Header list of 1kcp.pdb file
Complete list - 29 20 Bytes
HEADER NEUROTOXIN 27-JAN-98 1KCP
TITLE 3D STRUCTURE OF K-CONOTOXIN PVIIA, A NOVEL POTASSIUM CHANNEL-BLOCKING
TITLE 2 TOXIN FROM CONE SNAILS, NMR, 22 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KAPPA-CONOTOXIN PVIIA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS PURPURASCENS;
SOURCE 3 ORGANISM_TAXID: 41690
KEYWDS NEUROTOXIN, POTASSIUM CHANNEL INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR P.SAVARIN,M.GUENNEUGUES,B.GILQUIN,H.LAMTHANH,S.GASPARINI,S.ZINN-
AUTHOR 2 JUSTIN,A.MENEZ
REVDAT 3 29-NOV-17 1KCP 1 HELIX
REVDAT 2 24-FEB-09 1KCP 1 VERSN
REVDAT 1 14-OCT-98 1KCP 0
JRNL AUTH P.SAVARIN,M.GUENNEUGUES,B.GILQUIN,H.LAMTHANH,S.GASPARINI,
JRNL AUTH 2 S.ZINN-JUSTIN,A.MENEZ
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF KAPPA-CONOTOXIN PVIIA, A
JRNL TITL 2 NOVEL POTASSIUM CHANNEL-BLOCKING TOXIN FROM CONE SNAILS.
JRNL REF BIOCHEMISTRY V. 37 5407 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9548922
JRNL DOI 10.1021/BI9730341
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.TERLAU,K.J.SHON,M.GRILLEY,M.STOCKER,W.STUHMB,B.M.OLIVERA
REMARK 1 TITL STRATEGY FOR RAPID IMMOBILIZATION OF PREY BY A FISH-HUNTING
REMARK 1 TITL 2 MARINE SNAIL
REMARK 1 REF NATURE V. 381 148 1996
REMARK 1 REFN ISSN 0028-0836
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: NULL
REMARK 4
REMARK 4 1KCP 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_1000174405.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BRUKER UXNMR UXNMR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NOE DATA CAME FROM SPECTRA COLLECTED AT 15 DEGREES, PH
REMARK 210 5.0. A TOTAL OF 434 NOE RESTRAINTS WERE COMBINED WITH 20
REMARK 210 DIHEDRAL ANGLE CONSTRAINTS FOR THE FINAL STRUCTURE REFINEMENT.
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HG SER A 17 O VAL A 27 1.60
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 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 2 PHE A 9 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 2 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 3 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 3 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 4 ARG A 2 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 4 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 ARG A 2 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 6 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 6 PHE A 23 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 7 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 7 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 7 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 8 ARG A 2 NH1 - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 8 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 8 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 ARG A 2 NH1 - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 9 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 9 PHE A 9 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 9 PHE A 9 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 10 ARG A 2 NH1 - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 10 ARG A 2 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 PHE A 23 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 10 PHE A 23 CB - CG - CD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 11 ARG A 2 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 11 ARG A 18 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 11 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 11 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 12 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 12 CYS A 8 CB - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 13 ARG A 2 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 13 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 14 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 15 ARG A 2 NH1 - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 15 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 15 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 15 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 16 ARG A 2 NE - CZ - NH2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 17 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 17 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 18 ARG A 2 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 18 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 63 ANGLE DEVIATIONS.
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 ASN A 5 -8.48 92.65
REMARK 500 1 ASP A 14 46.96 -80.04
REMARK 500 1 ARG A 18 -42.14 103.79
REMARK 500 1 ASN A 24 15.35 80.87
REMARK 500 2 HYP A 4 42.10 -73.04
REMARK 500 2 ASN A 5 51.55 177.76
REMARK 500 2 HIS A 11 39.93 -96.24
REMARK 500 2 ARG A 18 -58.47 111.88
REMARK 500 3 CYS A 8 -152.91 -124.26
REMARK 500 3 ASP A 13 54.21 -148.53
REMARK 500 3 ASP A 14 47.21 -97.49
REMARK 500 3 ARG A 18 34.18 74.09
REMARK 500 3 ASN A 24 48.36 94.57
REMARK 500 4 CYS A 8 -148.34 -118.86
REMARK 500 4 ASP A 13 8.16 -68.05
REMARK 500 4 ASN A 24 61.37 79.33
REMARK 500 5 ASN A 5 4.04 100.61
REMARK 500 5 ASP A 14 40.68 -84.80
REMARK 500 5 ARG A 18 -45.81 89.87
REMARK 500 5 ARG A 22 -36.40 -31.00
REMARK 500 5 ASN A 24 25.58 98.07
REMARK 500 6 ASP A 14 48.72 -81.08
REMARK 500 6 ASN A 24 14.45 121.04
REMARK 500 7 ASN A 5 4.02 94.11
REMARK 500 7 CYS A 8 -139.98 -124.06
REMARK 500 7 ASP A 14 41.78 -141.11
REMARK 500 7 ARG A 18 -36.56 101.27
REMARK 500 7 ASN A 21 -148.20 -103.80
REMARK 500 7 ASN A 24 38.11 75.76
REMARK 500 8 HYP A 4 37.82 -60.04
REMARK 500 8 ASN A 5 9.75 -157.58
REMARK 500 8 ASP A 14 16.60 -140.76
REMARK 500 8 ARG A 18 -35.41 91.31
REMARK 500 9 ASN A 5 -21.23 102.43
REMARK 500 9 ASP A 14 39.54 -95.44
REMARK 500 9 ASN A 24 32.98 81.02
REMARK 500 10 ASN A 5 13.49 82.23
REMARK 500 10 CYS A 8 -154.24 -125.42
REMARK 500 10 ASP A 13 55.11 -104.71
REMARK 500 10 ARG A 18 36.83 73.73
REMARK 500 10 ASN A 21 -149.67 -100.84
REMARK 500 10 ASN A 24 24.49 81.67
REMARK 500 11 CYS A 8 -144.26 -115.96
REMARK 500 11 ARG A 18 -22.28 136.17
REMARK 500 11 ASN A 24 39.28 81.41
REMARK 500 12 CYS A 8 -144.73 -124.44
REMARK 500 12 ASN A 24 24.84 87.95
REMARK 500 13 ASN A 5 2.87 93.46
REMARK 500 13 CYS A 8 -137.35 -151.20
REMARK 500 13 CYS A 16 54.15 -91.97
REMARK 500
REMARK 500 THIS ENTRY HAS 91 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 2 0.11 SIDE CHAIN
REMARK 500 2 ARG A 2 0.13 SIDE CHAIN
REMARK 500 2 ARG A 22 0.17 SIDE CHAIN
REMARK 500 3 ARG A 2 0.08 SIDE CHAIN
REMARK 500 4 ARG A 2 0.14 SIDE CHAIN
REMARK 500 5 ARG A 18 0.08 SIDE CHAIN
REMARK 500 5 ARG A 22 0.15 SIDE CHAIN
REMARK 500 6 ARG A 18 0.10 SIDE CHAIN
REMARK 500 6 ARG A 22 0.12 SIDE CHAIN
REMARK 500 7 ARG A 18 0.08 SIDE CHAIN
REMARK 500 7 ARG A 22 0.10 SIDE CHAIN
REMARK 500 8 ARG A 2 0.08 SIDE CHAIN
REMARK 500 8 ARG A 18 0.09 SIDE CHAIN
REMARK 500 9 ARG A 22 0.08 SIDE CHAIN
REMARK 500 11 ARG A 22 0.10 SIDE CHAIN
REMARK 500 12 ARG A 22 0.14 SIDE CHAIN
REMARK 500 13 ARG A 22 0.08 SIDE CHAIN
REMARK 500 14 HIS A 11 0.09 SIDE CHAIN
REMARK 500 15 ARG A 18 0.14 SIDE CHAIN
REMARK 500 16 ARG A 2 0.15 SIDE CHAIN
REMARK 500 16 ARG A 22 0.10 SIDE CHAIN
REMARK 500 17 HIS A 11 0.09 SIDE CHAIN
REMARK 500 18 ARG A 22 0.08 SIDE CHAIN
REMARK 500 19 HIS A 11 0.09 SIDE CHAIN
REMARK 500 20 ARG A 18 0.09 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 28
DBREF 1KCP A 1 27 UNP P56633 CXK7A_CONPU 1 27
SEQADV 1KCP HYP A 4 UNP P56633 PRO 4 CONFLICT
SEQRES 1 A 28 CYS ARG ILE HYP ASN GLN LYS CYS PHE GLN HIS LEU ASP
SEQRES 2 A 28 ASP CYS CYS SER ARG LYS CYS ASN ARG PHE ASN LYS CYS
SEQRES 3 A 28 VAL NH2
MODRES 1KCP HYP A 4 PRO 4-HYDROXYPROLINE
HET HYP A 4 15
HET NH2 A 28 3
HETNAM HYP 4-HYDROXYPROLINE
HETNAM NH2 AMINO GROUP
HETSYN HYP HYDROXYPROLINE
FORMUL 1 HYP C5 H9 N O3
FORMUL 1 NH2 H2 N
SSBOND 1 CYS A 1 CYS A 16 1555 1555 2.03
SSBOND 2 CYS A 8 CYS A 20 1555 1555 2.03
SSBOND 3 CYS A 15 CYS A 26 1555 1555 2.04
LINK N HYP A 4 C ILE A 3 1555 1555 1.37
LINK C HYP A 4 N ASN A 5 1555 1555 1.35
LINK N NH2 A 28 C VAL A 27 1555 1555 1.35
SITE 1 AC1 1 VAL A 27
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 - 29 20 Bytes