HEADER SIGNALING PROTEIN/AGONIST 18-SEP-13 4MS3
TITLE CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN GABA(B)
TITLE 2 RECEPTOR BOUND TO THE ENDOGENOUS AGONIST GABA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAMMA-AMINOBUTYRIC ACID TYPE B RECEPTOR SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN (SEE REMARK 999);
COMPND 5 SYNONYM: GABA-B RECEPTOR 1, GABA-B-R1, GABA-BR1, GABABR1, GB1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GAMMA-AMINOBUTYRIC ACID TYPE B RECEPTOR SUBUNIT 2;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: EXTRACELLULAR DOMAIN (UNP RESIDUES 42-466);
COMPND 11 SYNONYM: GABA-B RECEPTOR 2, GABA-B-R2, GABA-BR2, GABABR2, GB2, G-
COMPND 12 PROTEIN COUPLED RECEPTOR 51, HG20;
COMPND 13 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: GABBR1, GPRC3A;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFBDM;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: GABBR2, GPR51, GPRC3B;
SOURCE 17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 18 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PFBDM
KEYWDS HETERODIMERIC PROTEIN COMPLEX, VENUS FLYTRAP MODULE, NEUROTRANSMITTER
KEYWDS 2 RECEPTOR, SIGNALING PROTEIN-AGONIST COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.GENG,M.BUSH,L.MOSYAK,F.WANG,Q.R.FAN
REVDAT 6 15-NOV-23 4MS3 1 ATOM
REVDAT 5 20-SEP-23 4MS3 1 HETSYN
REVDAT 4 29-JUL-20 4MS3 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE
REVDAT 3 05-FEB-14 4MS3 1 JRNL
REVDAT 2 18-DEC-13 4MS3 1 JRNL
REVDAT 1 11-DEC-13 4MS3 0
JRNL AUTH Y.GENG,M.BUSH,L.MOSYAK,F.WANG,Q.R.FAN
JRNL TITL STRUCTURAL MECHANISM OF LIGAND ACTIVATION IN HUMAN GABA(B)
JRNL TITL 2 RECEPTOR.
JRNL REF NATURE V. 504 254 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 24305054
JRNL DOI 10.1038/NATURE12725
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 33882
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180
REMARK 3 FREE R VALUE TEST SET COUNT : 1754
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.58
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.35
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2934
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2327
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2785
REMARK 3 BIN R VALUE (WORKING SET) : 0.2301
REMARK 3 BIN FREE R VALUE : 0.2841
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.08
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 149
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6419
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 306
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.51330
REMARK 3 B22 (A**2) : 3.70250
REMARK 3 B33 (A**2) : -9.21570
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.317
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.567
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.260
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.517
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.259
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.907
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2267 ; 2.000 ; SINUSOIDAL
REMARK 3 BOND ANGLES : 167 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 6600 ; 20.000 ; HARMONIC
REMARK 3 TRIGONAL CARBON PLANES : 6600 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 7632 ; 4.000 ; SEMIHARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8944 ; 2.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.91
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4MS3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000082296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : CRYO-COOLED DOUBLE CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33921
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 60.388
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.66100
REMARK 200 R SYM FOR SHELL (I) : 0.66100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4MQE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG2000, 5% GLYCEROL, 0.15 M
REMARK 280 AMMONIUM CHLORIDE, 0.1 M SODIUM CACODYLATE, PH 5.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 57.74000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.84500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 57.74000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.84500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 48
REMARK 465 GLU A 49
REMARK 465 ARG A 85
REMARK 465 ARG A 86
REMARK 465 ASP A 87
REMARK 465 ILE A 88
REMARK 465 LEU A 89
REMARK 465 PRO A 90
REMARK 465 ASP A 91
REMARK 465 LYS A 338
REMARK 465 ARG A 339
REMARK 465 HIS A 340
REMARK 465 PRO A 341
REMARK 465 GLU A 342
REMARK 465 GLU A 343
REMARK 465 GLY A 369
REMARK 465 GLY A 370
REMARK 465 GLY A 371
REMARK 465 GLY A 372
REMARK 465 ARG A 373
REMARK 465 SER A 374
REMARK 465 GLY A 375
REMARK 465 VAL A 376
REMARK 465 ASP A 466
REMARK 465 LYS A 467
REMARK 465 TRP B 42
REMARK 465 ALA B 43
REMARK 465 ARG B 44
REMARK 465 GLY B 45
REMARK 465 ALA B 46
REMARK 465 PRO B 47
REMARK 465 ARG B 48
REMARK 465 PRO B 49
REMARK 465 GLN B 292
REMARK 465 VAL B 293
REMARK 465 HIS B 294
REMARK 465 THR B 295
REMARK 465 GLU B 296
REMARK 465 ALA B 297
REMARK 465 ASN B 298
REMARK 465 SER B 299
REMARK 465 SER B 300
REMARK 465 ARG B 301
REMARK 465 TYR B 468
REMARK 465 LYS B 469
REMARK 465 ASP B 470
REMARK 465 ASP B 471
REMARK 465 ASP B 472
REMARK 465 ASP B 473
REMARK 465 LYS B 474
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 NE ARG B 197 OD1 ASP B 467 2.18
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 PRO A 66 49.90 -81.22
REMARK 500 CYS A 129 151.10 -49.34
REMARK 500 THR A 198 37.06 -77.38
REMARK 500 SER A 228 -34.84 -135.95
REMARK 500 LEU A 266 47.27 -93.98
REMARK 500 ASN A 317 49.25 -77.13
REMARK 500 SER A 400 97.16 -162.96
REMARK 500 ARG B 95 135.57 -38.40
REMARK 500 SER B 233 -65.87 -103.60
REMARK 500 MET B 272 58.45 -96.55
REMARK 500 GLN B 326 42.15 -92.62
REMARK 500 SER B 347 -57.01 -125.75
REMARK 500 ASN B 389 44.07 -143.65
REMARK 500 TYR B 390 -7.15 69.05
REMARK 500 ASN B 407 91.16 -165.67
REMARK 500 THR B 455 -65.68 -132.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MQE RELATED DB: PDB
REMARK 900 RELATED ID: 4MQF RELATED DB: PDB
REMARK 900 RELATED ID: 4MR7 RELATED DB: PDB
REMARK 900 RELATED ID: 4MR8 RELATED DB: PDB
REMARK 900 RELATED ID: 4MR9 RELATED DB: PDB
REMARK 900 RELATED ID: 4MRM RELATED DB: PDB
REMARK 900 RELATED ID: 4MS1 RELATED DB: PDB
REMARK 900 RELATED ID: 4MS4 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SUBUNIT 1 IS RESIDUES 48-459 OF ISOFORM 1B (UNP Q9UBS5-2).
DBREF 4MS3 A 48 459 UNP Q9UBS5 GABR1_HUMAN 48 459
DBREF 4MS3 B 42 466 UNP O75899 GABR2_HUMAN 42 466
SEQADV 4MS3 ASP A 460 UNP Q9UBS5 EXPRESSION TAG
SEQADV 4MS3 TYR A 461 UNP Q9UBS5 EXPRESSION TAG
SEQADV 4MS3 LYS A 462 UNP Q9UBS5 EXPRESSION TAG
SEQADV 4MS3 ASP A 463 UNP Q9UBS5 EXPRESSION TAG
SEQADV 4MS3 ASP A 464 UNP Q9UBS5 EXPRESSION TAG
SEQADV 4MS3 ASP A 465 UNP Q9UBS5 EXPRESSION TAG
SEQADV 4MS3 ASP A 466 UNP Q9UBS5 EXPRESSION TAG
SEQADV 4MS3 LYS A 467 UNP Q9UBS5 EXPRESSION TAG
SEQADV 4MS3 ASP B 467 UNP O75899 EXPRESSION TAG
SEQADV 4MS3 TYR B 468 UNP O75899 EXPRESSION TAG
SEQADV 4MS3 LYS B 469 UNP O75899 EXPRESSION TAG
SEQADV 4MS3 ASP B 470 UNP O75899 EXPRESSION TAG
SEQADV 4MS3 ASP B 471 UNP O75899 EXPRESSION TAG
SEQADV 4MS3 ASP B 472 UNP O75899 EXPRESSION TAG
SEQADV 4MS3 ASP B 473 UNP O75899 EXPRESSION TAG
SEQADV 4MS3 LYS B 474 UNP O75899 EXPRESSION TAG
SEQRES 1 A 420 SER GLU ARG ARG ALA VAL TYR ILE GLY ALA LEU PHE PRO
SEQRES 2 A 420 MET SER GLY GLY TRP PRO GLY GLY GLN ALA CYS GLN PRO
SEQRES 3 A 420 ALA VAL GLU MET ALA LEU GLU ASP VAL ASN SER ARG ARG
SEQRES 4 A 420 ASP ILE LEU PRO ASP TYR GLU LEU LYS LEU ILE HIS HIS
SEQRES 5 A 420 ASP SER LYS CYS ASP PRO GLY GLN ALA THR LYS TYR LEU
SEQRES 6 A 420 TYR GLU LEU LEU TYR ASN ASP PRO ILE LYS ILE ILE LEU
SEQRES 7 A 420 MET PRO GLY CYS SER SER VAL SER THR LEU VAL ALA GLU
SEQRES 8 A 420 ALA ALA ARG MET TRP ASN LEU ILE VAL LEU SER TYR GLY
SEQRES 9 A 420 SER SER SER PRO ALA LEU SER ASN ARG GLN ARG PHE PRO
SEQRES 10 A 420 THR PHE PHE ARG THR HIS PRO SER ALA THR LEU HIS ASN
SEQRES 11 A 420 PRO THR ARG VAL LYS LEU PHE GLU LYS TRP GLY TRP LYS
SEQRES 12 A 420 LYS ILE ALA THR ILE GLN GLN THR THR GLU VAL PHE THR
SEQRES 13 A 420 SER THR LEU ASP ASP LEU GLU GLU ARG VAL LYS GLU ALA
SEQRES 14 A 420 GLY ILE GLU ILE THR PHE ARG GLN SER PHE PHE SER ASP
SEQRES 15 A 420 PRO ALA VAL PRO VAL LYS ASN LEU LYS ARG GLN ASP ALA
SEQRES 16 A 420 ARG ILE ILE VAL GLY LEU PHE TYR GLU THR GLU ALA ARG
SEQRES 17 A 420 LYS VAL PHE CYS GLU VAL TYR LYS GLU ARG LEU PHE GLY
SEQRES 18 A 420 LYS LYS TYR VAL TRP PHE LEU ILE GLY TRP TYR ALA ASP
SEQRES 19 A 420 ASN TRP PHE LYS ILE TYR ASP PRO SER ILE ASN CYS THR
SEQRES 20 A 420 VAL ASP GLU MET THR GLU ALA VAL GLU GLY HIS ILE THR
SEQRES 21 A 420 THR GLU ILE VAL MET LEU ASN PRO ALA ASN THR ARG SER
SEQRES 22 A 420 ILE SER ASN MET THR SER GLN GLU PHE VAL GLU LYS LEU
SEQRES 23 A 420 THR LYS ARG LEU LYS ARG HIS PRO GLU GLU THR GLY GLY
SEQRES 24 A 420 PHE GLN GLU ALA PRO LEU ALA TYR ASP ALA ILE TRP ALA
SEQRES 25 A 420 LEU ALA LEU ALA LEU ASN LYS THR SER GLY GLY GLY GLY
SEQRES 26 A 420 ARG SER GLY VAL ARG LEU GLU ASP PHE ASN TYR ASN ASN
SEQRES 27 A 420 GLN THR ILE THR ASP GLN ILE TYR ARG ALA MET ASN SER
SEQRES 28 A 420 SER SER PHE GLU GLY VAL SER GLY HIS VAL VAL PHE ASP
SEQRES 29 A 420 ALA SER GLY SER ARG MET ALA TRP THR LEU ILE GLU GLN
SEQRES 30 A 420 LEU GLN GLY GLY SER TYR LYS LYS ILE GLY TYR TYR ASP
SEQRES 31 A 420 SER THR LYS ASP ASP LEU SER TRP SER LYS THR ASP LYS
SEQRES 32 A 420 TRP ILE GLY GLY SER PRO PRO ALA ASP ASP TYR LYS ASP
SEQRES 33 A 420 ASP ASP ASP LYS
SEQRES 1 B 433 TRP ALA ARG GLY ALA PRO ARG PRO PRO PRO SER SER PRO
SEQRES 2 B 433 PRO LEU SER ILE MET GLY LEU MET PRO LEU THR LYS GLU
SEQRES 3 B 433 VAL ALA LYS GLY SER ILE GLY ARG GLY VAL LEU PRO ALA
SEQRES 4 B 433 VAL GLU LEU ALA ILE GLU GLN ILE ARG ASN GLU SER LEU
SEQRES 5 B 433 LEU ARG PRO TYR PHE LEU ASP LEU ARG LEU TYR ASP THR
SEQRES 6 B 433 GLU CYS ASP ASN ALA LYS GLY LEU LYS ALA PHE TYR ASP
SEQRES 7 B 433 ALA ILE LYS TYR GLY PRO ASN HIS LEU MET VAL PHE GLY
SEQRES 8 B 433 GLY VAL CYS PRO SER VAL THR SER ILE ILE ALA GLU SER
SEQRES 9 B 433 LEU GLN GLY TRP ASN LEU VAL GLN LEU SER PHE ALA ALA
SEQRES 10 B 433 THR THR PRO VAL LEU ALA ASP LYS LYS LYS TYR PRO TYR
SEQRES 11 B 433 PHE PHE ARG THR VAL PRO SER ASP ASN ALA VAL ASN PRO
SEQRES 12 B 433 ALA ILE LEU LYS LEU LEU LYS HIS TYR GLN TRP LYS ARG
SEQRES 13 B 433 VAL GLY THR LEU THR GLN ASP VAL GLN ARG PHE SER GLU
SEQRES 14 B 433 VAL ARG ASN ASP LEU THR GLY VAL LEU TYR GLY GLU ASP
SEQRES 15 B 433 ILE GLU ILE SER ASP THR GLU SER PHE SER ASN ASP PRO
SEQRES 16 B 433 CYS THR SER VAL LYS LYS LEU LYS GLY ASN ASP VAL ARG
SEQRES 17 B 433 ILE ILE LEU GLY GLN PHE ASP GLN ASN MET ALA ALA LYS
SEQRES 18 B 433 VAL PHE CYS CYS ALA TYR GLU GLU ASN MET TYR GLY SER
SEQRES 19 B 433 LYS TYR GLN TRP ILE ILE PRO GLY TRP TYR GLU PRO SER
SEQRES 20 B 433 TRP TRP GLU GLN VAL HIS THR GLU ALA ASN SER SER ARG
SEQRES 21 B 433 CYS LEU ARG LYS ASN LEU LEU ALA ALA MET GLU GLY TYR
SEQRES 22 B 433 ILE GLY VAL ASP PHE GLU PRO LEU SER SER LYS GLN ILE
SEQRES 23 B 433 LYS THR ILE SER GLY LYS THR PRO GLN GLN TYR GLU ARG
SEQRES 24 B 433 GLU TYR ASN ASN LYS ARG SER GLY VAL GLY PRO SER LYS
SEQRES 25 B 433 PHE HIS GLY TYR ALA TYR ASP GLY ILE TRP VAL ILE ALA
SEQRES 26 B 433 LYS THR LEU GLN ARG ALA MET GLU THR LEU HIS ALA SER
SEQRES 27 B 433 SER ARG HIS GLN ARG ILE GLN ASP PHE ASN TYR THR ASP
SEQRES 28 B 433 HIS THR LEU GLY ARG ILE ILE LEU ASN ALA MET ASN GLU
SEQRES 29 B 433 THR ASN PHE PHE GLY VAL THR GLY GLN VAL VAL PHE ARG
SEQRES 30 B 433 ASN GLY GLU ARG MET GLY THR ILE LYS PHE THR GLN PHE
SEQRES 31 B 433 GLN ASP SER ARG GLU VAL LYS VAL GLY GLU TYR ASN ALA
SEQRES 32 B 433 VAL ALA ASP THR LEU GLU ILE ILE ASN ASP THR ILE ARG
SEQRES 33 B 433 PHE GLN GLY SER GLU PRO PRO LYS ASP ASP TYR LYS ASP
SEQRES 34 B 433 ASP ASP ASP LYS
MODRES 4MS3 ASN B 404 ASN GLYCOSYLATION SITE
HET ABU A 501 7
HET NAG B 501 14
HETNAM ABU GAMMA-AMINO-BUTANOIC ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN ABU GAMMA(AMINO)-BUTYRIC ACID
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 3 ABU C4 H9 N O2
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 HOH *306(H2 O)
HELIX 1 1 GLY A 67 SER A 84 1 18
HELIX 2 2 ASP A 104 ASN A 118 1 15
HELIX 3 3 CYS A 129 ALA A 140 1 12
HELIX 4 4 ARG A 141 ASN A 144 5 4
HELIX 5 5 SER A 154 ASN A 159 5 6
HELIX 6 6 SER A 172 THR A 174 5 3
HELIX 7 7 LEU A 175 GLY A 188 1 14
HELIX 8 8 THR A 199 ALA A 216 1 18
HELIX 9 9 PRO A 230 GLN A 240 1 11
HELIX 10 10 TYR A 250 ARG A 265 1 16
HELIX 11 11 ASN A 282 ILE A 286 5 5
HELIX 12 12 THR A 294 GLU A 303 1 10
HELIX 13 13 THR A 325 LEU A 337 1 13
HELIX 14 14 GLU A 349 SER A 368 1 20
HELIX 15 15 ARG A 377 PHE A 381 5 5
HELIX 16 16 GLN A 386 SER A 398 1 13
HELIX 17 17 TRP A 451 SER A 455 5 5
HELIX 18 18 LYS B 70 GLU B 91 1 22
HELIX 19 19 ASP B 109 GLY B 124 1 16
HELIX 20 20 CYS B 135 LEU B 146 1 12
HELIX 21 21 GLN B 147 ASN B 150 5 4
HELIX 22 22 THR B 160 ASP B 165 5 6
HELIX 23 23 SER B 178 ASN B 180 5 3
HELIX 24 24 ALA B 181 TYR B 193 1 13
HELIX 25 25 VAL B 205 TYR B 220 1 16
HELIX 26 26 PRO B 236 ASN B 246 1 11
HELIX 27 27 ASP B 256 GLU B 270 1 15
HELIX 28 28 LEU B 303 GLU B 312 1 10
HELIX 29 29 THR B 334 ARG B 346 1 13
HELIX 30 30 PHE B 354 MET B 373 1 20
HELIX 31 31 HIS B 377 PHE B 388 1 12
HELIX 32 32 ASP B 392 GLU B 405 1 14
SHEET 1 A 5 GLU A 93 ASP A 100 0
SHEET 2 A 5 ALA A 52 PHE A 59 1 N VAL A 53 O LYS A 95
SHEET 3 A 5 ILE A 124 MET A 126 1 O MET A 126 N GLY A 56
SHEET 4 A 5 ILE A 146 SER A 149 1 O LEU A 148 N LEU A 125
SHEET 5 A 5 PHE A 166 ARG A 168 1 O PHE A 167 N SER A 149
SHEET 1 B 8 GLU A 219 PHE A 226 0
SHEET 2 B 8 LYS A 191 GLN A 197 1 N ILE A 192 O GLU A 219
SHEET 3 B 8 ILE A 244 LEU A 248 1 O ILE A 244 N ALA A 193
SHEET 4 B 8 VAL A 272 ILE A 276 1 O VAL A 272 N ILE A 245
SHEET 5 B 8 ILE A 306 ILE A 310 1 O ILE A 306 N LEU A 275
SHEET 6 B 8 TRP A 419 GLN A 426 -1 O LEU A 421 N GLU A 309
SHEET 7 B 8 SER A 429 ASP A 437 -1 O GLY A 434 N ILE A 422
SHEET 8 B 8 ASP A 442 TRP A 445 -1 O SER A 444 N TYR A 435
SHEET 1 C 2 PHE A 401 GLY A 403 0
SHEET 2 C 2 GLY A 406 VAL A 408 -1 O GLY A 406 N GLY A 403
SHEET 1 D 5 PHE B 98 ASP B 105 0
SHEET 2 D 5 PRO B 55 MET B 62 1 N GLY B 60 O ARG B 102
SHEET 3 D 5 MET B 129 GLY B 132 1 O PHE B 131 N MET B 59
SHEET 4 D 5 VAL B 152 SER B 155 1 O LEU B 154 N GLY B 132
SHEET 5 D 5 PHE B 172 ARG B 174 1 O PHE B 173 N GLN B 153
SHEET 1 E 8 GLU B 225 PHE B 232 0
SHEET 2 E 8 ARG B 197 GLN B 203 1 N VAL B 198 O GLU B 225
SHEET 3 E 8 ILE B 250 GLN B 254 1 O GLN B 254 N GLN B 203
SHEET 4 E 8 GLN B 278 PRO B 282 1 O ILE B 280 N GLY B 253
SHEET 5 E 8 ILE B 315 PHE B 319 1 O ILE B 315 N ILE B 281
SHEET 6 E 8 THR B 425 PHE B 431 -1 O LYS B 427 N ASP B 318
SHEET 7 E 8 GLU B 436 ASN B 443 -1 O VAL B 437 N GLN B 430
SHEET 8 E 8 THR B 448 ILE B 451 -1 O GLU B 450 N GLU B 441
SHEET 1 F 3 ASN B 407 GLY B 410 0
SHEET 2 F 3 GLY B 413 ARG B 418 -1 O VAL B 415 N PHE B 408
SHEET 3 F 3 GLU B 421 MET B 423 -1 O GLU B 421 N ARG B 418
SSBOND 1 CYS A 103 CYS A 129 1555 1555 2.07
SSBOND 2 CYS A 259 CYS A 293 1555 1555 2.07
SSBOND 3 CYS B 108 CYS B 135 1555 1555 2.03
SSBOND 4 CYS B 237 CYS B 266 1555 1555 2.05
SSBOND 5 CYS B 265 CYS B 302 1555 1555 2.06
LINK ND2 ASN B 404 C1 NAG B 501 1555 1555 1.46
CISPEP 1 ASP A 119 PRO A 120 0 3.67
CISPEP 2 ARG B 95 PRO B 96 0 0.43
CRYST1 115.480 141.690 59.310 90.00 90.00 90.00 P 21 21 2 4
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 0.008660 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007058 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016861 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
