HEADER TRANSFERASE 20-OCT-13 2MFR
TITLE SOLUTION STRUCTURE OF THE TRANSMEMBRANE DOMAIN OF THE INSULIN RECEPTOR
TITLE 2 IN MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 940-988;
COMPND 5 SYNONYM: IR;
COMPND 6 EC: 2.7.10.1;
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: INSR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET29B
KEYWDS INSULIN RECEPOTR, MEMBRANE PROTEIN, DETERGENT MICELLES, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Q.LI,Y.L.WONG,C.KANG
REVDAT 2 14-JUN-23 2MFR 1 REMARK SEQADV
REVDAT 1 02-APR-14 2MFR 0
JRNL AUTH Q.LI,Y.L.WONG,C.KANG
JRNL TITL SOLUTION STRUCTURE OF THE TRANSMEMBRANE DOMAIN OF THE
JRNL TITL 2 INSULIN RECEPTOR IN DETERGENT MICELLES
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1838 1313 2014
JRNL REFN ISSN 0006-3002
JRNL PMID 24440425
JRNL DOI 10.1016/J.BBAMEM.2014.01.005
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, X-PLOR NIH
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3 (NMRPIPE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2MFR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000103574.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.2-0.4 MM [U-100% 15N] PROTEIN
REMARK 210 -1, 90% H2O/10% D2O; 0.2-0.4 MM
REMARK 210 [U-100% 13C; U-100% 15N] PROTEIN-
REMARK 210 2, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCO; 3D
REMARK 210 HNCA; 3D HNCACB; 3D CBCA(CO)NH;
REMARK 210 3D 1H-15N NOESY; 3D HBHA(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, X-PLOR NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 56
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: 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 O PRO A 46 H GLY A 48 1.55
REMARK 500 O HIS A 54 HD1 HIS A 55 1.60
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 ASP A 47 38.77 -67.60
REMARK 500 1 PRO A 49 108.74 -49.81
REMARK 500 1 LEU A 50 142.79 59.11
REMARK 500 1 GLU A 51 -109.91 -91.44
REMARK 500 1 HIS A 52 -107.28 37.99
REMARK 500 1 HIS A 53 26.40 40.10
REMARK 500 1 HIS A 54 -162.15 -128.55
REMARK 500 1 HIS A 55 -59.90 -130.00
REMARK 500 2 ARG A 44 -103.18 -50.19
REMARK 500 2 GLN A 45 71.94 172.85
REMARK 500 2 ASP A 47 38.89 -66.98
REMARK 500 2 HIS A 53 -158.56 54.56
REMARK 500 2 HIS A 56 -122.95 27.62
REMARK 500 3 LEU A 10 42.33 -96.37
REMARK 500 3 GLN A 45 53.40 71.68
REMARK 500 3 ASP A 47 38.75 -67.55
REMARK 500 3 HIS A 52 52.66 28.81
REMARK 500 3 HIS A 54 -157.39 -70.21
REMARK 500 3 HIS A 56 165.98 -44.65
REMARK 500 4 ARG A 44 124.56 62.41
REMARK 500 4 ASP A 47 38.73 -67.69
REMARK 500 4 LEU A 50 67.47 84.83
REMARK 500 4 HIS A 52 81.78 -62.33
REMARK 500 4 HIS A 55 -78.68 -163.41
REMARK 500 4 HIS A 56 70.69 -172.18
REMARK 500 5 LEU A 10 40.55 -89.67
REMARK 500 5 LYS A 43 13.73 -68.47
REMARK 500 5 PRO A 46 162.88 -46.95
REMARK 500 5 ASP A 47 38.78 -67.79
REMARK 500 5 LEU A 50 36.93 -156.02
REMARK 500 5 GLU A 51 -70.14 -43.19
REMARK 500 5 HIS A 54 17.95 -153.77
REMARK 500 5 HIS A 55 -144.84 72.89
REMARK 500 6 VAL A 12 104.13 -43.18
REMARK 500 6 ARG A 44 63.58 36.95
REMARK 500 6 PRO A 46 30.28 -70.23
REMARK 500 6 ASP A 47 39.02 -67.51
REMARK 500 6 PRO A 49 -165.99 -70.95
REMARK 500 7 TYR A 3 -8.60 -50.99
REMARK 500 7 LEU A 10 43.75 -94.65
REMARK 500 7 ARG A 44 -147.77 32.82
REMARK 500 7 ASP A 47 38.73 -67.82
REMARK 500 7 PRO A 49 104.20 -49.60
REMARK 500 7 LEU A 50 49.00 -69.94
REMARK 500 7 GLU A 51 61.61 27.63
REMARK 500 7 HIS A 56 -76.33 -64.30
REMARK 500 8 LEU A 10 40.01 -74.80
REMARK 500 8 ARG A 44 30.67 -85.19
REMARK 500 8 ASP A 47 38.85 -67.54
REMARK 500 8 PRO A 49 99.26 -51.42
REMARK 500
REMARK 500 THIS ENTRY HAS 142 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19568 RELATED DB: BMRB
DBREF 2MFR A 2 50 UNP P06213 INSR_HUMAN 940 988
SEQADV 2MFR MET A 1 UNP P06213 EXPRESSION TAG
SEQADV 2MFR GLU A 51 UNP P06213 EXPRESSION TAG
SEQADV 2MFR HIS A 52 UNP P06213 EXPRESSION TAG
SEQADV 2MFR HIS A 53 UNP P06213 EXPRESSION TAG
SEQADV 2MFR HIS A 54 UNP P06213 EXPRESSION TAG
SEQADV 2MFR HIS A 55 UNP P06213 EXPRESSION TAG
SEQADV 2MFR HIS A 56 UNP P06213 EXPRESSION TAG
SEQADV 2MFR HIS A 57 UNP P06213 EXPRESSION TAG
SEQRES 1 A 57 MET THR TYR PHE TYR VAL THR ASP TYR LEU ASP VAL PRO
SEQRES 2 A 57 SER ASN ILE ALA LYS ILE ILE ILE GLY PRO LEU ILE PHE
SEQRES 3 A 57 VAL PHE LEU PHE SER VAL VAL ILE GLY SER ILE TYR LEU
SEQRES 4 A 57 PHE LEU ARG LYS ARG GLN PRO ASP GLY PRO LEU GLU HIS
SEQRES 5 A 57 HIS HIS HIS HIS HIS
HELIX 1 1 THR A 2 TYR A 9 1 8
HELIX 2 2 SER A 14 ARG A 42 1 29
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
(ATOM LINES ARE NOT SHOWN.)
END