Header list of 1pxq.pdb file
Complete list - 25 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 04-JUL-03 1PXQ
TITLE STRUCTURE OF SUBTILISIN A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBTILISIN A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ANTILISTERIAL BACTERIOCIN SUBTILISIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 STRAIN: JH642
KEYWDS THIOETHER BRIDGE, CYCLIC PEPTIDE, BACTERIOCIN, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 8
AUTHOR K.E.KAWULKA,T.SPRULES,R.T.MCKAY,P.MERCIER,C.M.DIAPER,P.ZUBER,
AUTHOR 2 J.C.VEDERAS
REVDAT 3 05-OCT-11 1PXQ 1 CAVEAT HET HETATM LINK
REVDAT 3 2 1 REMARK SEQRES VERSN
REVDAT 2 24-FEB-09 1PXQ 1 VERSN
REVDAT 1 22-JUN-04 1PXQ 0
JRNL AUTH K.E.KAWULKA,T.SPRULES,C.M.DIAPER,R.M.WHITTAL,R.T.MCKAY,
JRNL AUTH 2 P.MERCIER,P.ZUBER,J.C.VEDERAS
JRNL TITL STRUCTURE OF SUBTILISIN A, A CYCLIC ANTIMICROBIAL PEPTIDE
JRNL TITL 2 FROM BACILLUS SUBTILIS WITH UNUSUAL SULFUR TO ALPHA-CARBON
JRNL TITL 3 CROSS-LINKS: FORMATION AND REDUCTION OF
JRNL TITL 4 ALPHA-THIO-ALPHA-AMINO ACID DERIVATIVES
JRNL REF BIOCHEMISTRY V. 43 3385 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15035610
JRNL DOI 10.1021/BI0359527
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.KAWULKA,T.SPRULES,R.T.MCKAY,P.MERCIER,C.M.DIAPER,P.ZUBER,
REMARK 1 AUTH 2 J.C.VEDERAS
REMARK 1 TITL STRUCTURE OF SUBTILISIN A, AN ANTIMICROBIAL PEPTIDE FROM
REMARK 1 TITL 2 BACILLUS SUBTILIS WITH UNUSUAL POSTTRANSLATIONAL
REMARK 1 TITL 3 MODIFICATIONS LINKING CYSTEINE SULFURS TO ALPHA-CARBONS OF
REMARK 1 TITL 4 PHENYLALANINE AND THREONINE
REMARK 1 REF J.AM.CHEM.SOC. V. 125 4726 2003
REMARK 1 REFN ISSN 0002-7863
REMARK 1 DOI 10.1021/JA029654T
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER, A.T., ADAMS, P.D., CLORE, G.M., DELANO,
REMARK 3 W.L., GROS, P., GROSSE-KUNSTLEVE, R.W., JIANG,
REMARK 3 J.S., KUSZEWSKI, J., NILGES, M., PANNU, N.S., READ,
REMARK 3 R.J., RICE, L.M., SIMONSON, T., WARREN, G.L.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 301 NOE-DERIVED DISTANCE CONSTRAINTS
REMARK 3 AND 20 DIHEDRAL ANGLE RESTRAINTS WERE USED TO CALCULATE THE
REMARK 3 STRUCTURES.
REMARK 4
REMARK 4 1PXQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-03.
REMARK 100 THE RCSB ID CODE IS RCSB019677.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : SUBA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 4D_13C/15N-
REMARK 210 SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR, NMRPIPE 2.2, NMRVIEW 5.0,
REMARK 210 CNS 1.1
REMARK 210 METHOD USED : DYNAMIC ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 8
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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 N ASN A 1 O GLY A 35 2.05
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 CYS A 4 49.90 -76.59
REMARK 500 1 CYS A 7 46.13 -154.78
REMARK 500 1 ILE A 9 -71.57 -44.57
REMARK 500 1 ALA A 12 89.87 -164.24
REMARK 500 1 ILE A 19 32.12 85.98
REMARK 500 1 ASP A 21 119.02 77.52
REMARK 500 1 PHE A 22 56.87 15.52
REMARK 500 1 2TL A 28 -28.85 -45.12
REMARK 500 2 LYS A 2 -81.37 -82.70
REMARK 500 2 CYS A 7 65.92 -155.02
REMARK 500 2 ILE A 9 102.03 -59.82
REMARK 500 2 ALA A 12 88.15 -158.83
REMARK 500 2 ILE A 19 35.02 86.01
REMARK 500 2 ASP A 21 109.58 78.61
REMARK 500 2 PHE A 22 55.29 32.20
REMARK 500 2 2TL A 28 -165.59 -54.55
REMARK 500 2 DPN A 31 -19.93 -59.42
REMARK 500 3 CYS A 4 26.29 -156.97
REMARK 500 3 THR A 6 41.93 -78.23
REMARK 500 3 CYS A 7 39.62 174.83
REMARK 500 3 ILE A 9 104.52 -52.25
REMARK 500 3 ALA A 12 80.08 -160.01
REMARK 500 3 ILE A 19 37.71 86.05
REMARK 500 3 ASP A 21 109.31 76.13
REMARK 500 3 PHE A 22 58.00 31.24
REMARK 500 3 GLU A 23 41.08 -93.64
REMARK 500 3 2TL A 28 19.45 -149.15
REMARK 500 4 CYS A 7 65.83 -154.89
REMARK 500 4 ALA A 11 106.46 -50.84
REMARK 500 4 ALA A 12 28.70 -167.13
REMARK 500 4 ASP A 16 31.66 -99.17
REMARK 500 4 ILE A 19 59.82 86.21
REMARK 500 4 ASP A 21 117.01 63.27
REMARK 500 4 PHE A 22 80.06 -24.78
REMARK 500 4 ILE A 24 -70.76 -88.89
REMARK 500 5 LYS A 2 41.51 -83.15
REMARK 500 5 CYS A 4 26.70 45.75
REMARK 500 5 CYS A 7 49.78 -155.27
REMARK 500 5 ALA A 12 57.15 -159.73
REMARK 500 5 ASP A 16 30.32 -97.60
REMARK 500 5 ILE A 19 58.83 86.03
REMARK 500 5 PRO A 20 38.82 -94.19
REMARK 500 5 ASP A 21 109.19 48.32
REMARK 500 5 PHE A 22 83.09 -14.67
REMARK 500 5 2TL A 28 -41.24 -36.56
REMARK 500 5 TRP A 34 -76.93 -131.09
REMARK 500 6 THR A 6 49.70 -78.21
REMARK 500 6 CYS A 7 44.38 -178.26
REMARK 500 6 ILE A 9 -74.86 -58.37
REMARK 500 6 ALA A 11 107.33 -54.63
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
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 DPN A 31
DBREF 1PXQ A 1 35 UNP O07623 SBOA_BACSU 9 43
SEQRES 1 A 35 ASN LYS GLY CYS ALA THR CYS SER ILE GLY ALA ALA CYS
SEQRES 2 A 35 LEU VAL ASP GLY PRO ILE PRO ASP PHE GLU ILE ALA GLY
SEQRES 3 A 35 ALA 2TL GLY LEU DPN GLY LEU TRP GLY
HET 2TL A 28 13
HET DPN A 31 19
HETNAM 2TL D-ALLOTHREONINE
HETNAM DPN D-PHENYLALANINE
FORMUL 1 2TL C4 H9 N O3
FORMUL 1 DPN C9 H11 N O2
HELIX 1 1 2TL A 28 GLY A 35 1 8
LINK C ALA A 27 N 2TL A 28 1555 1555 1.33
LINK C 2TL A 28 N GLY A 29 1555 1555 1.33
LINK C LEU A 30 N DPN A 31 1555 1555 1.33
LINK C DPN A 31 N GLY A 32 1555 1555 1.33
LINK N ASN A 1 C GLY A 35 1555 1555 1.33
LINK SG CYS A 7 CA 2TL A 28 1555 1555 1.77
LINK SG CYS A 13 CA PHE A 22 1555 1555 1.78
LINK SG CYS A 4 CA DPN A 31 1555 1555 1.78
SITE 1 AC1 8 ASN A 1 CYS A 4 2TL A 28 GLY A 29
SITE 2 AC1 8 LEU A 30 GLY A 32 LEU A 33 GLY 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 - 25 20 Bytes