO ASP VAL ASP LEU VAL ILE THR
SEQRES 6 A 125 HIS ARG ASP LEU THR GLU ARG ALA MET ARG GLN VAL PRO
SEQRES 7 A 125 GLN ALA GLN HIS ILE SER LEU THR ASN PHE LEU ASP SER
SEQRES 8 A 125 GLY LEU TYR THR SER LEU THR GLU ARG LEU VAL ALA ALA
SEQRES 9 A 125 GLN ARG HIS THR GLU ASN GLU VAL LYS VAL LYS ASP SER
SEQRES 10 A 125 LEU LYS ASP SER PHE ASP ASP SER
HELIX 1 1 MET A 388 ALA A 405 1 18
HELIX 2 2 ARG A 431 VAL A 441 1 11
HELIX 3 3 ASP A 454 HIS A 471 1 18
SHEET 1 A 4 SER A 411 ASN A 414 0
SHEET 2 A 4 LYS A 379 VAL A 382 1 N ILE A 380 O SER A 411
SHEET 3 A 4 LEU A 426 HIS A 430 1 O ILE A 428 N ILE A 381
SHEET 4 A 4 GLN A 445 LEU A 449 1 O GLN A 445 N VAL A 427
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 - 25 20 Bytes