Header list of 1bk8.pdb file
Complete list - v 29 2 Bytes
HEADER PLANT DEFENSIN 15-JUL-98 1BK8
TITLE DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF AESCULUS
TITLE 2 HIPPOCASTANUM ANTIMICROBIAL PROTEIN 1 (AH-AMP1) BY 1H NMR, 25
TITLE 3 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIMICROBIAL PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AH-AMP1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AESCULUS HIPPOCASTANUM;
SOURCE 3 ORGANISM_COMMON: COMMON HORSE CHESTNUT;
SOURCE 4 ORGANISM_TAXID: 43364;
SOURCE 5 ORGAN: SEED
KEYWDS PLANT DEFENSIN, ANTIMICROBIAL, CYSTEINE-STABILIZED ALFA/ BETA MOTIF
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR F.FANT,F.A.M.BORREMANS
REVDAT 4 29-NOV-17 1BK8 1 REMARK HELIX
REVDAT 3 24-FEB-09 1BK8 1 VERSN
REVDAT 2 01-APR-03 1BK8 1 JRNL
REVDAT 1 05-JAN-00 1BK8 0
JRNL AUTH F.FANT,W.F.VRANKEN,F.A.BORREMANS
JRNL TITL THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF AESCULUS
JRNL TITL 2 HIPPOCASTANUM ANTIMICROBIAL PROTEIN 1 DETERMINED BY 1H
JRNL TITL 3 NUCLEAR MAGNETIC RESONANCE.
JRNL REF PROTEINS V. 37 388 1999
JRNL REFN ISSN 0887-3585
JRNL PMID 10591099
JRNL DOI 10.1002/(SICI)1097-0134(19991115)37:3<388::AID-PROT7>3.3.CO;
JRNL DOI 2 2-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : BIOSYM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING PROTOCOL ADOPTED
REMARK 3 FROM NILGES ET AL. 1988, FEBS LETTERS, VOL. 239, PP129-136.
REMARK 4
REMARK 4 1BK8 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_1000171852.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 292.5
REMARK 210 PH : 4.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQFCOSY; E.COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AM500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA/REDAC, DISCOVER
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: 2D HOMONUCLEAR 1H NMR WAS USED TO EXTRACT DISTANCE AND
REMARK 210 TORSIONAL CONSTRAINTS. RMSD BACKBONE ATOMS 0.81 +/- 0.12. RMSD
REMARK 210 ALL ATOMS 1.25 +/- 0.13. THE AMBER FORCEFIELD WAS USED FOR THE
REMARK 210 SIMULATED ANNEALING.
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 4 CD GLU A 4 OE1 0.111
REMARK 500 1 GLU A 28 CD GLU A 28 OE2 0.110
REMARK 500 1 GLU A 39 CD GLU A 39 OE1 0.109
REMARK 500 2 GLU A 4 CD GLU A 4 OE1 0.107
REMARK 500 2 GLU A 28 CD GLU A 28 OE1 0.111
REMARK 500 2 GLU A 39 CD GLU A 39 OE1 0.107
REMARK 500 3 GLU A 4 CD GLU A 4 OE1 0.107
REMARK 500 3 GLU A 28 CD GLU A 28 OE2 0.111
REMARK 500 3 GLU A 39 CD GLU A 39 OE2 0.106
REMARK 500 4 GLU A 4 CD GLU A 4 OE1 0.108
REMARK 500 4 GLU A 28 CD GLU A 28 OE1 0.108
REMARK 500 4 GLU A 39 CD GLU A 39 OE1 0.107
REMARK 500 5 GLU A 4 CD GLU A 4 OE1 0.107
REMARK 500 5 GLU A 28 CD GLU A 28 OE1 0.108
REMARK 500 5 GLU A 39 CD GLU A 39 OE2 0.107
REMARK 500 6 GLU A 4 CD GLU A 4 OE1 0.109
REMARK 500 6 GLU A 28 CD GLU A 28 OE1 0.107
REMARK 500 6 GLU A 39 CD GLU A 39 OE2 0.107
REMARK 500 7 GLU A 4 CD GLU A 4 OE1 0.108
REMARK 500 7 GLU A 28 CD GLU A 28 OE2 0.107
REMARK 500 7 GLU A 39 CD GLU A 39 OE1 0.108
REMARK 500 8 GLU A 4 CD GLU A 4 OE1 0.112
REMARK 500 8 GLU A 28 CD GLU A 28 OE2 0.106
REMARK 500 8 GLU A 39 CD GLU A 39 OE2 0.106
REMARK 500 9 GLU A 4 CD GLU A 4 OE1 0.110
REMARK 500 9 GLU A 28 CD GLU A 28 OE2 0.110
REMARK 500 9 GLU A 39 CD GLU A 39 OE1 0.107
REMARK 500 10 GLU A 4 CD GLU A 4 OE1 0.107
REMARK 500 10 GLU A 28 CD GLU A 28 OE1 0.107
REMARK 500 10 GLU A 39 CD GLU A 39 OE1 0.107
REMARK 500 11 GLU A 4 CD GLU A 4 OE1 0.108
REMARK 500 11 GLU A 28 CD GLU A 28 OE2 0.106
REMARK 500 11 GLU A 39 CD GLU A 39 OE1 0.108
REMARK 500 12 GLU A 4 CD GLU A 4 OE1 0.111
REMARK 500 12 GLU A 28 CD GLU A 28 OE2 0.110
REMARK 500 12 GLU A 39 CD GLU A 39 OE1 0.107
REMARK 500 13 GLU A 4 CD GLU A 4 OE1 0.107
REMARK 500 13 GLU A 28 CD GLU A 28 OE2 0.107
REMARK 500 13 GLU A 39 CD GLU A 39 OE1 0.108
REMARK 500 14 GLU A 4 CD GLU A 4 OE1 0.106
REMARK 500 14 GLU A 28 CD GLU A 28 OE1 0.107
REMARK 500 14 GLU A 39 CD GLU A 39 OE1 0.107
REMARK 500 15 GLU A 4 CD GLU A 4 OE1 0.107
REMARK 500 15 GLU A 28 CD GLU A 28 OE2 0.108
REMARK 500 15 GLU A 39 CD GLU A 39 OE2 0.106
REMARK 500 16 GLU A 4 CD GLU A 4 OE1 0.108
REMARK 500 16 GLU A 28 CD GLU A 28 OE1 0.110
REMARK 500 16 GLU A 39 CD GLU A 39 OE1 0.108
REMARK 500 17 GLU A 4 CD GLU A 4 OE1 0.106
REMARK 500 17 GLU A 28 CD GLU A 28 OE2 0.107
REMARK 500
REMARK 500 THIS ENTRY HAS 75 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 1 CYS A 35 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 4 CYS A 35 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 5 CYS A 2 CA - CB - SG ANGL. DEV. = 10.2 DEGREES
REMARK 500 10 CYS A 35 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 14 CYS A 35 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 17 CYS A 2 CA - CB - SG ANGL. DEV. = 9.8 DEGREES
REMARK 500 20 CYS A 35 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 22 CYS A 35 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
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 7 105.50 -54.99
REMARK 500 1 SER A 11 -131.96 -90.86
REMARK 500 1 GLN A 23 47.48 -79.02
REMARK 500 1 CYS A 24 -48.46 -166.26
REMARK 500 1 GLU A 28 -142.09 -73.88
REMARK 500 1 LYS A 29 51.68 -160.46
REMARK 500 1 HIS A 32 -164.26 -161.34
REMARK 500 1 ASN A 49 45.94 32.25
REMARK 500 2 CYS A 2 86.53 -61.86
REMARK 500 2 PRO A 6 174.87 -54.86
REMARK 500 2 GLN A 8 -64.18 -94.25
REMARK 500 2 GLN A 23 33.28 -78.50
REMARK 500 2 CYS A 24 -50.54 -132.59
REMARK 500 2 TRP A 27 -79.82 -75.17
REMARK 500 2 LYS A 29 57.81 131.71
REMARK 500 2 PHE A 48 -75.97 -84.62
REMARK 500 2 ASN A 49 33.93 -84.75
REMARK 500 3 CYS A 2 97.94 -49.74
REMARK 500 3 SER A 7 105.49 -54.48
REMARK 500 3 TRP A 10 76.56 -65.65
REMARK 500 3 GLU A 28 -148.51 -78.36
REMARK 500 3 LYS A 29 52.83 -161.50
REMARK 500 3 ASN A 40 -15.33 69.23
REMARK 500 3 ASN A 49 19.41 59.50
REMARK 500 4 GLN A 23 34.75 -75.31
REMARK 500 4 CYS A 24 -49.32 -144.42
REMARK 500 4 GLU A 28 -135.87 -81.13
REMARK 500 4 LYS A 29 59.56 -161.93
REMARK 500 4 ASN A 49 42.98 31.51
REMARK 500 5 SER A 7 111.29 -35.16
REMARK 500 5 GLN A 8 -93.89 -92.46
REMARK 500 5 GLU A 28 -155.66 -73.95
REMARK 500 5 LYS A 29 55.92 -161.28
REMARK 500 6 CYS A 2 81.32 -62.14
REMARK 500 6 GLU A 4 71.24 40.79
REMARK 500 6 SER A 7 108.37 -51.59
REMARK 500 6 GLN A 8 -61.83 -102.14
REMARK 500 6 GLU A 28 -148.97 -80.07
REMARK 500 6 LYS A 29 50.50 -161.55
REMARK 500 6 ALA A 34 136.62 -170.28
REMARK 500 6 ASN A 40 -13.59 69.90
REMARK 500 7 CYS A 2 95.95 -56.94
REMARK 500 7 SER A 7 104.27 -53.97
REMARK 500 7 SER A 11 55.85 38.96
REMARK 500 7 GLN A 23 34.26 -75.69
REMARK 500 7 CYS A 24 -48.89 -146.59
REMARK 500 7 GLU A 28 -143.38 -75.01
REMARK 500 7 LYS A 29 56.99 -161.85
REMARK 500 7 ASN A 49 19.63 53.78
REMARK 500 8 CYS A 2 81.13 -64.17
REMARK 500
REMARK 500 THIS ENTRY HAS 173 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TRP A 27 GLU A 28 2 -147.03
REMARK 500 CYS A 2 ASN A 3 6 -149.09
REMARK 500 TRP A 27 GLU A 28 12 -144.73
REMARK 500 ASN A 3 GLU A 4 15 124.91
REMARK 500 TRP A 27 GLU A 28 15 -148.48
REMARK 500 GLU A 28 LYS A 29 18 149.47
REMARK 500 ASN A 3 GLU A 4 21 140.38
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 4 TYR A 47 0.10 SIDE CHAIN
REMARK 500 5 TYR A 47 0.08 SIDE CHAIN
REMARK 500 7 TYR A 47 0.09 SIDE CHAIN
REMARK 500 12 TYR A 47 0.12 SIDE CHAIN
REMARK 500 15 TYR A 47 0.08 SIDE CHAIN
REMARK 500 19 PHE A 48 0.09 SIDE CHAIN
REMARK 500 20 TYR A 47 0.08 SIDE CHAIN
REMARK 500 22 TYR A 47 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: 1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: SITE IMPORTANT FOR ANTIFUNGAL ACTIVITY. SEE
REMARK 800 REMARK 6.
DBREF 1BK8 A 1 50 UNP Q7M1F3 Q7M1F3_AESHI 1 50
SEQRES 1 A 50 LEU CYS ASN GLU ARG PRO SER GLN THR TRP SER GLY ASN
SEQRES 2 A 50 CYS GLY ASN THR ALA HIS CYS ASP LYS GLN CYS GLN ASP
SEQRES 3 A 50 TRP GLU LYS ALA SER HIS GLY ALA CYS HIS LYS ARG GLU
SEQRES 4 A 50 ASN HIS TRP LYS CYS PHE CYS TYR PHE ASN CYS
HELIX 1 H1 THR A 17 TRP A 27 1 11
SHEET 1 S1 3 CYS A 2 SER A 7 0
SHEET 2 S1 3 TRP A 42 PHE A 48 -1 O PHE A 48 N ASN A 3
SHEET 3 S1 3 HIS A 32 LYS A 37 -1 N HIS A 32 O TYR A 47
SSBOND 1 CYS A 2 CYS A 50 1555 1555 2.08
SSBOND 2 CYS A 14 CYS A 35 1555 1555 2.08
SSBOND 3 CYS A 20 CYS A 44 1555 1555 2.06
SSBOND 4 CYS A 24 CYS A 46 1555 1555 2.08
SITE 1 1 10 THR A 9 TRP A 27 LYS A 37 GLU A 39
SITE 2 1 10 LYS A 43 SER A 11 HIS A 41 PHE A 48
SITE 3 1 10 GLN A 8 ARG A 38
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 29 2 Bytes