Header list of 1dav.pdb file
Complete list - v 3 2 Bytes
HEADER HYDROLASE 31-OCT-99 1DAV
TITLE SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM
TITLE 2 THERMOCELLUM CELLULOSOME (20 STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE SS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TYPE I DOCKERIN DOMAIN (RESIDUES 673-741);
COMPND 5 SYNONYM: CELS;
COMPND 6 EC: 3.2.1.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 1515;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM109(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCYB2
KEYWDS CELLULOSE DEGRADATION, CELLULOSOME, CALCIUM-BINDING, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.L.LYTLE,B.F.VOLKMAN,W.M.WESTLER,M.P.HECKMAN,J.H.D.WU
REVDAT 5 03-NOV-21 1DAV 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1DAV 1 VERSN
REVDAT 3 24-FEB-04 1DAV 1 CRYST1
REVDAT 2 01-APR-03 1DAV 1 JRNL
REVDAT 1 04-APR-01 1DAV 0
JRNL AUTH B.L.LYTLE,B.F.VOLKMAN,W.M.WESTLER,M.P.HECKMAN,J.H.D.WU
JRNL TITL SOLUTION STRUCTURE OF A TYPE I DOCKERIN DOMAIN, A NOVEL
JRNL TITL 2 PROKARYOTIC, EXTRACELLULAR CALCIUM-BINDING DOMAIN.
JRNL REF J.MOL.BIOL. V. 307 745 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11273698
JRNL DOI 10.1006/JMBI.2001.4522
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.L.LYTLE,B.F.VOLKMAN,W.M.WESTLER,J.H.D.WU
REMARK 1 TITL SECONDARY STRUCTURE AND CALCIUM-INDUCED FOLDING OF THE
REMARK 1 TITL 2 CLOSTRIDIUM THERMOCELLUM DOCKERIN DOMAIN DETERMINED BY NMR
REMARK 1 TITL 3 SPECTROSCOPY
REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 379 237 2000
REMARK 1 REFN ISSN 0003-9861
REMARK 1 PMID 10898940
REMARK 1 DOI 10.1006/ABBI.2000.1882
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.LYTLE,J.H.D.WU
REMARK 1 TITL INVOLVEMENT OF BOTH DOCKERIN SUBDOMAINS IN ASSEMBLY OF THE
REMARK 1 TITL 2 CLOSTRIDIUM THERMOCELLUM CELLULOSOME
REMARK 1 REF J.BACTERIOL. V. 180 6581 1998
REMARK 1 REFN ISSN 0021-9193
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : P.GUENTERT, C.MUMENTHALER, K.WUETHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 728 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 79 DIHEDRAL ANGLE CONSTRAINTS,
REMARK 3 AND 12 CALCIUM ION RESTRAINTS.
REMARK 4
REMARK 4 1DAV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000009932.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 328; 328
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 100MM KCL; 100MM KCL
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 100MM POTASSIUM CHLORIDE; 20MM
REMARK 210 CALCIUM CHLORIDE; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; 3D_15N-SEPARATED_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, FELIX 95.0, NMRPIPE,
REMARK 210 XEASY 1.2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED BY STANDARD TECHNIQUES USING
REMARK 210 UNLABELED AND 15N- LABELED DOCKERIN.
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 O LEU A 55 H ILE A 59 1.47
REMARK 500 O LEU A 52 H LYS A 56 1.50
REMARK 500 OD1 ASP A 40 H ASP A 44 1.60
REMARK 500 O ASP A 8 HD21 ASN A 35 1.60
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 4 96.17 -170.60
REMARK 500 1 LYS A 14 -179.76 -172.80
REMARK 500 1 ASN A 35 61.51 -69.99
REMARK 500 1 ASP A 37 -74.94 -39.37
REMARK 500 1 LEU A 41 22.28 -145.96
REMARK 500 1 ASN A 42 24.02 -154.79
REMARK 500 1 ARG A 46 -93.59 -149.94
REMARK 500 1 SER A 49 -30.34 165.42
REMARK 500 1 LYS A 61 -37.16 -177.14
REMARK 500 1 ILE A 63 100.18 -32.83
REMARK 500 1 ASP A 64 -31.17 167.32
REMARK 500 1 THR A 65 -43.60 -134.15
REMARK 500 1 LEU A 66 111.74 66.64
REMARK 500 1 LYS A 69 98.06 56.89
REMARK 500 2 SER A 2 170.24 176.33
REMARK 500 2 LYS A 14 159.01 179.55
REMARK 500 2 SER A 30 -74.55 -40.53
REMARK 500 2 ASN A 35 56.14 -105.44
REMARK 500 2 ARG A 46 -70.87 -154.39
REMARK 500 2 SER A 49 -31.29 164.30
REMARK 500 2 LYS A 61 -38.18 -175.81
REMARK 500 2 ILE A 63 109.48 -34.55
REMARK 500 2 ASP A 64 -23.07 153.79
REMARK 500 2 THR A 65 -48.91 -138.19
REMARK 500 2 LEU A 66 98.01 67.42
REMARK 500 2 TYR A 68 157.98 -40.74
REMARK 500 3 ILE A 32 178.59 -59.74
REMARK 500 3 ASN A 35 61.95 -69.87
REMARK 500 3 ASN A 38 66.52 -116.54
REMARK 500 3 LEU A 41 -45.68 -148.45
REMARK 500 3 GLU A 43 36.21 75.01
REMARK 500 3 ARG A 46 -89.30 -145.00
REMARK 500 3 SER A 49 -30.91 166.31
REMARK 500 3 LYS A 61 38.56 -179.36
REMARK 500 3 ILE A 63 156.10 -41.01
REMARK 500 3 ASP A 64 -63.85 151.51
REMARK 500 3 LEU A 66 98.07 44.84
REMARK 500 3 LYS A 69 -75.95 70.92
REMARK 500 3 ASN A 70 162.28 176.76
REMARK 500 4 SER A 2 54.56 -178.04
REMARK 500 4 LEU A 5 147.84 -174.09
REMARK 500 4 LYS A 14 -172.39 -176.28
REMARK 500 4 ARG A 29 172.86 173.63
REMARK 500 4 ASN A 35 49.31 -93.90
REMARK 500 4 ASP A 37 -75.17 -53.86
REMARK 500 4 LEU A 41 14.74 -143.59
REMARK 500 4 ASN A 42 20.79 -152.81
REMARK 500 4 ARG A 46 -73.06 -140.51
REMARK 500 4 ASN A 48 -61.27 -120.43
REMARK 500 4 SER A 49 -40.66 -159.23
REMARK 500
REMARK 500 THIS ENTRY HAS 282 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 72 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 8 OD1
REMARK 620 2 ASN A 10 OD1 83.1
REMARK 620 3 ASP A 12 OD2 124.7 106.9
REMARK 620 4 GLY A 13 N 59.0 108.4 66.4
REMARK 620 5 LYS A 14 O 69.8 118.2 134.4 103.1
REMARK 620 6 LYS A 14 N 53.3 136.4 99.8 53.0 50.8
REMARK 620 7 ASP A 19 OD1 118.6 56.3 111.2 164.0 89.7 140.4
REMARK 620 8 ASP A 19 OD2 75.9 68.0 158.9 134.7 52.2 97.0 48.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 73 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 40 OD1
REMARK 620 2 ASN A 42 OD1 96.0
REMARK 620 3 ASP A 44 OD2 110.9 89.0
REMARK 620 4 ARG A 46 O 116.5 100.5 130.0
REMARK 620 5 ASP A 51 OD2 173.2 90.8 69.2 61.8
REMARK 620 6 ASP A 51 OD1 134.2 50.3 49.9 101.3 51.4
REMARK 620 N 1 2 3 4 5
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR-DETERMINED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: I
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: FIRST PREDICTED CA2+ BINDING LOOP
REMARK 800
REMARK 800 SITE_IDENTIFIER: II
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: SECOND PREDICTED CA2+ BINDING LOOP
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 72
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 73
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DAQ RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE
DBREF 1DAV A 1 70 UNP P38686 GUNS_CLOTM 672 741
SEQADV 1DAV MET A 1 UNP P38686 PRO 672 ENGINEERED MUTATION
SEQADV 1DAV GLY A 71 UNP P38686 INSERTION
SEQRES 1 A 71 MET SER THR LYS LEU TYR GLY ASP VAL ASN ASP ASP GLY
SEQRES 2 A 71 LYS VAL ASN SER THR ASP ALA VAL ALA LEU LYS ARG TYR
SEQRES 3 A 71 VAL LEU ARG SER GLY ILE SER ILE ASN THR ASP ASN ALA
SEQRES 4 A 71 ASP LEU ASN GLU ASP GLY ARG VAL ASN SER THR ASP LEU
SEQRES 5 A 71 GLY ILE LEU LYS ARG TYR ILE LEU LYS GLU ILE ASP THR
SEQRES 6 A 71 LEU PRO TYR LYS ASN GLY
HET CA A 72 1
HET CA A 73 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 1 ASP A 19 ARG A 29 1 11
HELIX 2 2 THR A 36 ALA A 39 5 4
HELIX 3 3 ASP A 51 ILE A 59 1 9
LINK OD1 ASP A 8 CA CA A 72 1555 1555 2.93
LINK OD1 ASN A 10 CA CA A 72 1555 1555 2.80
LINK OD2 ASP A 12 CA CA A 72 1555 1555 2.81
LINK N GLY A 13 CA CA A 72 1555 1555 3.05
LINK O LYS A 14 CA CA A 72 1555 1555 2.80
LINK N LYS A 14 CA CA A 72 1555 1555 3.30
LINK OD1 ASP A 19 CA CA A 72 1555 1555 2.80
LINK OD2 ASP A 19 CA CA A 72 1555 1555 2.63
LINK OD1 ASP A 40 CA CA A 73 1555 1555 3.10
LINK OD1 ASN A 42 CA CA A 73 1555 1555 2.81
LINK OD2 ASP A 44 CA CA A 73 1555 1555 2.86
LINK O ARG A 46 CA CA A 73 1555 1555 2.90
LINK OD2 ASP A 51 CA CA A 73 1555 1555 2.08
LINK OD1 ASP A 51 CA CA A 73 1555 1555 2.82
SITE 1 I 12 ASP A 8 VAL A 9 ASN A 10 ASP A 11
SITE 2 I 12 ASP A 12 GLY A 13 LYS A 14 VAL A 15
SITE 3 I 12 ASN A 16 SER A 17 THR A 18 ASP A 19
SITE 1 II 12 ASP A 40 LEU A 41 ASN A 42 GLU A 43
SITE 2 II 12 ASP A 44 GLY A 45 ARG A 46 VAL A 47
SITE 3 II 12 ASN A 48 SER A 49 THR A 50 ASP A 51
SITE 1 AC1 6 ASP A 8 ASN A 10 ASP A 12 GLY A 13
SITE 2 AC1 6 LYS A 14 ASP A 19
SITE 1 AC2 5 ASP A 40 ASN A 42 ASP A 44 ARG A 46
SITE 2 AC2 5 ASP A 51
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 - v 3 2 Bytes