Header list of 1mot.pdb file
Complete list - 23 20 Bytes
HEADER MEMBRANE PROTEIN 09-SEP-02 1MOT
TITLE NMR STRUCTURE OF EXTENDED SECOND TRANSMEMBRANE DOMAIN OF GLYCINE
TITLE 2 RECEPTOR ALPHA1 SUBUNIT IN SDS MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCINE RECEPTOR ALPHA-1 CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTENTED SECOND TRANSMEMBRANE DOMAIN;
COMPND 5 SYNONYM: GLYCINE RECEPTOR ALPHA1 SUBUNIT, GLYCINE RECEPTOR 48KDA
COMPND 6 SUBUNIT, STRYCHNINE BINDING SUBUNIT;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GLRA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-3X
KEYWDS GLYCINE RECEPTOR, SECOND TRANSMEMBRANE DOMAIN, MICELLES, MEMBRANE
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR V.E.YUSHMANOV,P.K.MANDAL,Z.LIU,P.TANG,Y.XU
REVDAT 3 23-FEB-22 1MOT 1 REMARK
REVDAT 2 24-FEB-09 1MOT 1 VERSN
REVDAT 1 23-SEP-03 1MOT 0
JRNL AUTH V.E.YUSHMANOV,P.K.MANDAL,Z.LIU,P.TANG,Y.XU
JRNL TITL NMR STRUCTURE AND BACKBONE DYNAMICS OF THE EXTENDED SECOND
JRNL TITL 2 TRANSMEMBRANE DOMAIN OF THE HUMAN NEURONAL GLYCINE RECEPTOR
JRNL TITL 3 ALPHA1 SUBUNIT
JRNL REF BIOCHEMISTRY V. 42 3989 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12667090
JRNL DOI 10.1021/BI026767G
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER, A.T. (X-PLOR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 187 RESTRAINTS, 169 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS,18 DISTANCE RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1MOT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000017061.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 300 MM SDS CONCENTRATION
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : SDS CONCENTRATION: 300 MM
REMARK 210 PEPTIDE CONCENTRATION: 2 MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; COSY; 15N T1;
REMARK 210 15N T2; 15N HET-NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
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: THE STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR
REMARK 210 AND TRIPLE-RESONANCE NMR SPECTROSCOPY.
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 GLN A 266 -47.37 68.67
REMARK 500 1 SER A 270 -52.89 69.65
REMARK 500 1 ALA A 272 -122.41 -75.45
REMARK 500 1 PRO A 275 56.82 -61.29
REMARK 500 2 PRO A 250 -147.02 -76.33
REMARK 500 2 ALA A 251 -70.33 -150.92
REMARK 500 2 THR A 264 46.05 -86.49
REMARK 500 2 THR A 265 43.76 -74.09
REMARK 500 3 SER A 267 -152.73 -91.09
REMARK 500 3 ARG A 271 43.86 71.43
REMARK 500 4 SER A 267 -126.08 61.66
REMARK 500 4 SER A 268 43.66 -77.24
REMARK 500 4 PRO A 275 60.30 -60.18
REMARK 500 5 SER A 267 -52.69 -163.68
REMARK 500 5 ARG A 271 -53.44 69.28
REMARK 500 6 PRO A 250 60.84 -66.06
REMARK 500 6 ALA A 251 -142.61 56.47
REMARK 500 6 SER A 268 56.48 -69.78
REMARK 500 6 SER A 270 -142.23 58.25
REMARK 500 6 ARG A 271 121.08 72.12
REMARK 500 6 ALA A 272 -140.20 57.27
REMARK 500 6 SER A 273 49.46 -86.41
REMARK 500 6 PRO A 275 50.03 -56.31
REMARK 500 7 PRO A 250 -137.98 -73.23
REMARK 500 7 ALA A 251 -148.41 -76.39
REMARK 500 7 GLN A 266 -61.99 67.50
REMARK 500 7 SER A 267 -141.47 -172.33
REMARK 500 7 SER A 268 -140.81 61.06
REMARK 500 7 ALA A 272 33.81 -81.23
REMARK 500 8 PRO A 250 49.50 -70.13
REMARK 500 8 ALA A 251 -123.62 47.34
REMARK 500 8 GLN A 266 92.04 -64.98
REMARK 500 8 SER A 267 46.89 -78.88
REMARK 500 8 SER A 268 -54.71 67.11
REMARK 500 8 ARG A 271 -74.93 68.07
REMARK 500 9 THR A 265 -142.48 -82.56
REMARK 500 9 SER A 273 51.96 -96.33
REMARK 500 10 PRO A 250 68.67 -68.90
REMARK 500 10 ALA A 251 -73.26 -67.26
REMARK 500 10 SER A 267 -141.55 62.94
REMARK 500 10 SER A 270 -130.66 55.97
REMARK 500 10 ALA A 272 -140.07 52.28
REMARK 500 10 PRO A 275 61.35 -64.55
REMARK 500 11 ALA A 251 -150.55 61.15
REMARK 500 11 THR A 265 58.18 33.47
REMARK 500 11 SER A 270 137.32 -173.88
REMARK 500 11 ALA A 272 -137.10 -87.31
REMARK 500 12 MET A 263 56.70 -159.67
REMARK 500 12 ARG A 271 -46.40 69.78
REMARK 500 12 ALA A 272 -135.66 -145.55
REMARK 500
REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MOT A 249 276 UNP P23415 GLRA1_HUMAN 277 304
SEQRES 1 A 28 ALA PRO ALA ARG VAL GLY LEU GLY ILE THR THR VAL LEU
SEQRES 2 A 28 THR MET THR THR GLN SER SER GLY SER ARG ALA SER LEU
SEQRES 3 A 28 PRO LYS
HELIX 1 1 PRO A 250 THR A 264 1 15
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