Header list of 1mmc.pdb file
Complete list - 29 20 Bytes
HEADER CHITIN-BINDING 25-OCT-95 1MMC
TITLE 1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIMICROBIAL PEPTIDE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AC-AMP2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AMARANTHUS CAUDATUS;
SOURCE 3 ORGANISM_COMMON: AMARANTH;
SOURCE 4 ORGANISM_TAXID: 3567;
SOURCE 5 TISSUE: SEED
KEYWDS ANTIFUNGAL ANTIMICROBIAL, CHITIN-BINDING
EXPDTA SOLUTION NMR
NUMMDL 26
AUTHOR J.C.MARTINS,D.MAES,R.LORIS,H.A.M.PEPERMANS,L.WYNS,R.WILLEM,
AUTHOR 2 P.VERHEYDEN
REVDAT 3 29-NOV-17 1MMC 1 REMARK HELIX
REVDAT 2 24-FEB-09 1MMC 1 VERSN
REVDAT 1 08-MAR-96 1MMC 0
JRNL AUTH J.C.MARTINS,D.MAES,R.LORIS,H.A.PEPERMANS,L.WYNS,R.WILLEM,
JRNL AUTH 2 P.VERHEYDEN
JRNL TITL H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2, A SUGAR
JRNL TITL 2 BINDING ANTIMICROBIAL PROTEIN ISOLATED FROM AMARANTHUS
JRNL TITL 3 CAUDATUS.
JRNL REF J.MOL.BIOL. V. 258 322 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8627629
JRNL DOI 10.1006/JMBI.1996.0253
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.VERHEYDEN,J.PLETINCKX,D.MAES,H.A.M.PEPERMANS,L.WYNS,
REMARK 1 AUTH 2 R.WILLEM,J.C.MARTINS
REMARK 1 TITL 1H NMR STUDY OF THE INTERACTION OF N,N',N''-TRIACETYL
REMARK 1 TITL 2 CHITOTRIOSE WITH AC-AMP2, A SUGAR BINDING ANTIMICROBIAL
REMARK 1 TITL 3 PROTEIN ISOLATED FROM AMARANTHUS CAUDATUS
REMARK 1 REF FEBS LETT. V. 370 245 1995
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 2
REMARK 1 AUTH W.F.BROEKAERT,W.MARIEN,F.R.G.TERRAS,M.F.C.DE BOLLE,P.PROOST,
REMARK 1 AUTH 2 J.VAN DAMME,L.DILLEN,M.CLAEYS,S.B.REES,J.VANDERLEYDEN,
REMARK 1 AUTH 3 B.P.A.CAMMUE
REMARK 1 TITL ANTIMICROBIAL PEPTIDES FROM AMARANTHUS CAUDATUS SEEDS WITH
REMARK 1 TITL 2 SEQUENCE HOMOLOGY TO THE CYSTEINE(SLASH)GLYCINE RICH DOMAIN
REMARK 1 TITL 3 OF CHITIN-BINDING PROTEINS
REMARK 1 REF BIOCHEMISTRY V. 31 4308 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA, AMBER
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA),
REMARK 3 SINGH,WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MMC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175068.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 3 CD GLU A 3 OE2 0.109
REMARK 500 1 ARG A 30 C ARG A 30 OXT 0.134
REMARK 500 2 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 2 ARG A 30 C ARG A 30 OXT 0.132
REMARK 500 3 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 3 ARG A 30 C ARG A 30 OXT 0.130
REMARK 500 4 GLU A 3 CD GLU A 3 OE2 0.110
REMARK 500 4 ARG A 30 C ARG A 30 OXT 0.131
REMARK 500 5 GLU A 3 CD GLU A 3 OE2 0.108
REMARK 500 5 ARG A 30 C ARG A 30 OXT 0.132
REMARK 500 6 GLU A 3 CD GLU A 3 OE2 0.108
REMARK 500 6 ARG A 30 C ARG A 30 OXT 0.132
REMARK 500 7 GLU A 3 CD GLU A 3 OE2 0.109
REMARK 500 7 ARG A 30 C ARG A 30 OXT 0.136
REMARK 500 8 GLU A 3 CD GLU A 3 OE2 0.110
REMARK 500 8 ARG A 30 C ARG A 30 OXT 0.130
REMARK 500 9 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 9 ARG A 30 C ARG A 30 OXT 0.132
REMARK 500 10 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 10 ARG A 30 C ARG A 30 OXT 0.130
REMARK 500 11 GLU A 3 CD GLU A 3 OE2 0.110
REMARK 500 11 ARG A 30 C ARG A 30 OXT 0.132
REMARK 500 12 GLU A 3 CD GLU A 3 OE2 0.109
REMARK 500 12 ARG A 30 C ARG A 30 OXT 0.129
REMARK 500 13 GLU A 3 CD GLU A 3 OE2 0.112
REMARK 500 13 ARG A 30 C ARG A 30 OXT 0.133
REMARK 500 14 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 14 ARG A 30 C ARG A 30 OXT 0.133
REMARK 500 15 GLU A 3 CD GLU A 3 OE2 0.109
REMARK 500 15 ARG A 30 C ARG A 30 OXT 0.131
REMARK 500 16 GLU A 3 CD GLU A 3 OE2 0.108
REMARK 500 16 ARG A 30 C ARG A 30 OXT 0.130
REMARK 500 17 GLU A 3 CD GLU A 3 OE2 0.106
REMARK 500 17 ARG A 30 C ARG A 30 OXT 0.130
REMARK 500 18 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 18 ARG A 30 C ARG A 30 OXT 0.133
REMARK 500 19 GLU A 3 CD GLU A 3 OE2 0.110
REMARK 500 19 ARG A 30 C ARG A 30 OXT 0.132
REMARK 500 20 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 20 ARG A 30 C ARG A 30 OXT 0.130
REMARK 500 21 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 21 ARG A 30 C ARG A 30 OXT 0.130
REMARK 500 22 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 22 ARG A 30 C ARG A 30 OXT 0.133
REMARK 500 23 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 23 ARG A 30 C ARG A 30 OXT 0.134
REMARK 500 24 GLU A 3 CD GLU A 3 OE2 0.107
REMARK 500 24 ARG A 30 C ARG A 30 OXT 0.132
REMARK 500 25 GLU A 3 CD GLU A 3 OE2 0.110
REMARK 500 25 ARG A 30 C ARG A 30 OXT 0.133
REMARK 500
REMARK 500 THIS ENTRY HAS 52 BOND DEVIATIONS.
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 SER A 11 41.87 37.80
REMARK 500 1 TYR A 27 -60.66 -92.79
REMARK 500 2 GLU A 3 123.65 101.97
REMARK 500 2 SER A 11 53.19 34.82
REMARK 500 3 GLU A 3 118.27 83.11
REMARK 500 3 VAL A 5 77.76 -116.12
REMARK 500 3 SER A 11 47.51 32.48
REMARK 500 4 SER A 11 54.10 34.65
REMARK 500 4 CYS A 28 37.25 -71.34
REMARK 500 5 SER A 11 48.97 33.21
REMARK 500 6 SER A 11 51.15 34.42
REMARK 500 6 SER A 16 173.07 -55.03
REMARK 500 7 GLU A 3 144.73 174.24
REMARK 500 7 SER A 11 51.33 32.71
REMARK 500 7 TYR A 20 -156.02 -90.41
REMARK 500 8 SER A 11 49.00 33.02
REMARK 500 8 TYR A 27 -65.86 -92.62
REMARK 500 9 SER A 11 47.67 32.68
REMARK 500 10 SER A 11 44.62 34.23
REMARK 500 11 SER A 16 -166.13 -69.52
REMARK 500 11 TYR A 20 -159.24 -90.05
REMARK 500 12 VAL A 5 59.70 -90.25
REMARK 500 12 SER A 11 38.74 34.96
REMARK 500 12 SER A 16 -169.99 -69.06
REMARK 500 12 TYR A 20 -154.55 -88.94
REMARK 500 13 GLU A 3 134.69 68.08
REMARK 500 13 SER A 11 46.16 33.87
REMARK 500 13 TYR A 27 -60.13 -94.23
REMARK 500 14 SER A 16 -166.27 -69.81
REMARK 500 15 TYR A 20 -153.17 -89.18
REMARK 500 16 GLU A 3 126.93 122.23
REMARK 500 16 SER A 11 47.26 33.61
REMARK 500 17 SER A 11 49.53 31.87
REMARK 500 17 TYR A 20 -169.97 -113.32
REMARK 500 17 TYR A 27 -60.34 -94.65
REMARK 500 18 SER A 11 55.22 32.19
REMARK 500 18 TYR A 27 -66.19 -90.86
REMARK 500 18 CYS A 28 -83.02 -63.47
REMARK 500 19 SER A 11 49.22 33.08
REMARK 500 19 TYR A 27 -60.15 -94.44
REMARK 500 20 GLU A 3 135.85 105.34
REMARK 500 20 SER A 16 -177.46 -68.64
REMARK 500 21 GLU A 3 119.61 80.27
REMARK 500 21 VAL A 5 78.56 -104.26
REMARK 500 21 SER A 16 -168.18 -73.33
REMARK 500 21 TYR A 20 -158.83 -93.95
REMARK 500 22 TYR A 27 -60.35 -96.22
REMARK 500 24 TYR A 27 -63.62 -91.49
REMARK 500 25 SER A 11 51.21 32.21
REMARK 500 26 SER A 16 -177.55 -60.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 30 0.11 SIDE CHAIN
REMARK 500 2 TYR A 27 0.10 SIDE CHAIN
REMARK 500 3 ARG A 8 0.14 SIDE CHAIN
REMARK 500 3 TYR A 20 0.12 SIDE CHAIN
REMARK 500 3 ARG A 30 0.25 SIDE CHAIN
REMARK 500 4 TYR A 27 0.07 SIDE CHAIN
REMARK 500 6 TYR A 27 0.09 SIDE CHAIN
REMARK 500 7 ARG A 8 0.16 SIDE CHAIN
REMARK 500 8 TYR A 20 0.31 SIDE CHAIN
REMARK 500 8 ARG A 30 0.12 SIDE CHAIN
REMARK 500 9 TYR A 20 0.10 SIDE CHAIN
REMARK 500 10 ARG A 8 0.13 SIDE CHAIN
REMARK 500 10 ARG A 30 0.12 SIDE CHAIN
REMARK 500 11 TYR A 27 0.08 SIDE CHAIN
REMARK 500 11 ARG A 30 0.08 SIDE CHAIN
REMARK 500 14 TYR A 20 0.10 SIDE CHAIN
REMARK 500 16 TYR A 27 0.12 SIDE CHAIN
REMARK 500 16 ARG A 30 0.09 SIDE CHAIN
REMARK 500 17 ARG A 30 0.14 SIDE CHAIN
REMARK 500 18 TYR A 20 0.12 SIDE CHAIN
REMARK 500 18 TYR A 27 0.10 SIDE CHAIN
REMARK 500 22 ARG A 8 0.13 SIDE CHAIN
REMARK 500 23 ARG A 6 0.11 SIDE CHAIN
REMARK 500 23 TYR A 20 0.09 SIDE CHAIN
REMARK 500 24 ARG A 8 0.09 SIDE CHAIN
REMARK 500 24 TYR A 27 0.07 SIDE CHAIN
REMARK 500 25 TYR A 20 0.16 SIDE CHAIN
REMARK 500 25 ARG A 30 0.08 SIDE CHAIN
REMARK 500 26 TYR A 20 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MMC A 1 30 UNP P27275 AMP_AMACA 26 55
SEQRES 1 A 30 VAL GLY GLU CYS VAL ARG GLY ARG CYS PRO SER GLY MET
SEQRES 2 A 30 CYS CYS SER GLN PHE GLY TYR CYS GLY LYS GLY PRO LYS
SEQRES 3 A 30 TYR CYS GLY ARG
HELIX 1 1 PRO A 25 CYS A 28 1 4
SHEET 1 A 2 CYS A 14 CYS A 15 0
SHEET 2 A 2 CYS A 21 GLY A 22 -1 N GLY A 22 O CYS A 14
SSBOND 1 CYS A 4 CYS A 15 1555 1555 2.08
SSBOND 2 CYS A 9 CYS A 21 1555 1555 2.08
SSBOND 3 CYS A 14 CYS A 28 1555 1555 2.09
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 - 29 20 Bytes