Header list of 1z6h.pdb file
Complete list - r 2 2 Bytes
HEADER BIOSYNTHETIC PROTEIN 22-MAR-05 1Z6H
TITLE SOLUTION STRUCTURE OF BACILLUS SUBTILIS BLAP BIOTINYLATED-FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIOTIN/LIPOYL ATTACHMENT PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET 21A(+)
KEYWDS BACILLUS SUBTILIS, SINGLE-DOMAIN BIOTIN/LIPOYL ATTACHMENT PROTEIN,
KEYWDS 2 SOLUTION STRUCTURE, BIOSYNTHETIC PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.CUI,B.XIA
REVDAT 4 02-MAR-22 1Z6H 1 REMARK LINK
REVDAT 3 24-FEB-09 1Z6H 1 VERSN
REVDAT 2 10-JUL-07 1Z6H 1 JRNL
REVDAT 1 22-MAR-06 1Z6H 0
JRNL AUTH G.CUI,B.NAN,J.HU,Y.WANG,C.JIN,B.XIA
JRNL TITL IDENTIFICATION AND SOLUTION STRUCTURES OF A SINGLE DOMAIN
JRNL TITL 2 BIOTIN/LIPOYL ATTACHMENT PROTEIN FROM BACILLUS SUBTILIS
JRNL REF J.BIOL.CHEM. V. 281 20598 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16699181
JRNL DOI 10.1074/JBC.M602660200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), DAVID CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 4560 RESTRAINTS, 4160 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 117
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 30 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS, 253 CHARITY RESTRAINTS.
REMARK 4
REMARK 4 1Z6H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032358.
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 : 150MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.2MM S-BCCP U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER NA; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5, CYANA
REMARK 210 1.0.6
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES
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: 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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 2 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
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 LYS A 35 7.20 90.66
REMARK 500 2 TRP A 12 -54.30 -24.86
REMARK 500 2 LYS A 35 8.48 84.36
REMARK 500 3 LYS A 35 7.19 88.62
REMARK 500 3 LEU A 65 -43.54 -137.31
REMARK 500 4 TRP A 12 -53.34 -29.30
REMARK 500 4 LYS A 35 6.36 86.66
REMARK 500 4 LEU A 65 -44.79 -130.06
REMARK 500 5 TRP A 12 -52.04 -29.57
REMARK 500 5 LYS A 35 7.28 85.11
REMARK 500 5 SER A 71 -38.27 -149.10
REMARK 500 6 LYS A 35 9.83 84.90
REMARK 500 6 LEU A 65 -42.86 -131.26
REMARK 500 7 LYS A 35 7.67 85.35
REMARK 500 7 LEU A 65 -43.17 -135.00
REMARK 500 8 LYS A 35 9.63 86.89
REMARK 500 8 LEU A 65 -42.57 -134.88
REMARK 500 9 LYS A 35 18.88 89.73
REMARK 500 9 LEU A 65 -38.52 -135.28
REMARK 500 10 LYS A 35 21.78 80.02
REMARK 500 10 LEU A 65 -42.70 -132.19
REMARK 500 11 LYS A 35 9.22 85.21
REMARK 500 11 LEU A 65 -40.17 -135.10
REMARK 500 12 TRP A 12 -52.93 -29.33
REMARK 500 12 LYS A 35 9.28 87.26
REMARK 500 12 LEU A 65 -42.41 -130.05
REMARK 500 12 ASN A 70 73.20 31.25
REMARK 500 13 TRP A 12 -51.49 -29.93
REMARK 500 13 LYS A 35 5.75 88.94
REMARK 500 13 LEU A 65 -42.18 -135.01
REMARK 500 14 LYS A 35 7.78 86.04
REMARK 500 14 LEU A 65 -44.60 -134.90
REMARK 500 15 LYS A 35 10.87 84.10
REMARK 500 15 LEU A 65 -41.80 -133.26
REMARK 500 15 ASN A 70 41.64 -147.38
REMARK 500 16 LYS A 35 7.11 91.27
REMARK 500 16 THR A 72 11.99 -142.11
REMARK 500 17 LYS A 35 12.36 87.69
REMARK 500 17 LEU A 65 -42.59 -135.07
REMARK 500 18 LYS A 35 6.57 85.42
REMARK 500 18 LEU A 65 -43.80 -135.77
REMARK 500 19 LEU A 65 -43.25 -134.76
REMARK 500 20 LYS A 35 15.18 86.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 31 GLU A 32 1 140.47
REMARK 500 LEU A 31 GLU A 32 2 135.16
REMARK 500 LEU A 31 GLU A 32 3 138.52
REMARK 500 LEU A 31 GLU A 32 4 136.94
REMARK 500 LEU A 31 GLU A 32 5 137.24
REMARK 500 LEU A 31 GLU A 32 6 138.72
REMARK 500 LEU A 31 GLU A 32 7 139.34
REMARK 500 LEU A 31 GLU A 32 8 138.23
REMARK 500 LEU A 31 GLU A 32 9 137.74
REMARK 500 LEU A 31 GLU A 32 10 140.97
REMARK 500 LEU A 31 GLU A 32 11 138.00
REMARK 500 LEU A 31 GLU A 32 12 137.46
REMARK 500 LEU A 31 GLU A 32 13 138.61
REMARK 500 LEU A 31 GLU A 32 14 136.67
REMARK 500 LEU A 31 GLU A 32 15 139.33
REMARK 500 LEU A 31 GLU A 32 16 136.01
REMARK 500 LEU A 31 GLU A 32 17 137.81
REMARK 500 LEU A 31 GLU A 32 18 138.37
REMARK 500 LEU A 31 GLU A 32 19 137.62
REMARK 500 LEU A 31 GLU A 32 20 139.05
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 BTI A 135
DBREF 1Z6H A 2 73 UNP Q9R9I3 Q9R9I3_BACSU 2 73
SEQRES 1 A 72 THR VAL SER ILE GLN MET ALA GLY ASN LEU TRP LYS VAL
SEQRES 2 A 72 HIS VAL LYS ALA GLY ASP GLN ILE GLU LYS GLY GLN GLU
SEQRES 3 A 72 VAL ALA ILE LEU GLU SER MET LYS MET GLU ILE PRO ILE
SEQRES 4 A 72 VAL ALA ASP ARG SER GLY ILE VAL LYS GLU VAL LYS LYS
SEQRES 5 A 72 LYS GLU GLY ASP PHE VAL ASN GLU GLY ASP VAL LEU LEU
SEQRES 6 A 72 GLU LEU SER ASN SER THR GLN
HET BTI A 135 30
HETNAM BTI 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)
HETNAM 2 BTI PENTANAL
FORMUL 2 BTI C10 H16 N2 O2 S
HELIX 1 1 ASN A 70 THR A 72 5 3
SHEET 1 A 4 VAL A 3 SER A 4 0
SHEET 2 A 4 VAL A 64 LEU A 68 -1 O LEU A 65 N VAL A 3
SHEET 3 A 4 GLY A 46 VAL A 51 -1 N GLU A 50 O GLU A 67
SHEET 4 A 4 GLN A 21 ILE A 22 -1 N ILE A 22 O GLY A 46
SHEET 1 B 4 MET A 36 VAL A 41 0
SHEET 2 B 4 GLU A 27 SER A 33 -1 N LEU A 31 O ILE A 38
SHEET 3 B 4 GLY A 9 VAL A 14 -1 N ASN A 10 O GLU A 32
SHEET 4 B 4 PHE A 58 VAL A 59 -1 O VAL A 59 N GLY A 9
LINK NZ LYS A 35 C11 BTI A 135 1555 1555 1.34
SITE 1 AC1 2 TRP A 12 LYS A 35
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 - r 2 2 Bytes