Header list of 1x60.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 17-MAY-05 1X60
TITLE SOLUTION STRUCTURE OF THE PEPTIDOGLYCAN BINDING DOMAIN OF B. SUBTILIS
TITLE 2 CELL WALL LYTIC ENZYME CWLC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPORULATION-SPECIFIC N-ACETYLMURAMOYL-L-ALANINE AMIDASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-79;
COMPND 5 SYNONYM: CELL WALL HYDROLASE, AUTOLYSIN;
COMPND 6 EC: 3.5.1.28;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS CWLC, CWLCR, PEPTIDOGLYCAN, CELL WALL LYTIC AMIDASE, TANDEM REPEATS,
KEYWDS 2 HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR M.MISHIMA,T.SHIDA,K.YABUKI,K.KATO,J.SEKIGUCHI,C.KOJIMA
REVDAT 3 02-MAR-22 1X60 1 REMARK
REVDAT 2 24-FEB-09 1X60 1 VERSN
REVDAT 1 09-AUG-05 1X60 0
JRNL AUTH M.MISHIMA,T.SHIDA,K.YABUKI,K.KATO,J.SEKIGUCHI,C.KOJIMA
JRNL TITL SOLUTION STRUCTURE OF THE PEPTIDOGLYCAN BINDING DOMAIN OF
JRNL TITL 2 BACILLUS SUBTILIS CELL WALL LYTIC ENZYME CWLC:
JRNL TITL 3 CHARACTERIZATION OF THE SPORULATION-RELATED REPEATS BY
JRNL TITL 4 NMR(,)
JRNL REF BIOCHEMISTRY V. 44 10153 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 16042392
JRNL DOI 10.1021/BI050624N
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, CNS 1.1
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X60 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024422.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : 70MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.7MM CWLCR U-15N,13C 50MM
REMARK 210 PHOSPHATE BUFFER K; 100% D2O;
REMARK 210 1.7MM CWLCR U-15N 50MM PHOSPHATE
REMARK 210 BUFFER K; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.110, CYANA 1.05
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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: 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 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: 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 2 104.07 59.84
REMARK 500 1 THR A 4 119.14 62.73
REMARK 500 1 SER A 7 91.62 -166.14
REMARK 500 1 ASP A 43 66.94 -55.18
REMARK 500 2 LYS A 2 170.69 58.79
REMARK 500 2 ASP A 43 65.16 -54.93
REMARK 500 3 LYS A 2 175.56 60.55
REMARK 500 3 THR A 4 31.49 -144.25
REMARK 500 3 SER A 6 122.16 -171.58
REMARK 500 3 ASP A 43 65.40 -54.80
REMARK 500 4 LYS A 3 -48.79 -133.46
REMARK 500 4 SER A 7 88.35 -154.95
REMARK 500 4 ASP A 43 65.96 -55.35
REMARK 500 5 LYS A 3 37.92 -165.70
REMARK 500 5 SER A 7 149.83 62.53
REMARK 500 5 ASP A 43 65.87 -55.08
REMARK 500 6 ASP A 43 68.55 -57.43
REMARK 500 7 SER A 5 76.36 -163.61
REMARK 500 7 ASP A 43 65.30 -53.72
REMARK 500 8 THR A 4 174.50 60.05
REMARK 500 8 SER A 6 99.06 61.29
REMARK 500 8 ASP A 43 66.67 -55.71
REMARK 500 9 LYS A 2 -52.67 -172.90
REMARK 500 9 SER A 5 -49.18 -141.14
REMARK 500 9 ASP A 43 66.08 -57.24
REMARK 500 10 THR A 4 163.83 64.96
REMARK 500 10 SER A 7 -167.51 -75.57
REMARK 500 10 ASP A 43 64.00 -56.02
REMARK 500 11 THR A 4 -177.92 50.52
REMARK 500 11 SER A 5 -75.12 -102.83
REMARK 500 11 ASP A 43 63.80 -56.18
REMARK 500 12 SER A 6 126.61 63.85
REMARK 500 12 SER A 7 -41.40 -174.77
REMARK 500 12 ASP A 43 65.68 -55.26
REMARK 500 13 LYS A 2 31.43 -144.51
REMARK 500 13 LYS A 3 -47.20 -138.64
REMARK 500 13 THR A 4 44.49 -94.60
REMARK 500 13 ASP A 43 64.91 -53.97
REMARK 500 14 LYS A 3 -77.11 65.89
REMARK 500 14 SER A 6 141.94 63.38
REMARK 500 14 SER A 7 41.52 -102.02
REMARK 500 14 ASP A 43 67.15 -55.92
REMARK 500 15 SER A 5 -42.74 -176.51
REMARK 500 15 SER A 6 83.20 59.62
REMARK 500 15 ASP A 43 64.62 -55.91
REMARK 500 16 SER A 7 126.72 63.64
REMARK 500 16 ASP A 43 64.06 -57.24
REMARK 500 17 SER A 5 79.11 -69.70
REMARK 500 17 ASP A 43 -85.39 38.73
REMARK 500 18 SER A 5 121.35 62.87
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1X60 A 1 79 UNP Q06320 CWLC_BACSU 177 255
SEQRES 1 A 79 LEU LYS LYS THR SER SER SER GLY LEU TYR LYS VAL GLN
SEQRES 2 A 79 ILE GLY ALA PHE LYS VAL LYS ALA ASN ALA ASP SER LEU
SEQRES 3 A 79 ALA SER ASN ALA GLU ALA LYS GLY PHE ASP SER ILE VAL
SEQRES 4 A 79 LEU LEU LYS ASP GLY LEU TYR LYS VAL GLN ILE GLY ALA
SEQRES 5 A 79 PHE SER SER LYS ASP ASN ALA ASP THR LEU ALA ALA ARG
SEQRES 6 A 79 ALA LYS ASN ALA GLY PHE ASP ALA ILE VAL ILE LEU GLU
SEQRES 7 A 79 SER
HELIX 1 1 VAL A 19 GLY A 34 1 16
HELIX 2 2 SER A 55 GLY A 70 1 16
SHEET 1 A 4 SER A 37 LYS A 42 0
SHEET 2 A 4 LEU A 45 PHE A 53 -1 O LEU A 45 N LYS A 42
SHEET 3 A 4 LEU A 9 PHE A 17 -1 N GLY A 15 O VAL A 48
SHEET 4 A 4 ILE A 74 GLU A 78 -1 O ILE A 74 N GLN A 13
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