Header list of 1hr1.pdb file
Complete list - 10 20 Bytes
HEADER ANTIBIOTIC, ANTIMICROBIAL PROTEIN 20-DEC-00 1HR1
TITLE STRUCTURE OF AN INDOLICIDIN PEPTIDE DERIVATIVE WITH P-->A SUBSTITUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INDOLICIDIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 4 ORGANISM_COMMON: CATTLE;
SOURCE 5 ORGANISM_TAXID: 9913;
SOURCE 6 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 7 OCCURS NATURALLY IN BOS TAURUS. THE SEQUENCE IS NATURALLY AMIDATED
SOURCE 8 AT C-TERMINUS.
KEYWDS ALPHA-HELIX, CATIONIC ANTIMICROBIAL PEPTIDE, ANTIBIOTIC,
KEYWDS 2 ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR C.L.FRIEDRICH,A.ROZEK,A.PATRZYKAT,R.E.W.HANCOCK
REVDAT 5 10-NOV-21 1HR1 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1HR1 1 VERSN
REVDAT 3 31-DEC-02 1HR1 1 REMARK
REVDAT 2 04-JUL-01 1HR1 1 JRNL REMARK
REVDAT 1 03-JAN-01 1HR1 0
JRNL AUTH C.L.FRIEDRICH,A.ROZEK,A.PATRZYKAT,R.E.W.HANCOCK
JRNL TITL STRUCTURE AND MECHANISM OF ACTION OF AN INDOLICIDIN PEPTIDE
JRNL TITL 2 DERIVATIVE WITH IMPROVED ACTIVITY AGAINST GRAM-POSITIVE
JRNL TITL 3 BACTERIA
JRNL REF J.BIOL.CHEM. V. 276 24015 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11294848
JRNL DOI 10.1074/JBC.M009691200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.ROZEK,C.L.FRIEDRICH,R.E.W.HANCOCK
REMARK 1 TITL STRUCTURE OF THE BOVINE ANTIMICROBIAL PEPTIDE INDOLICIDIN
REMARK 1 TITL 2 BOUND TO DODECYLPHOSPHOCHOLINE AND SODIUM DODECYL SULFATE
REMARK 1 TITL 3 MICELLES.
REMARK 1 REF BIOCHEMISTRY V. 39 15765 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI000714M
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, X-PLOR 3.851
REMARK 3 AUTHORS : DEALGLIO (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 167 (NON
REMARK 3 -REDUNDANT) NOE-DERIVED DISTANCE RESTRAINTS, 77 INTRARESIDUE AND
REMARK 3 90 INTER-RESIDUE RESTRAINTS. STRUCTURES WERE GENERATED USING
REMARK 3 DGII (MSI) AND THEN REFINED USING XPLOR.
REMARK 4
REMARK 4 1HR1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000012538.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : 200MM DPC
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM CP10A; 200MM
REMARK 210 DODECYLPHOSPHOCHOLINE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 4.0.3., DGII 97.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR 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: 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 ALA A 3 140.69 167.55
REMARK 500 1 TRP A 4 -60.28 171.33
REMARK 500 1 TRP A 8 -84.47 -51.02
REMARK 500 2 ALA A 3 137.32 168.12
REMARK 500 2 TRP A 4 -51.13 75.36
REMARK 500 2 TRP A 8 -86.19 -60.42
REMARK 500 3 ALA A 3 141.81 168.16
REMARK 500 3 TRP A 4 -60.64 172.56
REMARK 500 3 TRP A 8 -83.06 -49.42
REMARK 500 3 ARG A 12 -38.10 -37.46
REMARK 500 4 ALA A 3 140.18 168.27
REMARK 500 4 TRP A 4 -59.52 169.75
REMARK 500 4 TRP A 8 -84.85 -50.02
REMARK 500 4 ARG A 12 -36.64 -37.95
REMARK 500 5 ALA A 3 141.75 167.88
REMARK 500 5 TRP A 4 -60.58 171.51
REMARK 500 5 TRP A 8 -85.69 -59.01
REMARK 500 6 ALA A 3 138.81 72.95
REMARK 500 6 TRP A 4 -61.08 176.97
REMARK 500 6 TRP A 8 -82.63 -43.42
REMARK 500 7 ALA A 3 37.17 -92.25
REMARK 500 7 TRP A 8 -83.21 -52.87
REMARK 500 8 ALA A 3 139.51 169.92
REMARK 500 8 TRP A 4 -59.92 171.77
REMARK 500 8 TRP A 8 -84.64 -61.16
REMARK 500 9 LEU A 2 78.17 -115.91
REMARK 500 9 TRP A 8 -84.47 -55.09
REMARK 500 10 ALA A 3 140.88 167.87
REMARK 500 10 TRP A 4 -60.41 171.50
REMARK 500 10 TRP A 8 -83.02 -44.21
REMARK 500 10 ARG A 12 -38.77 -37.45
REMARK 500 11 ALA A 3 128.30 175.86
REMARK 500 11 TRP A 4 -52.87 74.26
REMARK 500 11 TRP A 8 -86.36 -65.12
REMARK 500 12 ALA A 3 126.52 172.23
REMARK 500 12 TRP A 4 -51.78 74.28
REMARK 500 12 TRP A 8 -84.71 -60.19
REMARK 500 13 ALA A 3 141.47 167.76
REMARK 500 13 TRP A 4 -59.78 170.37
REMARK 500 13 TRP A 8 -84.93 -68.10
REMARK 500 14 ALA A 3 124.14 64.08
REMARK 500 14 TRP A 4 -52.52 73.89
REMARK 500 14 TRP A 8 -82.44 -53.89
REMARK 500 15 ALA A 3 140.05 168.89
REMARK 500 15 TRP A 4 -59.34 170.07
REMARK 500 15 TRP A 8 -81.65 -51.98
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 12 0.24 SIDE CHAIN
REMARK 500 1 ARG A 13 0.32 SIDE CHAIN
REMARK 500 2 ARG A 12 0.18 SIDE CHAIN
REMARK 500 2 ARG A 13 0.27 SIDE CHAIN
REMARK 500 3 ARG A 12 0.32 SIDE CHAIN
REMARK 500 3 ARG A 13 0.31 SIDE CHAIN
REMARK 500 4 ARG A 12 0.20 SIDE CHAIN
REMARK 500 4 ARG A 13 0.28 SIDE CHAIN
REMARK 500 5 ARG A 12 0.22 SIDE CHAIN
REMARK 500 5 ARG A 13 0.30 SIDE CHAIN
REMARK 500 6 ARG A 12 0.19 SIDE CHAIN
REMARK 500 6 ARG A 13 0.29 SIDE CHAIN
REMARK 500 7 ARG A 12 0.24 SIDE CHAIN
REMARK 500 7 ARG A 13 0.32 SIDE CHAIN
REMARK 500 8 ARG A 12 0.24 SIDE CHAIN
REMARK 500 8 ARG A 13 0.24 SIDE CHAIN
REMARK 500 9 ARG A 12 0.21 SIDE CHAIN
REMARK 500 9 ARG A 13 0.27 SIDE CHAIN
REMARK 500 10 ARG A 12 0.25 SIDE CHAIN
REMARK 500 10 ARG A 13 0.29 SIDE CHAIN
REMARK 500 11 ARG A 12 0.28 SIDE CHAIN
REMARK 500 11 ARG A 13 0.30 SIDE CHAIN
REMARK 500 12 ARG A 12 0.29 SIDE CHAIN
REMARK 500 12 ARG A 13 0.29 SIDE CHAIN
REMARK 500 13 ARG A 12 0.31 SIDE CHAIN
REMARK 500 13 ARG A 13 0.26 SIDE CHAIN
REMARK 500 14 ARG A 12 0.27 SIDE CHAIN
REMARK 500 14 ARG A 13 0.24 SIDE CHAIN
REMARK 500 15 ARG A 12 0.32 SIDE CHAIN
REMARK 500 15 ARG A 13 0.23 SIDE CHAIN
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 NH2 A 14
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G89 RELATED DB: PDB
REMARK 900 1G89 CONTAINS INDOLICIDIN IN DPC MICELLES
REMARK 900 RELATED ID: 1G8C RELATED DB: PDB
REMARK 900 1G8C CONTAINS INDOLICIDIN IN SDS MICELLES
DBREF 1HR1 A 1 13 UNP P33046 INDC_BOVIN 131 143
SEQADV 1HR1 ALA A 3 UNP P33046 PRO 133 ENGINEERED MUTATION
SEQADV 1HR1 ALA A 7 UNP P33046 PRO 137 ENGINEERED MUTATION
SEQADV 1HR1 ALA A 10 UNP P33046 PRO 140 ENGINEERED MUTATION
SEQRES 1 A 14 ILE LEU ALA TRP LYS TRP ALA TRP TRP ALA TRP ARG ARG
SEQRES 2 A 14 NH2
HET NH2 A 14 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 TRP A 4 ARG A 13 1 10
LINK C ARG A 13 N NH2 A 14 1555 1555 1.31
SITE 1 AC1 2 TRP A 11 ARG 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 - 10 20 Bytes