Header list of 2aap.pdb file
Complete list - 9 20 Bytes
HEADER TOXIN 14-JUL-05 2AAP
TITLE SOLUTION STRUCTURE OF JINGZHAOTOXIN-VII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: JINGZHAOTOXIN-VII;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHILOBRACHYS JINGZHAO;
SOURCE 3 ORGANISM_TAXID: 278060
KEYWDS SPIDER TOXIN, ICK MOTIF, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Z.LIAO,S.P.LIANG
REVDAT 3 09-MAR-22 2AAP 1 REMARK
REVDAT 2 24-FEB-09 2AAP 1 VERSN
REVDAT 1 02-AUG-05 2AAP 0
JRNL AUTH Z.LIAO,S.P.LIANG
JRNL TITL SOLUTION STRUCTURE OF JINGZHAOTOXIN-VII
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98.0, X-PLOR NIH2.9.6
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 405 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 6 DIHEDRAL ANGLE RESTRAINTS, 9
REMARK 3 FAKE DISTANCE RESTRAINTS FROM DISULFIDE BONDS AND 22 H-BOND
REMARK 3 RESTRAINTS
REMARK 4
REMARK 4 2AAP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033689.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 6MM JINGZHAOTOXIN-VII; 20MM
REMARK 210 DEUTERIUM ACETIC ACID NA; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR NIH2.9.6
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 MATRIX RELAXATION, TORSION ANGLE
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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: 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 LEU A 5 83.82 56.80
REMARK 500 1 ASP A 10 77.85 59.41
REMARK 500 1 CYS A 16 -157.23 -80.88
REMARK 500 1 CYS A 17 -70.66 -78.93
REMARK 500 2 LEU A 5 91.42 58.50
REMARK 500 2 ASP A 10 96.60 63.11
REMARK 500 2 CYS A 16 -164.83 -124.84
REMARK 500 2 CYS A 17 -86.99 -74.00
REMARK 500 3 LEU A 5 95.63 62.55
REMARK 500 3 CYS A 9 -70.42 -106.12
REMARK 500 3 ASP A 10 73.18 49.19
REMARK 500 3 CYS A 17 -100.36 -83.02
REMARK 500 4 LEU A 5 95.34 59.55
REMARK 500 4 CYS A 9 -66.68 -105.82
REMARK 500 4 CYS A 16 -154.75 -87.44
REMARK 500 4 CYS A 17 -70.76 -89.01
REMARK 500 5 CYS A 2 76.95 -114.22
REMARK 500 5 LEU A 5 89.12 58.10
REMARK 500 5 CYS A 16 -166.81 -109.26
REMARK 500 5 CYS A 17 -74.27 -75.34
REMARK 500 6 LEU A 5 72.55 52.51
REMARK 500 6 ASP A 10 72.06 62.12
REMARK 500 6 THR A 14 -169.79 -72.58
REMARK 500 6 CYS A 17 -77.12 -69.23
REMARK 500 6 SER A 18 -46.67 -164.70
REMARK 500 7 LEU A 5 101.08 66.88
REMARK 500 7 CYS A 9 -71.16 -120.58
REMARK 500 7 ASP A 10 77.63 55.44
REMARK 500 7 CYS A 17 -74.97 -82.15
REMARK 500 8 LEU A 5 93.07 62.21
REMARK 500 8 CYS A 9 -60.10 -100.43
REMARK 500 8 ASP A 10 77.74 46.58
REMARK 500 8 CYS A 16 -162.45 -78.51
REMARK 500 8 CYS A 17 -84.64 -90.65
REMARK 500 9 LEU A 5 93.29 62.91
REMARK 500 9 CYS A 17 -87.49 -75.26
REMARK 500 10 LEU A 5 93.29 60.87
REMARK 500 10 CYS A 16 -161.11 -118.82
REMARK 500 10 CYS A 17 -82.28 -71.94
REMARK 500 10 ALA A 32 69.15 -101.05
REMARK 500 11 LEU A 5 97.05 64.46
REMARK 500 11 ASP A 10 87.06 54.87
REMARK 500 11 CYS A 16 -149.51 56.37
REMARK 500 11 CYS A 17 -65.75 -93.04
REMARK 500 11 SER A 18 117.88 -162.24
REMARK 500 12 LEU A 5 87.20 58.28
REMARK 500 12 ASP A 10 99.03 65.00
REMARK 500 12 CYS A 16 -160.51 -129.89
REMARK 500 12 SER A 18 -46.61 -171.40
REMARK 500 12 LYS A 27 -2.08 73.26
REMARK 500
REMARK 500 THIS ENTRY HAS 82 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 33 0.28 SIDE CHAIN
REMARK 500 2 ARG A 33 0.28 SIDE CHAIN
REMARK 500 3 ARG A 33 0.30 SIDE CHAIN
REMARK 500 4 ARG A 33 0.31 SIDE CHAIN
REMARK 500 5 ARG A 33 0.32 SIDE CHAIN
REMARK 500 6 ARG A 33 0.31 SIDE CHAIN
REMARK 500 7 ARG A 33 0.29 SIDE CHAIN
REMARK 500 8 ARG A 33 0.26 SIDE CHAIN
REMARK 500 9 ARG A 33 0.31 SIDE CHAIN
REMARK 500 10 ARG A 33 0.32 SIDE CHAIN
REMARK 500 11 ARG A 33 0.32 SIDE CHAIN
REMARK 500 12 ARG A 33 0.31 SIDE CHAIN
REMARK 500 13 ARG A 33 0.30 SIDE CHAIN
REMARK 500 14 ARG A 33 0.30 SIDE CHAIN
REMARK 500 15 ARG A 33 0.30 SIDE CHAIN
REMARK 500 16 ARG A 33 0.30 SIDE CHAIN
REMARK 500 17 ARG A 33 0.30 SIDE CHAIN
REMARK 500 18 ARG A 33 0.30 SIDE CHAIN
REMARK 500 19 ARG A 33 0.25 SIDE CHAIN
REMARK 500 20 ARG A 33 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZJQ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN CALCULATED WITHOUT H-BOND CONSTRAINTS
DBREF 2AAP A 1 34 PDB 2AAP 2AAP 1 34
SEQRES 1 A 34 GLY CYS GLY GLY LEU MET ALA GLY CYS ASP GLY LYS SER
SEQRES 2 A 34 THR PHE CYS CYS SER GLY TYR ASN CYS SER PRO THR TRP
SEQRES 3 A 34 LYS TRP CYS VAL TYR ALA ARG PRO
SHEET 1 A 3 ALA A 7 GLY A 8 0
SHEET 2 A 3 TRP A 28 TYR A 31 -1 O CYS A 29 N ALA A 7
SHEET 3 A 3 TYR A 20 SER A 23 -1 N ASN A 21 O VAL A 30
SSBOND 1 CYS A 2 CYS A 17 1555 1555 2.02
SSBOND 2 CYS A 9 CYS A 22 1555 1555 2.02
SSBOND 3 CYS A 16 CYS A 29 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 - 9 20 Bytes