Header list of 1koz.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 25-DEC-01 1KOZ
TITLE SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VOLTAGE-DEPENDENT CHANNEL INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OMEGA-GRAMMOTOXIN SIA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: CHEMICALLY SYNTHESIZED BY A SOLID-PHASE METHODOLOGY
KEYWDS TOXIN, CYSTINE KNOT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.TAKEUCHI,E.J.PARK,C.W.LEE,J.I.KIM,H.TAKAHASHI,K.J.SWARTZ,I.SHIMADA
REVDAT 4 23-FEB-22 1KOZ 1 REMARK
REVDAT 3 24-FEB-09 1KOZ 1 VERSN
REVDAT 2 01-APR-03 1KOZ 1 JRNL
REVDAT 1 28-AUG-02 1KOZ 0
JRNL AUTH K.TAKEUCHI,E.PARK,C.LEE,J.KIM,H.TAKAHASHI,K.SWARTZ,I.SHIMADA
JRNL TITL SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA, A GATING
JRNL TITL 2 MODIFIER OF P/Q AND N-TYPE CA(2+) CHANNEL.
JRNL REF J.MOL.BIOL. V. 321 517 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12162963
JRNL DOI 10.1016/S0022-2836(02)00595-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 ADDITIONAL COMMENTS ABOUT THE NMR REFINEMENT CAN BE PLACED HERE,
REMARK 3 E.G.
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 561 RESTRAINTS, 536 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 20 DIHEDRAL ANGLE RESTRAINTS,5 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1KOZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015186.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2.4MM GRAMMOTOXIN NA; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; E-COSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3, XWINNMR 1.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
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 CYS A 2 172.69 -49.44
REMARK 500 1 ARG A 4 -168.29 -102.58
REMARK 500 1 TRP A 6 81.04 58.27
REMARK 500 1 LYS A 8 119.19 -36.85
REMARK 500 1 GLN A 11 -39.50 -175.68
REMARK 500 1 ASP A 14 -89.54 -137.96
REMARK 500 1 CYS A 21 61.48 -101.34
REMARK 500 1 TRP A 25 -60.20 -177.25
REMARK 500 1 ASN A 28 38.31 167.50
REMARK 500 2 CYS A 2 166.70 -49.69
REMARK 500 2 ARG A 4 -166.09 -104.18
REMARK 500 2 TRP A 6 85.48 56.57
REMARK 500 2 LYS A 8 121.98 -36.84
REMARK 500 2 SER A 10 -87.89 -127.37
REMARK 500 2 GLN A 11 34.04 -154.18
REMARK 500 2 SER A 13 -84.17 65.92
REMARK 500 2 ASP A 14 -91.05 58.56
REMARK 500 2 CYS A 15 -176.90 -66.67
REMARK 500 2 LYS A 22 97.54 -161.69
REMARK 500 2 LYS A 24 28.56 -146.21
REMARK 500 2 TRP A 25 -57.50 174.74
REMARK 500 2 ARG A 27 105.32 61.19
REMARK 500 2 ASN A 28 76.08 69.89
REMARK 500 3 PHE A 5 129.31 -39.25
REMARK 500 3 TRP A 6 77.56 60.39
REMARK 500 3 LYS A 8 122.37 -37.65
REMARK 500 3 SER A 10 33.20 -161.88
REMARK 500 3 THR A 12 87.96 55.10
REMARK 500 3 SER A 13 91.33 54.55
REMARK 500 3 LYS A 22 108.24 179.11
REMARK 500 3 TRP A 25 -59.84 -174.53
REMARK 500 3 ARG A 27 49.35 26.21
REMARK 500 3 ASN A 28 30.47 179.64
REMARK 500 4 ARG A 4 -167.89 -107.90
REMARK 500 4 TRP A 6 84.05 55.74
REMARK 500 4 LYS A 8 120.28 -37.40
REMARK 500 4 SER A 10 113.67 -160.51
REMARK 500 4 GLN A 11 166.65 66.81
REMARK 500 4 THR A 12 -149.08 46.77
REMARK 500 4 LYS A 22 121.93 179.80
REMARK 500 4 TRP A 25 -54.96 172.66
REMARK 500 4 ARG A 27 93.89 66.02
REMARK 500 4 ASN A 28 91.31 57.59
REMARK 500 5 ARG A 4 -168.49 -110.54
REMARK 500 5 LYS A 8 121.55 -37.78
REMARK 500 5 THR A 12 -179.99 62.97
REMARK 500 5 ASP A 14 11.09 -146.17
REMARK 500 5 LYS A 22 121.76 179.31
REMARK 500 5 TRP A 25 -58.23 176.71
REMARK 500 5 ARG A 27 112.57 62.79
REMARK 500
REMARK 500 THIS ENTRY HAS 206 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 0.15 SIDE CHAIN
REMARK 500 2 ARG A 4 0.25 SIDE CHAIN
REMARK 500 2 ARG A 27 0.27 SIDE CHAIN
REMARK 500 3 ARG A 4 0.31 SIDE CHAIN
REMARK 500 3 ARG A 27 0.30 SIDE CHAIN
REMARK 500 4 ARG A 4 0.31 SIDE CHAIN
REMARK 500 4 ARG A 27 0.30 SIDE CHAIN
REMARK 500 5 ARG A 4 0.24 SIDE CHAIN
REMARK 500 5 ARG A 27 0.30 SIDE CHAIN
REMARK 500 6 ARG A 4 0.28 SIDE CHAIN
REMARK 500 6 ARG A 27 0.27 SIDE CHAIN
REMARK 500 7 ARG A 4 0.16 SIDE CHAIN
REMARK 500 7 ARG A 27 0.31 SIDE CHAIN
REMARK 500 8 ARG A 27 0.31 SIDE CHAIN
REMARK 500 9 ARG A 4 0.26 SIDE CHAIN
REMARK 500 9 ARG A 27 0.20 SIDE CHAIN
REMARK 500 10 ARG A 4 0.26 SIDE CHAIN
REMARK 500 10 ARG A 27 0.09 SIDE CHAIN
REMARK 500 11 ARG A 27 0.31 SIDE CHAIN
REMARK 500 12 ARG A 4 0.21 SIDE CHAIN
REMARK 500 12 ARG A 27 0.32 SIDE CHAIN
REMARK 500 13 ARG A 4 0.16 SIDE CHAIN
REMARK 500 13 ARG A 27 0.22 SIDE CHAIN
REMARK 500 14 ARG A 4 0.31 SIDE CHAIN
REMARK 500 14 ARG A 27 0.23 SIDE CHAIN
REMARK 500 15 ARG A 4 0.24 SIDE CHAIN
REMARK 500 15 ARG A 27 0.22 SIDE CHAIN
REMARK 500 16 ARG A 4 0.27 SIDE CHAIN
REMARK 500 16 ARG A 27 0.21 SIDE CHAIN
REMARK 500 17 ARG A 27 0.21 SIDE CHAIN
REMARK 500 18 ARG A 4 0.27 SIDE CHAIN
REMARK 500 18 ARG A 27 0.16 SIDE CHAIN
REMARK 500 19 ARG A 4 0.32 SIDE CHAIN
REMARK 500 19 ARG A 27 0.24 SIDE CHAIN
REMARK 500 20 ARG A 4 0.31 SIDE CHAIN
REMARK 500 20 ARG A 27 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KOZ A 1 36 UNP P60590 WGRTX_GRASP 1 36
SEQRES 1 A 36 ASP CYS VAL ARG PHE TRP GLY LYS CYS SER GLN THR SER
SEQRES 2 A 36 ASP CYS CYS PRO HIS LEU ALA CYS LYS SER LYS TRP PRO
SEQRES 3 A 36 ARG ASN ILE CYS VAL TRP ASP GLY SER VAL
SHEET 1 A 2 LEU A 19 ALA A 20 0
SHEET 2 A 2 VAL A 31 TRP A 32 -1 O VAL A 31 N ALA A 20
SSBOND 1 CYS A 2 CYS A 16 1555 1555 2.02
SSBOND 2 CYS A 9 CYS A 21 1555 1555 2.02
SSBOND 3 CYS A 15 CYS A 30 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 - 23 20 Bytes