Header list of 1mr6.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 18-SEP-02 1MR6
TITLE SOLUTION STRUCTURE OF GAMMA-BUNGAROTOXIN:IMPLICATION FOR THE ROLE OF
TITLE 2 THE RESIDUES ADJACENT TO RGD IN INTEGRIN BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROTOXIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GAMMA-BUNGAROTOXIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS;
SOURCE 3 ORGANISM_COMMON: MANY-BANDED KRAIT;
SOURCE 4 ORGANISM_TAXID: 8616
KEYWDS NEUROTOXIN, VENOM, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.-J.CHUANG,J.-H.SHIU,C.-Y.CHEN,Y.-C.CHEN,L.-S.CHANG
REVDAT 4 23-FEB-22 1MR6 1 REMARK
REVDAT 3 24-FEB-09 1MR6 1 VERSN
REVDAT 2 16-NOV-04 1MR6 1 JRNL
REVDAT 1 18-MAY-04 1MR6 0
JRNL AUTH J.-H.SHIU,C.-Y.CHEN,L.-S.CHANG,Y.-C.CHEN,Y.-C.CHEN,Y.-H.LO,
JRNL AUTH 2 Y.-C.LIU,W.-J.CHUANG
JRNL TITL SOLUTION STRUCTURE OF GAMMA-BUNGAROTOXIN: THE FUNCTIONAL
JRNL TITL 2 SIGNIFICANCE OF AMINO ACID RESIDUES FLANKING THE RGD MOTIF
JRNL TITL 3 IN INTEGRIN BINDING
JRNL REF PROTEINS V. 57 839 2004
JRNL REFN ISSN 0887-3585
JRNL PMID 15390258
JRNL DOI 10.1002/PROT.20269
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.85
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 817 RESTRAINTS, 770 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 47
REMARK 3 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1MR6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000017127.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300
REMARK 210 PH : 6; 4
REMARK 210 IONIC STRENGTH : NO SALT ADDED; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM BUNGAROTOXIN; 3MM
REMARK 210 BUNGAROTOXIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 3.0, XWINNMR 2.6
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 : 6
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: 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 10 69.90 179.61
REMARK 500 1 ASN A 13 179.39 -59.27
REMARK 500 1 ASP A 19 172.20 66.22
REMARK 500 1 LYS A 21 -156.08 -78.17
REMARK 500 1 ASN A 22 42.98 179.74
REMARK 500 1 ALA A 31 112.11 178.40
REMARK 500 1 ARG A 33 -68.07 -104.86
REMARK 500 1 PRO A 37 -161.99 -78.03
REMARK 500 1 LYS A 38 -80.10 -97.14
REMARK 500 1 ARG A 42 160.90 -39.75
REMARK 500 1 GLU A 44 171.31 168.17
REMARK 500 1 ALA A 46 -164.77 -161.70
REMARK 500 1 CYS A 49 -177.91 -178.34
REMARK 500 1 LEU A 54 -12.71 82.05
REMARK 500 1 ASP A 64 177.33 -56.10
REMARK 500 1 ASN A 65 107.17 -22.48
REMARK 500 1 CYS A 66 -78.55 -119.19
REMARK 500 1 ASN A 67 99.22 -59.46
REMARK 500 2 THR A 5 48.86 -159.29
REMARK 500 2 CYS A 6 -129.84 -90.49
REMARK 500 2 SER A 7 17.67 -147.46
REMARK 500 2 GLU A 15 -92.83 -160.80
REMARK 500 2 ASP A 19 44.52 -82.91
REMARK 500 2 ASN A 22 5.03 -159.71
REMARK 500 2 ALA A 31 101.44 -57.62
REMARK 500 2 ARG A 33 -63.65 -91.97
REMARK 500 2 ASP A 35 59.22 -145.77
REMARK 500 2 GLU A 40 105.36 -59.18
REMARK 500 2 ALA A 47 -101.98 -69.33
REMARK 500 2 THR A 48 -80.31 -67.58
REMARK 500 2 PRO A 51 -81.82 -76.62
REMARK 500 2 SER A 52 -80.74 -157.17
REMARK 500 2 LYS A 53 -74.34 -162.41
REMARK 500 2 LEU A 56 -147.97 -105.94
REMARK 500 2 PHE A 59 79.99 -160.13
REMARK 500 2 THR A 62 30.80 -93.34
REMARK 500 2 ASP A 64 -170.64 -55.69
REMARK 500 2 ASN A 65 96.93 -37.92
REMARK 500 3 GLN A 2 119.91 -160.15
REMARK 500 3 THR A 5 62.08 -117.93
REMARK 500 3 CYS A 6 -142.40 -72.89
REMARK 500 3 SER A 7 -38.67 -145.77
REMARK 500 3 GLU A 15 117.06 -160.45
REMARK 500 3 ASP A 19 -167.87 53.28
REMARK 500 3 LYS A 21 -159.95 -79.65
REMARK 500 3 ASN A 22 12.55 -174.71
REMARK 500 3 ALA A 31 127.60 178.47
REMARK 500 3 ARG A 33 -36.67 -130.24
REMARK 500 3 ASP A 35 15.69 -150.99
REMARK 500 3 LYS A 38 -156.89 -173.47
REMARK 500
REMARK 500 THIS ENTRY HAS 366 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 27 0.27 SIDE CHAIN
REMARK 500 1 ARG A 33 0.14 SIDE CHAIN
REMARK 500 1 ARG A 39 0.23 SIDE CHAIN
REMARK 500 1 ARG A 42 0.29 SIDE CHAIN
REMARK 500 1 ARG A 43 0.14 SIDE CHAIN
REMARK 500 2 ARG A 27 0.27 SIDE CHAIN
REMARK 500 2 ARG A 33 0.26 SIDE CHAIN
REMARK 500 2 ARG A 39 0.28 SIDE CHAIN
REMARK 500 2 ARG A 42 0.30 SIDE CHAIN
REMARK 500 2 ARG A 43 0.30 SIDE CHAIN
REMARK 500 3 ARG A 27 0.32 SIDE CHAIN
REMARK 500 3 ARG A 33 0.30 SIDE CHAIN
REMARK 500 3 ARG A 39 0.28 SIDE CHAIN
REMARK 500 3 ARG A 42 0.29 SIDE CHAIN
REMARK 500 3 ARG A 43 0.23 SIDE CHAIN
REMARK 500 4 ARG A 27 0.19 SIDE CHAIN
REMARK 500 4 ARG A 33 0.32 SIDE CHAIN
REMARK 500 4 ARG A 39 0.19 SIDE CHAIN
REMARK 500 4 ARG A 42 0.23 SIDE CHAIN
REMARK 500 4 ARG A 43 0.21 SIDE CHAIN
REMARK 500 5 ARG A 27 0.26 SIDE CHAIN
REMARK 500 5 ARG A 33 0.23 SIDE CHAIN
REMARK 500 5 ARG A 39 0.15 SIDE CHAIN
REMARK 500 5 ARG A 42 0.32 SIDE CHAIN
REMARK 500 6 ARG A 27 0.26 SIDE CHAIN
REMARK 500 6 ARG A 33 0.32 SIDE CHAIN
REMARK 500 6 ARG A 39 0.27 SIDE CHAIN
REMARK 500 6 ARG A 42 0.13 SIDE CHAIN
REMARK 500 6 ARG A 43 0.32 SIDE CHAIN
REMARK 500 7 ARG A 27 0.21 SIDE CHAIN
REMARK 500 7 ARG A 39 0.23 SIDE CHAIN
REMARK 500 7 ARG A 42 0.32 SIDE CHAIN
REMARK 500 7 ARG A 43 0.32 SIDE CHAIN
REMARK 500 8 ARG A 27 0.13 SIDE CHAIN
REMARK 500 8 ARG A 33 0.31 SIDE CHAIN
REMARK 500 8 ARG A 39 0.31 SIDE CHAIN
REMARK 500 8 ARG A 42 0.31 SIDE CHAIN
REMARK 500 8 ARG A 43 0.25 SIDE CHAIN
REMARK 500 9 ARG A 27 0.16 SIDE CHAIN
REMARK 500 9 ARG A 33 0.25 SIDE CHAIN
REMARK 500 9 ARG A 39 0.26 SIDE CHAIN
REMARK 500 9 ARG A 42 0.20 SIDE CHAIN
REMARK 500 9 ARG A 43 0.32 SIDE CHAIN
REMARK 500 10 ARG A 27 0.26 SIDE CHAIN
REMARK 500 10 ARG A 33 0.30 SIDE CHAIN
REMARK 500 10 ARG A 39 0.27 SIDE CHAIN
REMARK 500 10 ARG A 42 0.24 SIDE CHAIN
REMARK 500 10 ARG A 43 0.31 SIDE CHAIN
REMARK 500 11 ARG A 33 0.23 SIDE CHAIN
REMARK 500 11 ARG A 39 0.20 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 92 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5322 RELATED DB: BMRB
REMARK 900 BMRB 5322 CONTAINS CHEMICAL SHIFTS FILE
DBREF 1MR6 A 1 68 UNP Q9W796 NXLH5_BUNMU 22 89
SEQRES 1 A 68 MET GLN CYS LYS THR CYS SER PHE TYR THR CYS PRO ASN
SEQRES 2 A 68 SER GLU THR CYS PRO ASP GLY LYS ASN ILE CYS VAL LYS
SEQRES 3 A 68 ARG SER TRP THR ALA VAL ARG GLY ASP GLY PRO LYS ARG
SEQRES 4 A 68 GLU ILE ARG ARG GLU CYS ALA ALA THR CYS PRO PRO SER
SEQRES 5 A 68 LYS LEU GLY LEU THR VAL PHE CYS CYS THR THR ASP ASN
SEQRES 6 A 68 CYS ASN HIS
SHEET 1 A 2 CYS A 24 ARG A 27 0
SHEET 2 A 2 ARG A 42 CYS A 45 -1 O ARG A 42 N ARG A 27
SSBOND 1 CYS A 3 CYS A 24 1555 1555 2.02
SSBOND 2 CYS A 6 CYS A 11 1555 1555 2.02
SSBOND 3 CYS A 17 CYS A 45 1555 1555 2.02
SSBOND 4 CYS A 49 CYS A 60 1555 1555 2.02
SSBOND 5 CYS A 61 CYS A 66 1555 1555 2.02
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 - b 23 2 Bytes