Header list of 1b4i.pdb file
Complete list - 23 20 Bytes
HEADER PROTON TRANSPORT 22-DEC-98 1B4I
TITLE CONTROL OF K+ CHANNEL GATING BY PROTEIN PHOSPHORYLATION: STRUCTURAL
TITLE 2 SWITCHES OF THE INACTIVATION GATE, NMR, 22 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM CHANNEL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: INACTIVATION GATE;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: SER 15 AND SER 21 ARE PHOSPHORLYATED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606
KEYWDS POTASSIUM CHANNEL, INACTIVATION GATE, PHOSPHORYLATION, PROTON
KEYWDS 2 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR C.ANTZ,T.BAUER,H.KALBACHER,R.FRANK,M.COVARRUBIAS,H.R.KALBITZER,
AUTHOR 2 J.P.RUPPERSBERG,T.BAUKROWITZ,B.FAKLER
REVDAT 4 23-MAR-22 1B4I 1 REMARK LINK
REVDAT 3 19-MAY-10 1B4I 1 SOURCE
REVDAT 2 24-FEB-09 1B4I 1 VERSN
REVDAT 1 27-APR-99 1B4I 0
JRNL AUTH C.ANTZ,T.BAUER,H.KALBACHER,R.FRANK,M.COVARRUBIAS,
JRNL AUTH 2 H.R.KALBITZER,J.P.RUPPERSBERG,T.BAUKROWITZ,B.FAKLER
JRNL TITL CONTROL OF K+ CHANNEL GATING BY PROTEIN PHOSPHORYLATION:
JRNL TITL 2 STRUCTURAL SWITCHES OF THE INACTIVATION GATE.
JRNL REF NAT.STRUCT.BIOL. V. 6 146 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10048926
JRNL DOI 10.1038/5833
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: NULL
REMARK 4
REMARK 4 1B4I 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_1000171473.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 3.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 OG SER A 9 HH21 ARG A 13 1.51
REMARK 500 O PRO A 19 HZ3 LYS A 22 1.55
REMARK 500 OG SER A 4 HG SER A 9 1.59
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 PRO A 20 C - N - CD ANGL. DEV. = -15.6 DEGREES
REMARK 500 3 PRO A 20 C - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 4 PRO A 20 C - N - CD ANGL. DEV. = -22.6 DEGREES
REMARK 500 6 PRO A 20 C - N - CD ANGL. DEV. = -21.5 DEGREES
REMARK 500 7 PRO A 20 C - N - CD ANGL. DEV. = -15.3 DEGREES
REMARK 500 8 PRO A 20 C - N - CD ANGL. DEV. = -19.7 DEGREES
REMARK 500 9 PRO A 20 C - N - CD ANGL. DEV. = -21.7 DEGREES
REMARK 500 10 PRO A 20 C - N - CD ANGL. DEV. = -23.6 DEGREES
REMARK 500 11 PRO A 20 C - N - CD ANGL. DEV. = -19.2 DEGREES
REMARK 500 12 PRO A 20 C - N - CD ANGL. DEV. = -20.1 DEGREES
REMARK 500 13 PRO A 20 C - N - CD ANGL. DEV. = -18.4 DEGREES
REMARK 500 14 PRO A 20 C - N - CD ANGL. DEV. = -18.6 DEGREES
REMARK 500 15 PRO A 20 C - N - CD ANGL. DEV. = -16.9 DEGREES
REMARK 500 16 PRO A 20 C - N - CD ANGL. DEV. = -18.2 DEGREES
REMARK 500 17 PRO A 20 C - N - CD ANGL. DEV. = -16.5 DEGREES
REMARK 500 18 PRO A 20 C - N - CD ANGL. DEV. = -18.5 DEGREES
REMARK 500 19 PRO A 20 C - N - CD ANGL. DEV. = -16.0 DEGREES
REMARK 500 20 PRO A 20 C - N - CD ANGL. DEV. = -17.8 DEGREES
REMARK 500 21 PRO A 20 C - N - CD ANGL. DEV. = -16.1 DEGREES
REMARK 500 22 PRO A 20 C - N - CD ANGL. DEV. = -19.2 DEGREES
REMARK 500 23 PRO A 20 C - N - CD ANGL. DEV. = -15.0 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 VAL A 5 -150.74 -96.46
REMARK 500 1 ARG A 13 38.20 -80.82
REMARK 500 1 SEP A 15 -17.77 111.88
REMARK 500 1 CYS A 24 -76.79 -58.97
REMARK 500 1 LYS A 26 32.92 36.68
REMARK 500 1 GLU A 27 54.63 -151.61
REMARK 500 1 GLU A 28 61.91 35.03
REMARK 500 2 SER A 4 -140.81 -145.14
REMARK 500 2 CYS A 6 -56.14 69.54
REMARK 500 2 SER A 9 -48.87 -160.87
REMARK 500 2 SEP A 15 -59.63 -158.63
REMARK 500 2 THR A 23 -8.17 -140.31
REMARK 500 3 SER A 3 -142.02 -164.12
REMARK 500 3 VAL A 5 101.84 31.81
REMARK 500 3 CYS A 6 -155.12 -86.01
REMARK 500 3 SER A 9 -60.07 -161.82
REMARK 500 3 TYR A 10 -178.08 -64.50
REMARK 500 3 SEP A 15 -78.55 -115.77
REMARK 500 3 GLU A 27 -33.33 -151.52
REMARK 500 3 GLU A 28 -66.94 -94.75
REMARK 500 4 SER A 3 -51.04 -140.39
REMARK 500 4 SER A 4 -149.91 -134.44
REMARK 500 4 VAL A 5 -148.28 -80.59
REMARK 500 4 SER A 9 -46.68 -162.21
REMARK 500 4 TYR A 10 177.65 -55.81
REMARK 500 4 SEP A 15 -49.19 -169.09
REMARK 500 4 SEP A 21 80.33 56.36
REMARK 500 4 LEU A 25 -85.79 -88.12
REMARK 500 4 LYS A 26 27.56 36.46
REMARK 500 4 GLU A 27 -64.15 -149.14
REMARK 500 4 MET A 29 140.69 69.50
REMARK 500 5 SER A 4 35.23 -155.23
REMARK 500 5 SER A 9 -49.73 -161.87
REMARK 500 5 TYR A 10 175.77 -56.37
REMARK 500 5 SEP A 15 -27.55 106.43
REMARK 500 5 LYS A 26 -74.35 -25.42
REMARK 500 5 GLU A 28 -48.58 -130.24
REMARK 500 5 MET A 29 153.93 66.42
REMARK 500 6 VAL A 5 84.35 33.55
REMARK 500 6 TYR A 10 -164.29 -70.23
REMARK 500 6 SEP A 21 71.84 53.61
REMARK 500 6 LYS A 26 -88.11 30.94
REMARK 500 7 VAL A 7 -89.71 -82.87
REMARK 500 7 SER A 8 29.69 47.90
REMARK 500 7 SEP A 15 -86.95 -108.79
REMARK 500 7 LEU A 25 -91.22 -82.15
REMARK 500 7 LYS A 26 -160.12 -166.12
REMARK 500 8 SER A 3 -153.57 57.07
REMARK 500 8 SER A 4 -124.40 -108.24
REMARK 500 8 CYS A 6 -69.63 -134.00
REMARK 500
REMARK 500 THIS ENTRY HAS 148 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 11 0.31 SIDE CHAIN
REMARK 500 1 ARG A 13 0.30 SIDE CHAIN
REMARK 500 2 ARG A 11 0.32 SIDE CHAIN
REMARK 500 2 ARG A 13 0.29 SIDE CHAIN
REMARK 500 3 ARG A 11 0.32 SIDE CHAIN
REMARK 500 3 ARG A 13 0.31 SIDE CHAIN
REMARK 500 4 ARG A 11 0.30 SIDE CHAIN
REMARK 500 4 ARG A 13 0.32 SIDE CHAIN
REMARK 500 5 ARG A 11 0.31 SIDE CHAIN
REMARK 500 5 ARG A 13 0.30 SIDE CHAIN
REMARK 500 6 ARG A 11 0.31 SIDE CHAIN
REMARK 500 6 ARG A 13 0.29 SIDE CHAIN
REMARK 500 7 ARG A 11 0.32 SIDE CHAIN
REMARK 500 7 ARG A 13 0.28 SIDE CHAIN
REMARK 500 8 ARG A 11 0.31 SIDE CHAIN
REMARK 500 8 ARG A 13 0.31 SIDE CHAIN
REMARK 500 9 ARG A 11 0.31 SIDE CHAIN
REMARK 500 9 ARG A 13 0.30 SIDE CHAIN
REMARK 500 10 ARG A 11 0.32 SIDE CHAIN
REMARK 500 10 ARG A 13 0.32 SIDE CHAIN
REMARK 500 11 ARG A 11 0.28 SIDE CHAIN
REMARK 500 11 ARG A 13 0.30 SIDE CHAIN
REMARK 500 12 ARG A 11 0.24 SIDE CHAIN
REMARK 500 12 ARG A 13 0.31 SIDE CHAIN
REMARK 500 13 ARG A 11 0.31 SIDE CHAIN
REMARK 500 13 ARG A 13 0.30 SIDE CHAIN
REMARK 500 14 ARG A 11 0.32 SIDE CHAIN
REMARK 500 14 ARG A 13 0.31 SIDE CHAIN
REMARK 500 15 ARG A 11 0.32 SIDE CHAIN
REMARK 500 15 ARG A 13 0.30 SIDE CHAIN
REMARK 500 16 ARG A 11 0.31 SIDE CHAIN
REMARK 500 16 ARG A 13 0.30 SIDE CHAIN
REMARK 500 17 ARG A 11 0.30 SIDE CHAIN
REMARK 500 17 ARG A 13 0.31 SIDE CHAIN
REMARK 500 18 ARG A 11 0.31 SIDE CHAIN
REMARK 500 18 ARG A 13 0.30 SIDE CHAIN
REMARK 500 19 ARG A 11 0.29 SIDE CHAIN
REMARK 500 19 ARG A 13 0.31 SIDE CHAIN
REMARK 500 20 ARG A 11 0.32 SIDE CHAIN
REMARK 500 20 ARG A 13 0.31 SIDE CHAIN
REMARK 500 21 ARG A 11 0.32 SIDE CHAIN
REMARK 500 21 ARG A 13 0.32 SIDE CHAIN
REMARK 500 22 ARG A 11 0.32 SIDE CHAIN
REMARK 500 22 ARG A 13 0.25 SIDE CHAIN
REMARK 500 23 ARG A 11 0.26 SIDE CHAIN
REMARK 500 23 ARG A 13 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1B4I A 1 30 UNP Q03721 KCNC4_HUMAN 1 30
SEQRES 1 A 30 MET ILE SER SER VAL CYS VAL SER SER TYR ARG GLY ARG
SEQRES 2 A 30 LYS SEP GLY ASN LYS PRO PRO SEP LYS THR CYS LEU LYS
SEQRES 3 A 30 GLU GLU MET ALA
MODRES 1B4I SEP A 15 SER PHOSPHOSERINE
MODRES 1B4I SEP A 21 SER PHOSPHOSERINE
HET SEP A 15 15
HET SEP A 21 15
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
LINK C LYS A 14 N SEP A 15 1555 1555 1.32
LINK C SEP A 15 N GLY A 16 1555 1555 1.32
LINK C PRO A 20 N SEP A 21 1555 1555 1.31
LINK C SEP A 21 N LYS A 22 1555 1555 1.31
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