Header list of 1wcr.pdb file
Complete list - 25 20 Bytes
HEADER TRANSFERASE 19-NOV-04 1WCR
TITLE TRIMERIC STRUCTURE OF THE ENZYME IIA FROM ESCHERICHIA COLI
TITLE 2 PHOSPHOTRANSFERASE SYSTEM SPECIFIC FOR N,N'-
TITLE 3 DIACETYLCHITOBIOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTS SYSTEM, N, N'-DIACETYLCHITOBIOSE-SPECIFIC
COMPND 3 IIA COMPONENT;
COMPND 4 CHAIN: A, B, C;
COMPND 5 FRAGMENT: RESIDUES 14-116;
COMPND 6 SYNONYM: EIIA-CHB, N, N'-DIACETYLCHITOBIOSE-PERMEASE IIA
COMPND 7 COMPONENT, PHOSPHOTRANSFERASE ENZYME II A COMPONENT,
COMPND 8 EIII-CHB;
COMPND 9 EC: 2.7.1.69;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS IIA, PTS, MUTAGENESIS, CHITOBIOSE, TRANSFERASE, SUGAR
KEYWDS 2 TRANSPORT, PHOSPHOTRANSFERASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR C.TANG,G.M.CLORE
REVDAT 3 24-FEB-09 1WCR 1 VERSN
REVDAT 2 23-MAR-05 1WCR 1 JRNL
REVDAT 1 19-JAN-05 1WCR 0
JRNL AUTH C.TANG,D.C.WILLIAMS,R.GHIRLANDO,G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF ENZYME IIACHITOBIOSE FROM
JRNL TITL 2 THE N,N'-DIACETYLCHITOBIOSE BRANCH OF THE
JRNL TITL 3 ESCHERICHIA COLI PHOSPHOTRANSFERASE SYSTEM
JRNL REF J.BIOL.CHEM. V. 280 11770 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15654077
JRNL DOI 10.1074/JBC.M414300200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH (HTTP://NMR.CIT.NIH.GOV/XPLOR_NIH)
REMARK 3 (HTTP://NMR.CIT.NIH.GOV/XPLOR_NIH)
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE TARGET FUNCTION COMPRISES TERMS
REMARK 3 FOR THE NOE-DERIVED INTERPROTON DISTANCE RESTRAINTS, TORSION
REMARK 3 ANGLE RESTRAINTS, 13CALPHA/BETA CHEMICAL SHIFT RESTRAINTS, AND
REMARK 3 RESIDUAL DIPOLAR COUPLING RESTRAINTS (N-H, N-C' AND C'-CA).
REMARK 3 NON-BONDED INTERACTIONS ARE REPRESENTED BY A QUARTIC VAN DER
REMARK 3 WAALS REPULSION TERM, TORSION ANGLE AND HYDROGEN BONDING
REMARK 3 DATABASE POTENTIALS OF MEAN FORCE, AND A RADIUS OF GYRATION
REMARK 3 RESTRAINT. IN THIS ENTRY THE LAST COLUMN REPRESENTS THE
REMARK 3 AVERAGE ATOMIC RMS DIFFERENCE IN ANGSTROMS BETWEEN THE 80
REMARK 3 INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN
REMARK 3 COORDINATES RESIDUES 1-3, 61-69 AND 102-103 ARE DISORDERED IN
REMARK 3 SOLUTION.
REMARK 4
REMARK 4 1WCR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-NOV-04.
REMARK 100 THE PDBE ID CODE IS EBI-21734.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.0
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 10MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : 1.0
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210 NMR EXPERIMENTS CONDUCTED : (1) TROSY TRIPLE RESONANCE FOR
REMARK 210 ASSIGNMENT OF PROTEIN, (2)
REMARK 210 QUANTITATIVE J CORRELATION FOR
REMARK 210 SIDECHAIN COUPLING CONSTANTS,
REMARK 210 (3) 3D, 4D HETERONUCLEAR SEPARATED
REMARK 210 NOE EXPTS, (4) TROSY HNCO AND
REMARK 210 HN(CO)CA EXPERIMENTS FOR DIPOLAR
REMARK 210 COUPLINGS. DIPOLAR COUPLINGS
REMARK 210 WERE MEASURED IN PF1 PHAGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500; 600; 600; 750; 800
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600; DRX600;
REMARK 210 DMX750; DRX800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR-NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING IN TORSION ANGL
REMARK 210 SPACE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : RESTRAINED REGULARIZED MEAN
REMARK 210 STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: EXPERIMENTAL RESTRAINTS:
REMARK 210 1290 INTERPROTON DISTANCE RESTRAINTS:
REMARK 210 246 SEQUENTIAL, 258 MEDIUM-RANGE,
REMARK 210 90 LONG-RANGE INTRAMOLECULAR RESTRAINTS;
REMARK 210 234 INTERMOLECULAR DISTANCE RESTRAINTS;
REMARK 210 462 DISTANCE RESTRAINTS FOR BACKBONE H-BONDS
REMARK 210 FOR 231 H-BONDS (71 PER SUBUNIT)
REMARK 210 729 TORSION ANGLE RESTRAINTS (255 PHI, 255 PSI, 219 CHI)
REMARK 210 585 CALPHA/CBETA CHEMICAL SHIFT RESTRAINTS
REMARK 210 759 RESIDUAL DIPOLAR COUPLING RESTRAINTS
REMARK 210 (252 N-H, 255 N-C', 249 C'-CA)
REMARK 210 DIPOLAR COUPLING R-FACTORS FOR THE RESTRAINED REGULARIZED
REMARK 210 MEAN STRUCTURE
REMARK 210 N-H 7.1%
REMARK 210 N-C' 15.2%
REMARK 210 C'-CA 17.7%
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE ASP 92 LEU (RESIDUE 79 IN COORDINATES).
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 ALA A 1 - H GLU A 5 1.47
REMARK 500 O GLU A 3 - H VAL A 7 1.46
REMARK 500 HG SER A 71 - H LEU A 74 1.44
REMARK 500 O ALA B 1 - H GLU B 5 1.47
REMARK 500 O GLU B 3 - H VAL B 7 1.46
REMARK 500 HG SER B 71 - H LEU B 74 1.44
REMARK 500 O ALA C 1 - H GLU C 5 1.47
REMARK 500 O GLU C 3 - H VAL C 7 1.46
REMARK 500 HG SER C 71 - H LEU C 74 1.44
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 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 2 -89.42 -25.19
REMARK 500 ASP A 62 -86.73 -65.83
REMARK 500 LYS A 67 142.51 -17.32
REMARK 500 LYS A 69 -125.49 -17.51
REMARK 500 LYS A 102 -96.46 147.86
REMARK 500 GLU B 2 -89.40 -25.38
REMARK 500 ASP B 62 -87.65 -66.90
REMARK 500 LYS B 67 143.47 -17.36
REMARK 500 LYS B 69 -125.35 -17.54
REMARK 500 LYS B 102 -99.73 144.06
REMARK 500 GLU C 2 -89.44 -25.17
REMARK 500 ASP C 62 -87.74 -66.60
REMARK 500 LYS C 67 143.32 -17.37
REMARK 500 LYS C 69 -125.93 -17.16
REMARK 500 LYS C 102 -109.35 87.88
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WCR A 1 103 UNP P17335 PTCA_ECOLI 14 116
DBREF 1WCR B 1 103 UNP P17335 PTCA_ECOLI 14 116
DBREF 1WCR C 1 103 UNP P17335 PTCA_ECOLI 14 116
SEQADV 1WCR LEU A 79 UNP P17335 ASP 92 ENGINEERED MUTATION
SEQADV 1WCR LEU B 79 UNP P17335 ASP 92 ENGINEERED MUTATION
SEQADV 1WCR LEU C 79 UNP P17335 ASP 92 ENGINEERED MUTATION
SEQRES 1 A 103 ALA GLU GLU LEU GLU GLU VAL VAL MET GLY LEU ILE ILE
SEQRES 2 A 103 ASN SER GLY GLN ALA ARG SER LEU ALA TYR ALA ALA LEU
SEQRES 3 A 103 LYS GLN ALA LYS GLN GLY ASP PHE ALA ALA ALA LYS ALA
SEQRES 4 A 103 MET MET ASP GLN SER ARG MET ALA LEU ASN GLU ALA HIS
SEQRES 5 A 103 LEU VAL GLN THR LYS LEU ILE GLU GLY ASP ALA GLY GLU
SEQRES 6 A 103 GLY LYS MET LYS VAL SER LEU VAL LEU VAL HIS ALA GLN
SEQRES 7 A 103 LEU HIS LEU MET THR SER MET LEU ALA ARG GLU LEU ILE
SEQRES 8 A 103 THR GLU LEU ILE GLU LEU HIS GLU LYS LEU LYS ALA
SEQRES 1 B 103 ALA GLU GLU LEU GLU GLU VAL VAL MET GLY LEU ILE ILE
SEQRES 2 B 103 ASN SER GLY GLN ALA ARG SER LEU ALA TYR ALA ALA LEU
SEQRES 3 B 103 LYS GLN ALA LYS GLN GLY ASP PHE ALA ALA ALA LYS ALA
SEQRES 4 B 103 MET MET ASP GLN SER ARG MET ALA LEU ASN GLU ALA HIS
SEQRES 5 B 103 LEU VAL GLN THR LYS LEU ILE GLU GLY ASP ALA GLY GLU
SEQRES 6 B 103 GLY LYS MET LYS VAL SER LEU VAL LEU VAL HIS ALA GLN
SEQRES 7 B 103 LEU HIS LEU MET THR SER MET LEU ALA ARG GLU LEU ILE
SEQRES 8 B 103 THR GLU LEU ILE GLU LEU HIS GLU LYS LEU LYS ALA
SEQRES 1 C 103 ALA GLU GLU LEU GLU GLU VAL VAL MET GLY LEU ILE ILE
SEQRES 2 C 103 ASN SER GLY GLN ALA ARG SER LEU ALA TYR ALA ALA LEU
SEQRES 3 C 103 LYS GLN ALA LYS GLN GLY ASP PHE ALA ALA ALA LYS ALA
SEQRES 4 C 103 MET MET ASP GLN SER ARG MET ALA LEU ASN GLU ALA HIS
SEQRES 5 C 103 LEU VAL GLN THR LYS LEU ILE GLU GLY ASP ALA GLY GLU
SEQRES 6 C 103 GLY LYS MET LYS VAL SER LEU VAL LEU VAL HIS ALA GLN
SEQRES 7 C 103 LEU HIS LEU MET THR SER MET LEU ALA ARG GLU LEU ILE
SEQRES 8 C 103 THR GLU LEU ILE GLU LEU HIS GLU LYS LEU LYS ALA
HELIX 1 1 ALA A 1 GLN A 31 1 31
HELIX 2 2 ASP A 33 ASP A 62 1 30
HELIX 3 3 SER A 71 LYS A 102 1 32
HELIX 4 4 ALA B 1 GLN B 31 1 31
HELIX 5 5 ASP B 33 ASP B 62 1 30
HELIX 6 6 SER B 71 LYS B 102 1 32
HELIX 7 7 ALA C 1 GLN C 31 1 31
HELIX 8 8 ASP C 33 ASP C 62 1 30
HELIX 9 9 SER C 71 LEU C 101 1 31
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 3
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