Header list of 1bh1.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 11-JUN-98 1BH1
TITLE STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MELITTIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: APIS MELLIFERA;
SOURCE 3 ORGANISM_COMMON: HONEY BEE;
SOURCE 4 ORGANISM_TAXID: 7460
KEYWDS TOXIN, HEMOLYTIC POLYPEPTIDE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.J.BARNHAM,D.HEWISH,J.WERKMEISTER,C.CURTAIN,A.KIRKPATRICK,N.BARTONE,
AUTHOR 2 S.T.LIU,R.NORTON,D.RIVETT
REVDAT 4 16-FEB-22 1BH1 1 REMARK LINK
REVDAT 3 24-FEB-09 1BH1 1 VERSN
REVDAT 2 16-FEB-99 1BH1 1 SOURCE COMPND REMARK TITLE
REVDAT 2 2 1 SEQRES AUTHOR
REVDAT 1 06-JAN-99 1BH1 0
JRNL AUTH D.R.HEWISH,K.J.BARNHAM,J.A.WERKMEISTER,A.KIRKPATRICK,
JRNL AUTH 2 N.BARTONE,S.T.LIU,R.S.NORTON,C.CURTAIN,D.E.RIVETTA
JRNL TITL STRUCTURE AND ACTIVITY OF D-PRO14 MELITTIN.
JRNL REF J.PROTEIN CHEM. V. 21 243 2002
JRNL REFN ISSN 0277-8033
JRNL PMID 12168695
JRNL DOI 10.1023/A:1019741202601
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1000 STRUCTURES WERE INITIALLY
REMARK 3 GENERATED USING THE DISTANCE GEOMETRY PROGRAM DYANA 1.4. THESE
REMARK 3 STRUCTURES WERE REFINED USING SIMULATED ANNEALING IN X-PLOR3.8
REMARK 3 WITH THE DISTANCE GEOMETRY FORCE FIELD, THEN ENERGY MINIMIZED
REMARK 3 USING THE CHARMM FORCE FIELD WITH A DISTANCE-DEPENDENT
REMARK 3 DILECTRIC. THE 20 BEST STRUCTURES BASED ON THEIR STEREOCHEMICAL
REMARK 3 AND NOE ENERGIES WERE CHOSEN FOR ANALYSIS.
REMARK 4
REMARK 4 1BH1 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_1000171747.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 277
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : 2MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : METHANOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.4, X-PLOR 3.8
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST STEREOCHEMICAL AND NOE
REMARK 210 ENERGIES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D NMR SPECTROSCOPY
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 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 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 2 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 3 ARG A 22 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 3 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 5 ARG A 22 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 5 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 7 ARG A 22 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 7 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 8 ARG A 22 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 8 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 9 ARG A 22 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 9 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 10 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 12 ARG A 22 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 12 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 13 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 14 ARG A 22 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 15 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 17 ARG A 22 NH1 - CZ - NH2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 17 ARG A 22 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 18 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 19 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 20 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 20 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.4 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 THR A 11 -76.65 -121.24
REMARK 500 1 LEU A 13 70.95 179.41
REMARK 500 1 PRO A 14 -86.64 59.31
REMARK 500 1 LEU A 16 -39.68 -38.52
REMARK 500 1 TRP A 19 -63.11 -102.25
REMARK 500 1 GLN A 25 66.70 -100.18
REMARK 500 2 ILE A 2 -119.03 -120.38
REMARK 500 2 LEU A 13 63.40 -156.26
REMARK 500 2 PRO A 14 -100.85 61.26
REMARK 500 2 TRP A 19 -61.44 -101.59
REMARK 500 3 ILE A 2 -154.36 -116.54
REMARK 500 3 VAL A 5 -33.74 -29.86
REMARK 500 3 THR A 11 -61.49 -120.08
REMARK 500 3 LEU A 13 32.88 -150.32
REMARK 500 3 PRO A 14 175.54 94.77
REMARK 500 3 ALA A 15 -25.30 -26.74
REMARK 500 3 TRP A 19 -78.40 -101.36
REMARK 500 4 THR A 11 -61.88 -122.95
REMARK 500 4 LEU A 13 61.01 -150.55
REMARK 500 4 PRO A 14 -99.04 62.88
REMARK 500 4 TRP A 19 -61.10 -101.53
REMARK 500 4 ARG A 24 1.60 -52.97
REMARK 500 5 LEU A 13 66.23 -163.15
REMARK 500 5 PRO A 14 -85.75 58.16
REMARK 500 5 TRP A 19 -70.98 -102.05
REMARK 500 6 THR A 11 -63.09 -121.65
REMARK 500 6 LEU A 13 65.33 179.52
REMARK 500 6 PRO A 14 -93.04 60.19
REMARK 500 6 TRP A 19 -67.28 -102.30
REMARK 500 6 ARG A 24 -9.94 -47.88
REMARK 500 7 THR A 11 -78.97 -120.84
REMARK 500 7 LEU A 13 79.86 179.15
REMARK 500 7 PRO A 14 -99.66 64.07
REMARK 500 7 TRP A 19 -69.62 -101.37
REMARK 500 7 ARG A 22 -60.38 -90.02
REMARK 500 8 THR A 11 -64.64 -106.84
REMARK 500 8 LEU A 13 67.27 -152.64
REMARK 500 8 PRO A 14 -81.31 56.84
REMARK 500 8 TRP A 19 -69.88 -101.89
REMARK 500 9 PRO A 14 -83.65 61.56
REMARK 500 9 TRP A 19 -64.30 -102.77
REMARK 500 10 VAL A 5 -30.80 -28.28
REMARK 500 10 LEU A 13 57.78 -169.72
REMARK 500 10 PRO A 14 -102.90 59.08
REMARK 500 10 TRP A 19 -74.82 -100.75
REMARK 500 10 ARG A 22 -62.23 -90.67
REMARK 500 10 ARG A 24 -18.82 -47.17
REMARK 500 11 LEU A 13 68.19 -152.13
REMARK 500 11 PRO A 14 -83.19 54.15
REMARK 500 11 TRP A 19 -67.57 -101.58
REMARK 500
REMARK 500 THIS ENTRY HAS 87 RAMACHANDRAN OUTLIERS.
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 22 0.30 SIDE CHAIN
REMARK 500 1 ARG A 24 0.30 SIDE CHAIN
REMARK 500 2 ARG A 22 0.31 SIDE CHAIN
REMARK 500 2 ARG A 24 0.27 SIDE CHAIN
REMARK 500 3 ARG A 22 0.20 SIDE CHAIN
REMARK 500 3 ARG A 24 0.28 SIDE CHAIN
REMARK 500 4 ARG A 22 0.31 SIDE CHAIN
REMARK 500 4 ARG A 24 0.32 SIDE CHAIN
REMARK 500 5 ARG A 22 0.30 SIDE CHAIN
REMARK 500 5 ARG A 24 0.31 SIDE CHAIN
REMARK 500 6 ARG A 22 0.30 SIDE CHAIN
REMARK 500 6 ARG A 24 0.31 SIDE CHAIN
REMARK 500 7 ARG A 22 0.30 SIDE CHAIN
REMARK 500 7 ARG A 24 0.32 SIDE CHAIN
REMARK 500 8 ARG A 22 0.27 SIDE CHAIN
REMARK 500 8 ARG A 24 0.30 SIDE CHAIN
REMARK 500 9 ARG A 22 0.30 SIDE CHAIN
REMARK 500 9 ARG A 24 0.32 SIDE CHAIN
REMARK 500 10 ARG A 22 0.29 SIDE CHAIN
REMARK 500 10 ARG A 24 0.30 SIDE CHAIN
REMARK 500 11 ARG A 22 0.32 SIDE CHAIN
REMARK 500 11 ARG A 24 0.28 SIDE CHAIN
REMARK 500 12 ARG A 22 0.30 SIDE CHAIN
REMARK 500 12 ARG A 24 0.31 SIDE CHAIN
REMARK 500 13 ARG A 22 0.27 SIDE CHAIN
REMARK 500 13 ARG A 24 0.31 SIDE CHAIN
REMARK 500 14 ARG A 22 0.32 SIDE CHAIN
REMARK 500 14 ARG A 24 0.30 SIDE CHAIN
REMARK 500 15 ARG A 22 0.09 SIDE CHAIN
REMARK 500 15 ARG A 24 0.32 SIDE CHAIN
REMARK 500 16 ARG A 22 0.28 SIDE CHAIN
REMARK 500 16 ARG A 24 0.28 SIDE CHAIN
REMARK 500 17 ARG A 22 0.32 SIDE CHAIN
REMARK 500 17 ARG A 24 0.31 SIDE CHAIN
REMARK 500 18 ARG A 22 0.31 SIDE CHAIN
REMARK 500 18 ARG A 24 0.30 SIDE CHAIN
REMARK 500 19 ARG A 22 0.32 SIDE CHAIN
REMARK 500 19 ARG A 24 0.31 SIDE CHAIN
REMARK 500 20 ARG A 22 0.13 SIDE CHAIN
REMARK 500 20 ARG A 24 0.31 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 27
DBREF 1BH1 A 1 26 UNP P01501 MEL_APIME 44 69
SEQRES 1 A 27 GLY ILE GLY ALA VAL LEU LYS VAL LEU THR THR GLY LEU
SEQRES 2 A 27 PRO ALA LEU ILE SER TRP ILE LYS ARG LYS ARG GLN GLN
SEQRES 3 A 27 NH2
HET NH2 A 27 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 VAL A 5 VAL A 8 1 4
HELIX 2 2 LEU A 16 TRP A 19 1 4
HELIX 3 3 LYS A 21 ARG A 24 1 4
LINK C GLN A 26 N NH2 A 27 1555 1555 1.30
SITE 1 AC1 1 GLN A 26
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 - 16 20 Bytes