HEADER MEMBRANE PROTEIN 06-NOV-07 2JX4
TITLE NMR STRUCTURE OF THE INTRACELLULAR LOOP (I3) OF THE VASOPRESSIN V2
TITLE 2 RECEPTOR (GPCR)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VASOPRESSIN V2 RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 225-273;
COMPND 5 SYNONYM: RENAL-TYPE ARGININE VASOPRESSIN RECEPTOR, ANTIDIURETIC
COMPND 6 HORMONE RECEPTOR, AVPR V2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: SYNTHESIS UNDER A CYCLIZED FORM: THIO-ETHER BRIDGE
COMPND 10 BETWEEN THE C-TERMINAL CYSTEINE RESIDUE (CYC) AND THE N-TERMINAL
COMPND 11 GLYCINE WERE CONSTRUCTED
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SOURCE
SOURCE 4 SEQUENCE IS NATURALLY FOUND IN RAT (V2 RAT RECEPTOR).
KEYWDS PROTEIN, G-PROTEIN COUPLED RECEPTOR, GLYCOPROTEIN, LIPOPROTEIN,
KEYWDS 2 MEMBRANE, PALMITATE, PHOSPHORYLATION, RECEPTOR, TRANSDUCER,
KEYWDS 3 TRANSMEMBRANE, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.BELLOT,H.DEMENE
REVDAT 3 10-NOV-21 2JX4 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2JX4 1 VERSN
REVDAT 1 18-NOV-08 2JX4 0
JRNL AUTH G.BELLOT,S.GRANIER,W.BOURGUET,R.SEYER,R.RAHMEH,B.MOUILLAC,
JRNL AUTH 2 R.PASCAL,C.MENDRE,H.DEMENE
JRNL TITL STRUCTURE OF THE THIRD INTRACELLULAR LOOP OF THE VASOPRESSIN
JRNL TITL 2 V2 RECEPTOR AND CONFORMATIONAL CHANGES UPON BINDING TO GC1QR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 2.0, ARIA 2.0
REMARK 3 AUTHORS : LINGE, O'DONOGHUE AND NILGES (ARIA), LINGE,
REMARK 3 O'DONOGHUE AND NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2JX4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000100400.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308; 318; 293
REMARK 210 PH : 4; 4; 4
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM H2O, 90% H2O/10% D2O; 1MM
REMARK 210 D2O, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-1H TOCSY; 2D DQF-COSY; 2D
REMARK 210 1H-1H NOESY; 2D 1H-13C HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 800
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 DGN A 225 H ILE A 228 1.55
REMARK 500 N GLY A 1 CD CCS A 51 1.84
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 DGN A 225 64.60 160.64
REMARK 500 1 VAL A 226 -26.67 -37.62
REMARK 500 1 ARG A 248 -79.09 -102.29
REMARK 500 1 ARG A 249 -179.22 -59.34
REMARK 500 1 ARG A 251 34.41 -88.94
REMARK 500 1 ARG A 252 -34.42 -140.28
REMARK 500 1 THR A 273 -75.13 -84.97
REMARK 500 2 DGN A 225 64.87 161.35
REMARK 500 2 VAL A 226 -26.74 -37.16
REMARK 500 2 ARG A 248 -98.99 -69.54
REMARK 500 2 ARG A 249 -170.76 -63.54
REMARK 500 2 ARG A 251 39.94 -78.74
REMARK 500 2 THR A 273 -78.80 -84.14
REMARK 500 3 DGN A 225 65.77 160.65
REMARK 500 3 VAL A 226 -26.94 -37.42
REMARK 500 3 ARG A 243 -9.27 -55.50
REMARK 500 3 ALA A 244 -5.72 -156.22
REMARK 500 3 ARG A 248 -149.04 -95.89
REMARK 500 3 ARG A 249 -167.85 -58.06
REMARK 500 3 ARG A 251 43.60 -82.79
REMARK 500 3 THR A 273 -79.33 -83.87
REMARK 500 4 DGN A 225 65.98 160.56
REMARK 500 4 VAL A 226 -26.84 -37.70
REMARK 500 4 ARG A 243 0.39 -69.05
REMARK 500 4 ALA A 244 -5.53 -154.57
REMARK 500 4 ARG A 248 -134.81 -119.61
REMARK 500 4 ARG A 251 45.71 -79.79
REMARK 500 4 ARG A 252 -31.01 -135.56
REMARK 500 4 THR A 273 -78.30 -83.03
REMARK 500 5 DGN A 225 65.82 160.00
REMARK 500 5 VAL A 226 -26.93 -37.18
REMARK 500 5 ARG A 243 42.88 -76.88
REMARK 500 5 ALA A 244 -48.52 -143.10
REMARK 500 5 ARG A 247 -51.75 -29.53
REMARK 500 5 ARG A 248 -169.82 -114.80
REMARK 500 5 ARG A 249 161.30 -49.64
REMARK 500 5 ARG A 251 -126.47 -104.18
REMARK 500 5 THR A 273 -78.89 -84.65
REMARK 500 6 DGN A 225 65.67 161.63
REMARK 500 6 VAL A 226 -26.96 -37.52
REMARK 500 6 ARG A 243 41.14 -79.05
REMARK 500 6 ALA A 244 -62.33 -126.69
REMARK 500 6 ARG A 248 -85.22 -90.85
REMARK 500 6 ARG A 249 174.18 -56.69
REMARK 500 6 ARG A 251 40.97 -80.49
REMARK 500 6 ARG A 252 -35.01 -132.35
REMARK 500 6 THR A 273 -78.76 -84.29
REMARK 500 7 DGN A 225 67.54 160.54
REMARK 500 7 VAL A 226 -26.32 -37.59
REMARK 500 7 ARG A 248 -144.97 -69.10
REMARK 500
REMARK 500 THIS ENTRY HAS 136 RAMACHANDRAN OUTLIERS.
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 52
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THESE ARE LINKER. THIO-ETHER BRIDGE BETWEEN CCS AND GLY WERE
REMARK 999 CONSTRUCTED.
DBREF 2JX4 A 225 273 UNP Q00788 V2R_RAT 225 273
SEQADV 2JX4 GLY A 1 UNP Q00788 SEE REMARK 999
SEQADV 2JX4 NLE A 266 UNP Q00788 MET 266 ENGINEERED MUTATION
SEQADV 2JX4 NLE A 272 UNP Q00788 MET 272 ENGINEERED MUTATION
SEQADV 2JX4 CCS A 51 UNP Q00788 SEE REMARK 999
SEQRES 1 A 52 GLY DGN VAL LEU ILE PHE ARG GLU ILE HIS ALA SER LEU
SEQRES 2 A 52 VAL PRO GLY PRO SER GLU ARG ALA GLY ARG ARG ARG ARG
SEQRES 3 A 52 GLY ARG ARG THR GLY SER PRO SER GLU GLY ALA HIS VAL
SEQRES 4 A 52 SER ALA ALA NLE ALA LYS THR VAL ARG NLE THR CCS NH2
MODRES 2JX4 DGN A 225 GLN D-GLUTAMINE
MODRES 2JX4 NLE A 266 LEU NORLEUCINE
MODRES 2JX4 NLE A 272 LEU NORLEUCINE
MODRES 2JX4 CCS A 51 CYS CARBOXYMETHYLATED CYSTEINE
HET DGN A 225 17
HET NLE A 266 19
HET NLE A 272 19
HET CCS A 51 15
HET NH2 A 52 3
HETNAM DGN D-GLUTAMINE
HETNAM NLE NORLEUCINE
HETNAM CCS CARBOXYMETHYLATED CYSTEINE
HETNAM NH2 AMINO GROUP
FORMUL 1 DGN C5 H10 N2 O3
FORMUL 1 NLE 2(C6 H13 N O2)
FORMUL 1 CCS C5 H9 N O4 S
FORMUL 1 NH2 H2 N
HELIX 1 1 DGN A 225 VAL A 237 1 13
HELIX 2 2 VAL A 237 ARG A 243 1 7
HELIX 3 3 THR A 253 CCS A 51 1 22
LINK N GLY A 1 CE CCS A 51 1555 1555 1.34
LINK C GLY A 1 N DGN A 225 1555 1555 1.33
LINK C CCS A 51 N NH2 A 52 1555 1555 1.33
LINK N CCS A 51 C THR A 273 1555 1555 1.33
LINK C DGN A 225 N VAL A 226 1555 1555 1.32
LINK C ALA A 265 N NLE A 266 1555 1555 1.31
LINK C NLE A 266 N ALA A 267 1555 1555 1.33
LINK C ARG A 271 N NLE A 272 1555 1555 1.32
LINK C NLE A 272 N THR A 273 1555 1555 1.33
SITE 1 AC1 6 GLY A 1 CCS A 51 PHE A 229 VAL A 270
SITE 2 AC1 6 ARG A 271 THR A 273
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
