Header list of 1jei.pdb file
Complete list - 23 20 Bytes
HEADER MEMBRANE PROTEIN 18-JUN-01 1JEI
TITLE LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN EMERIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EMERIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LEM DOMAIN (RESIDUES 2-54);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: CHEMICAL SYNTHESIS
KEYWDS EMERIN NUCLEUS MEMBRANE DOMAIN DYSTROPHY, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR N.WOLFF,B.GILQUIN,K.COURCHAY,I.CALLEBAUT,S.ZINN-JUSTIN
REVDAT 4 23-FEB-22 1JEI 1 REMARK
REVDAT 3 24-FEB-09 1JEI 1 VERSN
REVDAT 2 17-JUN-03 1JEI 1 JRNL
REVDAT 1 04-JUL-01 1JEI 0
JRNL AUTH N.WOLFF,B.GILQUIN,K.COURCHAY,I.CALLEBAUT,H.J.WORMAN,
JRNL AUTH 2 S.ZINN-JUSTIN
JRNL TITL STRUCTURAL ANALYSIS OF EMERIN, AN INNER NUCLEAR MEMBRANE
JRNL TITL 2 PROTEIN MUTATED IN X-LINKED EMERY-DREIFUSS MUSCULAR
JRNL TITL 3 DYSTROPHY
JRNL REF FEBS LETT. V. 501 171 2001
JRNL REFN ISSN 0014-5793
JRNL PMID 11470279
JRNL DOI 10.1016/S0014-5793(01)02649-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.LAGURI,B.GILQUIN,N.WOLFF,R.ROMI-LEBRUN,K.COURCHAY,
REMARK 1 AUTH 2 I.CALLEBAUT,H.J.WORMAN,S.ZINN-JUSTIN
REMARK 1 TITL STRUCTURAL CHARACTERIZATION OF THE LEM MOTIF COMMON TO THREE
REMARK 1 TITL 2 HUMAN INNER NUCLAR MEMBRANE PROTEINS.
REMARK 1 REF STRUCTURE V. 9 503 2001
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(01)00611-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2.0, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JEI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013682.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 20MM
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : LEM DOMAIN OF EMERIN 1MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SEMI-AUTOMATED ITERATIVE
REMARK 210 PROCEDURE USING X-PLOR AND HOME-
REMARK 210 WRITTEN C-SHELL PROGRAMS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: 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
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 2 50.54 -179.09
REMARK 500 1 ASP A 5 -50.92 -134.42
REMARK 500 1 LEU A 6 166.28 -48.75
REMARK 500 1 SER A 7 -165.04 -121.32
REMARK 500 1 ASN A 19 43.04 83.60
REMARK 500 1 PRO A 21 89.78 -63.11
REMARK 500 1 THR A 29 40.65 -82.20
REMARK 500 1 ILE A 37 4.52 -57.17
REMARK 500 1 PHE A 38 -63.77 -92.19
REMARK 500 1 GLN A 43 -36.27 177.99
REMARK 500 1 ARG A 45 -49.85 -169.41
REMARK 500 1 ARG A 46 -69.18 -137.73
REMARK 500 1 SER A 48 166.34 -43.64
REMARK 500 1 SER A 51 -71.79 -114.47
REMARK 500 1 SER A 52 -79.46 -136.88
REMARK 500 2 ASN A 2 42.81 -166.98
REMARK 500 2 LEU A 6 52.67 -175.19
REMARK 500 2 SER A 7 167.97 -38.42
REMARK 500 2 ASP A 8 -48.89 -29.04
REMARK 500 2 ASN A 19 35.31 95.34
REMARK 500 2 PRO A 21 88.05 -62.66
REMARK 500 2 SER A 28 -60.35 -141.06
REMARK 500 2 LYS A 36 37.14 -86.95
REMARK 500 2 TYR A 40 -19.72 -47.98
REMARK 500 2 GLU A 41 -54.01 -122.34
REMARK 500 2 ARG A 44 -120.33 96.86
REMARK 500 2 ARG A 45 -80.68 -166.08
REMARK 500 2 ARG A 46 -50.09 -125.16
REMARK 500 3 ASN A 2 44.61 -142.11
REMARK 500 3 ASP A 5 -58.49 -134.72
REMARK 500 3 LEU A 6 167.88 -43.81
REMARK 500 3 SER A 7 -164.57 -124.00
REMARK 500 3 ASN A 19 38.11 83.62
REMARK 500 3 PRO A 21 94.95 -61.78
REMARK 500 3 THR A 29 35.79 -141.26
REMARK 500 3 LYS A 36 30.98 -87.03
REMARK 500 3 ARG A 44 -139.48 79.67
REMARK 500 3 ARG A 45 -84.53 -178.64
REMARK 500 3 ARG A 46 -76.58 -115.24
REMARK 500 3 LEU A 47 -7.71 80.32
REMARK 500 3 SER A 48 177.12 178.36
REMARK 500 3 SER A 51 -135.58 -147.39
REMARK 500 3 SER A 52 -69.61 -98.44
REMARK 500 4 ASN A 2 55.00 -177.29
REMARK 500 4 TYR A 3 42.49 -85.06
REMARK 500 4 ALA A 4 26.26 -159.54
REMARK 500 4 ASP A 5 42.60 -170.30
REMARK 500 4 LEU A 6 32.38 -140.11
REMARK 500 4 SER A 7 -154.04 18.23
REMARK 500 4 ASN A 19 33.93 91.93
REMARK 500
REMARK 500 THIS ENTRY HAS 139 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 16 0.28 SIDE CHAIN
REMARK 500 1 ARG A 17 0.27 SIDE CHAIN
REMARK 500 1 ARG A 30 0.16 SIDE CHAIN
REMARK 500 1 ARG A 31 0.10 SIDE CHAIN
REMARK 500 1 ARG A 44 0.30 SIDE CHAIN
REMARK 500 1 ARG A 45 0.28 SIDE CHAIN
REMARK 500 1 ARG A 46 0.31 SIDE CHAIN
REMARK 500 2 ARG A 16 0.10 SIDE CHAIN
REMARK 500 2 ARG A 17 0.27 SIDE CHAIN
REMARK 500 2 ARG A 30 0.10 SIDE CHAIN
REMARK 500 2 ARG A 31 0.27 SIDE CHAIN
REMARK 500 2 ARG A 44 0.18 SIDE CHAIN
REMARK 500 2 ARG A 45 0.31 SIDE CHAIN
REMARK 500 2 ARG A 46 0.24 SIDE CHAIN
REMARK 500 3 ARG A 16 0.25 SIDE CHAIN
REMARK 500 3 ARG A 17 0.20 SIDE CHAIN
REMARK 500 3 ARG A 30 0.25 SIDE CHAIN
REMARK 500 3 ARG A 31 0.32 SIDE CHAIN
REMARK 500 3 ARG A 44 0.31 SIDE CHAIN
REMARK 500 3 ARG A 45 0.26 SIDE CHAIN
REMARK 500 3 ARG A 46 0.23 SIDE CHAIN
REMARK 500 4 ARG A 16 0.14 SIDE CHAIN
REMARK 500 4 ARG A 17 0.31 SIDE CHAIN
REMARK 500 4 ARG A 30 0.31 SIDE CHAIN
REMARK 500 4 ARG A 31 0.21 SIDE CHAIN
REMARK 500 4 ARG A 44 0.15 SIDE CHAIN
REMARK 500 4 ARG A 45 0.26 SIDE CHAIN
REMARK 500 4 ARG A 46 0.22 SIDE CHAIN
REMARK 500 5 ARG A 16 0.31 SIDE CHAIN
REMARK 500 5 ARG A 17 0.16 SIDE CHAIN
REMARK 500 5 ARG A 30 0.20 SIDE CHAIN
REMARK 500 5 ARG A 31 0.28 SIDE CHAIN
REMARK 500 5 ARG A 44 0.11 SIDE CHAIN
REMARK 500 5 ARG A 45 0.20 SIDE CHAIN
REMARK 500 5 ARG A 46 0.24 SIDE CHAIN
REMARK 500 6 ARG A 16 0.28 SIDE CHAIN
REMARK 500 6 ARG A 17 0.31 SIDE CHAIN
REMARK 500 6 ARG A 30 0.32 SIDE CHAIN
REMARK 500 6 ARG A 31 0.28 SIDE CHAIN
REMARK 500 6 ARG A 44 0.29 SIDE CHAIN
REMARK 500 6 ARG A 45 0.31 SIDE CHAIN
REMARK 500 6 ARG A 46 0.30 SIDE CHAIN
REMARK 500 7 ARG A 16 0.31 SIDE CHAIN
REMARK 500 7 ARG A 17 0.21 SIDE CHAIN
REMARK 500 7 ARG A 30 0.26 SIDE CHAIN
REMARK 500 7 ARG A 31 0.29 SIDE CHAIN
REMARK 500 7 ARG A 44 0.22 SIDE CHAIN
REMARK 500 7 ARG A 46 0.32 SIDE CHAIN
REMARK 500 8 ARG A 16 0.32 SIDE CHAIN
REMARK 500 8 ARG A 17 0.15 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 67 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1H9E RELATED DB: PDB
REMARK 900 1H9E CONTAINS LEM-LIKE DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE
REMARK 900 PROTEIN LAP2
REMARK 900 RELATED ID: 1H9F RELATED DB: PDB
REMARK 900 1H9F CONTAINS LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN
REMARK 900 LAP2
DBREF 1JEI A 1 53 UNP P50402 EMD_HUMAN 2 54
SEQRES 1 A 53 ASP ASN TYR ALA ASP LEU SER ASP THR GLU LEU THR THR
SEQRES 2 A 53 LEU LEU ARG ARG TYR ASN ILE PRO HIS GLY PRO VAL VAL
SEQRES 3 A 53 GLY SER THR ARG ARG LEU TYR GLU LYS LYS ILE PHE GLU
SEQRES 4 A 53 TYR GLU THR GLN ARG ARG ARG LEU SER PRO PRO SER SER
SEQRES 5 A 53 SER
HELIX 1 1 SER A 7 ARG A 16 1 10
HELIX 2 2 GLY A 27 THR A 29 5 3
HELIX 3 3 ARG A 30 ILE A 37 1 8
HELIX 4 4 PHE A 38 THR A 42 5 5
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